13:06:2021 12:12
PSI-MOD
1.2
Joshua Klein
Annotation note 01 - "[PSI-MOD:ref]" has been replaced by PubMed:18688235.
Annotation note 02 - When an entry in the RESID Database is annotated with different sources because the same modification can arise from different encoded amino acids, then the PSI-MOD definition for each different source instance carries the RESID cross-reference followed by a hash symbol "#" and a 3 or 4 character label. When an entry in the RESID Database is annotated as a general modification with the same enzymatic activity producing different chemical structures depending on natural variation in the nonproteinaceous substrate, on secondary modifications that do not change the nature of the primary modification, or on a combination of a primary and one or more secondary modifications on the same residue, then the PSI-MOD definition for each different instance carries the RESID cross-reference followed by the special tag "#var".
Annotation note 03 - When an entry in the Unimod database is annotated as a general modification, and one or more instance sites are listed, then the PSI-MOD definition for each different site instance carries the Unimod cross-reference followed by a hash symbol and an amino acid code, "N-term" or "C-term".
Annotation note 04 - The elemental formulas are in strict alphabetical order, not in CAS ("C" and "H" first) order. Isotope numbers are in parentheses before the element symbol, and an element should not occur in a formula both with and without an isotope number. In difference formulas, counts can be zero or negative.
Annotation note 05 - In entries with an isotope indicator in the formula, average masses are meaningless and are assigned the value equal to the monoisotopic mass, but rounded to a lower precision; monoisotopic masses are calculated by using the masses for the indicated isotopes and the most common isotopes for other elements without isotope indicators in the formulas.
Annotation note 06 - For cross-link modifications, the number following "Cross-link" in the comment record indicates the number of amino acid residues that appear in the origin record, used to check the difference formula and masses. This usage differs from RESID, where the cross-link number indicates the maximum number of peptide chains that can be cross-linked.
Annotation note 07 - The synonym cross-reference "MOD:old name" has been replaced by "MOD:alternate name".
Annotation note 08 - The DeltaMass listings for free amino acids have been removed. Most Unimod entries that have not been "approved" have by general agreement not been incorporated unless there has been a request for a specific term by a PRIDE submitter.
Annotation note 09 - The Open Mass Spectrometry Search Algorithm, OMSSA, enumerated list of modifications are being incorporated. The string values are synonyms with the synonymtypedef "OMSSA-label", and their integer values (which are supposed to be stable) are definition cross-references.
Annotation note 10 - GNOme is the Glycan Naming and Subsumption Ontology (https://gnome.glyomics.org/), an ontology for the support of glycomics. PSI-MOD does not have all possible glycans in its entries, just the ones that are noted to be on proteins and have been requested for addition. GNOme uses GlyTouCan (http://glytoucan.org/) to provide stable accessions for glycans described at varyious degrees of characterization, including compositions (no linkage) and topologies (no carbon bond positions or anomeric configurations).
ISO-8601 date: 2022-06-13 12:12Z
PSI-MOD version: 1.031.6
RESID release: 75.00
definition
term replaced by
Label from MS DeltaMass
Short label from OMSSA
Alternate name curated by PSI-MOD
Short label curated by PSI-MOD
subset of protein modifications
Agreed label from MS community
Alternate name from RESID
Misnomer tagged alternate name from RESID
Name from RESID
Systematic name from RESID
Protein feature description from UniProtKB
Alternate name from Unimod
Description (full_name) from Unimod
Interim label from Unimod
subset_property
synonym_type_property
database_cross_reference
has_exact_synonym
has_obo_format_version
has_obo_namespace
has_related_synonym
has_scope
has_synonym_type
in_subset
'Entity A' contains 'Entity B' implies that 'Entity B' is a part of the structure of 'Entity A'.
PSI-MOD
contains
The inverse relationship to "part of".
contains
'Entity A' contains 'Entity B' implies that 'Entity B' is a part of the structure of 'Entity A'.
PubMed:18688235
'Entity A' derives_from 'Entity B' implies that 'Entity A' is chemically derived from 'Entity B'.
PSI-MOD
derives_from
derives from
'Entity A' derives_from 'Entity B' implies that 'Entity A' is chemically derived from 'Entity B'.
PubMed:18688235
'Entity A' has_functional_parent 'Entity B' implies that 'Entity B' has at least one chacteristic group from which 'Entity A' can be derived by functional modification.
PSI-MOD
has_functional_parent
This relationship indicates that the formula and mass of the child are not inherited from the mass of the parent.
has functional parent
'Entity A' has_functional_parent 'Entity B' implies that 'Entity B' has at least one chacteristic group from which 'Entity A' can be derived by functional modification.
PubMed:18688235
'Entity A' part_of 'Entity B' implies that 'Entity A' is a part of the structure of 'Entity B'.
PSI-MOD
part_of
part of
'Entity A' part_of 'Entity B' implies that 'Entity A' is a part of the structure of 'Entity B'.
PubMed:18688235
Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue.
ModRes
PSI-MOD
MOD:00000
protein modification
Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue.
PubMed:18688235
ModRes
A protein modification that effectively replaces a hydrogen atom with an alkyl group.
AlkylRes
PSI-MOD
MOD:00001
alkylated residue
A protein modification that effectively replaces a hydrogen atom with an alkyl group.
PubMed:18688235
AlkylRes
A protein modification that effectively converts an L-serine residue to O3-glycosylserine.
S
natural
OGlycoSer
PSI-MOD
MOD:00002
O-glycosyl-L-serine
OGlycoSer
A protein modification that effectively converts an L-serine residue to O3-glycosylserine.
PubMed:18688235
Entry from Unimod.
PSI-MOD
MOD:00003
This term is for organizational use only and should not be assigned. [JSG]
Unimod
Entry from Unimod.
PubMed:18688235
Artifact entry from Unimod - OBSOLETE because organizational use is no longer required.
PSI-MOD
MOD:00004
artifact
true
Artifact entry from Unimod - OBSOLETE because organizational use is no longer required.
PubMed:18688235
A protein modification that effectively converts an L-threonine residue to O3-glycosylthreonine.
T
natural
OGlycoThr
PSI-MOD
MOD:00005
O-glycosyl-L-threonine
A protein modification that effectively converts an L-threonine residue to O3-glycosylthreonine.
PubMed:18688235
OGlycoThr
A protein modification that effectively replaces a residue hydrogen atom on a nitrogen with a carbohydrate-like group through a glycosidic bond.
NGlycoRes
PSI-MOD
MOD:00006
N-glycosylated residue
A protein modification that effectively replaces a residue hydrogen atom on a nitrogen with a carbohydrate-like group through a glycosidic bond.
PubMed:18688235
NGlycoRes
A protein modification that effectively substitutes a selenium atom for a sulfur atom.
46.91
C 0 H 0 N 0 O 0 S -1 Se 1
47.94445
X
natural
Unimod:162
Se(S)Res
PSI-MOD
Delta:S(-1)Se(1)
Selenium replaces sulphur
MOD:00007
selenium substitution for sulfur
A protein modification that effectively substitutes a selenium atom for a sulfur atom.
PubMed:12148805
Unimod:162
Se(S)Res
Delta:S(-1)Se(1)
Selenium replaces sulphur
Entry from Unimod representing one or more entries in RESID. OBSOLETE because organizational use is no longer required.
PSI-MOD
MOD:00008
common
true
Entry from Unimod representing one or more entries in RESID. OBSOLETE because organizational use is no longer required.
PubMed:18688235
A protein modification that removes a residue, or inserts or replaces a residue with a natural, standard or nonstandard, encoded residue.
X
natural
Res
alpha-amino acid
PSI-MOD
MOD:00009
natural residue
A protein modification that removes a residue, or inserts or replaces a residue with a natural, standard or nonstandard, encoded residue.
PubMed:6692818
RESID:AA0000
Res
alpha-amino acid
A protein modification that effectively converts a source amino acid residue to an L-alanine.
0.0
C 0 H 0 N 0 O 0
0.0
C 3 H 5 N 1 O 1
71.08
71.03712
A
natural
(2S)-2-aminopropanoic acid
2-aminopropionic acid
2-azanylpropanoic acid
Ala
L-alanine
alpha-alanine
alpha-aminopropionic acid
PSI-MOD
MOD:00010
L-alanine residue
A protein modification that effectively converts a source amino acid residue to an L-alanine.
ChEBI:29948
DeltaMass:0
PubMed:6692818
RESID:AA0001
(2S)-2-aminopropanoic acid
2-aminopropionic acid
2-azanylpropanoic acid
Ala
L-alanine
alpha-alanine
alpha-aminopropionic acid
A protein modification that effectively converts a source amino acid residue to an L-arginine.
0.0
C 0 H 0 N 0 O 0
0.0
C 6 H 12 N 4 O 1
156.19
156.1011
R
natural
(2S)-2-amino-5-[(diaminomethylidene)amino]pentanoic acid
2-amino-5-(carbamimidamido)pentanoic acid [tautomer]
2-amino-5-[(aminoiminomethyl)amino]pentanoic acid [tautomer]
2-amino-5-guanidinopentanoic acid
2-amino-5-guanidinovaleric acid
2-azanyl-5-[bis(azanyl)methylideneazanyl]pentanoic acid
Arg
L-arginine
alpha-amino-delta-guanidinovaleric acid
PSI-MOD
MOD:00011
L-arginine residue
A protein modification that effectively converts a source amino acid residue to an L-arginine.
ChEBI:29952
DeltaMass:0
PubMed:518876
PubMed:6692818
RESID:AA0002
(2S)-2-amino-5-[(diaminomethylidene)amino]pentanoic acid
2-amino-5-(carbamimidamido)pentanoic acid [tautomer]
2-amino-5-[(aminoiminomethyl)amino]pentanoic acid [tautomer]
2-amino-5-guanidinopentanoic acid
2-amino-5-guanidinovaleric acid
2-azanyl-5-[bis(azanyl)methylideneazanyl]pentanoic acid
Arg
L-arginine
alpha-amino-delta-guanidinovaleric acid
A protein modification that effectively converts a source amino acid residue to an L-asparagine.
0.0
C 0 H 0 N 0 O 0
0.0
C 4 H 6 N 2 O 2
114.1
114.04293
N
natural
(2S)-2-amino-4-butanediamic acid
2,4-bis(azanyl)-4-oxobutanoic acid
2,4-diamino-4-oxobutanoic acid
2-amino-3-carbamoylpropanoic acid
2-amino-4-butanediamic acid
2-aminosuccinamic acid
2-aminosuccinic acid 4-amide
Asn
L-asparagine
alpha-amino-beta-carbamylpropionic acid
alpha-aminosuccinamic acid
aspartic acid 4-amide
aspartic acid beta-amide
beta-asparagine
PSI-MOD
MOD:00012
L-asparagine residue
A protein modification that effectively converts a source amino acid residue to an L-asparagine.
ChEBI:29956
DeltaMass:0
PubMed:15736973
PubMed:5681232
PubMed:6692818
PubMed:9789001
RESID:AA0003
(2S)-2-amino-4-butanediamic acid
2,4-bis(azanyl)-4-oxobutanoic acid
2,4-diamino-4-oxobutanoic acid
2-amino-3-carbamoylpropanoic acid
2-amino-4-butanediamic acid
2-aminosuccinamic acid
2-aminosuccinic acid 4-amide
Asn
L-asparagine
alpha-amino-beta-carbamylpropionic acid
alpha-aminosuccinamic acid
aspartic acid 4-amide
aspartic acid beta-amide
beta-asparagine
A protein modification that effectively converts a source amino acid residue to an L-aspartic acid.
0.0
C 0 H 0 N 0 O 0
0.0
C 4 H 5 N 1 O 3
115.09
115.02694
D
natural
(2S)-2-aminobutanedioic acid
2-azanylbutanedioic acid
Asp
L-aspartic acid
aminosuccinic acid
PSI-MOD
MOD:00013
L-aspartic acid residue
A protein modification that effectively converts a source amino acid residue to an L-aspartic acid.
ChEBI:29958
DeltaMass:0
PubMed:1097438
PubMed:339692
PubMed:4399050
PubMed:5764436
PubMed:6692818
PubMed:8089117
PubMed:9521123
PubMed:9582379
RESID:AA0004
(2S)-2-aminobutanedioic acid
2-azanylbutanedioic acid
Asp
L-aspartic acid
aminosuccinic acid
A protein modification that effectively converts a source amino acid residue to an L-cysteine.
0.0
C 0 H 0 N 0 O 0 S 0
0.0
C 3 H 5 N 1 O 1 S 1
103.14
103.009186
C
natural
(2R)-2-amino-3-sulfanylpropanoic acid
(R)-cysteine
2-amino-3-mercaptopropanoic acid
2-amino-3-mercaptopropionic acid
2-azanyl-3-sulfanylpropanoic acid
3-mercapto-L-alanine
Cys
Cysteine (C, Cys)
L-(+)-cysteine
L-cysteine
alpha-amino-beta-mercaptopropanoic acid
alpha-amino-beta-mercaptopropionic acid
alpha-amino-beta-thiolpropionic acid
beta-mercaptoalanine
half-cystine
thioserine
PSI-MOD
MOD:00014
From DeltaMass: Average Mass: 121.
L-cysteine residue
A protein modification that effectively converts a source amino acid residue to an L-cysteine.
ChEBI:29950
DeltaMass:0
PubMed:1310545
PubMed:15790858
PubMed:3447159
PubMed:6692818
PubMed:7338899
RESID:AA0005
(2R)-2-amino-3-sulfanylpropanoic acid
(R)-cysteine
2-amino-3-mercaptopropanoic acid
2-amino-3-mercaptopropionic acid
2-azanyl-3-sulfanylpropanoic acid
3-mercapto-L-alanine
Cys
Cysteine (C, Cys)
L-(+)-cysteine
L-cysteine
alpha-amino-beta-mercaptopropanoic acid
alpha-amino-beta-mercaptopropionic acid
alpha-amino-beta-thiolpropionic acid
beta-mercaptoalanine
half-cystine
thioserine
A protein modification that effectively converts a source amino acid residue to an L-glutamic acid.
0.0
C 0 H 0 N 0 O 0
0.0
C 5 H 7 N 1 O 3
129.12
129.04259
E
natural
(2S)-2-aminopentanedioic acid
1-aminopropane-1,3-dicarboxylic acid
2-aminoglutaric acid
2-azanylpentanedioic acid
Glu
L-glutamic acid
alpha-aminoglutaric acid
glutaminic acid
PSI-MOD
MOD:00015
L-glutamic acid residue
A protein modification that effectively converts a source amino acid residue to an L-glutamic acid.
ChEBI:29972
DeltaMass:0
PubMed:1881881
PubMed:4565668
PubMed:4922541
PubMed:6692818
PubMed:9326660
PubMed:957425
RESID:AA0006
(2S)-2-aminopentanedioic acid
1-aminopropane-1,3-dicarboxylic acid
2-aminoglutaric acid
2-azanylpentanedioic acid
Glu
L-glutamic acid
alpha-aminoglutaric acid
glutaminic acid
A protein modification that effectively converts a source amino acid residue to an L-glutamine.
0.0
C 0 H 0 N 0 O 0
0.0
C 5 H 8 N 2 O 2
128.13
128.05858
Q
natural
(2S)-2-amino-5-pentanediamic acid
2,5-bis(azanyl)-5-oxopentanoic acid
2,5-diamino-5-oxopentanoic acid
2-amino-4-carbamoylbutanoic acid
2-aminoglutaramic acid
Gln
L-glutamine
alpha-amino-gamma-carbamylbutyric acid
glutamic acid 5-amide
glutamic acid gamma-amide
glutamide
PSI-MOD
MOD:00016
L-glutamine residue
glutamic acid gamma-amide
glutamide
A protein modification that effectively converts a source amino acid residue to an L-glutamine.
ChEBI:30011
DeltaMass:0
PubMed:3340166
PubMed:6692818
PubMed:9342308
RESID:AA0007
(2S)-2-amino-5-pentanediamic acid
2,5-bis(azanyl)-5-oxopentanoic acid
2,5-diamino-5-oxopentanoic acid
2-amino-4-carbamoylbutanoic acid
2-aminoglutaramic acid
Gln
L-glutamine
alpha-amino-gamma-carbamylbutyric acid
glutamic acid 5-amide
A protein modification that effectively converts a source amino acid residue to a glycine.
0.0
C 0 H 0 N 0 O 0
0.0
C 2 H 3 N 1 O 1
57.05
57.021465
G
natural
Gly
aminoacetic acid
aminoethanoic acid
azanylethanoic acid
glycine
glycocoll
PSI-MOD
MOD:00017
glycine residue
A protein modification that effectively converts a source amino acid residue to a glycine.
ChEBI:29947
DeltaMass:0
PubMed:1310545
PubMed:6692818
RESID:AA0008
Gly
aminoacetic acid
aminoethanoic acid
azanylethanoic acid
glycine
glycocoll
A protein modification that effectively converts a source amino acid residue to an L-histidine.
0.0
C 0 H 0 N 0 O 0
0.0
C 6 H 7 N 3 O 1
137.14
137.05891
H
natural
(2S)-2-amino-3-(1H-imidazol-4-yl)propanoic acid
(2S)-2-amino-3-(1H-imidazol-5-yl)propanoic acid [tautomer]
2-azanyl-3-(1H-imidazol-4-yl)propanoic acid
2-azanyl-3-(1H-imidazol-5-yl)propanoic acid [tautomer]
4-(2-amino-2-carboxyethyl)imidazole
His
L-histidine
alpha-amino-beta-(4-imidazole)propionic acid
glyoxaline-5-alanine
PSI-MOD
MOD:00018
L-histidine residue
A protein modification that effectively converts a source amino acid residue to an L-histidine.
ChEBI:29979
DeltaMass:0
PubMed:14342316
PubMed:2722967
PubMed:512
PubMed:5460889
PubMed:6129252
PubMed:6692818
PubMed:6876174
RESID:AA0009
(2S)-2-amino-3-(1H-imidazol-4-yl)propanoic acid
(2S)-2-amino-3-(1H-imidazol-5-yl)propanoic acid [tautomer]
2-azanyl-3-(1H-imidazol-4-yl)propanoic acid
2-azanyl-3-(1H-imidazol-5-yl)propanoic acid [tautomer]
4-(2-amino-2-carboxyethyl)imidazole
His
L-histidine
alpha-amino-beta-(4-imidazole)propionic acid
glyoxaline-5-alanine
A protein modification that effectively converts a source amino acid residue to an L-isoleucine.
0.0
C 0 H 0 N 0 O 0
0.0
C 6 H 11 N 1 O 1
113.16
113.08406
I
natural
(2S,3S)-2-amino-3-methylpentanoic acid
2-azanyl-3-methylpentanoic acid
3-methyl-norvaline
Ile
Isoleucyl
L-erythro-isoleucine
L-isoleucine
alpha-amino-beta-methylvaleric acid
PSI-MOD
MOD:00019
L-isoleucine residue
A protein modification that effectively converts a source amino acid residue to an L-isoleucine.
ChEBI:30009
DeltaMass:0
PubMed:6692818
RESID:AA0010
(2S,3S)-2-amino-3-methylpentanoic acid
2-azanyl-3-methylpentanoic acid
3-methyl-norvaline
Ile
Isoleucyl
L-erythro-isoleucine
L-isoleucine
alpha-amino-beta-methylvaleric acid
A protein modification that effectively converts a source amino acid residue to an L-leucine.
0.0
C 0 H 0 N 0 O 0
0.0
C 6 H 11 N 1 O 1
113.16
113.08406
L
natural
(2S)-2-amino-4-methylpentanoic acid
2-azanyl-4-methylpentanoic acid
4-methyl-norvaline
L-leucine
Leu
alpha-amino-gamma-methylvaleric acid
alpha-aminoisocaproic acid
PSI-MOD
MOD:00020
L-leucine residue
A protein modification that effectively converts a source amino acid residue to an L-leucine.
ChEBI:30006
DeltaMass:0
PubMed:11478885
PubMed:6692818
RESID:AA0011
(2S)-2-amino-4-methylpentanoic acid
2-azanyl-4-methylpentanoic acid
4-methyl-norvaline
L-leucine
Leu
alpha-amino-gamma-methylvaleric acid
alpha-aminoisocaproic acid
A protein modification that effectively converts a source amino acid residue to L-lysine.
0.0
C 0 H 0 N 0 O 0
0.0
C 6 H 12 N 2 O 1
128.18
128.09496
K
natural
(2S)-2,6-diaminohexanoic acid
2,6-bis(azanyl)hexanoic acid
6-amino-L-norleucine
ACT_SITE Schiff-base intermediate with substrate
L-lysine
Lys
alpha,epsilon-diaminocaproic acid
PSI-MOD
MOD:00021
L-lysine residue
A protein modification that effectively converts a source amino acid residue to L-lysine.
ChEBI:29967
DeltaMass:0
PubMed:3106962
PubMed:6120171
PubMed:6692818
RESID:AA0012
(2S)-2,6-diaminohexanoic acid
2,6-bis(azanyl)hexanoic acid
6-amino-L-norleucine
ACT_SITE Schiff-base intermediate with substrate
L-lysine
Lys
alpha,epsilon-diaminocaproic acid
A protein modification that effectively converts a source amino acid residue to L-methionine.
0.0
C 0 H 0 N 0 O 0 S 0
0.0
C 5 H 9 N 1 O 1 S 1
131.19
131.04048
M
natural
(2S)-2-amino-4-(methylsulfanyl)butanoic acid
2-amino-4-(methylthio)butanoic acid
2-amino-4-(methylthio)butyric acid
2-azanyl-4-(methylsulfanyl)butanoic acid
L-(-)-methionine
L-methionine
Met
S-methyl-L-homocysteine
alpha-amino-gamma-methylmercaptobutyric acid
alpha-amino-gamma-methylthiobutyric acid
gamma-methylthio-alpha-aminobutyric acid
PSI-MOD
MOD:00022
From DeltaMass: Average Mass: 149
L-methionine residue
A protein modification that effectively converts a source amino acid residue to L-methionine.
ChEBI:29983
DeltaMass:0
PubMed:6411710
PubMed:6692818
RESID:AA0013
(2S)-2-amino-4-(methylsulfanyl)butanoic acid
2-amino-4-(methylthio)butanoic acid
2-amino-4-(methylthio)butyric acid
2-azanyl-4-(methylsulfanyl)butanoic acid
L-(-)-methionine
L-methionine
Met
S-methyl-L-homocysteine
alpha-amino-gamma-methylmercaptobutyric acid
alpha-amino-gamma-methylthiobutyric acid
gamma-methylthio-alpha-aminobutyric acid
A protein modification that effectively converts a source amino acid residue to L-phenylalanine.
0.0
C 0 H 0 N 0 O 0
0.0
C 9 H 9 N 1 O 1
147.18
147.06842
F
natural
(2S)-2-amino-3-phenylpropanoic acid
2-azanyl-3-phenylpropanoic acid
L-phenylalanine
Phe
alpha-amino-beta-phenylpropionic acid
PSI-MOD
MOD:00023
L-phenylalanine residue
A protein modification that effectively converts a source amino acid residue to L-phenylalanine.
ChEBI:29997
DeltaMass:0
PubMed:6692818
RESID:AA0014
(2S)-2-amino-3-phenylpropanoic acid
2-azanyl-3-phenylpropanoic acid
L-phenylalanine
Phe
alpha-amino-beta-phenylpropionic acid
A protein modification that effectively converts a source amino acid residue to L-proline.
0.0
C 0 H 0 N 0 O 0
0.0
C 5 H 7 N 1 O 1
97.12
97.052765
P
natural
(2S)-2-pyrrolidinecarboxylic acid
L-proline
Pro
pyrrolidine-2-carboxylic acid
PSI-MOD
MOD:00024
L-proline residue
A protein modification that effectively converts a source amino acid residue to L-proline.
ChEBI:30017
DeltaMass:0
PubMed:6692818
PubMed:8547259
RESID:AA0015
(2S)-2-pyrrolidinecarboxylic acid
L-proline
Pro
pyrrolidine-2-carboxylic acid
A protein modification that effectively converts a source amino acid residue to L-serine.
0.0
C 0 H 0 N 0 O 0
0.0
C 3 H 5 N 1 O 2
87.08
87.03203
S
natural
(2S)-2-amino-3-hydroxypropanoic acid
2-azanyl-3-hydroxypropanoic acid
3-hydroxy-L-alanine
L-serine
Ser
alpha-amino-beta-hydroxypropionic acid
beta-hydroxyalanine
PSI-MOD
MOD:00025
L-serine residue
A protein modification that effectively converts a source amino acid residue to L-serine.
ChEBI:29999
DeltaMass:0
PubMed:4399050
PubMed:6692818
RESID:AA0016
(2S)-2-amino-3-hydroxypropanoic acid
2-azanyl-3-hydroxypropanoic acid
3-hydroxy-L-alanine
L-serine
Ser
alpha-amino-beta-hydroxypropionic acid
beta-hydroxyalanine
A protein modification that effectively converts a source amino acid residue to L-threonine.
0.0
C 0 H 0 N 0 O 0
0.0
C 4 H 7 N 1 O 2
101.1
101.047676
T
natural
(2S,3R)-2-amino-3-hydroxybutanoic acid
2-azanyl-3-hydroxybutanoic acid
L-threo-threonine
L-threonine
Thr
alpha-amino-beta-hydroxybutyric acid
beta-methylserine
PSI-MOD
MOD:00026
L-threonine residue
A protein modification that effectively converts a source amino acid residue to L-threonine.
ChEBI:30013
DeltaMass:0
PubMed:2989287
PubMed:6692818
RESID:AA0017
(2S,3R)-2-amino-3-hydroxybutanoic acid
2-azanyl-3-hydroxybutanoic acid
L-threo-threonine
L-threonine
Thr
alpha-amino-beta-hydroxybutyric acid
beta-methylserine
A protein modification that effectively converts a source amino acid residue to L-tryptophan.
0.0
C 0 H 0 N 0 O 0
0.0
C 11 H 10 N 2 O 1
186.21
186.07932
W
natural
(2S)-2-amino-3-(1H-indol-3-yl)propanoic acid
2-azanyl-3-(1H-indol-3-yl)propanoic acid
L-tryptophan
Trp
alpha-amino-beta-(3-indolyl)propionoic acid
beta(3-indolyl)alanine
PSI-MOD
MOD:00027
L-tryptophan residue
A protein modification that effectively converts a source amino acid residue to L-tryptophan.
ChEBI:29954
DeltaMass:0
PubMed:2059637
PubMed:6692818
PubMed:9324768
RESID:AA0018
(2S)-2-amino-3-(1H-indol-3-yl)propanoic acid
2-azanyl-3-(1H-indol-3-yl)propanoic acid
L-tryptophan
Trp
alpha-amino-beta-(3-indolyl)propionoic acid
beta(3-indolyl)alanine
A protein modification that effectively converts a source amino acid residue to L-tyrosine.
0.0
C 0 H 0 N 0 O 0
0.0
C 9 H 9 N 1 O 2
163.18
163.06332
Y
natural
(2S)-2-amino-3-(4-hydoxyphenyl)propanoic acid
2-azanyl-3-(4-hydoxyphenyl)propanoic acid
L-tyrosine
Tyr
alpha-amino-beta-(para-hydroxyphenyl)propionic acid
p-tyrosine
para-hydroxyphenylalanine
PSI-MOD
MOD:00028
L-tyrosine residue
A protein modification that effectively converts a source amino acid residue to L-tyrosine.
ChEBI:29975
DeltaMass:0
PubMed:2190093
PubMed:2542938
PubMed:5550972
PubMed:6061414
PubMed:6120171
PubMed:6692818
RESID:AA0019
(2S)-2-amino-3-(4-hydoxyphenyl)propanoic acid
2-azanyl-3-(4-hydoxyphenyl)propanoic acid
L-tyrosine
Tyr
alpha-amino-beta-(para-hydroxyphenyl)propionic acid
p-tyrosine
para-hydroxyphenylalanine
A protein modification that effectively converts a source amino acid residue to an L-valine.
0.0
C 0 H 0 N 0 O 0
0.0
C 5 H 9 N 1 O 1
99.13
99.06841
V
natural
(2S)-2-amino-3-methylbutanoic acid
2-azanyl-3-methylbutanoic acid
L-valine
Val
alpha-amino-beta-methylbutyric acid
alpha-aminoisovaleric acid
PSI-MOD
MOD:00029
L-valine residue
A protein modification that effectively converts a source amino acid residue to an L-valine.
ChEBI:30015
DeltaMass:0
PubMed:6692818
RESID:AA0020
(2S)-2-amino-3-methylbutanoic acid
2-azanyl-3-methylbutanoic acid
L-valine
Val
alpha-amino-beta-methylbutyric acid
alpha-aminoisovaleric acid
A protein modification that effectively converts a source amino acid residue to an N-formyl-L-methionine, a natural pretranslational modification.
0.0
C 0 H 0 N 0 O 0 S 0
0.0
C 6 H 10 N 1 O 2 S 1
160.21
160.04323
M
natural
N-term
(2S)-2-formylamino-4-(methylsulfanyl)butanoic acid
2-formamido-4-(methylsulfanyl)butanoic acid
2-formylamino-4-(methylthio)butanoic acid
2-formylazanyl-4-(methylsulfanyl)butanoic acid
MOD_RES N-formylmethionine
N-formyl-L-methionine
N-formylated L-methionine
fMet
nformylmet
PSI-MOD
FormylMet
MOD:00030
N-formyl-L-methionine residue
A protein modification that effectively converts a source amino acid residue to an N-formyl-L-methionine, a natural pretranslational modification.
ChEBI:33718
OMSSA:22
PubMed:10825024
PubMed:11152118
PubMed:2165784
PubMed:3042771
PubMed:8758896
RESID:AA0021#FMET
(2S)-2-formylamino-4-(methylsulfanyl)butanoic acid
2-formamido-4-(methylsulfanyl)butanoic acid
2-formylamino-4-(methylthio)butanoic acid
2-formylazanyl-4-(methylsulfanyl)butanoic acid
MOD_RES N-formylmethionine
N-formyl-L-methionine
N-formylated L-methionine
fMet
nformylmet
FormylMet
A protein modification that effectively converts a source amino acid residue to an L-selenocysteine, a natural pretranslational modification.
0.0
C 0 H 0 N 0 O 0 Se 0
0.0
C 3 H 5 N 1 O 1 Se 1
150.05
150.95363
U
natural
(2R)-2-amino-3-selanylpropanoic acid
2-azanyl-3-selanylpropanoic acid
3-selenylalanine
L-selenocysteine
NON_STD Selenocysteine
SeCys
Sec
selenium cysteine
PSI-MOD
MOD:00031
L-selenocysteine residue
A protein modification that effectively converts a source amino acid residue to an L-selenocysteine, a natural pretranslational modification.
ChEBI:30000
PubMed:10523135
PubMed:1066676
PubMed:2037562
PubMed:2963330
PubMed:4734725
PubMed:6076213
PubMed:6217842
PubMed:6714945
RESID:AA0022
(2R)-2-amino-3-selanylpropanoic acid
2-azanyl-3-selanylpropanoic acid
3-selenylalanine
L-selenocysteine
NON_STD Selenocysteine
SeCys
Sec
selenium cysteine
A protein modification that is not chemically categorized.
PSI-MOD
MOD:00032
This term is for organizational use only and should not be assigned. [JSG]
uncategorized protein modification
A protein modification that is not chemically categorized.
PubMed:18688235
A protein modification that crosslinks two or more amino acid residues with covalent bonds.
XLNK-Res-Res
PSI-MOD
MOD:00033
The covalent bond is formed directly between sidechain atoms. If non-aminoacid atoms are involved in connecting two or more peptide chain residues peptide chain, the connection is classified as a multivalent binding site.
crosslinked residues
A protein modification that crosslinks two or more amino acid residues with covalent bonds.
PubMed:18688235
XLNK-Res-Res
A protein modification that effectively cross-links two L-cysteine residues to form L-cystine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 6 H 8 N 2 O 2 S 2
204.26
204.00272
C, C
natural
(2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid)
3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid)
3,3'-dithiobis(2-aminopropanoic acid)
3,3'-dithiobisalanine
3,3'-dithiodialanine
Cys2
Cystine ((Cys)2)
DISULFID
DISULFID Interchain
L-cystine
XLNK-SCys-SCys
beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide
beta,beta'-dithiodialanine
bis(alpha-aminopropionic acid)-beta-disulfide
bis(beta-amino-beta-carboxyethyl)disulfide
dicysteine
PSI-MOD
2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid
MOD:00034
Cross-link 2; for formation of a disulfide bond between a peptide cysteine and a free cysteine, see MOD:00765.
L-cystine (cross-link)
A protein modification that effectively cross-links two L-cysteine residues to form L-cystine.
ChEBI:16283
DeltaMass:0
PubMed:1988019
PubMed:2001356
PubMed:2076469
PubMed:3083866
PubMed:366603
PubMed:7918467
PubMed:8344916
RESID:AA0025#CYS2
(2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid)
3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid)
3,3'-dithiobis(2-aminopropanoic acid)
3,3'-dithiobisalanine
3,3'-dithiodialanine
Cys2
Cystine ((Cys)2)
DISULFID
DISULFID Interchain
L-cystine
XLNK-SCys-SCys
beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide
beta,beta'-dithiodialanine
bis(alpha-aminopropionic acid)-beta-disulfide
bis(beta-amino-beta-carboxyethyl)disulfide
dicysteine
2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid
A protein modification that effectively converts an L-asparagine residue to (2S,3R)-3-hydroxyasparagine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 4 H 6 N 2 O 3
130.1
130.03784
N
natural
uniprot.ptm:PTM-0369
(2S,3R)-2,4-diamino-3-hydroxy-4-oxobutanoic acid
(2S,3R)-2-amino-3-hydroxy-4-butanediamic acid
(2S,3R)-3-hydroxyasparagine
(3R)3HyAsn
2-azanyl-3-hydroxy-4-butanediamic acid
L-erythro-beta-hydroxyasparagine
MOD_RES (3R)-3-hydroxyasparagine
erythro-beta-hydroxylated L-asparagine
PSI-MOD
MOD:00035
(2S,3R)-3-hydroxyasparagine
A protein modification that effectively converts an L-asparagine residue to (2S,3R)-3-hydroxyasparagine.
ChEBI:141853
PubMed:11823643
PubMed:2820791
RESID:AA0026
(2S,3R)-2,4-diamino-3-hydroxy-4-oxobutanoic acid
(2S,3R)-2-amino-3-hydroxy-4-butanediamic acid
(2S,3R)-3-hydroxyasparagine
(3R)3HyAsn
2-azanyl-3-hydroxy-4-butanediamic acid
L-erythro-beta-hydroxyasparagine
MOD_RES (3R)-3-hydroxyasparagine
erythro-beta-hydroxylated L-asparagine
A protein modification that effectively converts an L-aspartic acid residue to (2S,3R)-3-hydroxyaspartic acid.
16.0
C 0 H 0 N 0 O 1
15.994915
C 4 H 5 N 1 O 4
131.09
131.02185
D
natural
Unimod:35
uniprot.ptm:PTM-0371
(2S,3R)-2-amino-3-hydroxybutanedioic acid
(2S,3R)-3-hydroxyaspartic acid
(3R)3HyAsp
2-amino-3-hydroxysuccinic acid
2-azanyl-3-hydroxybutanedioic acid
3-hydroxyaspartic acid
L-erythro-beta-hydroxyaspartic acid
MOD_RES (3R)-3-hydroxyaspartate
erythro-beta-hydroxylated L-aspartic acid
hydroxylationd
PSI-MOD
Oxidation
MOD:00036
(2S,3R)-3-hydroxyaspartic acid
A protein modification that effectively converts an L-aspartic acid residue to (2S,3R)-3-hydroxyaspartic acid.
ChEBI:141848
OMSSA:59
PubMed:6572939
PubMed:6871167
PubMed:8355279
RESID:AA0027
Unimod:35#D
(2S,3R)-2-amino-3-hydroxybutanedioic acid
(2S,3R)-3-hydroxyaspartic acid
(3R)3HyAsp
2-amino-3-hydroxysuccinic acid
2-azanyl-3-hydroxybutanedioic acid
3-hydroxyaspartic acid
L-erythro-beta-hydroxyaspartic acid
MOD_RES (3R)-3-hydroxyaspartate
erythro-beta-hydroxylated L-aspartic acid
hydroxylationd
Oxidation
A protein modification that effectively converts an L-lysine residue to one of the diastereomeric 5-hydroxy-L-lysine residues.
16.0
C 0 H 0 N 0 O 1
15.994915
C 6 H 12 N 2 O 2
144.17
144.08987
K
natural
uniprot.ptm:PTM-0044
5-hydroxylated L-lysine
5HyLys
PSI-MOD
MOD:00037
5-hydroxy-L-lysine
A protein modification that effectively converts an L-lysine residue to one of the diastereomeric 5-hydroxy-L-lysine residues.
ChEBI:60175
PubMed:18688235
5-hydroxylated L-lysine
5HyLys
A protein modification that effectively converts an L-proline residue to 3-hydroxy-L-proline.
16.0
C 0 H 0 N 0 O 1
15.994915
C 5 H 7 N 1 O 2
113.12
113.047676
P
natural
uniprot.ptm:PTM-0030
(2S,3S)-3-hydroxypyrrolidine-2-carboxylic acid
3-hydroxy-L-proline
3-hydroxylated L-proline
3-trans-hydroxy-L-proline
3HyPro
L-threo-3-hydroxyproline
MOD_RES 3-hydroxyproline
beta-hydroxypyrrolidine-alpha-carboxylic acid
PSI-MOD
MOD:00038
3-hydroxy-L-proline
A protein modification that effectively converts an L-proline residue to 3-hydroxy-L-proline.
ChEBI:16889
PubMed:2400108
PubMed:3734192
PubMed:4343807
RESID:AA0029
(2S,3S)-3-hydroxypyrrolidine-2-carboxylic acid
3-hydroxy-L-proline
3-hydroxylated L-proline
3-trans-hydroxy-L-proline
3HyPro
L-threo-3-hydroxyproline
MOD_RES 3-hydroxyproline
beta-hydroxypyrrolidine-alpha-carboxylic acid
A protein modification that effectively converts an L-proline residue to 4-hydroxy-L-proline
16.0
C 0 H 0 N 0 O 1
15.994915
C 5 H 7 N 1 O 2
113.12
113.047676
P
natural
uniprot.ptm:PTM-0043
(2S,4R)-4-hydroxypyrrolidine-2-carboxylic acid
4-hydroxy-L-proline
4-hydroxylated L-proline
4-hydroxyproline
4-trans-hydroxy-L-proline
4HyPro
L-threo-4-hydroxyproline
MOD_RES 4-hydroxyproline
gamma-hydroxypyrrolidine-alpha-carboxylic acid
PSI-MOD
MOD:00039
4-hydroxy-L-proline
A protein modification that effectively converts an L-proline residue to 4-hydroxy-L-proline
ChEBI:18095
PubMed:11292863
PubMed:2400108
PubMed:3734192
RESID:AA0030
(2S,4R)-4-hydroxypyrrolidine-2-carboxylic acid
4-hydroxy-L-proline
4-hydroxylated L-proline
4-hydroxyproline
4-trans-hydroxy-L-proline
4HyPro
L-threo-4-hydroxyproline
MOD_RES 4-hydroxyproline
gamma-hydroxypyrrolidine-alpha-carboxylic acid
A protein modification that effectively converts an L-glutamine residue to 2-pyrrolidone-5-carboxylic acid.
-17.03
C 0 H -3 N -1 O 0
-17.026548
C 5 H 6 N 1 O 2
112.11
112.039856
Q
natural
N-term
Unimod:28
uniprot.ptm:PTM-0261
(2S)-5-oxo-2-pyrrolidinecarboxylic acid
2-oxopyrrolidine-5-carboxylic acid
2-pyrrolidone-5-carboxylic acid
5-oxoproline
5-oxopyrrolidine-2-carboxylic acid
5-pyrrolidone-2-carboxylic acid
MOD_RES Pyrrolidone carboxylic acid
N-pyrrolidone carboxyl (N terminus)
PCA
PyrGlu(Gln)
Pyroglutamic Acid formed from Gln
Pyroglutamyl
ntermpeppyroq
pyroglutamic acid
PSI-MOD
Gln->pyro-Glu
Pyro-glu from Q
MOD:00040
DeltaMass gives a formula C 5 H 5 N 1 O 2 with mass 111.1
2-pyrrolidone-5-carboxylic acid (Gln)
A protein modification that effectively converts an L-glutamine residue to 2-pyrrolidone-5-carboxylic acid.
ChEBI:30652
DeltaMass:123
OMSSA:110
PubMed:10214721
PubMed:1836357
PubMed:26343
PubMed:3473473
RESID:AA0031#GLN
Unimod:28#Q
(2S)-5-oxo-2-pyrrolidinecarboxylic acid
2-oxopyrrolidine-5-carboxylic acid
2-pyrrolidone-5-carboxylic acid
5-oxoproline
5-oxopyrrolidine-2-carboxylic acid
5-pyrrolidone-2-carboxylic acid
MOD_RES Pyrrolidone carboxylic acid
N-pyrrolidone carboxyl (N terminus)
PCA
PyrGlu(Gln)
Pyroglutamic Acid formed from Gln
Pyroglutamyl
ntermpeppyroq
pyroglutamic acid
Gln->pyro-Glu
Pyro-glu from Q
A protein modification that effectively converts an L-glutamic acid residue to L-gamma-carboxyglutamic acid.
44.01
C 1 H 0 N 0 O 2
43.98983
C 6 H 7 N 1 O 5
173.12
173.03242
E
natural
Unimod:299
uniprot.ptm:PTM-0039
(3S)-3-aminopropane-1,1,3-tricarboxylic acid
(3S)-3-azanylpropane-1,1,3-tricarboxylic acid
3-amino-1,1,3-propanetricarboxylic acid
3-azanylpropane-1,1,3-tricarboxylic acid
4-carboxyglutamic acid
4CbxGlu
Carboxy Glutamyl
L-gamma-carboxyglutamic acid
MOD_RES 4-carboxyglutamate
gamma-carboxylated L-glutamic acid
gammacarboxyle
PSI-MOD
1-carboxyglutamic acid
Carboxy
Carboxylation
MOD:00041
DeltaMass has an incorrect formula C 6 H 7 N 5 O 1 (N and O reversed) with mass 173.
L-gamma-carboxyglutamic acid
A protein modification that effectively converts an L-glutamic acid residue to L-gamma-carboxyglutamic acid.
DeltaMass:217
OMSSA:48
PubMed:10517147
PubMed:1807167
PubMed:3263814
PubMed:4528109
PubMed:7457858
PubMed:8135347
PubMed:8868490
PubMed:9188685
RESID:AA0032
Unimod:299#E
(3S)-3-aminopropane-1,1,3-tricarboxylic acid
(3S)-3-azanylpropane-1,1,3-tricarboxylic acid
3-amino-1,1,3-propanetricarboxylic acid
3-azanylpropane-1,1,3-tricarboxylic acid
4-carboxyglutamic acid
4CbxGlu
Carboxy Glutamyl
L-gamma-carboxyglutamic acid
MOD_RES 4-carboxyglutamate
gamma-carboxylated L-glutamic acid
gammacarboxyle
1-carboxyglutamic acid
Carboxy
Carboxy
Carboxylation
A protein modification that effectively converts an L-aspartic acid residue to L-aspartic 4-phosphoric anhydride.
79.98
C 0 H 1 N 0 O 3 P 1
79.96633
C 4 H 6 N 1 O 6 P 1
195.07
194.99327
D
natural
Unimod:21
uniprot.ptm:PTM-0038
(2S)-2-amino-4-oxo-4-(phosphonooxy)butanoic acid
2-aminobutanedioic 4-phosphoric anhydride
2-azanyl-4-oxo-4-(phosphonooxy)butanoic acid
4-oxo-O-phosphono-L-homoserine
4-phosphoaspartic acid
4-phosphorylated L-aspartatic acid
ACT_SITE 4-aspartylphosphate intermediate
L-aspartic 4-phosphoric anhydride
MOD_RES 4-aspartylphosphate
PAsp
beta-aspartyl phosphate
PSI-MOD
Phospho
Phosphorylation
MOD:00042
L-aspartic 4-phosphoric anhydride
A protein modification that effectively converts an L-aspartic acid residue to L-aspartic 4-phosphoric anhydride.
ChEBI:15836
PubMed:4357737
RESID:AA0033
Unimod:21#D
(2S)-2-amino-4-oxo-4-(phosphonooxy)butanoic acid
2-aminobutanedioic 4-phosphoric anhydride
2-azanyl-4-oxo-4-(phosphonooxy)butanoic acid
4-oxo-O-phosphono-L-homoserine
4-phosphoaspartic acid
4-phosphorylated L-aspartatic acid
ACT_SITE 4-aspartylphosphate intermediate
L-aspartic 4-phosphoric anhydride
MOD_RES 4-aspartylphosphate
PAsp
beta-aspartyl phosphate
Phospho
Phosphorylation
A protein modification that effectively converts an L-cysteine residue to S-phospho-L-cysteine.
79.98
C 0 H 1 N 0 O 3 P 1 S 0
79.96633
C 3 H 6 N 1 O 4 P 1 S 1
183.12
182.97551
C
natural
Unimod:21
uniprot.ptm:PTM-0251
(2R)-2-amino-3-(phosphonosulfanyl)propanoic acid
2-azanyl-3-(phosphonosulfanyl)propanoic acid
ACT_SITE Phosphocysteine intermediate
MOD_RES Phosphocysteine
PCys
S-phospho-L-cysteine
S-phosphonocysteine
S-phosphorylated L-cysteine
S3-phosphocysteine
cysteine phosphate thioester
PSI-MOD
Phospho
Phosphorylation
MOD:00043
S-phospho-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-phospho-L-cysteine.
PubMed:3142516
PubMed:7961745
PubMed:8128219
RESID:AA0034
Unimod:21#C
(2R)-2-amino-3-(phosphonosulfanyl)propanoic acid
2-azanyl-3-(phosphonosulfanyl)propanoic acid
ACT_SITE Phosphocysteine intermediate
MOD_RES Phosphocysteine
PCys
S-phospho-L-cysteine
S-phosphonocysteine
S-phosphorylated L-cysteine
S3-phosphocysteine
cysteine phosphate thioester
Phospho
Phosphorylation
A protein modification that effectively converts an L-histidine residue to tele-phospho-L-histidine (N-tau-phospho-L-histidine, 1'-phospho-L-histidine).
79.98
C 0 H 1 N 0 O 3 P 1
79.96633
C 6 H 8 N 3 O 4 P 1
217.12
217.02524
H
natural
uniprot.ptm:PTM-0325
(2S)-2-amino-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid
1'-phospho-L-histidine
2-azanyl-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid
ACT_SITE Tele-phosphohistidine intermediate
MOD_RES Tele-phosphohistidine
N(tau)-phosphohistidine
N1-phosphonohistidine
NE2-phosphonohistidine
NtPHis
Ntau-phosphorylated L-histidine
histidine-N(epsilon)-phosphate
histidine-N1'-phosphate
tele-phosphohistidine
PSI-MOD
Phospho
Phosphorylation
histidine-3-phosphate
MOD:00044
1'-phospho-L-histidine
A protein modification that effectively converts an L-histidine residue to tele-phospho-L-histidine (N-tau-phospho-L-histidine, 1'-phospho-L-histidine).
PubMed:11038361
PubMed:5642389
PubMed:6692818
RESID:AA0035
(2S)-2-amino-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid
1'-phospho-L-histidine
2-azanyl-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid
ACT_SITE Tele-phosphohistidine intermediate
MOD_RES Tele-phosphohistidine
N(tau)-phosphohistidine
N1-phosphonohistidine
NE2-phosphonohistidine
NtPHis
Ntau-phosphorylated L-histidine
histidine-N(epsilon)-phosphate
histidine-N1'-phosphate
tele-phosphohistidine
Phospho
Phosphorylation
histidine-3-phosphate
A protein modification that effectively converts an L-histidine residue to pros-phospho-L-histidine (N-pi-phospho-L-histidine, 3'-phospho-L-histidine).
79.98
C 0 H 1 N 0 O 3 P 1
79.96633
C 6 H 8 N 3 O 4 P 1
217.12
217.02524
H
natural
uniprot.ptm:PTM-0260
(2S)-2-amino-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid
2-azanyl-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid
3'-phospho-L-histidine
ACT_SITE Pros-phosphohistidine intermediate
MOD_RES Pros-phosphohistidine
N(pi)-phosphohistidine
N3-phosphonohistidine
ND1-phosphonohistidine
NpPHis
Npi-phosphorylated L-histidine
histidine-N(delta)-phosphate
histidine-N3'-phosphate
pros-phosphohistidine
PSI-MOD
Phospho
Phosphorylation
histidine-1-phosphate
MOD:00045
3'-phospho-L-histidine
A protein modification that effectively converts an L-histidine residue to pros-phospho-L-histidine (N-pi-phospho-L-histidine, 3'-phospho-L-histidine).
PubMed:1549615
PubMed:5642389
PubMed:6692818
PubMed:7669763
PubMed:7803390
RESID:AA0036
(2S)-2-amino-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid
2-azanyl-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid
3'-phospho-L-histidine
ACT_SITE Pros-phosphohistidine intermediate
MOD_RES Pros-phosphohistidine
N(pi)-phosphohistidine
N3-phosphonohistidine
ND1-phosphonohistidine
NpPHis
Npi-phosphorylated L-histidine
histidine-N(delta)-phosphate
histidine-N3'-phosphate
pros-phosphohistidine
Phospho
Phosphorylation
histidine-1-phosphate
A protein modification that effectively converts an L-serine residue to O-phospho-L-serine.
79.98
C 0 H 1 N 0 O 3 P 1
79.96633
C 3 H 6 N 1 O 5 P 1
167.06
166.99835
S
natural
Unimod:21
uniprot.ptm:PTM-0253
(2S)-2-amino-3-(phosphonooxy)propanoic acid
2-amino-3-hydroxypropanoic acid 3-phosphate
2-azanyl-3-(phosphonooxy)propanoic acid
ACT_SITE Phosphoserine intermediate
MOD_RES Phosphoserine
O-phospho-L-serine
O-phosphonoserine
O-phosphorylated L-serine
O3-phosphoserine
OPSer
Phospho Seryl
phosphorylations
serine phosphate ester
PSI-MOD
Phospho
Phosphorylation
MOD:00046
O-phospho-L-serine
A protein modification that effectively converts an L-serine residue to O-phospho-L-serine.
ChEBI:15811
DeltaMass:0
OMSSA:6
PubMed:12923550
PubMed:4065410
PubMed:8061611
RESID:AA0037
Unimod:21#S
(2S)-2-amino-3-(phosphonooxy)propanoic acid
2-amino-3-hydroxypropanoic acid 3-phosphate
2-azanyl-3-(phosphonooxy)propanoic acid
ACT_SITE Phosphoserine intermediate
MOD_RES Phosphoserine
O-phospho-L-serine
O-phosphonoserine
O-phosphorylated L-serine
O3-phosphoserine
OPSer
Phospho Seryl
phosphorylations
serine phosphate ester
Phospho
Phosphorylation
A protein modification that effectively converts an L-threonine residue to O-phospho-L-threonine.
79.98
C 0 H 1 N 0 O 3 P 1
79.96633
C 4 H 8 N 1 O 5 P 1
181.08
181.014
T
natural
Unimod:21
uniprot.ptm:PTM-0254
(2S,3R)-2-amino-3-(phosphonooxy)butanoic acid
2-amino-3-hydroxybutanoic acid 3-phosphate
2-azanyl-3-(phosphonooxy)butanoic acid
MOD_RES Phosphothreonine
O-phospho-L-threonine
O-phosphorylated L-threonine
O3-phosphothreonine
OPThr
Phospho Threonyl
phosphorylationt
threonine phosphate ester
PSI-MOD
Phospho
Phosphorylation
MOD:00047
O-phospho-L-threonine
A protein modification that effectively converts an L-threonine residue to O-phospho-L-threonine.
ChEBI:21967
DeltaMass:0
OMSSA:7
PubMed:12923550
PubMed:7678926
RESID:AA0038
Unimod:21#T
(2S,3R)-2-amino-3-(phosphonooxy)butanoic acid
2-amino-3-hydroxybutanoic acid 3-phosphate
2-azanyl-3-(phosphonooxy)butanoic acid
MOD_RES Phosphothreonine
O-phospho-L-threonine
O-phosphorylated L-threonine
O3-phosphothreonine
OPThr
Phospho Threonyl
phosphorylationt
threonine phosphate ester
Phospho
Phosphorylation
A protein modification that effectively converts an L-tyrosine residue to O4'-phospho-L-tyrosine.
79.98
C 0 H 1 N 0 O 3 P 1
79.96633
C 9 H 10 N 1 O 5 P 1
243.15
243.02966
Y
natural
Unimod:21
uniprot.ptm:PTM-0255
(2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid
2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate
2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid
MOD_RES Phosphotyrosine
O4'-phospho-L-tyrosine
O4'-phosphorylated L-tyrosine
O4-phosphotyrosine
OPTyr
Phospho Tyrosinyl
phosphorylationy
tyrosine phosphate
PSI-MOD
Phospho
Phosphorylation
MOD:00048
O4'-phospho-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to O4'-phospho-L-tyrosine.
DeltaMass:0
OMSSA:8
PubMed:10226369
PubMed:1725475
RESID:AA0039
Unimod:21#Y
(2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid
2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate
2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid
MOD_RES Phosphotyrosine
O4'-phospho-L-tyrosine
O4'-phosphorylated L-tyrosine
O4-phosphotyrosine
OPTyr
Phospho Tyrosinyl
phosphorylationy
tyrosine phosphate
Phospho
Phosphorylation
A protein modification that effectively converts an L-histidine residue to diphthamide.
143.21
C 7 H 15 N 2 O 1
143.11789
1+
C 13 H 22 N 5 O 2
280.35
280.1768
H
natural
Unimod:375
uniprot.ptm:PTM-0118
(2R)-1-amino-4-(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-aminium
(3-[4-(2-amino-2-carboxy-ethyl)-1H-imidazol-2-yl]-1-carbamoyl-propyl)-trimethylammonium
1-azanyl-4-(4-[2-azanyl-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-azanium
2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine
2-[(R)-3-carboxamido-3-(trimethylammonio)propyl]-4-((S)-2-amino-2-carboxyethyl)-1H-imidazole
2-[3-carboxamido-3-(trimethylammonio)propyl]histidine
2-amino-3-[[2-(3-amino-3-carbamoyl-prop-1-enyl)-1,1,3-trimethyl-2,3-dihydroimidazol-5-yl]]propanoic acid
2-amino-4-[[5-(2-amino-2-carboxylato-ethyl)-1,1,3-trimethyl-2,3-dihydroimidazol-2-yl]]but-3-enamide
Diphth
MOD_RES Diphthamide
alpha-(aminocarbonyl)-4-(2-amino-2-carboxyethyl)-N,N,N-trimethyl-1H-imidazole-2-propanaminium
diphthamide
diphthamide (from histidine)
PSI-MOD
Diphthamide
MOD:00049
2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine
A protein modification that effectively converts an L-histidine residue to diphthamide.
ChEBI:16692
DeltaMass:122
PubMed:15316019
PubMed:7430147
RESID:AA0040
Unimod:375#H
(2R)-1-amino-4-(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-aminium
(3-[4-(2-amino-2-carboxy-ethyl)-1H-imidazol-2-yl]-1-carbamoyl-propyl)-trimethylammonium
1-azanyl-4-(4-[2-azanyl-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-azanium
2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine
2-[(R)-3-carboxamido-3-(trimethylammonio)propyl]-4-((S)-2-amino-2-carboxyethyl)-1H-imidazole
2-[3-carboxamido-3-(trimethylammonio)propyl]histidine
2-amino-3-[[2-(3-amino-3-carbamoyl-prop-1-enyl)-1,1,3-trimethyl-2,3-dihydroimidazol-5-yl]]propanoic acid
2-amino-4-[[5-(2-amino-2-carboxylato-ethyl)-1,1,3-trimethyl-2,3-dihydroimidazol-2-yl]]but-3-enamide
Diphth
MOD_RES Diphthamide
alpha-(aminocarbonyl)-4-(2-amino-2-carboxyethyl)-N,N,N-trimethyl-1H-imidazole-2-propanaminium
diphthamide
diphthamide (from histidine)
Diphthamide
Diphthamide
A protein modification that effectively converts an L-alanine residue to N-acetyl-L-alanine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 5 H 8 N 1 O 2
114.12
114.055504
A
natural
N-term
uniprot.ptm:PTM-0199
(2S)-2-(acetamido)propanoic acid
2-(acetylamino)propanoic acid
2-(acetylazanyl)propanoic acid
AcAla
MOD_RES N-acetylalanine
N-acetyl-L-alanine
N-acetylated L-alanine
acetylalanine
PSI-MOD
MOD:00050
N-acetyl-L-alanine
A protein modification that effectively converts an L-alanine residue to N-acetyl-L-alanine.
PubMed:363452
PubMed:4700463
RESID:AA0041
(2S)-2-(acetamido)propanoic acid
2-(acetylamino)propanoic acid
2-(acetylazanyl)propanoic acid
AcAla
MOD_RES N-acetylalanine
N-acetyl-L-alanine
N-acetylated L-alanine
acetylalanine
A protein modification that effectively converts an L-aspartic acid residue to N-acetyl-L-aspartic acid.
42.04
C 2 H 2 N 0 O 1
42.010567
C 6 H 8 N 1 O 4
158.13
158.04533
D
natural
N-term
uniprot.ptm:PTM-0200
(2S)-2-(acetamido)butanedioic acid
2-(acetylamino)butanedioic acid
2-(acetylazanyl)butanedioic acid
AcAsp
MOD_RES N-acetylaspartate
N-acetyl-L-aspartic acid
N-acetylated L-aspartic acid
acetylaspartic acid
PSI-MOD
MOD:00051
N-acetyl-L-aspartic acid
A protein modification that effectively converts an L-aspartic acid residue to N-acetyl-L-aspartic acid.
ChEBI:21547
PubMed:1560020
PubMed:2395459
RESID:AA0042
(2S)-2-(acetamido)butanedioic acid
2-(acetylamino)butanedioic acid
2-(acetylazanyl)butanedioic acid
AcAsp
MOD_RES N-acetylaspartate
N-acetyl-L-aspartic acid
N-acetylated L-aspartic acid
acetylaspartic acid
A protein modification that effectively converts an L-cysteine residue to N-acetyl-L-cysteine.
42.04
C 2 H 2 N 0 O 1 S 0
42.010567
C 5 H 8 N 1 O 2 S 1
146.18
146.02757
C
natural
N-term
uniprot.ptm:PTM-0201
(2R)-2-acetamido-3-sulfanylpropanoic acid
2-acetylamino-3-mercaptopropanoic acid
2-acetylamino-3-sulfanylpropanoic acid
2-acetylazanyl-3-sulfanylpropanoic acid
MOD_RES N-acetylcysteine
N-acetyl-L-cysteine
N-acetylated cysteine
N-acetylcysteine
NAcCys
PSI-MOD
Acetyl
MOD:00052
incidental to RESID:AA0223
N-acetyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to N-acetyl-L-cysteine.
ChEBI:28939
PubMed:11857757
PubMed:11999733
PubMed:12175151
PubMed:14730666
PubMed:1500421
PubMed:15350136
PubMed:6725286
RESID:AA0043
(2R)-2-acetamido-3-sulfanylpropanoic acid
2-acetylamino-3-mercaptopropanoic acid
2-acetylamino-3-sulfanylpropanoic acid
2-acetylazanyl-3-sulfanylpropanoic acid
MOD_RES N-acetylcysteine
N-acetyl-L-cysteine
N-acetylated cysteine
N-acetylcysteine
NAcCys
Acetyl
A protein modification that effectively converts an L-glutamic acid residue to N-acetyl-L-glutamic acid.
42.04
C 2 H 2 N 0 O 1
42.010567
C 7 H 10 N 1 O 4
172.16
172.06099
E
natural
N-term
uniprot.ptm:PTM-0202
(2S)-2-(acetamido)pentanedioic acid
2-(acetylamino)pentanedioic acid
2-(acetylazanyl)pentanedioic acid
AcGlu
MOD_RES N-acetylglutamate
N-acetyl-L-glutamic acid
N-acetylated L-glutamic acid
acetylglutamic acid
PSI-MOD
MOD:00053
N-acetyl-L-glutamic acid
A protein modification that effectively converts an L-glutamic acid residue to N-acetyl-L-glutamic acid.
ChEBI:17533
PubMed:6725286
RESID:AA0044
(2S)-2-(acetamido)pentanedioic acid
2-(acetylamino)pentanedioic acid
2-(acetylazanyl)pentanedioic acid
AcGlu
MOD_RES N-acetylglutamate
N-acetyl-L-glutamic acid
N-acetylated L-glutamic acid
acetylglutamic acid
A protein modification that effectively converts an L-glutamine residue to N-acetyl-L-glutamine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 7 H 11 N 2 O 3
171.18
171.07697
Q
artifact
N-term
(2S)-2-acetamido-5-pentanediamic acid
2-acetylamino-5-amino-5-oxopentanoic acid
2-acetylamino-5-pentanediamic acid
2-acetylazanyl-5-azanyl-5-oxopentanoic acid
AcGln
N-acetyl-L-glutamine
N-acetylated L-glutamine
acetylglutamine
PSI-MOD
MOD:00054
This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
N-acetyl-L-glutamine
A protein modification that effectively converts an L-glutamine residue to N-acetyl-L-glutamine.
RESID:AA0045
(2S)-2-acetamido-5-pentanediamic acid
2-acetylamino-5-amino-5-oxopentanoic acid
2-acetylamino-5-pentanediamic acid
2-acetylazanyl-5-azanyl-5-oxopentanoic acid
AcGln
N-acetyl-L-glutamine
N-acetylated L-glutamine
acetylglutamine
A protein modification that effectively converts a glycine residue to N-acetylglycine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 4 H 6 N 1 O 2
100.1
100.039856
G
natural
N-term
uniprot.ptm:PTM-0203
(acetylamino)acetic acid
(acetylazanyl)ethanoic acid
2-(acetamido)ethanoic acid
2-(acetylamino)ethanoic acid
AcGly
MOD_RES N-acetylglycine
N-acetylated glycine
N-acetylglycine
aceturic acid
PSI-MOD
MOD:00055
N-acetylglycine
A protein modification that effectively converts a glycine residue to N-acetylglycine.
PubMed:272676
PubMed:5545094
PubMed:6754709
RESID:AA0046
(acetylamino)acetic acid
(acetylazanyl)ethanoic acid
2-(acetamido)ethanoic acid
2-(acetylamino)ethanoic acid
AcGly
MOD_RES N-acetylglycine
N-acetylated glycine
N-acetylglycine
aceturic acid
A protein modification that effectively converts an L-isoleucine residue to N-acetyl-L-isoleucine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 8 H 14 N 1 O 2
156.2
156.10245
I
artifact
N-term
uniprot.ptm:PTM-0204
(2S,3S)-2-acetamido-3-methylpentanoic acid
2-acetylamino-3-methylpentanoic acid
2-acetylazanyl-3-methylpentanoic acid
AcIle
N-acetyl-L-isoleucine
N-acetylated L-isoleucine
acetylisoleucine
PSI-MOD
MOD:00056
This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
N-acetyl-L-isoleucine
A protein modification that effectively converts an L-isoleucine residue to N-acetyl-L-isoleucine.
PubMed:8034631
RESID:AA0047
(2S,3S)-2-acetamido-3-methylpentanoic acid
2-acetylamino-3-methylpentanoic acid
2-acetylazanyl-3-methylpentanoic acid
AcIle
N-acetyl-L-isoleucine
N-acetylated L-isoleucine
acetylisoleucine
A protein modification that effectively converts an L-lysine residue to N2-acetyl-L-lysine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 8 H 15 N 2 O 2
171.22
171.11336
K
artifact
N-term
(2S)-2-acetamido-6-aminohexanoic acid
2-acetylamino-6-aminohexanoic acid
2-acetylazanyl-6-azanylhexanoic acid
N2-acetyl-L-lysine
N2-acetylated L-lysine
N2-acetyllysine
N2AcLys
PSI-MOD
Acetyl
MOD:00057
This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
N2-acetyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N2-acetyl-L-lysine.
PubMed:11857757
PubMed:11999733
PubMed:12175151
PubMed:14730666
PubMed:15350136
RESID:AA0048
(2S)-2-acetamido-6-aminohexanoic acid
2-acetylamino-6-aminohexanoic acid
2-acetylazanyl-6-azanylhexanoic acid
N2-acetyl-L-lysine
N2-acetylated L-lysine
N2-acetyllysine
N2AcLys
Acetyl
A protein modification that effectively converts an L-methionine to N-acetyl-L-methionine.
42.04
C 2 H 2 N 0 O 1 S 0
42.010567
C 7 H 12 N 1 O 2 S 1
174.24
174.05887
M
natural
N-term
uniprot.ptm:PTM-0205
(2S)-2-acetamido-4-(methylsulfanyl)butanoic acid
2-acetylamino-4-(methylsulfanyl)butanoic acid
2-acetylamino-4-(methylthio)butanoic acid
2-acetylazanyl-4-(methylsulfanyl)butanoic acid
AcMet
MOD_RES N-acetylmethionine
N-acetyl-L-methionine
N-acetylated L-methionine
acetylmethionine
methionamine
PSI-MOD
MOD:00058
N-acetyl-L-methionine
A protein modification that effectively converts an L-methionine to N-acetyl-L-methionine.
PubMed:7944406
RESID:AA0049
(2S)-2-acetamido-4-(methylsulfanyl)butanoic acid
2-acetylamino-4-(methylsulfanyl)butanoic acid
2-acetylamino-4-(methylthio)butanoic acid
2-acetylazanyl-4-(methylsulfanyl)butanoic acid
AcMet
MOD_RES N-acetylmethionine
N-acetyl-L-methionine
N-acetylated L-methionine
acetylmethionine
methionamine
A protein modification that effectively converts an L-proline residue to N-acetyl-L-proline.
42.04
C 2 H 2 N 0 O 1
42.010567
C 7 H 10 N 1 O 2
140.16
140.07115
P
natural
N-term
uniprot.ptm:PTM-0206
(2S)-1-acetyl-2-pyrrolidinecarboxylic acid
1-acetylproline
MOD_RES N-acetylproline
N-acetyl-L-proline
N-acetylated L-proline
N-acetylproline
NAcPro
acetylproline
PSI-MOD
MOD:00059
N-acetyl-L-proline
A protein modification that effectively converts an L-proline residue to N-acetyl-L-proline.
PubMed:2928307
RESID:AA0050
(2S)-1-acetyl-2-pyrrolidinecarboxylic acid
1-acetylproline
MOD_RES N-acetylproline
N-acetyl-L-proline
N-acetylated L-proline
N-acetylproline
NAcPro
acetylproline
A protein modification that effectively converts an L-serine residue to N-acetyl-L-serine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 5 H 8 N 1 O 3
130.12
130.05042
S
natural
N-term
uniprot.ptm:PTM-0207
(2S)-2-acetamido-3-hydroxypropanoic acid
2-acetylamino-3-hydroxypropanoic acid
2-acetylazanyl-3-hydroxypropanoic acid
MOD_RES N-acetylserine
N-acetyl-L-serine
N-acetylated L-serine
N-acetylserine
NAcSer
PSI-MOD
Acetyl
MOD:00060
N-acetyl-L-serine
A protein modification that effectively converts an L-serine residue to N-acetyl-L-serine.
PubMed:11857757
PubMed:11999733
PubMed:12175151
PubMed:14730666
PubMed:15350136
PubMed:1880797
PubMed:2106685
PubMed:6997045
RESID:AA0051
(2S)-2-acetamido-3-hydroxypropanoic acid
2-acetylamino-3-hydroxypropanoic acid
2-acetylazanyl-3-hydroxypropanoic acid
MOD_RES N-acetylserine
N-acetyl-L-serine
N-acetylated L-serine
N-acetylserine
NAcSer
Acetyl
A protein modification that effectively converts an L-threonine residue to N-acetyl-L-threonine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 6 H 10 N 1 O 3
144.15
144.06607
T
natural
N-term
uniprot.ptm:PTM-0208
(2S,3R)-2-acetamido-3-hydroxybutanoic acid
2-acetylamino-3-hydroxybutanoic acid
2-acetylazanyl-3-hydroxybutanoic acid
MOD_RES N-acetylthreonine
N-acetyl-L-threonine
N-acetylated L-threonine
N-acetylthreonine
N-methylcarbonylthreonine
NAcThr
PSI-MOD
Acetyl
Acetylation
MOD:00061
N-acetyl-L-threonine
A protein modification that effectively converts an L-threonine residue to N-acetyl-L-threonine.
PubMed:11857757
PubMed:11999733
PubMed:12175151
PubMed:14730666
PubMed:15350136
PubMed:2106685
PubMed:6997045
RESID:AA0052
(2S,3R)-2-acetamido-3-hydroxybutanoic acid
2-acetylamino-3-hydroxybutanoic acid
2-acetylazanyl-3-hydroxybutanoic acid
MOD_RES N-acetylthreonine
N-acetyl-L-threonine
N-acetylated L-threonine
N-acetylthreonine
N-methylcarbonylthreonine
NAcThr
Acetyl
Acetylation
A protein modification that effectively converts an L-tyrosine residue to N-acetyl-L-tyrosine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 11 H 12 N 1 O 3
206.22
206.08171
Y
natural
N-term
uniprot.ptm:PTM-0209
(2S)-2-acetamido-3-(4-hydoxyphenyl)propanoic acid
2-acetylamino-3-(4-hydoxyphenyl)propanoic acid
2-acetylazanyl-3-(4-hydoxyphenyl)propanoic acid
AcTyr
MOD_RES N-acetyltyrosine
N-acetyl-L-tyrosine
N-acetylated L-tyrosine
N-acetyltyrosine
PSI-MOD
Acetyl
MOD:00062
N-acetyl-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to N-acetyl-L-tyrosine.
PubMed:11857757
PubMed:11999733
PubMed:12175151
PubMed:14730666
PubMed:15350136
PubMed:2506074
PubMed:475783
RESID:AA0053
(2S)-2-acetamido-3-(4-hydoxyphenyl)propanoic acid
2-acetylamino-3-(4-hydoxyphenyl)propanoic acid
2-acetylazanyl-3-(4-hydoxyphenyl)propanoic acid
AcTyr
MOD_RES N-acetyltyrosine
N-acetyl-L-tyrosine
N-acetylated L-tyrosine
N-acetyltyrosine
Acetyl
A protein modification that effectively converts an L-valine residue to N-acetyl-L-valine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 7 H 12 N 1 O 2
142.18
142.0868
V
natural
N-term
uniprot.ptm:PTM-0210
(2S)-2-acetamido-3-methylbutanoic acid
2-acetylamino-3-methylbutanoic acid
2-acetylazanyl-3-methylbutanoic acid
AcVal
MOD_RES N-acetylvaline
N-acetyl-L-valine
N-acetylated L-valine
N-acetylvaline
PSI-MOD
MOD:00063
N-acetyl-L-valine
A protein modification that effectively converts an L-valine residue to N-acetyl-L-valine.
PubMed:1735421
RESID:AA0054
(2S)-2-acetamido-3-methylbutanoic acid
2-acetylamino-3-methylbutanoic acid
2-acetylazanyl-3-methylbutanoic acid
AcVal
MOD_RES N-acetylvaline
N-acetyl-L-valine
N-acetylated L-valine
N-acetylvaline
A protein modification that effectively converts an L-lysine residue to N6-acetyl-L-lysine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 8 H 14 N 2 O 2
170.21
170.10553
K
natural
Unimod:1
uniprot.ptm:PTM-0190
(2S)-6-acetamido-2-aminohexanoic acid
6-acetylamino-2-aminohexanoic acid
6-acetylazanyl-2-aminohexanoic acid
MOD_RES N6-acetyllysine
N(zeta)-acetyllysine
N6-acetyl-L-lysine
N6-acetylated L-lysine
N6AcLys
acetylk
epsilon-acetyllysine
PSI-MOD
Acetyl
Acetylation
MOD:00064
N6-acetyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-acetyl-L-lysine.
ChEBI:17752
DeltaMass:214
OMSSA:24
PubMed:11369851
PubMed:11857757
PubMed:11999733
PubMed:12175151
PubMed:14730666
PubMed:15350136
PubMed:1680872
PubMed:670159
RESID:AA0055
Unimod:1#K
(2S)-6-acetamido-2-aminohexanoic acid
6-acetylamino-2-aminohexanoic acid
6-acetylazanyl-2-aminohexanoic acid
MOD_RES N6-acetyllysine
N(zeta)-acetyllysine
N6-acetyl-L-lysine
N6-acetylated L-lysine
N6AcLys
acetylk
epsilon-acetyllysine
Acetyl
Acetylation
A protein modification that effectively converts an L-cysteine residue to S-acetyl-L-cysteine.
42.04
C 2 H 2 N 0 O 1 S 0
42.010567
C 5 H 7 N 1 O 2 S 1
145.18
145.01974
C
natural
Unimod:1
(2R)-3-acetylsulfanyl-2-aminopropanoic acid
2-amino-3-(acetylthio)propanoic acid
2-azanyl-3-(acetylsulfanyl)propanoic acid
ACT_SITE S-acetylcysteine intermediate
S-acetyl-L-cysteine
S-acetylcysteine
SAcCys
cysteine acetate thioester
PSI-MOD
Acetyl
Acetylation
MOD:00065
S-acetyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-acetyl-L-cysteine.
PubMed:11857757
PubMed:11999733
PubMed:12175151
PubMed:1310545
PubMed:14730666
PubMed:15350136
RESID:AA0056
Unimod:1#C
(2R)-3-acetylsulfanyl-2-aminopropanoic acid
2-amino-3-(acetylthio)propanoic acid
2-azanyl-3-(acetylsulfanyl)propanoic acid
ACT_SITE S-acetylcysteine intermediate
S-acetyl-L-cysteine
S-acetylcysteine
SAcCys
cysteine acetate thioester
Acetyl
Acetylation
A protein modification that effectively converts a glycine residue to N-formylglycine.
28.01
C 1 H 0 N 0 O 1
27.994915
C 3 H 4 N 1 O 2
86.07
86.0242
G
natural
N-term
uniprot.ptm:PTM-0211
(formylamino)acetic acid
(formylamino)ethanoic acid
(formylazanyl)ethanoic acid
2-formamidoacetic acid
2-formamidoethanoic acid
MOD_RES N-formylglycine
N(alpha)-formylglycine
N-formylated glycine
N-formylglycine
NFoGly
PSI-MOD
MOD:00066
N-formylglycine
A protein modification that effectively converts a glycine residue to N-formylglycine.
PubMed:5139483
RESID:AA0057
(formylamino)acetic acid
(formylamino)ethanoic acid
(formylazanyl)ethanoic acid
2-formamidoacetic acid
2-formamidoethanoic acid
MOD_RES N-formylglycine
N(alpha)-formylglycine
N-formylated glycine
N-formylglycine
NFoGly
A protein modification that effectively converts a glycine residue to N-D-glucuronoylglycine.
176.12
C 6 H 8 N 0 O 6
176.03209
C 8 H 12 N 1 O 7
234.18
234.06137
G
natural
N-term
uniprot.ptm:PTM-0331
2-(glucuronoylamino)ethanoic acid
MOD_RES N-D-glucuronoyl glycine
N-D-glucuronoyl-glycine
N-D-glucuronyl-glycine
NGlcAGly
ntermpepglucuronylg
PSI-MOD
Glucuronyl
MOD:00067
N-D-glucuronoylglycine
A protein modification that effectively converts a glycine residue to N-D-glucuronoylglycine.
OMSSA:50
PubMed:10858503
PubMed:12716131
PubMed:6493057
PubMed:7398618
RESID:AA0058
2-(glucuronoylamino)ethanoic acid
MOD_RES N-D-glucuronoyl glycine
N-D-glucuronoyl-glycine
N-D-glucuronyl-glycine
NGlcAGly
ntermpepglucuronylg
Glucuronyl
A protein modification that effectively converts a glycine residue to N-myristoylglycine.
210.36
C 14 H 26 N 0 O 1
210.19836
C 16 H 30 N 1 O 2
268.42
268.22766
G
natural
N-term
Unimod:45
uniprot.ptm:PTM-0221
(tetradecanoylamino)ethanoic acid
LIPID N-myristoyl glycine
N-(1-oxotetradecyl)glycine
N-(C14:0 aliphatic acyl)glycine
N-myristoyl-glycine
N-myristoylated glycine
N-myristylglycine
N-tetradecanoylglycine
NMyrGly
ntermpepmyristoylationg
PSI-MOD
Myristoyl
Myristoylation
MOD:00068
N-myristoylglycine
A protein modification that effectively converts a glycine residue to N-myristoylglycine.
OMSSA:80
PubMed:11955007
PubMed:11955008
PubMed:1326520
PubMed:1386601
PubMed:6436247
PubMed:7543369
RESID:AA0059
Unimod:45#G
(tetradecanoylamino)ethanoic acid
LIPID N-myristoyl glycine
N-(1-oxotetradecyl)glycine
N-(C14:0 aliphatic acyl)glycine
N-myristoyl-glycine
N-myristoylated glycine
N-myristylglycine
N-tetradecanoylglycine
NMyrGly
ntermpepmyristoylationg
Myristoyl
Myristoylation
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-L-cysteine.
238.41
C 16 H 30 N 0 O 1 S 0
238.22966
C 19 H 36 N 1 O 2 S 1
342.56
342.24667
C
natural
N-term
uniprot.ptm:PTM-0222
(2R)-2-hexadecanoylamino-3-sulfanylpropanoic acid
2-hexadecanamido-3-sulfanylpropanoic acid
2-hexadecanoylamino-3-mercaptopropanoic acid
LIPID N-palmitoyl cysteine
N-(1-oxahexadecyl)-L-cysteine
N-hexadecanoylated L-cysteine
N-palmitoyl-L-cysteine
N-palmitoylated L-cysteine
NPamCys
PSI-MOD
Palmitoyl
Palmitoylation
MOD:00069
incidental to RESID:AA0107 incidental to RESID:AA0309
N-palmitoyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-L-cysteine.
PubMed:10896212
PubMed:4575979
PubMed:9056182
PubMed:9593755
RESID:AA0060
(2R)-2-hexadecanoylamino-3-sulfanylpropanoic acid
2-hexadecanamido-3-sulfanylpropanoic acid
2-hexadecanoylamino-3-mercaptopropanoic acid
LIPID N-palmitoyl cysteine
N-(1-oxahexadecyl)-L-cysteine
N-hexadecanoylated L-cysteine
N-palmitoyl-L-cysteine
N-palmitoylated L-cysteine
NPamCys
Palmitoyl
Palmitoylation
A protein modification that effectively converts an L-alanine residue to N-methyl-L-alanine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 4 H 7 N 1 O 1
85.11
85.052765
A
natural
N-term
uniprot.ptm:PTM-0214
(2S)-2-methylaminopropanoic acid
2-methylazanylpropanoic acid
MOD_RES N-methylalanine
N-methyl-L-alanine
N-methylalanine
N-methylated L-alanine
NMe1Ala
PSI-MOD
Methyl
Methylation
MOD:00070
Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG].
N-methyl-L-alanine
A protein modification that effectively converts an L-alanine residue to N-methyl-L-alanine.
ChEBI:17519
PubMed:323502
PubMed:337304
PubMed:7007074
RESID:AA0061
(2S)-2-methylaminopropanoic acid
2-methylazanylpropanoic acid
MOD_RES N-methylalanine
N-methyl-L-alanine
N-methylalanine
N-methylated L-alanine
NMe1Ala
Methyl
Methylation
A protein modification that effectively converts an L-alanine residue to N,N,N-trimethyl-L-alanine.
43.09
C 3 H 7 N 0 O 0
43.054226
1+
C 6 H 13 N 1 O 1
115.18
115.09917
A
natural
N-term
uniprot.ptm:PTM-0177
(1S)-1-carboxy-N,N,N-trimethylethanaminium
(1S)-1-carboxy-N,N,N-trimethylethanazanium
(2S)-2-(trimethylammonio)propanoic acid
MOD_RES N,N,N-trimethylalanine
N,N,N-trimethyl-L-alanine
N,N,N-trimethylalanine cation
N,N,N-trimethylalaninium
N,N,N-trimethylated L-alanine
N2Me3+Ala
NMe3Ala
PSI-MOD
Trimethyl
tri-Methylation
MOD:00071
N,N,N-trimethyl-L-alanine
A protein modification that effectively converts an L-alanine residue to N,N,N-trimethyl-L-alanine.
PubMed:12590383
PubMed:332162
PubMed:3979397
PubMed:6778808
PubMed:7715456
RESID:AA0062
(1S)-1-carboxy-N,N,N-trimethylethanaminium
(1S)-1-carboxy-N,N,N-trimethylethanazanium
(2S)-2-(trimethylammonio)propanoic acid
MOD_RES N,N,N-trimethylalanine
N,N,N-trimethyl-L-alanine
N,N,N-trimethylalanine cation
N,N,N-trimethylalaninium
N,N,N-trimethylated L-alanine
N2Me3+Ala
NMe3Ala
Trimethyl
tri-Methylation
A protein modification that effectively converts a glycine residue to N-methylglycine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 3 H 5 N 1 O 1
71.08
71.03712
G
natural
N-term
uniprot.ptm:PTM-0483
L-sarcosine
MOD_RES N-methylglycine
N-methylated glycine
N-methylglycine
NMe1Gly
Sar
Sarcosine
Sarcosyl
methylaminoacetic acid
methylaminoethanoic acid
PSI-MOD
Methyl
Methylation
MOD:00072
DeltaMass also has an entry for the free amino acid. Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG].
N-methylglycine
A protein modification that effectively converts a glycine residue to N-methylglycine.
ChEBI:15611
DeltaMass:0
PubMed:1593629
RESID:AA0063
L-sarcosine
MOD_RES N-methylglycine
N-methylated glycine
N-methylglycine
NMe1Gly
Sar
Sarcosine
Sarcosyl
methylaminoacetic acid
methylaminoethanoic acid
Methyl
Methylation
A protein modification that effectively converts an L-methionine residue to N-methyl-L-methionine.
14.03
C 1 H 2 N 0 O 0 S 0
14.01565
C 6 H 11 N 1 O 1 S 1
145.22
145.05614
M
natural
N-term
uniprot.ptm:PTM-0217
(2S)-2-methylamino-4-(methylsulfanyl)butanoic acid
2-methylamino-4-(methylthio)butanoic acid
MOD_RES N-methylmethionine
Methyl Methionyl
N-methyl-L-methionine
N-methylated L-methionine
N-methylmethionine
NMe1Met
PSI-MOD
Methyl
Methylation
MOD:00073
Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG].
N-methyl-L-methionine
A protein modification that effectively converts an L-methionine residue to N-methyl-L-methionine.
DeltaMass:169
PubMed:323502
PubMed:3298225
RESID:AA0064
(2S)-2-methylamino-4-(methylsulfanyl)butanoic acid
2-methylamino-4-(methylthio)butanoic acid
MOD_RES N-methylmethionine
Methyl Methionyl
N-methyl-L-methionine
N-methylated L-methionine
N-methylmethionine
NMe1Met
Methyl
Methylation
A protein modification that effectively converts an L-phenylalanine residue to N-methyl-L-phenylalanine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 10 H 11 N 1 O 1
161.2
161.08406
F
natural
N-term
uniprot.ptm:PTM-0218
(2S)-2-methylamino-3-phenylpropanoic acid
MOD_RES N-methylphenylalanine
N-methyl-L-phenylalanine
N-methylated L-phenylalanine
N-methylphenylalanine
NMe1Phe
PSI-MOD
Methyl
Methylation
MOD:00074
Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG].
N-methyl-L-phenylalanine
A protein modification that effectively converts an L-phenylalanine residue to N-methyl-L-phenylalanine.
PubMed:2577730
PubMed:413571
RESID:AA0065
(2S)-2-methylamino-3-phenylpropanoic acid
MOD_RES N-methylphenylalanine
N-methyl-L-phenylalanine
N-methylated L-phenylalanine
N-methylphenylalanine
NMe1Phe
Methyl
Methylation
A protein modification that effectively converts an L-proline residue to N,N-dimethyl-L-proline.
29.06
C 2 H 5 N 0 O 0
29.038576
1+
C 7 H 13 N 1 O 1
127.19
127.09917
P
natural
N-term
Unimod:529
uniprot.ptm:PTM-0179
(2S)-2-carboxy-1,1-dimethylpyrrolidinium
1,1-dimethyl-L-prolinium
MOD_RES N,N-dimethylproline
N,N-dimethyl-L-proline
N,N-dimethyl-L-prolinium
N,N-dimethylated L-proline
NMe2Pro
stachydrin
PSI-MOD
Delta:H(5)C(2)
Dimethyl
Dimethylation of proline residue
MOD:00075
Unimod terminal specification corrected [JSG].
N,N-dimethyl-L-proline
A protein modification that effectively converts an L-proline residue to N,N-dimethyl-L-proline.
ChEBI:21451
PubMed:12964758
PubMed:14570711
PubMed:193025
PubMed:3882426
PubMed:6254758
RESID:AA0066
Unimod:529
(2S)-2-carboxy-1,1-dimethylpyrrolidinium
1,1-dimethyl-L-prolinium
MOD_RES N,N-dimethylproline
N,N-dimethyl-L-proline
N,N-dimethyl-L-prolinium
N,N-dimethylated L-proline
NMe2Pro
stachydrin
Delta:H(5)C(2)
Dimethyl
Dimethylation of proline residue
A protein modification that effectively converts an L-arginine residue to symmetric dimethylarginine, N(omega),N'(omega)-dimethyl-L-arginine.
28.05
C 2 H 4 N 0 O 0
28.0313
C 8 H 16 N 4 O 1
184.24
184.13242
R
natural
Unimod:36
uniprot.ptm:PTM-0287
(2S)-2-amino-5-[((methylamino)(methylimino)methyl)amino]pentanoic acid
MOD_RES Omega-N-methylated arginine
MOD_RES Symmetric dimethylarginine
N3,N4-dimethylarginine
N5-[(methylamino)(methylimino)methyl]ornithine
NG,N'G-dimethylarginine
NoNo'Me2Arg
omega-N,omega-N'-dimethyl-L-arginine
omega-N,omega-N'-dimethylated L-arginine
symmetric dimethylarginine
PSI-MOD
Dimethyl
di-Methylation
MOD:00076
symmetric dimethyl-L-arginine
A protein modification that effectively converts an L-arginine residue to symmetric dimethylarginine, N(omega),N'(omega)-dimethyl-L-arginine.
PubMed:12964758
PubMed:14570711
PubMed:15835918
PubMed:2426402
PubMed:5128665
RESID:AA0067
Unimod:36#R
(2S)-2-amino-5-[((methylamino)(methylimino)methyl)amino]pentanoic acid
MOD_RES Omega-N-methylated arginine
MOD_RES Symmetric dimethylarginine
N3,N4-dimethylarginine
N5-[(methylamino)(methylimino)methyl]ornithine
NG,N'G-dimethylarginine
NoNo'Me2Arg
omega-N,omega-N'-dimethyl-L-arginine
omega-N,omega-N'-dimethylated L-arginine
symmetric dimethylarginine
Dimethyl
di-Methylation
A protein modification that effectively converts an L-arginine residue to asymmetric dimethylarginine, N(omega),N(omega)-dimethyl-L-arginine.
28.05
C 2 H 4 N 0 O 0
28.0313
C 8 H 16 N 4 O 1
184.24
184.13242
R
natural
Unimod:36
uniprot.ptm:PTM-0066
(2S)-2-amino-5-([(dimethylamino)(imino)methyl]amino)pentanoic acid
MOD_RES Asymmetric dimethylarginine
MOD_RES Omega-N-methylated arginine
N5-[(dimethylamino)(imino)methyl]ornithine
NG,NG-dimethylarginine
NoNoMe2Arg
asymmetric dimethylarginine
omega-N,omega-N-dimethlyated L-arginine
omega-N,omega-N-dimethyl-L-arginine
PSI-MOD
Dimethyl
di-Methylation
MOD:00077
asymmetric dimethyl-L-arginine
A protein modification that effectively converts an L-arginine residue to asymmetric dimethylarginine, N(omega),N(omega)-dimethyl-L-arginine.
ChEBI:17929
PubMed:11152131
PubMed:12964758
PubMed:14570711
PubMed:15835918
PubMed:3032834
RESID:AA0068
Unimod:36#R
(2S)-2-amino-5-([(dimethylamino)(imino)methyl]amino)pentanoic acid
MOD_RES Asymmetric dimethylarginine
MOD_RES Omega-N-methylated arginine
N5-[(dimethylamino)(imino)methyl]ornithine
NG,NG-dimethylarginine
NoNoMe2Arg
asymmetric dimethylarginine
omega-N,omega-N-dimethlyated L-arginine
omega-N,omega-N-dimethyl-L-arginine
Dimethyl
di-Methylation
A protein modification that effectively converts an L-arginine residue to N(omega)-methyl-L-arginine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 7 H 14 N 4 O 1
170.22
170.11676
R
natural
uniprot.ptm:PTM-0237
(2S)-2-amino-5-[(imino(methylamino)methyl)amino]pentanoic acid
MOD_RES Omega-N-methylarginine
MOD_RES Omega-N-methylated arginine
NG-methylarginine
NoMeArg
omega-N-methyl-L-arginine
omega-N-methylated L-arginine
PSI-MOD
Methyl
Methylation
MOD:00078
omega-N-methyl-L-arginine
A protein modification that effectively converts an L-arginine residue to N(omega)-methyl-L-arginine.
PubMed:11875433
PubMed:15835918
PubMed:2426402
PubMed:5128665
RESID:AA0069
(2S)-2-amino-5-[(imino(methylamino)methyl)amino]pentanoic acid
MOD_RES Omega-N-methylarginine
MOD_RES Omega-N-methylated arginine
NG-methylarginine
NoMeArg
omega-N-methyl-L-arginine
omega-N-methylated L-arginine
Methyl
Methylation
A protein modification that effectively converts an L-asparagine residue to N4-methyl-L-asparagine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 5 H 8 N 2 O 2
128.13
128.05858
N
natural
Unimod:34
uniprot.ptm:PTM-0183
(2S)-2-amino-N4-methylbutanediamic acid
MOD_RES N4-methylasparagine
N(gamma)-methylasparagine
N-methylasparagine
N4-methyl-L-asparagine
N4-methylated L-asparagine
N4Me1Asn
beta-aspartyl methylamide
methyln
PSI-MOD
Methyl
Methylation
beta-methylasparagine
MOD:00079
N4-methyl-L-asparagine
A protein modification that effectively converts an L-asparagine residue to N4-methyl-L-asparagine.
OMSSA:75
PubMed:11875433
PubMed:2356973
PubMed:3782095
RESID:AA0070
Unimod:34#N
(2S)-2-amino-N4-methylbutanediamic acid
MOD_RES N4-methylasparagine
N(gamma)-methylasparagine
N-methylasparagine
N4-methyl-L-asparagine
N4-methylated L-asparagine
N4Me1Asn
beta-aspartyl methylamide
methyln
Methyl
Methylation
beta-methylasparagine
A protein modification that effectively converts an L-glutamine residue to N5-methyl-L-glutamine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 6 H 10 N 2 O 2
142.16
142.07423
Q
natural
uniprot.ptm:PTM-0185
(2S)-2-amino-5-methylamino-5-oxopentanoic acid
2-amino-N5-methylpentanediamic acid
MOD_RES N5-methylglutamine
N(delta)-methylglutamine
N-methylglutamine
N5-methyl-L-glutamine
N5-methylated L-glutamine
N5Me1Gln
gamma-methylglutamine
PSI-MOD
Methyl
Methylation
MOD:00080
N5-methyl-L-glutamine
A protein modification that effectively converts an L-glutamine residue to N5-methyl-L-glutamine.
ChEBI:17592
DeltaMass:166
PubMed:11118225
PubMed:11875433
PubMed:365579
RESID:AA0071
(2S)-2-amino-5-methylamino-5-oxopentanoic acid
2-amino-N5-methylpentanediamic acid
MOD_RES N5-methylglutamine
N(delta)-methylglutamine
N-methylglutamine
N5-methyl-L-glutamine
N5-methylated L-glutamine
N5Me1Gln
gamma-methylglutamine
Methyl
Methylation
A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-methyl ester.
14.03
C 1 H 2 N 0 O 0
14.01565
C 6 H 9 N 1 O 3
143.14
143.05824
E
natural
Unimod:34
uniprot.ptm:PTM-0128
(2S)-2-amino-5-methoxy-5-oxopentanoic acid
(5)-methyl L-hydrogen glutamate
2-aminopentanedioic acid 5-methyl ester
5-methyl L-2-aminoglutarate
5-methyl L-glutamate
5-methyl esterified L-glutamic acid
L-glutamic acid 5-methyl ester
MOD_RES Glutamate methyl ester (Glu)
O-methyl Glutamyl
O5MeGlu
glutamic acid 5-methyl ester
glutamic acid gamma-methyl ester
meestere
methyle
PSI-MOD
Methyl
Methylation
methyl ester
MOD:00081
DeltaMass gives the formula "C 6 H 9 O 1 N 3" with mass 143 (formula incorrect, N and O reversed) [JSG].
L-glutamic acid 5-methyl ester (Glu)
A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-methyl ester.
DeltaMass:167
OMSSA:17
OMSSA:70
PubMed:16888
PubMed:6300110
RESID:AA0072#GLU
Unimod:34#E
(2S)-2-amino-5-methoxy-5-oxopentanoic acid
(5)-methyl L-hydrogen glutamate
2-aminopentanedioic acid 5-methyl ester
5-methyl L-2-aminoglutarate
5-methyl L-glutamate
5-methyl esterified L-glutamic acid
L-glutamic acid 5-methyl ester
MOD_RES Glutamate methyl ester (Glu)
O-methyl Glutamyl
O5MeGlu
glutamic acid 5-methyl ester
glutamic acid gamma-methyl ester
meestere
methyle
Methyl
Methylation
methyl ester
A protein modification that effectively converts an L-histidine residue to pros-methyl-L-histidine (N-pi-methyl-L-histidine, 3'-methyl-L-histidine).
14.03
C 1 H 2 N 0 O 0
14.01565
C 7 H 9 N 3 O 1
151.17
151.07455
H
natural
uniprot.ptm:PTM-0259
(2S)-2-amino-3-(3-methyl-3H-imidazol-4-yl)propanoic acid
3'-methyl-L-histidine
MOD_RES Pros-methylhistidine
N(delta)-methylhistidine
N(pi)-methylhistidine
NpMeHis
pros-methylated L-histidine
pros-methylhistidine
PSI-MOD
1-methylhistidine
Methyl
Methylation
MOD:00082
3'-methyl-L-histidine
A protein modification that effectively converts an L-histidine residue to pros-methyl-L-histidine (N-pi-methyl-L-histidine, 3'-methyl-L-histidine).
PubMed:10660523
PubMed:11875433
PubMed:3467365
PubMed:6692818
PubMed:8076
PubMed:8645219
RESID:AA0073
(2S)-2-amino-3-(3-methyl-3H-imidazol-4-yl)propanoic acid
3'-methyl-L-histidine
MOD_RES Pros-methylhistidine
N(delta)-methylhistidine
N(pi)-methylhistidine
NpMeHis
pros-methylated L-histidine
pros-methylhistidine
1-methylhistidine
Methyl
Methylation
A protein modification that effectively converts an L-lysine residue to N6,N6,N6-trimethyl-L-lysine.
43.09
C 3 H 7 N 0 O 0
43.054226
1+
C 9 H 19 N 2 O 1
171.26
171.14919
K
natural
uniprot.ptm:PTM-0187
(5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium
2-amino-6-(trimethylammonio)hexanoic acid
5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium
MOD_RES N6,N6,N6-trimethyllysine
N(zeta)-trimethyllysine
N-trimethylation (of lysine)
N6,N6,N6-trimethyl-L-lysine
N6,N6,N6-trimethylated L-lysine
N6,N6,N6-trimethyllysin-N6-ium
N6,N6,N6-trimethyllysine cation
N6Me3+Lys
epsilon-trimethyllysine
PSI-MOD
Trimethyl
tri-Methylation
MOD:00083
DeltaMass calculates the mass difference from protonated lysine rather than neutral lysine; for trimethylated lysine starting from protonated lysine see MOD:00855
N6,N6,N6-trimethyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6,N6,N6-trimethyl-L-lysine.
ChEBI:17311
PubMed:12590383
PubMed:3145979
PubMed:4304194
PubMed:6778808
PubMed:7093227
PubMed:8453381
RESID:AA0074
(5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium
2-amino-6-(trimethylammonio)hexanoic acid
5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium
MOD_RES N6,N6,N6-trimethyllysine
N(zeta)-trimethyllysine
N-trimethylation (of lysine)
N6,N6,N6-trimethyl-L-lysine
N6,N6,N6-trimethylated L-lysine
N6,N6,N6-trimethyllysin-N6-ium
N6,N6,N6-trimethyllysine cation
N6Me3+Lys
epsilon-trimethyllysine
Trimethyl
tri-Methylation
A protein modification that effectively converts an L-lysine residue to N6,N6-dimethyl-L-lysine.
28.05
C 2 H 4 N 0 O 0
28.0313
C 8 H 16 N 2 O 1
156.23
156.12627
K
natural
Unimod:36
uniprot.ptm:PTM-0188
(2S)-2-amino-6-(dimethylamino)hexanoic acid
MOD_RES N6,N6-dimethyllysine
N(zeta)-dimethyllysine
N6,N6-dimethyl-L-lysine
N6,N6-dimethylated L-lysine
N6Me2Lys
dimethylk
epsilon-dimethyllysine
lysine derivative Lys(y)
PSI-MOD
Dimethyl
di-Methylation
MOD:00084
N6,N6-dimethyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6,N6-dimethyl-L-lysine.
OMSSA:36
PubMed:10550045
PubMed:12964758
PubMed:14570711
PubMed:3100523
PubMed:8453381
RESID:AA0075
Unimod:36#K
(2S)-2-amino-6-(dimethylamino)hexanoic acid
MOD_RES N6,N6-dimethyllysine
N(zeta)-dimethyllysine
N6,N6-dimethyl-L-lysine
N6,N6-dimethylated L-lysine
N6Me2Lys
dimethylk
epsilon-dimethyllysine
lysine derivative Lys(y)
Dimethyl
di-Methylation
A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 7 H 14 N 2 O 1
142.2
142.11061
K
natural
Unimod:34
uniprot.ptm:PTM-0194
(2S)-2-amino-6-methylaminohexanoic acid
MOD_RES N6-methyllysine
N(zeta)-methyllysine
N-methyl Lysyl
N6-methyl-L-lysine
N6-methylated L-lysine
N6Me1Lys
epsilon-methyllysine
PSI-MOD
Methyl
Methylation
MOD:00085
N6-methyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine.
ChEBI:17604
DeltaMass:165
PubMed:11875433
PubMed:3926756
RESID:AA0076
Unimod:34#K
(2S)-2-amino-6-methylaminohexanoic acid
MOD_RES N6-methyllysine
N(zeta)-methyllysine
N-methyl Lysyl
N6-methyl-L-lysine
N6-methylated L-lysine
N6Me1Lys
epsilon-methyllysine
Methyl
Methylation
A protein modification that effectively converts an L-lysine residue to N6-palmitoyl-L-lysine.
238.41
C 16 H 30 N 0 O 1
238.22966
C 22 H 42 N 2 O 2
366.59
366.32462
K
natural
Unimod:47
uniprot.ptm:PTM-0197
(2S)-2-amino-6-(hexadecanoylamino)hexanoic acid
2-amino-6-(hexadecanamido)hexanoic acid
LIPID N6-palmitoyl lysine
N(zeta)-palmitoyllysine
N6-(1-oxohexadecyl)-L-lysine
N6-hexadecanoylated L-lysine
N6-palmitoyl-L-lysine
N6-palmitoylated L-lysine
N6PamLys
epsilon-palmitoyllysine
palmitoylationk
PSI-MOD
Palmitoyl
Palmitoylation
MOD:00086
N6-palmitoyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-palmitoyl-L-lysine.
OMSSA:93
PubMed:2498336
PubMed:7801126
PubMed:7939682
RESID:AA0077
Unimod:47#K
(2S)-2-amino-6-(hexadecanoylamino)hexanoic acid
2-amino-6-(hexadecanamido)hexanoic acid
LIPID N6-palmitoyl lysine
N(zeta)-palmitoyllysine
N6-(1-oxohexadecyl)-L-lysine
N6-hexadecanoylated L-lysine
N6-palmitoyl-L-lysine
N6-palmitoylated L-lysine
N6PamLys
epsilon-palmitoyllysine
palmitoylationk
Palmitoyl
Palmitoylation
A protein modification that effectively converts an L-lysine residue to N6-myristoyl-L-lysine.
210.36
C 14 H 26 N 0 O 1
210.19836
C 20 H 38 N 2 O 2
338.54
338.29333
K
natural
Unimod:45
uniprot.ptm:PTM-0196
(2S)-2-amino-6-(tetradecanoylamino)hexanoic acid
2-amino-6-(tetradecanamido)hexanoic acid
LIPID N6-myristoyl lysine
N(zeta)-myristoyllysine
N6-(1-oxotetradecyl)-L-lysine
N6-(C14:0 aliphatic acyl)lysine
N6-myristoyl-L-lysine
N6-myristoylated L-lysine
N6MyrLys
epsilon-myristoyllysine
myristoylationk
PSI-MOD
Myristoyl
Myristoylation
MOD:00087
N6-myristoyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-myristoyl-L-lysine.
OMSSA:81
PubMed:1402651
PubMed:8346241
RESID:AA0078
Unimod:45#K
(2S)-2-amino-6-(tetradecanoylamino)hexanoic acid
2-amino-6-(tetradecanamido)hexanoic acid
LIPID N6-myristoyl lysine
N(zeta)-myristoyllysine
N6-(1-oxotetradecyl)-L-lysine
N6-(C14:0 aliphatic acyl)lysine
N6-myristoyl-L-lysine
N6-myristoylated L-lysine
N6MyrLys
epsilon-myristoyllysine
myristoylationk
Myristoyl
Myristoylation
A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine.
238.41
C 16 H 30 N 0 O 1
238.22966
C 20 H 37 N 1 O 3
339.52
339.27734
T
natural
Unimod:47
uniprot.ptm:PTM-0242
(2S,3R)-2-amino-3-(hexadecanoyloxy)butanoic acid
L-threonine hexadecanoate ester
LIPID O-palmitoyl threonine
O-hexadecanoylated L-threonine
O-palmitoyl-L-threonine
O-palmitoylated L-threonine
O3-palmitoyl-threonine
OPamThr
palmitoylationt
threonine palmitate ester
PSI-MOD
Palmitoyl
Palmitoylation
MOD:00088
O-palmitoyl-L-threonine
A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine.
OMSSA:95
PubMed:6642431
PubMed:8413602
RESID:AA0079
Unimod:47#T
(2S,3R)-2-amino-3-(hexadecanoyloxy)butanoic acid
L-threonine hexadecanoate ester
LIPID O-palmitoyl threonine
O-hexadecanoylated L-threonine
O-palmitoyl-L-threonine
O-palmitoylated L-threonine
O3-palmitoyl-threonine
OPamThr
palmitoylationt
threonine palmitate ester
Palmitoyl
Palmitoylation
A protein modification that effectively converts an L-serine residue to O-palmitoyl-L-serine.
238.41
C 16 H 30 N 0 O 1
238.22966
C 19 H 35 N 1 O 3
325.49
325.2617
S
natural
Unimod:47
uniprot.ptm:PTM-0241
(2S)-2-amino-3-(hexadecanoyloxy)propanoic acid
ACT_SITE O-palmitoyl serine intermediate
L-serine hexadecanoate ester
LIPID O-palmitoyl serine
O-hexadecanoylated L-serine
O-palmitoyl-L-serine
O-palmitoylated L-serine
O3-palmitoyl-serine
OPamSer
palmitoylations
serine palmitate ester
PSI-MOD
Palmitoyl
Palmitoylation
MOD:00089
O-palmitoyl-L-serine
A protein modification that effectively converts an L-serine residue to O-palmitoyl-L-serine.
OMSSA:94
PubMed:3467339
RESID:AA0080
Unimod:47#S
(2S)-2-amino-3-(hexadecanoyloxy)propanoic acid
ACT_SITE O-palmitoyl serine intermediate
L-serine hexadecanoate ester
LIPID O-palmitoyl serine
O-hexadecanoylated L-serine
O-palmitoyl-L-serine
O-palmitoylated L-serine
O3-palmitoyl-serine
OPamSer
palmitoylations
serine palmitate ester
Palmitoyl
Palmitoylation
A protein modification that effectively converts an L-alanine residue to L-alanine amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 3 H 7 N 2 O 1
87.1
87.05584
A
natural
C-term
uniprot.ptm:PTM-0057
(2S)-2-aminopropanamide
AlaN
L-alanine amide
MOD_RES Alanine amide
alaninamide
amidated L-alanine
PSI-MOD
MOD:00090
L-alanine amide
A protein modification that effectively converts an L-alanine residue to L-alanine amide.
PubMed:1377792
PubMed:2069951
PubMed:8472537
PubMed:952951
RESID:AA0081
(2S)-2-aminopropanamide
AlaN
L-alanine amide
MOD_RES Alanine amide
alaninamide
amidated L-alanine
A protein modification that effectively converts an L-arginine residue to L-arginine amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 6 H 14 N 5 O 1
172.21
172.11984
R
natural
C-term
uniprot.ptm:PTM-0060
(2S)-2-amino-5-[(diaminomethylidene)amino]pentanamide
2-amino-5-carbamimidamidopentanamide
2-amino-5-guanidinopentanamide
ArgN
L-arginine amide
MOD_RES Arginine amide
amidated L-arginine
argininamide
PSI-MOD
MOD:00091
L-arginine amide
A protein modification that effectively converts an L-arginine residue to L-arginine amide.
ChEBI:145897
PubMed:2229025
PubMed:2753890
PubMed:743209
RESID:AA0082
(2S)-2-amino-5-[(diaminomethylidene)amino]pentanamide
2-amino-5-carbamimidamidopentanamide
2-amino-5-guanidinopentanamide
ArgN
L-arginine amide
MOD_RES Arginine amide
amidated L-arginine
argininamide
A protein modification that effectively converts an L-asparagine residue to L-asparagine amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 4 H 8 N 3 O 2
130.13
130.06165
N
natural
C-term
uniprot.ptm:PTM-0062
(2S)-2-aminobutanediamide
AsnN
L-asparagine amide
MOD_RES Asparagine amide
amidated L-asparagine
asparaginamide
PSI-MOD
MOD:00092
L-asparagine amide
A protein modification that effectively converts an L-asparagine residue to L-asparagine amide.
ChEBI:145898
PubMed:2753132
PubMed:279902
PubMed:3415690
RESID:AA0083
(2S)-2-aminobutanediamide
AsnN
L-asparagine amide
MOD_RES Asparagine amide
amidated L-asparagine
asparaginamide
A protein modification that effectively converts an L-aspartic acid residue to L-aspartic acid 1-amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 4 H 7 N 2 O 3
131.11
131.04567
D
natural
C-term
uniprot.ptm:PTM-0063
(2S)-2-amino-1-butanediamic acid
1-amidated L-aspartic acid
3,4-diamino-4-oxobutanoic acid
3-amino-succinamic acid
AspN
L-aspartic acid 1-amide
MOD_RES Aspartic acid 1-amide
alpha-asparagine
isoasparagine
PSI-MOD
MOD:00093
L-aspartic acid 1-amide
A protein modification that effectively converts an L-aspartic acid residue to L-aspartic acid 1-amide.
PubMed:2542051
RESID:AA0084
(2S)-2-amino-1-butanediamic acid
1-amidated L-aspartic acid
3,4-diamino-4-oxobutanoic acid
3-amino-succinamic acid
AspN
L-aspartic acid 1-amide
MOD_RES Aspartic acid 1-amide
alpha-asparagine
isoasparagine
A protein modification that effectively converts an L-cysteine residue to L-cysteine amide.
-0.98
C 0 H 1 N 1 O -1 S 0
-0.984016
C 3 H 7 N 2 O 1 S 1
119.16
119.02791
C
natural
C-term
uniprot.ptm:PTM-0102
(2R)-2-amino-3-sulfanylpropanamide
2-amino-3-mercaptopropanamide
CysN
L-cysteine amide
MOD_RES Cysteine amide
amidated L-cysteine
cysteinamide
PSI-MOD
MOD:00094
L-cysteine amide
A protein modification that effectively converts an L-cysteine residue to L-cysteine amide.
PubMed:1892838
PubMed:7149738
RESID:AA0085
(2R)-2-amino-3-sulfanylpropanamide
2-amino-3-mercaptopropanamide
CysN
L-cysteine amide
MOD_RES Cysteine amide
amidated L-cysteine
cysteinamide
A protein modification that effectively converts an L-glutamine residue to L-glutamine amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 5 H 10 N 3 O 2
144.15
144.0773
Q
natural
C-term
uniprot.ptm:PTM-0130
(2S)-2-aminopentanediamide
GlnN
L-glutamine amide
MOD_RES Glutamine amide
amidated L-glutamine
glutaminamide
PSI-MOD
MOD:00095
L-glutamine amide
A protein modification that effectively converts an L-glutamine residue to L-glutamine amide.
PubMed:7673220
PubMed:9048550
RESID:AA0086
(2S)-2-aminopentanediamide
GlnN
L-glutamine amide
MOD_RES Glutamine amide
amidated L-glutamine
glutaminamide
A protein modification that effectively converts an L-glutamic acid residue to L-glutamic acid 1-amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 5 H 9 N 2 O 3
145.14
145.06131
E
natural
C-term
uniprot.ptm:PTM-0129
(2S)-2-amino-1-pentanediamic acid
1-amidated L-glutamic acid
4,5-diamino-5-oxopentanoic acid
GluN
L-glutamic acid 1-amide
MOD_RES Glutamic acid 1-amide
isoglutamine
PSI-MOD
MOD:00096
L-glutamic acid 1-amide
A protein modification that effectively converts an L-glutamic acid residue to L-glutamic acid 1-amide.
PubMed:1093875
PubMed:14550575
RESID:AA0087
(2S)-2-amino-1-pentanediamic acid
1-amidated L-glutamic acid
4,5-diamino-5-oxopentanoic acid
GluN
L-glutamic acid 1-amide
MOD_RES Glutamic acid 1-amide
isoglutamine
A protein modification that effectively converts a glycine residue to glycine amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 2 H 5 N 2 O 1
73.07
73.04019
G
natural
C-term
uniprot.ptm:PTM-0132
2-aminoacetamide
2-aminoethanamide
2-azanylethanamide
GlyN
MOD_RES Glycine amide
amidated glycine
glycinamide
glycine amide
PSI-MOD
MOD:00097
glycine amide
A protein modification that effectively converts a glycine residue to glycine amide.
PubMed:13591312
RESID:AA0088
2-aminoacetamide
2-aminoethanamide
2-azanylethanamide
GlyN
MOD_RES Glycine amide
amidated glycine
glycinamide
glycine amide
A protein modification that effectively converts an L-histidine residue to L-histidine amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 6 H 9 N 4 O 1
153.16
153.07764
H
natural
C-term
uniprot.ptm:PTM-0148
(2S)-2-amino-3-(1H-imidazol-4-yl)propanamide
HisN
L-histidine amide
MOD_RES Histidine amide
amidated L-histidine
histidinamide
PSI-MOD
MOD:00098
L-histidine amide
A protein modification that effectively converts an L-histidine residue to L-histidine amide.
PubMed:2153586
PubMed:2307683
PubMed:2839478
RESID:AA0089
(2S)-2-amino-3-(1H-imidazol-4-yl)propanamide
HisN
L-histidine amide
MOD_RES Histidine amide
amidated L-histidine
histidinamide
A protein modification that effectively converts an L-isoleucine residue to L-isoleucine amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 6 H 13 N 2 O 1
129.18
129.10278
I
natural
C-term
uniprot.ptm:PTM-0161
(2S,3S)-2-amino-3-methylpentanamide
IleN
L-isoleucine amide
MOD_RES Isoleucine amide
amidated L-isoleucine
isoleucinamide
PSI-MOD
MOD:00099
L-isoleucine amide
A protein modification that effectively converts an L-isoleucine residue to L-isoleucine amide.
RESID:AA0090
(2S,3S)-2-amino-3-methylpentanamide
IleN
L-isoleucine amide
MOD_RES Isoleucine amide
amidated L-isoleucine
isoleucinamide
A protein modification that effectively converts an L-leucine residue to L-leucine amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 6 H 13 N 2 O 1
129.18
129.10278
L
natural
C-term
uniprot.ptm:PTM-0166
(2S)-2-amino-4-methylpentanamide
2-amino-4-methylvaleramide
2-azanyl-4-methylpentanamide
L-leucine amide
LeuN
MOD_RES Leucine amide
alpha-aminoisocaproamide
amidated L-leucine
leucinamide
PSI-MOD
MOD:00100
L-leucine amide
A protein modification that effectively converts an L-leucine residue to L-leucine amide.
PubMed:2578459
RESID:AA0091
(2S)-2-amino-4-methylpentanamide
2-amino-4-methylvaleramide
2-azanyl-4-methylpentanamide
L-leucine amide
LeuN
MOD_RES Leucine amide
alpha-aminoisocaproamide
amidated L-leucine
leucinamide
A protein modification that effectively converts an L-lysine residue to L-lysine amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 6 H 14 N 3 O 1
144.2
144.1137
K
natural
C-term
uniprot.ptm:PTM-0168
(2S)-2,6-diaminohexanamide
L-lysine amide
LysN
MOD_RES Lysine amide
amidated L-lysine
lysinamide
PSI-MOD
MOD:00101
L-lysine amide
A protein modification that effectively converts an L-lysine residue to L-lysine amide.
PubMed:6579533
RESID:AA0092
(2S)-2,6-diaminohexanamide
L-lysine amide
LysN
MOD_RES Lysine amide
amidated L-lysine
lysinamide
A protein modification that effectively converts an L-methionine residue to L-methionine amide.
-0.98
C 0 H 1 N 1 O -1 S 0
-0.984016
C 5 H 11 N 2 O 1 S 1
147.22
147.0592
M
natural
C-term
uniprot.ptm:PTM-0164
(2S)-2-amino-4-(methylsulfanyl)butanamide
2-amino-4-(methylthio)butanamide
L-methionine amide
MOD_RES Methionine amide
MetN
amidated L-methionine
methioninamide
PSI-MOD
MOD:00102
L-methionine amide
methioninamide
A protein modification that effectively converts an L-methionine residue to L-methionine amide.
PubMed:4375977
RESID:AA0093
(2S)-2-amino-4-(methylsulfanyl)butanamide
2-amino-4-(methylthio)butanamide
L-methionine amide
MOD_RES Methionine amide
MetN
amidated L-methionine
A protein modification that effectively converts an L-phenylalanine residue to L-phenylalanine amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 9 H 11 N 2 O 1
163.2
163.08714
F
natural
C-term
uniprot.ptm:PTM-0248
(2S)-2-amino-3-phenylpropanamide
L-phenylalanine amide
MOD_RES Phenylalanine amide
PheN
amidated L-phenylalanine
phenylalaninamide
PSI-MOD
MOD:00103
L-phenylalanine amide
A protein modification that effectively converts an L-phenylalanine residue to L-phenylalanine amide.
PubMed:2905621
PubMed:8868490
RESID:AA0094
(2S)-2-amino-3-phenylpropanamide
L-phenylalanine amide
MOD_RES Phenylalanine amide
PheN
amidated L-phenylalanine
phenylalaninamide
A protein modification that effectively converts an L-proline residue to L-proline amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 5 H 9 N 2 O 1
113.14
113.07149
P
natural
C-term
uniprot.ptm:PTM-0257
(2S)-pyrrolidine-2-carboxamide
L-proline amide
MOD_RES Proline amide
ProN
amidated L-proline
prolinamide
PSI-MOD
MOD:00104
L-proline amide
A protein modification that effectively converts an L-proline residue to L-proline amide.
PubMed:4982117
PubMed:5760861
RESID:AA0095
(2S)-pyrrolidine-2-carboxamide
L-proline amide
MOD_RES Proline amide
ProN
amidated L-proline
prolinamide
A protein modification that effectively converts an L-serine residue to L-serine amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 3 H 7 N 2 O 2
103.1
103.05075
S
natural
C-term
uniprot.ptm:PTM-0275
(2S)-2-amino-3-hydroxypropanamide
L-serine amide
MOD_RES Serine amide
SerN
amidated L-serine
serinamide
PSI-MOD
MOD:00105
L-serine amide
A protein modification that effectively converts an L-serine residue to L-serine amide.
PubMed:743209
RESID:AA0096
(2S)-2-amino-3-hydroxypropanamide
L-serine amide
MOD_RES Serine amide
SerN
amidated L-serine
serinamide
A protein modification that effectively converts an L-threonine residue to L-threonine amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 4 H 9 N 2 O 2
117.13
117.06641
T
natural
C-term
uniprot.ptm:PTM-0293
(2S,3R)-2-amino-3-hydroxybutanamide
L-threonine amide
MOD_RES Threonine amide
ThrN
amidated L-threonine
threoninamide
PSI-MOD
MOD:00106
L-threonine amide
A protein modification that effectively converts an L-threonine residue to L-threonine amide.
PubMed:1390774
RESID:AA0097
(2S,3R)-2-amino-3-hydroxybutanamide
L-threonine amide
MOD_RES Threonine amide
ThrN
amidated L-threonine
threoninamide
A protein modification that effectively converts an L-tryptophan residue to L-tryptophan amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 11 H 12 N 3 O 1
202.24
202.09804
W
natural
C-term
uniprot.ptm:PTM-0296
(2S)-2-amino-3-(1H-indol-3-yl)propanamide
L-tryptophan amide
MOD_RES Tryptophan amide
TrpN
amidated L-tryptophan
tryptophanamide
PSI-MOD
MOD:00107
L-tryptophan amide
A protein modification that effectively converts an L-tryptophan residue to L-tryptophan amide.
PubMed:3947348
RESID:AA0098
(2S)-2-amino-3-(1H-indol-3-yl)propanamide
L-tryptophan amide
MOD_RES Tryptophan amide
TrpN
amidated L-tryptophan
tryptophanamide
A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 9 H 11 N 2 O 2
179.2
179.08205
Y
natural
C-term
uniprot.ptm:PTM-0302
(2S)-2-amino-3-(4-hydoxyphenyl)propanamide
L-tyrosine amide
MOD_RES Tyrosine amide
TyrN
amidated L-tyrosine
tyrosinamide
PSI-MOD
MOD:00108
L-tyrosine amide
A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide.
PubMed:1377792
PubMed:3562898
PubMed:6509012
RESID:AA0099
(2S)-2-amino-3-(4-hydoxyphenyl)propanamide
L-tyrosine amide
MOD_RES Tyrosine amide
TyrN
amidated L-tyrosine
tyrosinamide
A protein modification that effectively converts an L-valine residue to L-valine amide.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 5 H 11 N 2 O 1
115.16
115.087135
V
natural
C-term
uniprot.ptm:PTM-0303
(2S)-2-amino-3-methylbutanamide
L-valine amide
MOD_RES Valine amide
ValN
valinamide
PSI-MOD
MOD:00109
L-valine amide
A protein modification that effectively converts an L-valine residue to L-valine amide.
PubMed:2578459
PubMed:5465996
RESID:AA0100
(2S)-2-amino-3-methylbutanamide
L-valine amide
MOD_RES Valine amide
ValN
valinamide
A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl disulfide.
46.09
C 1 H 2 N 0 O 0 S 1
45.98772
C 4 H 7 N 1 O 1 S 2
149.23
148.9969
C
natural
Unimod:39
uniprot.ptm:PTM-0104
(2R)-2-amino-3-(methyldisulfanediyl)propanoic acid
2-amino-3-(methyldisulfanediyl)propanoic acid
2-amino-3-(methyldithio)propanoic acid
2-amino-3-methyldisulfanylpropanoic acid
2-azanyl-3-(methyldisulfanediyl)-propanoic acid
L-3-(methyldithio)alanine
L-cysteine methyl disulfide
MOD_RES Cysteine methyl disulfide
S-methylthio-L-cysteine
S-methylthiocysteine
methyl methanethiolsulfonate derivatized cysteine
methyl methanethiosulfonate derivatized cysteine
mmts
PSI-MOD
Beta-methylthiolation
Methylthio
MOD:00110
Produced artifactually by reaction of cysteine residues with methyl methanethiosulfonate (MMTS) [JSG], but also naturally in bacteria [PMT].
L-cysteine methyl disulfide
A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl disulfide.
OMSSA:179
PubMed:10555576
PubMed:163643
PubMed:2056535
PubMed:6381494
RESID:AA0101
Unimod:39#C
(2R)-2-amino-3-(methyldisulfanediyl)propanoic acid
2-amino-3-(methyldisulfanediyl)propanoic acid
2-amino-3-(methyldithio)propanoic acid
2-amino-3-methyldisulfanylpropanoic acid
2-azanyl-3-(methyldisulfanediyl)-propanoic acid
L-3-(methyldithio)alanine
L-cysteine methyl disulfide
MOD_RES Cysteine methyl disulfide
S-methylthio-L-cysteine
S-methylthiocysteine
methyl methanethiolsulfonate derivatized cysteine
methyl methanethiosulfonate derivatized cysteine
mmts
Beta-methylthiolation
Methylthio
Methylthio
A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine.
204.36
C 15 H 24 N 0 O 0 S 0
204.1878
C 18 H 29 N 1 O 1 S 1
307.5
307.197
C
natural
Unimod:44
uniprot.ptm:PTM-0277
(2R)-2-amino-3-([(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid
2-amino-3-(3,7,11-trimethyl-2,6,10-dodecatrienylthio)propanoic acid
LIPID S-farnesyl cysteine
S-farnesyl Cystenyl
S-farnesyl-L-cysteine
SFarnCys
farnesylationc
PSI-MOD
Farnesyl
Farnesylation
MOD:00111
From DeltaMass: (name misspelled "S-farnesyl cystenyl")
S-farnesyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine.
DeltaMass:293
OMSSA:42
PubMed:1409665
PubMed:15609361
PubMed:1872463
PubMed:2684976
RESID:AA0102
Unimod:44#C
(2R)-2-amino-3-([(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid
2-amino-3-(3,7,11-trimethyl-2,6,10-dodecatrienylthio)propanoic acid
LIPID S-farnesyl cysteine
S-farnesyl Cystenyl
S-farnesyl-L-cysteine
SFarnCys
farnesylationc
Farnesyl
Farnesylation
A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine.
220.36
C 15 H 24 N 0 O 1 S 0
220.18271
C 18 H 29 N 1 O 2 S 1
323.5
323.1919
C
natural
Unimod:376
uniprot.ptm:PTM-0269
(2R)-2-amino-3-([(2E,6E,10Z)-12-hydroxy-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid
2-amino-3-(12-hydroxy-3,7,11-trimethyl-3,6,10-dodecatrienylthio)propanoic acid
LIPID S-12-hydroxyfarnesyl cysteine
S-12-hydroxyfarnesyl-L-cysteine
S12HyFarnCys
PSI-MOD
Hydroxyfarnesyl
hydroxyfarnesyl
MOD:00112
S-12-hydroxyfarnesyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine.
PubMed:17790543
RESID:AA0103
Unimod:376
(2R)-2-amino-3-([(2E,6E,10Z)-12-hydroxy-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid
2-amino-3-(12-hydroxy-3,7,11-trimethyl-3,6,10-dodecatrienylthio)propanoic acid
LIPID S-12-hydroxyfarnesyl cysteine
S-12-hydroxyfarnesyl-L-cysteine
S12HyFarnCys
Hydroxyfarnesyl
hydroxyfarnesyl
A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine.
272.48
C 20 H 32 N 0 O 0 S 0
272.2504
C 23 H 37 N 1 O 1 S 1
375.62
375.25958
C
natural
Unimod:48
uniprot.ptm:PTM-0278
(2R)-2-amino-3-([(2E,6E,10Z)-12-hydroxy-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid
2-amino-3-(3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylthio)propanoic acid
LIPID S-geranylgeranyl cysteine
S-geranylgeranyl
S-geranylgeranyl-L-cysteine
SGergerCys
geranylgeranylc
PSI-MOD
Geranyl-geranyl
GeranylGeranyl
MOD:00113
DeltaMass calculates the mass with two double bonds rather than four
S-geranylgeranyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine.
DeltaMass:0
OMSSA:49
PubMed:1483450
PubMed:15609361
RESID:AA0104
Unimod:48#C
(2R)-2-amino-3-([(2E,6E,10Z)-12-hydroxy-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]sulfanyl)propanoic acid
2-amino-3-(3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylthio)propanoic acid
LIPID S-geranylgeranyl cysteine
S-geranylgeranyl
S-geranylgeranyl-L-cysteine
SGergerCys
geranylgeranylc
Geranyl-geranyl
GeranylGeranyl
A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl ester.
14.03
C 1 H 2 N 0 O 0 S 0
14.01565
C 4 H 8 N 1 O 2 S 1
134.17
134.02757
C
natural
C-term
Unimod:34
uniprot.ptm:PTM-0105
2-amino-3-mercaptopropanoic methyl ester
2-amino-3-sulfanylpropanoic methyl ester
L-cysteine methyl ester
MOD_RES Cysteine methyl ester
OMeCys
mecysteine
methyl (2R)-2-amino-3-sulfanylpropanoate
methyl L-cysteinate
methyl esterified L-cysteine
PSI-MOD
Methyl
Methylation
MOD:00114
Secondary to RESID:AA0102; secondary to RESID:AA0103; secondary to RESID:AA0104.
L-cysteine methyl ester
A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl ester.
PubMed:11875433
PubMed:1872463
RESID:AA0105
Unimod:34#C-term
2-amino-3-mercaptopropanoic methyl ester
2-amino-3-sulfanylpropanoic methyl ester
L-cysteine methyl ester
MOD_RES Cysteine methyl ester
OMeCys
mecysteine
methyl (2R)-2-amino-3-sulfanylpropanoate
methyl L-cysteinate
methyl esterified L-cysteine
Methyl
Methylation
A protein modification that effectively converts an L-cysteine residue to S-palmitoyl-L-cysteine.
238.41
C 16 H 30 N 0 O 1 S 0
238.22966
C 19 H 35 N 1 O 2 S 1
341.55
341.23886
C
natural
Unimod:47
uniprot.ptm:PTM-0281
(2R)-2-amino-3-(hexadecanoylsulfanyl)propanoic acid
2-amino-3-(hexadecanoylthio)propanoic acid
ACT_SITE S-palmitoyl cysteine intermediate
LIPID S-palmitoyl cysteine
S-hexadecanoylated L-cysteine
S-palmitoyl-L-cysteine
S-palmitoylated L-cysteine
S-palmityl Cystenyl
SPamCys
cysteine hexadecanoate thioester
cysteine palmitate thioester
PSI-MOD
Palmitoyl
Palmitoylation
MOD:00115
From DeltaMass: (name misspelled "S-palmityl Cystenyl" and formula incorrect, N and O reversed) Formula: C19H35O1N2S1 Monoisotopic Mass Change: 341.239 Average Mass Change: 341.556
S-palmitoyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-palmitoyl-L-cysteine.
DeltaMass:303
PubMed:1872406
PubMed:3166978
PubMed:8180229
PubMed:8824274
RESID:AA0106
Unimod:47#C
(2R)-2-amino-3-(hexadecanoylsulfanyl)propanoic acid
2-amino-3-(hexadecanoylthio)propanoic acid
ACT_SITE S-palmitoyl cysteine intermediate
LIPID S-palmitoyl cysteine
S-hexadecanoylated L-cysteine
S-palmitoyl-L-cysteine
S-palmitoylated L-cysteine
S-palmityl Cystenyl
SPamCys
cysteine hexadecanoate thioester
cysteine palmitate thioester
Palmitoyl
Palmitoylation
A protein modification that effectively converts an L-cysteine residue to S-diacylglycerol-L-cysteine.
C
natural
uniprot.ptm:PTM-0274
(2R)-2-amino-3-[(2S)-2-((9Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]sulfanylpropanoic acid
2-amino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]thiopropanoic acid
LIPID S-diacylglycerol cysteine
S-(1-2'-oleoyl-3'-palmitoyl-glycerol)cysteine
S-(2',3'-diacylglycerol)-L-cysteine
S-diacylglycerol-L-cysteine
SAcyl2GlyceroCys
PSI-MOD
Diacylglycerol
diacylglycerol
MOD:00116
Incidental to RESID:AA0060.
S-diacylglycerol-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-diacylglycerol-L-cysteine.
PubMed:10896212
PubMed:4575979
PubMed:9056182
RESID:AA0107
Unimod:377#C
(2R)-2-amino-3-[(2S)-2-((9Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]sulfanylpropanoic acid
2-amino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]thiopropanoic acid
LIPID S-diacylglycerol cysteine
S-(1-2'-oleoyl-3'-palmitoyl-glycerol)cysteine
S-(2',3'-diacylglycerol)-L-cysteine
S-diacylglycerol-L-cysteine
SAcyl2GlyceroCys
Diacylglycerol
diacylglycerol
A protein modification that effectively crosslinks an L-cysteine residue and an L-glutamine residue by a thioester bond with the formation of S-(L-isoglutamyl)-L-cysteine and the release of ammonia.
-17.03
C 0 H -3 N -1 O 0 S 0
-17.026548
C 8 H 10 N 2 O 3 S 1
214.24
214.04121
C, Q
natural
uniprot.ptm:PTM-0156
(2S)-2-amino-5-[(2R)-2-amino-2-carboxyethyl]sulfanyl-5-oxopentanoic acid
(S,R)-2-amino-4-[S-(2-amino-2-carboxyethyl)thiocarboxy]butanoic acid
2-amino-5-(2-amino-2-carboxyethyl)thio-5-oxopentanoic acid
CROSSLNK Isoglutamyl cysteine thioester (Cys-Gln)
S-(L-isoglutamyl)-L-cysteine
S-gamma-glutamyl (crosslinked to cysteine)
XLNK-SCys-5Glu(Gln)
gamma-(S-cysteinyl)glutamic acid
PSI-MOD
MOD:00117
Cross-link 2; DeltaMass calculates the mass difference from glutamic acid rather than glutamine.
S-(L-isoglutamyl)-L-cysteine
A protein modification that effectively crosslinks an L-cysteine residue and an L-glutamine residue by a thioester bond with the formation of S-(L-isoglutamyl)-L-cysteine and the release of ammonia.
ChEBI:22021
DeltaMass:0
PubMed:6838833
RESID:AA0108
(2S)-2-amino-5-[(2R)-2-amino-2-carboxyethyl]sulfanyl-5-oxopentanoic acid
(S,R)-2-amino-4-[S-(2-amino-2-carboxyethyl)thiocarboxy]butanoic acid
2-amino-5-(2-amino-2-carboxyethyl)thio-5-oxopentanoic acid
CROSSLNK Isoglutamyl cysteine thioester (Cys-Gln)
S-(L-isoglutamyl)-L-cysteine
S-gamma-glutamyl (crosslinked to cysteine)
XLNK-SCys-5Glu(Gln)
gamma-(S-cysteinyl)glutamic acid
A protein modification that effectively cross-links an L-cysteine residue and an L-histidine residue by a thioether bond to form 2'-(S-L-cysteinyl)-L-histidine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 9 H 10 N 4 O 2 S 1
238.26
238.05244
C, H
natural
uniprot.ptm:PTM-0005
(2R)-2-amino-3-[(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)sulfanyl]propanoic acid
(2S)-2-amino-3-[2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-1H-imidazol-4-yl]propanoic acid
2'-(L-cystein-S-yl)-L-histidine
CROSSLNK 2'-(S-cysteinyl)-histidine (Cys-His)
S-(2'-histidyl)cysteine
S-(2-histidyl)- (crosslinked to cysteine)
XLNK-SCys-2'His
PSI-MOD
MOD:00118
Cross-link 2.
2'-(S-L-cysteinyl)-L-histidine
A protein modification that effectively cross-links an L-cysteine residue and an L-histidine residue by a thioether bond to form 2'-(S-L-cysteinyl)-L-histidine.
DeltaMass:0
PubMed:6210696
RESID:AA0109
(2R)-2-amino-3-[(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)sulfanyl]propanoic acid
(2S)-2-amino-3-[2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-1H-imidazol-4-yl]propanoic acid
2'-(L-cystein-S-yl)-L-histidine
CROSSLNK 2'-(S-cysteinyl)-histidine (Cys-His)
S-(2'-histidyl)cysteine
S-(2-histidyl)- (crosslinked to cysteine)
XLNK-SCys-2'His
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 6 H 8 N 2 O 2 S 1
172.2
172.03065
C, S
artifact
(2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid)
(R)-S-(2-amino-2-carboxyethyl)-L-cysteine
(R,R)-2,6-diamino-4-thiaheptanedioic acid
(R,R)-3,3'-thiobis-(2-aminopropanoic acid)
(R,R)-bis(2-amino-2-carboxyethyl)sulfide
2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid
3,3'-thiobis-L-alanine
L-lanthionine
XLNK-SCys-(L)3Dha
PSI-MOD
MOD:00119
Cross-link 2. The natural occurrence of this modification is rare. For the more common modification see MOD:00120 meso-lanthionine [JSG].
L-lanthionine (Cys-Ser)
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine.
ChEBI:21347
DeltaMass:7
RESID:AA0110#CSX
(2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid)
(R)-S-(2-amino-2-carboxyethyl)-L-cysteine
(R,R)-2,6-diamino-4-thiaheptanedioic acid
(R,R)-3,3'-thiobis-(2-aminopropanoic acid)
(R,R)-bis(2-amino-2-carboxyethyl)sulfide
2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid
3,3'-thiobis-L-alanine
L-lanthionine
XLNK-SCys-(L)3Dha
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form meso-lanthionine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 6 H 8 N 2 O 2 S 1
172.2
172.03065
C, S
natural
uniprot.ptm:PTM-0164
(2R,2'S)-3,3'-sulfanediylbis(2-aminopropanoic acid)
(2R,2'S)-3,3'-thiobis-(2-aminopropanoic acid)
(2R,6S)-2,6-diamino-4-thiaheptanedioic acid
(2R,6S)-meso-lanthionine
(2S)-2-amino-3-[[(2R)-2-amino-2-carboxyethyl]sulfanyl]propanoic acid
(R)-S-(2-amino-2-carboxyethyl)-D-cysteine
(R,S)-bis(2-amino-2-carboxyethyl)sulfide
3,3'-thiobis-meso-alanine
CROSSLNK Lanthionine (Cys-Ser)
CROSSLNK Lanthionine (Ser-Cys)
XLNK-SCys-(D)3Dha
cysteine-3-D-alanine thioether
meso-lanthionine
PSI-MOD
(2S,6R)-meso-lanthionine
MOD:00120
Cross-link 2.
meso-lanthionine
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form meso-lanthionine.
PubMed:15023056
PubMed:3769923
RESID:AA0111
(2R,2'S)-3,3'-sulfanediylbis(2-aminopropanoic acid)
(2R,2'S)-3,3'-thiobis-(2-aminopropanoic acid)
(2R,6S)-2,6-diamino-4-thiaheptanedioic acid
(2R,6S)-meso-lanthionine
(2S)-2-amino-3-[[(2R)-2-amino-2-carboxyethyl]sulfanyl]propanoic acid
(R)-S-(2-amino-2-carboxyethyl)-D-cysteine
(R,S)-bis(2-amino-2-carboxyethyl)sulfide
3,3'-thiobis-meso-alanine
CROSSLNK Lanthionine (Cys-Ser)
CROSSLNK Lanthionine (Ser-Cys)
XLNK-SCys-(D)3Dha
cysteine-3-D-alanine thioether
meso-lanthionine
(2S,6R)-meso-lanthionine
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2S,3S,2'R)-3-methyllanthionine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 7 H 10 N 2 O 2 S 1
186.23
186.0463
C, T
natural
uniprot.ptm:PTM-0067
(2S,3S)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanoic acid
(2S,3S,2'R)-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid
(2S,3S,2'R)-3-methyllanthionine
(2S,3S,6R)-2,6-diamino-3-methyl-4-thiaheptanedioic acid
(2S,3S,6R)-3-methyllanthionine
(2S-[2R*,3R*(S*)])-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid
3-methyl-D,L-lanthionine
CROSSLNK Beta-methyllanthionine (Cys-Thr)
CROSSLNK Beta-methyllanthionine (Thr-Cys)
XLNK-SCys-3Dhb
cysteine-3-D-butyrine thioether
PSI-MOD
MOD:00121
Cross-link 2.
(2S,3S,2'R)-3-methyllanthionine
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2S,3S,2'R)-3-methyllanthionine.
PubMed:3769923
RESID:AA0112
(2S,3S)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanoic acid
(2S,3S,2'R)-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid
(2S,3S,2'R)-3-methyllanthionine
(2S,3S,6R)-2,6-diamino-3-methyl-4-thiaheptanedioic acid
(2S,3S,6R)-3-methyllanthionine
(2S-[2R*,3R*(S*)])-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid
3-methyl-D,L-lanthionine
CROSSLNK Beta-methyllanthionine (Cys-Thr)
CROSSLNK Beta-methyllanthionine (Thr-Cys)
XLNK-SCys-3Dhb
cysteine-3-D-butyrine thioether
A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-tyrosine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 12 H 12 N 2 O 3 S 1
264.3
264.05685
C, Y
natural
uniprot.ptm:PTM-0019
(2S)-2-amino-3-(3-[(2R)2-amino-2-carboxyethylsulfanyl]-4-hydroxyphenyl)propanoic acid
2-amino-3-[3-(2-amino-2-carboxyethylthio)-4-hydroxyphenyl]propanoic acid
3'-(L-cystein-S-yl)-L-tyrosine
3'-(cystein-S-yl)tyrosine
CROSSLNK 3'-(S-cysteinyl)-tyrosine (Cys-Tyr)
CROSSLNK 3'-(S-cysteinyl)-tyrosine (Tyr-Cys)
S-(3-Tyr) (Crosslinked to Cysteine)
S-(tyros-3'-yl)cysteine
XLNK-SCys-3'Tyr
PSI-MOD
MOD:00122
Cross-link 2.
3'-(S-L-cysteinyl)-L-tyrosine
A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-tyrosine.
DeltaMass:0
PubMed:15917234
PubMed:2002850
RESID:AA0113
(2S)-2-amino-3-(3-[(2R)2-amino-2-carboxyethylsulfanyl]-4-hydroxyphenyl)propanoic acid
2-amino-3-[3-(2-amino-2-carboxyethylthio)-4-hydroxyphenyl]propanoic acid
3'-(L-cystein-S-yl)-L-tyrosine
3'-(cystein-S-yl)tyrosine
CROSSLNK 3'-(S-cysteinyl)-tyrosine (Cys-Tyr)
CROSSLNK 3'-(S-cysteinyl)-tyrosine (Tyr-Cys)
S-(3-Tyr) (Crosslinked to Cysteine)
S-(tyros-3'-yl)cysteine
XLNK-SCys-3'Tyr
A protein modification that effectively converts an L-lysine residue to N6-carboxy-L-lysine.
44.01
C 1 H 0 N 0 O 2
43.98983
C 7 H 12 N 2 O 3
172.18
172.0848
K
natural
Unimod:299
uniprot.ptm:PTM-0191
(2S)-2-amino-6-(carboxyamino)hexanoic acid
2-amino-6-carbamic hexanoic acid
MOD_RES N6-carboxylysine
N6-carboxy-L-lysine
N6-carboxylysine
N6CbxLys
lysine NZ-carboxylic acid
PSI-MOD
Carboxy
Carboxylation
N6-carbamyllysine
MOD:00123
N6-carboxy-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-carboxy-L-lysine.
PubMed:11369851
PubMed:4436319
PubMed:637859
PubMed:7754395
RESID:AA0114
Unimod:299#K
(2S)-2-amino-6-(carboxyamino)hexanoic acid
2-amino-6-carbamic hexanoic acid
MOD_RES N6-carboxylysine
N6-carboxy-L-lysine
N6-carboxylysine
N6CbxLys
lysine NZ-carboxylic acid
Carboxy
Carboxylation
N6-carbamyllysine
A protein modification that effectively converts an L-lysine residue to N6-1-carboxyethyl-L-lysine.
72.06
C 3 H 4 N 0 O 2
72.021126
C 9 H 16 N 2 O 3
200.24
200.11609
K
natural
Unimod:378
uniprot.ptm:PTM-0189
(2S)-2-amino-6-([(1S)-1-carboxyethyl]amino)hexanoic acid
MOD_RES N6-1-carboxyethyl lysine
N6-(1-carboxyethyl)-L-lysine
N6-(1-carboxyethyl)lysine
N6CbzEtLys
NZ-(1-carboxyethyl)lysine
PSI-MOD
Carboxyethyl
carboxyethyl
MOD:00124
N6-1-carboxyethyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-1-carboxyethyl-L-lysine.
PubMed:3123486
PubMed:8253186
PubMed:8421682
RESID:AA0115
Unimod:378#K
(2S)-2-amino-6-([(1S)-1-carboxyethyl]amino)hexanoic acid
MOD_RES N6-1-carboxyethyl lysine
N6-(1-carboxyethyl)-L-lysine
N6-(1-carboxyethyl)lysine
N6CbzEtLys
NZ-(1-carboxyethyl)lysine
Carboxyethyl
carboxyethyl
A protein modification that effectively converts an L-lysine residue to hypusine, N6-(4-amino-2-hydroxybutyl)-L-lysine.
87.12
C 4 H 9 N 1 O 1
87.06841
C 10 H 21 N 3 O 2
215.3
215.16338
K
natural
Unimod:379
uniprot.ptm:PTM-0150
(2S)-2-amino-6-([(2R)-4-amino-2-hydroxybutyl]amino)hexanoic acid
(2S,9R)-2,11-diazanyl-9-hydroxy-7-azaundecanoic acid
(2S,9R)-hypusine
2-azanyl-6-[(4-azanyl-2-hydroxybutyl)azanyl]hexanoic acid
Hypu
L-hypusine
MOD_RES Hypusine
N-(4-NH2-2-OH-butyl)- (of Lysine)
N6-(4-amino-2-hydroxybutyl)-L-lysine
PSI-MOD
Hypusine
hypusine
MOD:00125
This modification occurs uniquely in translation initiation factor eIF-5A [JSG].
hypusine
A protein modification that effectively converts an L-lysine residue to hypusine, N6-(4-amino-2-hydroxybutyl)-L-lysine.
DeltaMass:0
PubMed:6806267
PubMed:8108861
RESID:AA0116
Unimod:379#K
(2S)-2-amino-6-([(2R)-4-amino-2-hydroxybutyl]amino)hexanoic acid
(2S,9R)-2,11-diazanyl-9-hydroxy-7-azaundecanoic acid
(2S,9R)-hypusine
2-azanyl-6-[(4-azanyl-2-hydroxybutyl)azanyl]hexanoic acid
Hypu
L-hypusine
MOD_RES Hypusine
N-(4-NH2-2-OH-butyl)- (of Lysine)
N6-(4-amino-2-hydroxybutyl)-L-lysine
Hypusine
hypusine
A protein modification that effectively converts an L-lysine residue to N6-biotinyl-L-lysine.
226.29
C 10 H 14 N 2 O 2 S 1
226.0776
C 16 H 26 N 4 O 3 S 1
354.47
354.17258
K
natural
Unimod:3
uniprot.ptm:PTM-0382
(2S)-2-amino-6-(5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoylamino)hexanoic acid
(3aS-(3aalpha,4beta,6aalpha))-N6-(5-(hexahydro-2-oxo-1H-thieno(3,4-d)imidazol-4-yl)-1-oxopentyl)-L-lysine
MOD_RES N6-biotinyllysine
N6-[5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl]-L-lysine
N6-biotinyl-L-lysine
N6-biotinyllysine
N6BtnLys
biocytin
biotinyl lysyl
epsilon-N-biotinyllysine
PSI-MOD
Biotin
Biotinylation
MOD:00126
From DeltaMass: Average Mass: 354 Formula:C 16 H 26 O 4 N 3 S 1 (formula incorrect, N and O reversed) Monoisotopic Mass Change:354.172 Average Mass Change:354.471 References:PE Sciex.
N6-biotinyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-biotinyl-L-lysine.
DeltaMass:305
PubMed:16109483
PubMed:3178228
PubMed:7948875
PubMed:8747466
RESID:AA0117
Unimod:3#K
(2S)-2-amino-6-(5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoylamino)hexanoic acid
(3aS-(3aalpha,4beta,6aalpha))-N6-(5-(hexahydro-2-oxo-1H-thieno(3,4-d)imidazol-4-yl)-1-oxopentyl)-L-lysine
MOD_RES N6-biotinyllysine
N6-[5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl]-L-lysine
N6-biotinyl-L-lysine
N6-biotinyllysine
N6BtnLys
biocytin
biotinyl lysyl
epsilon-N-biotinyllysine
Biotin
Biotinylation
A protein modification that effectively converts an L-lysine residue to N6-lipoyl-L-lysine.
188.3
C 8 H 12 N 0 O 1 S 2
188.03296
C 14 H 24 N 2 O 2 S 2
316.48
316.12793
K
natural
Unimod:42
uniprot.ptm:PTM-0383
(2S)-2-amino-6-(5-[(3R)-1,2-dithiolan-3-yl]pentanamido)hexanoic acid
(2S)-2-amino-6-[(5-[(3R)-1,2-dithiolan-3-yl]pentanoyl)amino]hexanoic acid
(2S,6'R)-2-amino-6-(6,8-dithiooctanamido)hexanoic acid
2-amino-6-(5-[1,2-dithiolan-3-yl]-1-oxopentyl)aminohexanoic acid
MOD_RES N6-lipoyllysine
N-Lipoyl- (on Lysine)
N6-6,8-dithiooctanoyllysine
N6-lipoyl-L-lysine
N6-lipoyllysine
N6LipLys
lipoylk
PSI-MOD
Lipoyl
MOD:00127
N6-lipoyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-lipoyl-L-lysine.
DeltaMass:0
OMSSA:67
PubMed:3421911
PubMed:3522581
PubMed:7719855
RESID:AA0118
Unimod:42#K
(2S)-2-amino-6-(5-[(3R)-1,2-dithiolan-3-yl]pentanamido)hexanoic acid
(2S)-2-amino-6-[(5-[(3R)-1,2-dithiolan-3-yl]pentanoyl)amino]hexanoic acid
(2S,6'R)-2-amino-6-(6,8-dithiooctanamido)hexanoic acid
2-amino-6-(5-[1,2-dithiolan-3-yl]-1-oxopentyl)aminohexanoic acid
MOD_RES N6-lipoyllysine
N-Lipoyl- (on Lysine)
N6-6,8-dithiooctanoyllysine
N6-lipoyl-L-lysine
N6-lipoyllysine
N6LipLys
lipoylk
Lipoyl
Lipoyl
A protein modification that effectively converts an L-lysine residue to N6-pyridoxal phosphate-L-lysine.
229.13
C 8 H 8 N 1 O 5 P 1
229.014
C 14 H 20 N 3 O 6 P 1
357.3
357.10898
K
natural
Unimod:46
uniprot.ptm:PTM-0387
(2S)-2-amino-6-[([3-hydroxy-2-methyl-5-phosphonooxymethylpyridin-4-yl]methylidene)amino]hexanoic acid
MOD_RES N6-(pyridoxal phosphate)lysine
N6-pyridoxal phosphate-L-lysine
N6PydoxLys
Pyridoxal phosphate (Schiff Base formed to lysine)
PSI-MOD
Pyridoxal phosphate
PyridoxalPhosphate
MOD:00128
From DeltaMass: Average Mass: 231
N6-pyridoxal phosphate-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-pyridoxal phosphate-L-lysine.
DeltaMass:0
PubMed:1544460
RESID:AA0119
Unimod:46#K
(2S)-2-amino-6-[([3-hydroxy-2-methyl-5-phosphonooxymethylpyridin-4-yl]methylidene)amino]hexanoic acid
MOD_RES N6-(pyridoxal phosphate)lysine
N6-pyridoxal phosphate-L-lysine
N6PydoxLys
Pyridoxal phosphate (Schiff Base formed to lysine)
Pyridoxal phosphate
PyridoxalPhosphate
A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine, the adduct of retinal.
266.43
C 20 H 26 N 0 O 0
266.20346
C 26 H 38 N 2 O 1
394.6
394.2984
K
natural
Unimod:380
uniprot.ptm:PTM-0388
(2S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid
MOD_RES N6-(retinylidene)lysine
N6-retinal-L-lysine
N6-retinyl-lysine
N6-retinylidene-L-lysine
N6RetalLys
PSI-MOD
Retinylidene
retinal
MOD:00129
N6-retinylidene-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine, the adduct of retinal.
PubMed:6794028
PubMed:6870827
RESID:AA0120
Unimod:380#K
(2S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid
MOD_RES N6-(retinylidene)lysine
N6-retinal-L-lysine
N6-retinyl-lysine
N6-retinylidene-L-lysine
N6RetalLys
Retinylidene
retinal
A protein modification that effectively converts an L-lysine residue to L-allysine.
-1.03
C 0 H -3 N -1 O 1
-1.031634
C 6 H 9 N 1 O 2
127.14
127.06333
K
natural
Unimod:352
uniprot.ptm:PTM-0059
(2S)-2-amino-6-oxohexanoic acid
2-amino-5-formylvaleric acid
2-amino-adipic acid semialdahyde
2-aminoadipate 6-semialdehyde
5-formyl-norvaline
6-oxonorleucine
AASA
Allysine (from Lysine)
L-allysine
Lysal
MOD_RES Allysine
Oxidation of lysine (to aminoadipic semialdehyde)
alpha-amino-adipic acid delta-semialdahyde
PSI-MOD
Lys->Allysine
Lysine oxidation to aminoadipic semialdehyde
MOD:00130
From DeltaMass: Average Mass: -1
L-allysine
A protein modification that effectively converts an L-lysine residue to L-allysine.
ChEBI:17917
DeltaMass:0
PubMed:11120890
PubMed:11332453
PubMed:358196
PubMed:5337886
PubMed:5529814
RESID:AA0121
Unimod:352#K
(2S)-2-amino-6-oxohexanoic acid
2-amino-5-formylvaleric acid
2-amino-adipic acid semialdahyde
2-aminoadipate 6-semialdehyde
5-formyl-norvaline
6-oxonorleucine
AASA
Allysine (from Lysine)
L-allysine
Lysal
MOD_RES Allysine
Oxidation of lysine (to aminoadipic semialdehyde)
alpha-amino-adipic acid delta-semialdahyde
Lys->Allysine
Lysine oxidation to aminoadipic semialdehyde
A protein modification that effectively converts an L-lysine residue to L-2-aminoadipic acid.
14.97
C 0 H -3 N -1 O 2
14.96328
C 6 H 9 N 1 O 3
143.14
143.05824
K
natural
Unimod:381
(2S)-2-aminohexanedioic acid
2-amino-1,4-butanedicarboxylic acid
L-2-aminoadipic acid
L-alpha-aminoadipic acid
Lysoic
Oxidation of lysine (to aminoadipic acid)
PSI-MOD
Lys->AminoadipicAcid
alpha-amino adipic acid
MOD:00131
From DeltaMass: References:Amici A, Levine, RL, Tsai, L, and Stadtman, ER: Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. Journal of Biological Chemistry 264: 3341-3346 1989.Requena JR, Chao CC, Levine RL, and Stadtman ER: Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proceedings of the National Academy of Sciences USA 98: 69-74 2001. Notes:Expected reaction following oxidation of lysine to aminoadipic semialdehyde. Not proven experimentally but deduced by reference to the similar known reaction of oxidation of Arg to Glu via the semialdehyde. [This has been observed as a natural modification, see RESID:AA0122. JSG]
L-2-aminoadipic acid
A protein modification that effectively converts an L-lysine residue to L-2-aminoadipic acid.
DeltaMass:353
PubMed:336041
PubMed:358196
PubMed:7419498
RESID:AA0122
Unimod:381#K
(2S)-2-aminohexanedioic acid
2-amino-1,4-butanedicarboxylic acid
L-2-aminoadipic acid
L-alpha-aminoadipic acid
Lysoic
Oxidation of lysine (to aminoadipic acid)
Lys->AminoadipicAcid
alpha-amino adipic acid
A protein modification that effectively crosslinks an L-serine residue and an L-lysine residue to release water and form 2-amino-6-(2-amino-2-carboxyethylamino)hexanoic acid.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 9 H 15 N 3 O 2
197.24
197.11642
K, S
natural
uniprot.ptm:PTM-0172
(2R,9S)-lysinoalanine
(2S)-2-amino-6-([(2R)-2-amino-2-carboxyethyl]amino)hexanoic acid
CROSSLNK Lysinoalanine (Ser-Lys)
L-lysinoalanine
LAL
Lysinoalanine (from Cysteine)
N-epsilon-(2-amino-2-carboxyethyl)-L-lysine
N6-(2-amino-2-carboxyethyl)-L-lysine
XLNK-N6Lys-3Dha(Ser)
alaninolysine
PSI-MOD
MOD:00132
Cross-link 2. This entry is for the crosslink of peptidyl serine and peptidyl lysine. For the modification of peptidyl lysine by a free serine see MOD:01838. From DeltaMass: Average Mass: -34.
L-lysinoalanine (Lys-Ser)
A protein modification that effectively crosslinks an L-serine residue and an L-lysine residue to release water and form 2-amino-6-(2-amino-2-carboxyethylamino)hexanoic acid.
DeltaMass:0
PubMed:2544544
RESID:AA0123#KSX
(2R,9S)-lysinoalanine
(2S)-2-amino-6-([(2R)-2-amino-2-carboxyethyl]amino)hexanoic acid
CROSSLNK Lysinoalanine (Ser-Lys)
L-lysinoalanine
LAL
Lysinoalanine (from Cysteine)
N-epsilon-(2-amino-2-carboxyethyl)-L-lysine
N6-(2-amino-2-carboxyethyl)-L-lysine
XLNK-N6Lys-3Dha(Ser)
alaninolysine
A protein modification that effectively crosslinks an L-glutamine residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoglutamyl)-L-lysine and the release of ammonia.
-17.03
C 0 H -3 N -1 O 0
-17.026548
C 11 H 17 N 3 O 3
239.27
239.12698
K, Q
natural
uniprot.ptm:PTM-0158
(2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid
2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid
5-glutamyl N6-lysine
CROSSLNK Isoglutamyl lysine isopeptide (Lys-Gln)
N alpha -(gamma-Glutamyl)-lysine
N(epsilon)-(gamma-glutamyl)lysine
N6-(L-isoglutamyl)-L-lysine
XLNK-N6Lys-5Glu(Gln)
PSI-MOD
MOD:00133
Cross-link 2.
N6-(L-isoglutamyl)-L-lysine (Gln)
A protein modification that effectively crosslinks an L-glutamine residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoglutamyl)-L-lysine and the release of ammonia.
ChEBI:21863
DeltaMass:0
PubMed:2461365
PubMed:5637041
PubMed:5656070
PubMed:8598899
RESID:AA0124#GLN
(2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid
2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid
5-glutamyl N6-lysine
CROSSLNK Isoglutamyl lysine isopeptide (Lys-Gln)
N alpha -(gamma-Glutamyl)-lysine
N(epsilon)-(gamma-glutamyl)lysine
N6-(L-isoglutamyl)-L-lysine
XLNK-N6Lys-5Glu(Gln)
A protein modification that effectively crosslinks an L-lysine residue and a glycine residue by an isopeptide bond to form N6-glycyl-L-lysine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 8 H 14 N 3 O 2
184.22
184.1086
G, K
natural
C-term
uniprot.ptm:PTM-0134
(2S)-2-amino-6-[(aminoacetyl)amino]hexanoic acid
CROSSLNK Glycyl lysine isopeptide (Gly-Lys) (interchain with K-...)
CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-...)
N6-(glycyl)-L-lysine
N6-glycyllysine
XLNK-N6Lys-1Gly
PSI-MOD
MOD:00134
Cross-link 2; this is the common crosslink structure formed by ubiquitin, SUMO, and similar proteins.
N6-glycyl-L-lysine
A protein modification that effectively crosslinks an L-lysine residue and a glycine residue by an isopeptide bond to form N6-glycyl-L-lysine.
ChEBI:21885
RESID:AA0125
(2S)-2-amino-6-[(aminoacetyl)amino]hexanoic acid
CROSSLNK Glycyl lysine isopeptide (Gly-Lys) (interchain with K-...)
CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-...)
N6-(glycyl)-L-lysine
N6-glycyllysine
XLNK-N6Lys-1Gly
A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)glycine and the release of ammonia.
-17.03
C 0 H -3 N -1 O 0
-17.026548
C 6 H 7 N 2 O 3
155.13
155.04567
G, N
natural
N-term
uniprot.ptm:PTM-0489
(2S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid
2-amino-N4-(carboxymethyl)-butanediamic acid
CROSSLNK Isoaspartyl glycine isopeptide (Asn-Gly)
CROSSLNK Isoaspartyl glycine isopeptide (Gly-Asn)
N-(L-isoaspartyl)-glycine
N-beta-aspartylglycine
N4-(carboxymethyl)-asparagine
XLNK-4Asp-NGly(Asn)
isoaspartyl glycine
PSI-MOD
MOD:00135
Cross-link 2.
N-(L-isoaspartyl)-glycine (Asn)
A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)glycine and the release of ammonia.
ChEBI:21479
PubMed:1826288
RESID:AA0126
(2S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid
2-amino-N4-(carboxymethyl)-butanediamic acid
CROSSLNK Isoaspartyl glycine isopeptide (Asn-Gly)
CROSSLNK Isoaspartyl glycine isopeptide (Gly-Asn)
N-(L-isoaspartyl)-glycine
N-beta-aspartylglycine
N4-(carboxymethyl)-asparagine
XLNK-4Asp-NGly(Asn)
isoaspartyl glycine
A protein modification that effectively converts an L-cysteine residue to pyruvic acid.
-33.09
C 0 H -3 N -1 O 1 S -1
-33.003704
C 3 H 3 O 2
71.06
71.013306
C
natural
N-term
Unimod:382
uniprot.ptm:PTM-0265
2-oxopropanoic acid
MOD_RES Pyruvic acid (Cys)
Pyruv(Cys)
pyruvic acid
PSI-MOD
MOD:00136
pyruvic acid (Cys)
A protein modification that effectively converts an L-cysteine residue to pyruvic acid.
PubMed:10085076
PubMed:3042771
PubMed:8464063
RESID:AA0127#CYS
Unimod:382
2-oxopropanoic acid
MOD_RES Pyruvic acid (Cys)
Pyruv(Cys)
pyruvic acid
A protein modification that effectively converts an L-phenylalanine residue into L-3-phenyllactic acid.
0.98
C 0 H -1 N -1 O 1
0.984016
C 9 H 9 O 2
149.17
149.06026
F
N-term
Unimod:7
uniprot.ptm:PTM-0035
(2S)-2-hydroxy-3-phenylpropanoic acid
L-3-phenyllactic acid
MOD_RES 3-phenyllactic acid
PSI-MOD
Deamidated
Deamidation
MOD:00137
This modification is not the result of deamidation, instead the alpha amino group is replaced with an hydroxyl group.
L-3-phenyllactic acid
A protein modification that effectively converts an L-phenylalanine residue into L-3-phenyllactic acid.
PubMed:1973541
RESID:AA0128
Unimod:7#F
(2S)-2-hydroxy-3-phenylpropanoic acid
L-3-phenyllactic acid
MOD_RES 3-phenyllactic acid
Deamidated
Deamidation
A protein modification that effectively converts an L-threonine residue into 2-oxobutanoic acid.
-17.03
C 0 H -3 N -1 O 0
-17.026548
C 4 H 5 O 2
85.08
85.02895
T
N-term
Unimod:385
uniprot.ptm:PTM-0017
2-ketobutyric acid
2-oxobutanoic acid
2-oxobutyric acid
MOD_RES 2-oxobutanoic acid
PSI-MOD
Ammonia-loss
Loss of ammonia
MOD:00138
2-oxobutanoic acid
A protein modification that effectively converts an L-threonine residue into 2-oxobutanoic acid.
ChEBI:149508
PubMed:15023056
PubMed:1680314
PubMed:2253617
PubMed:2764678
RESID:AA0129
Unimod:385#T
2-ketobutyric acid
2-oxobutanoic acid
2-oxobutanoic acid
2-oxobutyric acid
MOD_RES 2-oxobutanoic acid
Ammonia-loss
Loss of ammonia
A protein modification that effectively converts an L-tryptophan residue to N2-succinyl-L-tryptophan.
100.07
C 4 H 4 N 0 O 3
100.016045
C 15 H 15 N 2 O 4
287.29
287.10318
W
natural
N-term
Unimod:64
uniprot.ptm:PTM-0181
(2S)-2-(3-carboxypropanoyl)amino-3-(1H-indol-3-yl)propanoic acid
(2S)-2-amino-(6,7-dihydro-6,7-dioxo-1H-indole)-3-propanoic acid
MOD_RES N2-succinyltryptophan
N2-succinyl-L-tryptophan
PSI-MOD
Succinic anhydride labeling reagent light form (N-term)
Succinyl
MOD:00139
N2-succinyl-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to N2-succinyl-L-tryptophan.
PubMed:11857757
PubMed:12175151
PubMed:8471040
RESID:AA0130
Unimod:64#N-term
(2S)-2-(3-carboxypropanoyl)amino-3-(1H-indol-3-yl)propanoic acid
(2S)-2-amino-(6,7-dihydro-6,7-dioxo-1H-indole)-3-propanoic acid
MOD_RES N2-succinyltryptophan
N2-succinyl-L-tryptophan
Succinic anhydride labeling reagent light form (N-term)
Succinyl
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycocyanobilin.
586.69
C 33 H 38 N 4 O 6 S 0
586.2791
C 36 H 43 N 5 O 7 S 1
689.83
689.2883
C
natural
Unimod:387
(2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-18-ethyl-1,2,3,19,21,22,24-heptahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid
(2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-2,7,13,17-tetramethyl-1,2,3,19,21,22,24-heptahydrobilin-1,19(21H,22H,24H)-dione
BINDING Phycocyanobilin chromophore (covalent; via 1 link)
PCB
S-Phycocyanobilin (on Cysteine)
S-phycocyanobilin-L-cysteine
phycobilin cysteine
phycocyanobilin cysteine adduct
PSI-MOD
Phycocyanobilin
phycocyanobilin
MOD:00140
From DeltaMass: Average Mass: 587.
S-phycocyanobilin-L-cysteine
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycocyanobilin.
ChEBI:15617
DeltaMass:0
PubMed:16644722
PubMed:3208761
PubMed:3838747
PubMed:7918400
RESID:AA0131
Unimod:387#C
(2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-18-ethyl-1,2,3,19,21,22,24-heptahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid
(2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-2,7,13,17-tetramethyl-1,2,3,19,21,22,24-heptahydrobilin-1,19(21H,22H,24H)-dione
BINDING Phycocyanobilin chromophore (covalent; via 1 link)
PCB
S-Phycocyanobilin (on Cysteine)
S-phycocyanobilin-L-cysteine
phycobilin cysteine
phycocyanobilin cysteine adduct
Phycocyanobilin
phycocyanobilin
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoerythrobilin.
588.7
C 33 H 40 N 4 O 6 S 0
588.2948
C 36 H 45 N 5 O 7 S 1
691.84
691.30396
C
natural
Unimod:388
(2S,3R,16R)-18-ethenyl-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione
18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,3,15,16-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid
BINDING Phycoerythrobilin chromophore (covalent; via 1 link)
PEB
S-phycoerythrobilin-L-cysteine
phycoerythrobilin cysteine adduct
PSI-MOD
Phycoerythrobilin
phycoerythrobilin
MOD:00141
S-phycoerythrobilin-L-cysteine
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoerythrobilin.
ChEBI:15618
PubMed:14588022
PubMed:3208761
PubMed:3838747
PubMed:8876649
RESID:AA0132
Unimod:388#C
(2S,3R,16R)-18-ethenyl-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione
18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,3,15,16-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid
BINDING Phycoerythrobilin chromophore (covalent; via 1 link)
PEB
S-phycoerythrobilin-L-cysteine
phycoerythrobilin cysteine adduct
Phycoerythrobilin
phycoerythrobilin
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phytochromobilin.
584.67
C 33 H 36 N 4 O 6 S 0
584.2635
C 36 H 41 N 5 O 7 S 1
687.81
687.27264
C
natural
Unimod:389
(2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-2,7,13,17-tetramethyl-1,2,3,19,21,22,24-heptahydrobilin-1,19(21H,22H,24H)-dione
18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-1,2,3,19,22,24-hexahydro-2,7,13,17-tetramethyl-1,19-dioxo-21H-biline-8,12-dipropanoic acid
BINDING Phytochromobilin chromophore (covalent; via 1 link)
S-phytochromobilin-L-cysteine
phytochrome chromophore
phytochromobilin cysteine adduct
PSI-MOD
Phytochromobilin
phytochromobilin
MOD:00142
S-phytochromobilin-L-cysteine
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phytochromobilin.
ChEBI:15619
PubMed:1634523
PubMed:16593380
PubMed:3208761
PubMed:7918400
RESID:AA0133
Unimod:389#C
(2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-2,7,13,17-tetramethyl-1,2,3,19,21,22,24-heptahydrobilin-1,19(21H,22H,24H)-dione
18-ethenyl-3-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-1,2,3,19,22,24-hexahydro-2,7,13,17-tetramethyl-1,19-dioxo-21H-biline-8,12-dipropanoic acid
BINDING Phytochromobilin chromophore (covalent; via 1 link)
S-phytochromobilin-L-cysteine
phytochrome chromophore
phytochromobilin cysteine adduct
Phytochromobilin
phytochromobilin
A protein modification that effectively results from forming an adduct between two cysteine residues and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
616.5
C 34 Fe 1 H 32 N 4 O 4 S 0
616.1773
C 40 Fe 1 H 42 N 6 O 6 S 2
822.78
822.1957
C, C
natural
(7,12-bis[(1S)-1-([(2R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis[2-carboxyethyl]-N21,N22,N23,N24)-ferrate
2,4-bis[1-(S-cysteinyl)ethyl]protoporphyrin IX
BINDING Heme (covalent)
HemeCys2
biscysteinyl heme
heme-bis-L-cysteine
PSI-MOD
MOD:00143
Cross-link 2.
heme-bis-L-cysteine
A protein modification that effectively results from forming an adduct between two cysteine residues and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
ChEBI:17627
PubMed:5545094
PubMed:8827449
RESID:AA0134
(7,12-bis[(1S)-1-([(2R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis[2-carboxyethyl]-N21,N22,N23,N24)-ferrate
2,4-bis[1-(S-cysteinyl)ethyl]protoporphyrin IX
BINDING Heme (covalent)
HemeCys2
biscysteinyl heme
heme-bis-L-cysteine
A protein modification that effectively results from forming an adduct between a cysteine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
616.5
C 34 Fe 1 H 32 N 4 O 4 S 0
616.1773
C 37 Fe 1 H 37 N 5 O 5 S 1
719.64
719.18646
C
natural
Unimod:390
(12-ethenyl-7-[(1S)-1-([(2R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis[2-carboxyethyl]-N21,N22,N23,N24)-ferrate
4-[1-(S-cysteinyl)ethyl]protoporphyrin IX
BINDING Heme (covalent; via 1 link)
HemeCys1
S-Heme (on Cysteine)
cysteinyl heme
heme-L-cysteine
PSI-MOD
Heme
heme
MOD:00144
From DeltaMass: Average Mass: 617.
heme-L-cysteine
A protein modification that effectively results from forming an adduct between a cysteine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
ChEBI:17627
DeltaMass:0
PubMed:170910
PubMed:192772
PubMed:2536325
PubMed:9535866
RESID:AA0135
Unimod:390#C
(12-ethenyl-7-[(1S)-1-([(2R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis[2-carboxyethyl]-N21,N22,N23,N24)-ferrate
4-[1-(S-cysteinyl)ethyl]protoporphyrin IX
BINDING Heme (covalent; via 1 link)
HemeCys1
S-Heme (on Cysteine)
cysteinyl heme
heme-L-cysteine
Heme
heme
A protein modification that effectively converts four L-cysteine residues iron atom to tetrakis-L-cysteinyl iron.
51.81
C 0 Fe 1 H -4 N 0 O 0 S 0
51.904736
2-
C 12 Fe 1 H 16 N 4 O 4 S 4
464.37
463.94147
C, C, C, C
natural
METAL Iron
tetrakis(cysteinato-kappaS)-iron
tetrakis-L-cysteinyl iron
PSI-MOD
MOD:00145
Cross-link 4.
tetrakis-L-cysteinyl iron
A protein modification that effectively converts four L-cysteine residues iron atom to tetrakis-L-cysteinyl iron.
PubMed:1303768
PubMed:2244884
RESID:AA0136
METAL Iron
tetrakis(cysteinato-kappaS)-iron
tetrakis-L-cysteinyl iron
A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to tetrakis-L-cysteinyl diiron disulfide.
171.78
C 0 Fe 2 H -4 N 0 O 0 S 2
171.78381
2-
C 12 Fe 2 H 16 N 4 O 4 S 6
584.34
583.82056
C, C, C, C
natural
METAL Iron-sulfur (2Fe-2S)
METAL Iron-sulfur (2Fe-2S); shared with dimeric partner
tetrakis-L-cysteinyl diiron disulfide
tetrakiscysteinato-1kappa(2)S,2kappa(2)S-di-mu-sulfido-diiron
PSI-MOD
MOD:00146
Cross-link 4.
tetrakis-L-cysteinyl diiron disulfide
A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to tetrakis-L-cysteinyl diiron disulfide.
PubMed:2123937
PubMed:6801028
PubMed:7763242
PubMed:8688437
RESID:AA0137
METAL Iron-sulfur (2Fe-2S)
METAL Iron-sulfur (2Fe-2S); shared with dimeric partner
tetrakis-L-cysteinyl diiron disulfide
tetrakiscysteinato-1kappa(2)S,2kappa(2)S-di-mu-sulfido-diiron
A protein modification that effectively converts six L-cysteine residues and a three-iron three-sulfur cluster to hexakis-L-cysteinyl triiron trisulfide.
257.67
C 0 Fe 3 H -6 N 0 O 0 S 3
257.67572
3-
C 18 Fe 3 H 24 N 6 O 6 S 9
876.5
875.73083
C, C, C, C, C, C
hypothetical
hexakis-L-cysteinyl triiron trisulfide
tri-mu-sulfido-hexakiscysteinato-1kappa(2)S,2kappa(2)S,3kappa(2)S-triiron
tri-mu-sulfidotris(biscysteinato-kappaS-iron)
PSI-MOD
MOD:00147
Cross-link 6. This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
hexakis-L-cysteinyl triiron trisulfide
A protein modification that effectively converts six L-cysteine residues and a three-iron three-sulfur cluster to hexakis-L-cysteinyl triiron trisulfide.
PubMed:3379067
PubMed:3932661
PubMed:7354058
RESID:AA0138
hexakis-L-cysteinyl triiron trisulfide
tri-mu-sulfido-hexakiscysteinato-1kappa(2)S,2kappa(2)S,3kappa(2)S-triiron
tri-mu-sulfidotris(biscysteinato-kappaS-iron)
A protein modification that effectively converts three L-cysteine residues and a three-iron four-sulfur cluster to tris-L-cysteinyl triiron tetrasulfide.
292.75
C 0 Fe 3 H -3 N 0 O 0 S 4
292.67126
3-
C 9 Fe 3 H 12 N 3 O 3 S 7
602.17
601.6988
C, C, C
natural
METAL Iron-sulfur (3Fe-4S)
mu3-sulfido tri-mu-sulfido tris-S-L-cysteinyl triiron
mu3-sulfido-tri-mu-sulfido-triscysteinato-1kappaS,2kappaS,3kappaS-triiron
tris-L-cysteinyl triiron tetrasulfide
tris-L-cysteinyl triiron tetrasulfide C3 cluster
tris-L-cysteinyl triiron tetrasulfide cubane form
tris-L-cysteinyl triiron tetrasulfide cuboid cluster
tris-L-cysteinyl triiron tetrasulfide trigonal cluster
PSI-MOD
MOD:00148
Cross-link 3.
tris-L-cysteinyl triiron tetrasulfide
A protein modification that effectively converts three L-cysteine residues and a three-iron four-sulfur cluster to tris-L-cysteinyl triiron tetrasulfide.
PubMed:10555576
PubMed:2056535
PubMed:3422475
PubMed:6848518
PubMed:7819255
PubMed:9063899
RESID:AA0139
METAL Iron-sulfur (3Fe-4S)
mu3-sulfido tri-mu-sulfido tris-S-L-cysteinyl triiron
mu3-sulfido-tri-mu-sulfido-triscysteinato-1kappaS,2kappaS,3kappaS-triiron
tris-L-cysteinyl triiron tetrasulfide
tris-L-cysteinyl triiron tetrasulfide C3 cluster
tris-L-cysteinyl triiron tetrasulfide cubane form
tris-L-cysteinyl triiron tetrasulfide cuboid cluster
tris-L-cysteinyl triiron tetrasulfide trigonal cluster
A protein modification that effectively converts four L-cysteine residues and a four-iron four-sulfur cluster to tetrakis-L-cysteinyl tetrairon tetrasulfide.
347.59
C 0 Fe 4 H -4 N 0 O 0 S 4
347.59784
2-
C 12 Fe 4 H 16 N 4 O 4 S 8
760.15
759.6346
C, C, C, C
natural
METAL Iron-sulfur (4Fe-4S)
METAL Iron-sulfur (4Fe-4S); shared with dimeric partner
tetra-mu3-sulfido-tetrakis(cysteinato)-1kappaS,2kappaS,3kappaS,4kappaS-tetrahedro-tetrairon
tetra-mu3-sulfidotetrakis(S-cysteinyliron)
tetrakis-L-cysteinyl tetrairon tetrasulfide
PSI-MOD
MOD:00149
Cross-link 4.
tetrakis-L-cysteinyl tetrairon tetrasulfide
A protein modification that effectively converts four L-cysteine residues and a four-iron four-sulfur cluster to tetrakis-L-cysteinyl tetrairon tetrasulfide.
PubMed:3351918
PubMed:7803404
PubMed:7819196
PubMed:932007
RESID:AA0140
METAL Iron-sulfur (4Fe-4S)
METAL Iron-sulfur (4Fe-4S); shared with dimeric partner
tetra-mu3-sulfido-tetrakis(cysteinato)-1kappaS,2kappaS,3kappaS,4kappaS-tetrahedro-tetrairon
tetra-mu3-sulfidotetrakis(S-cysteinyliron)
tetrakis-L-cysteinyl tetrairon tetrasulfide
A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and a one-molybdenum seven-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide.
991.53
C 7 Fe 7 H 6 Mo 1 N 1 O 7 S 9
993.213
C 16 Fe 7 H 18 Mo 1 N 5 O 9 S 10
1231.81
1233.2811
C, H
natural
L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide carbide
cysteinato-8kappaS-histidino-1kappaN(tau)-[(2R)-4-carboxy-2-(carboxymethyl)-2-oxidobutanoate-1kappaO(1),1kappaO(2)]-mu6-carbido-2:3:4:5:6:7kappa(6)C-hexa-mu3-sulfido-1:2:3kappa(3)S;1:2:4kappa(3)S;1:3:4kappa(3)S;5:6:8kappa(3)S;5:7:8kappa(3)S;6:7:8kappa(3)S-tri-mu2-sulfido-2:5kappa(2)S;3:6kappa(2)S;4:7kappa(2)S molybdenum heptairon
nitrogenase iron-molybdenum cofactor
PSI-MOD
MOD:00150
Cross-link 2; incidental to RESID:AA0300.
L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide
A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and a one-molybdenum seven-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide.
PubMed:10525412
PubMed:12215645
PubMed:12733878
PubMed:1529354
PubMed:8027059
RESID:AA0141
L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide carbide
cysteinato-8kappaS-histidino-1kappaN(tau)-[(2R)-4-carboxy-2-(carboxymethyl)-2-oxidobutanoate-1kappaO(1),1kappaO(2)]-mu6-carbido-2:3:4:5:6:7kappa(6)C-hexa-mu3-sulfido-1:2:3kappa(3)S;1:2:4kappa(3)S;1:3:4kappa(3)S;5:6:8kappa(3)S;5:7:8kappa(3)S;6:7:8kappa(3)S-tri-mu2-sulfido-2:5kappa(2)S;3:6kappa(2)S;4:7kappa(2)S molybdenum heptairon
nitrogenase iron-molybdenum cofactor
A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdopterin.
520.27
C 10 H 11 Mo 1 N 5 O 8 P 1 S 2
521.8841
C 13 H 16 Mo 1 N 6 O 9 P 1 S 3
623.41
624.89325
C
natural
Unimod:391
(4R,5aR,11aR)-8-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-4,5a,6,9,10,11,11a-heptahydro-4-(phosphoric acid)methyl-2,2,10-trioxo-pteridino[6,7-5,6]pyrano[3,4-4,3][1,2,5]molybdadithiolene
L-cysteinyl molybdopterin
METAL Molybdenum-pterin
MoPterCys
cysteinyl Mo-molybdopterin
cysteinyl Mo-pterin
molybdoenzyme molybdenum cofactor
PSI-MOD
Molybdopterin
molybdopterin
MOD:00151
L-cysteinyl molybdopterin
A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdopterin.
PubMed:14527393
PubMed:7878465
PubMed:9428520
RESID:AA0142
Unimod:391#C
(4R,5aR,11aR)-8-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-4,5a,6,9,10,11,11a-heptahydro-4-(phosphoric acid)methyl-2,2,10-trioxo-pteridino[6,7-5,6]pyrano[3,4-4,3][1,2,5]molybdadithiolene
L-cysteinyl molybdopterin
METAL Molybdenum-pterin
MoPterCys
cysteinyl Mo-molybdopterin
cysteinyl Mo-pterin
molybdoenzyme molybdenum cofactor
Molybdopterin
molybdopterin
A protein modification that effectively converts an L-cysteine residue to S'-(8alpha-FAD)-L-cystine.
783.54
C 27 H 31 N 9 O 15 P 2 S 0
783.1415
C 30 H 36 N 10 O 16 P 2 S 1
886.68
886.1507
C
natural
Unimod:50
uniprot.ptm:PTM-0272
(2R)-2-amino-3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]sulfanylpropanoic acid
8alpha-(S-cysteinyl)FAD
MOD_RES S-8alpha-FAD cysteine
S-(8alpha-FAD)-L-cysteine
S8aFADCys
PSI-MOD
FAD
Flavin adenine dinucleotide
MOD:00152
S-(8alpha-FAD)-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S'-(8alpha-FAD)-L-cystine.
PubMed:10220347
RESID:AA0143
Unimod:50#C
(2R)-2-amino-3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]sulfanylpropanoic acid
8alpha-(S-cysteinyl)FAD
MOD_RES S-8alpha-FAD cysteine
S-(8alpha-FAD)-L-cysteine
S8aFADCys
FAD
Flavin adenine dinucleotide
A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FAD)-L-histidine.
783.54
C 27 H 31 N 9 O 15 P 2
783.1415
C 33 H 38 N 12 O 16 P 2
920.68
920.2004
H
natural
Unimod:50
uniprot.ptm:PTM-0258
(2S)-2-amino-3-(3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid
3'-(8alpha-FAD)-L-histidine
8alpha-(N(delta)-histidyl)FAD
8alpha-(N3'-histidyl)FAD
MOD_RES Pros-8alpha-FAD histidine
N(pi)-(8alpha-FAD)-histidine
Np8aFADHis
pros-(8alpha-FAD)-histidine
PSI-MOD
8alpha-N1-histidyl FAD
FAD
Flavin adenine dinucleotide
MOD:00153
3'-(8alpha-FAD)-L-histidine
A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FAD)-L-histidine.
PubMed:241294
PubMed:8076
RESID:AA0144
Unimod:50#H
(2S)-2-amino-3-(3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid
3'-(8alpha-FAD)-L-histidine
8alpha-(N(delta)-histidyl)FAD
8alpha-(N3'-histidyl)FAD
MOD_RES Pros-8alpha-FAD histidine
N(pi)-(8alpha-FAD)-histidine
Np8aFADHis
pros-(8alpha-FAD)-histidine
8alpha-N1-histidyl FAD
FAD
Flavin adenine dinucleotide
A protein modification that effectively converts an L-tyrosine residue to O4'-(8alpha-FAD)-L-tyrosine.
783.54
C 27 H 31 N 9 O 15 P 2
783.1415
C 36 H 40 N 10 O 17 P 2
946.72
946.20483
Y
natural
Unimod:50
uniprot.ptm:PTM-0231
(2S)-2-amino-3-(4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxyphenyl)propanoic acid
8alpha-(O4'-tyrosyl)FAD
MOD_RES O-8alpha-FAD tyrosine
O-8 alpha-Flavin [FAD])- (of Tyrosine)
O4'-(8alpha-FAD)-L-tyrosine
O8aFADTyr
PSI-MOD
FAD
Flavin adenine dinucleotide
MOD:00154
From DeltaMass: Average Mass: 783
O4'-(8alpha-FAD)-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to O4'-(8alpha-FAD)-L-tyrosine.
DeltaMass:0
PubMed:7391034
RESID:AA0145
Unimod:50#Y
(2S)-2-amino-3-(4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxyphenyl)propanoic acid
8alpha-(O4'-tyrosyl)FAD
MOD_RES O-8alpha-FAD tyrosine
O-8 alpha-Flavin [FAD])- (of Tyrosine)
O4'-(8alpha-FAD)-L-tyrosine
O8aFADTyr
FAD
Flavin adenine dinucleotide
A protein modification that effectively converts an L-tyrosine residue to L-3',4'-dihydroxyphenylalanine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 9 H 9 N 1 O 3
179.18
179.05824
Y
natural
Unimod:35
uniprot.ptm:PTM-0023
(2S)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid
3,4-Dihydroxy-Phenylalanine (from Tyrosine) (DOPA)
3HyTyr
L-3',4'-dihydroxyphenylalanine
L-3'-hydroxytyrosine
L-DOPA
MOD_RES 3',4'-dihydroxyphenylalanine
hydroxylationy
levodopa
mod194
PSI-MOD
MOD:00155
incidental to RESID:AA0368 From DeltaMass: Average Mass: 16
L-3',4'-dihydroxyphenylalanine
A protein modification that effectively converts an L-tyrosine residue to L-3',4'-dihydroxyphenylalanine.
ChEBI:141815
DeltaMass:0
OMSSA:194
OMSSA:64
PubMed:1610822
PubMed:1903612
PubMed:3734192
RESID:AA0146
Unimod:35#Y
(2S)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid
3,4-Dihydroxy-Phenylalanine (from Tyrosine) (DOPA)
3HyTyr
L-3',4'-dihydroxyphenylalanine
L-3'-hydroxytyrosine
L-DOPA
MOD_RES 3',4'-dihydroxyphenylalanine
hydroxylationy
levodopa
mod194
A protein modification that effectively converts an L-tyrosine residue to an L-2',4',5'-topaquinone.
29.98
C 0 H -2 N 0 O 2
29.974178
C 9 H 7 N 1 O 4
193.16
193.0375
Y
natural
Unimod:392
uniprot.ptm:PTM-0009
(2S)-2-amino-3-(5-hydroxy-2,5-cyclohexadien-1,4-dion-2-yl)propanoic acid
2,4,5-trihydroxyphenylalanine quinone
5-(2-carboxy-2-aminoethyl)-2-hydroxy-1,4-benzoquinone
L-2',4',5'-topaquinone
L-2,4,5-TOPAquinone
MOD_RES 2',4',5'-topaquinone
TPQ
TopaQ
PSI-MOD
Quinone
quinone
MOD:00156
L-2',4',5'-topaquinone
A protein modification that effectively converts an L-tyrosine residue to an L-2',4',5'-topaquinone.
ChEBI:21187
PubMed:10387067
PubMed:1457410
PubMed:1569055
PubMed:2111581
RESID:AA0147
Unimod:392#Y
(2S)-2-amino-3-(5-hydroxy-2,5-cyclohexadien-1,4-dion-2-yl)propanoic acid
2,4,5-trihydroxyphenylalanine quinone
5-(2-carboxy-2-aminoethyl)-2-hydroxy-1,4-benzoquinone
L-2',4',5'-topaquinone
L-2,4,5-TOPAquinone
MOD_RES 2',4',5'-topaquinone
TPQ
TopaQ
Quinone
quinone
A protein modification that effectively converts an L-tryptophan residue to an L-tryptophan quinone.
29.98
C 0 H -2 N 0 O 2
29.974178
C 11 H 8 N 2 O 3
216.2
216.0535
W
natural
Unimod:392
uniprot.ptm:PTM-0299
(2S)-2-amino-3-(6,7-dioxo-1H-indol-3-yl)propanoic acid
2-amino-3-(6,7-dioxo-6,7-dihydro-1H-indol-3-yl)-propionic acid
3-[(2S)-2-amino-2-carboxyethyl]-6,7-indolinedione
6,7 Dione (from Tryptophan)
L-tryptophyl quinone
MOD_RES Tryptophylquinone
N-(3-carboxy-1-oxopropyl)-L-tryptophan
TrpQ
PSI-MOD
Quinone
quinone
MOD:00157
incidental to RESID:AA0149; incidental to RESID:AA0313; From DeltaMass: Average Mass: 30.
L-tryptophyl quinone
A protein modification that effectively converts an L-tryptophan residue to an L-tryptophan quinone.
DeltaMass:0
PubMed:2028257
RESID:AA0148
Unimod:392#W
(2S)-2-amino-3-(6,7-dioxo-1H-indol-3-yl)propanoic acid
2-amino-3-(6,7-dioxo-6,7-dihydro-1H-indol-3-yl)-propionic acid
3-[(2S)-2-amino-2-carboxyethyl]-6,7-indolinedione
6,7 Dione (from Tryptophan)
L-tryptophyl quinone
MOD_RES Tryptophylquinone
N-(3-carboxy-1-oxopropyl)-L-tryptophan
TrpQ
Quinone
quinone
A protein modification that effectively cross-links two L-tryptophan residues by a carbon-carbon bond to form 4'-(L-tryptophan)-L-tryptophyl quinone.
27.97
C 0 H -4 N 0 O 2
27.958529
C 22 H 16 N 4 O 4
400.39
400.11716
W, W
natural
uniprot.ptm:PTM-0298
2,4-BisTrp-6,7-dione (from Tryptophan)
2-amino-3-[2-[2-amino-3-(2-carboxyethyl)-6,7-dioxo-1H-indol-4-yl]-1H-indol-3-yl]propanoic acid
3-[(2S)-2-amino-2-carboxyethyl]-4-(3-[(2S)-2-amino-2-carboxyethyl]-1H-indol-2-yl)-6,7-indolinedione
4'-tryptophan-tryptophylquinone
4-(2'-tryptophyl)tryptophan-6,7-dione
4-(L-tryptophan-2-yl)-L-tryptophyl quinone
CROSSLNK Tryptophan tryptophylquinone (Trp-Trp)
TTQ
XLNK-4'Trp-TrpQ
alpha,alpha'-diamino-6',7'-dihydro-6',7'-dioxo-(2,4'-bi-1H-indole)-3,3'-dipropanoic acid
PSI-MOD
MOD:00158
Cross-link 2; secondary to RESID:AA0148; From DeltaMass: Average Mass: 28.
4'-(L-tryptophan)-L-tryptophyl quinone
A protein modification that effectively cross-links two L-tryptophan residues by a carbon-carbon bond to form 4'-(L-tryptophan)-L-tryptophyl quinone.
ChEBI:20251
DeltaMass:0
PubMed:2028257
RESID:AA0149
2,4-BisTrp-6,7-dione (from Tryptophan)
2-amino-3-[2-[2-amino-3-(2-carboxyethyl)-6,7-dioxo-1H-indol-4-yl]-1H-indol-3-yl]propanoic acid
3-[(2S)-2-amino-2-carboxyethyl]-4-(3-[(2S)-2-amino-2-carboxyethyl]-1H-indol-2-yl)-6,7-indolinedione
4'-tryptophan-tryptophylquinone
4-(2'-tryptophyl)tryptophan-6,7-dione
4-(L-tryptophan-2-yl)-L-tryptophyl quinone
CROSSLNK Tryptophan tryptophylquinone (Trp-Trp)
TTQ
XLNK-4'Trp-TrpQ
alpha,alpha'-diamino-6',7'-dihydro-6',7'-dioxo-(2,4'-bi-1H-indole)-3,3'-dipropanoic acid
A protein modification that effectively converts an L-serine residue to O-phosphopantetheine-L-serine.
340.33
C 11 H 21 N 2 O 6 P 1 S 1
340.0858
C 14 H 26 N 3 O 8 P 1 S 1
427.41
427.11783
S
natural
Unimod:49
uniprot.ptm:PTM-0391
(2R)-2-hydroxy-3,3-dimethyl-4-[(2S)-2-amino-2-carboxyethyl]phosphonato-N-(3-oxo-3-[(2-sulfanylethyl)amino]propyl)butanamide
4'-Phosphopantetheine
MOD_RES O-(pantetheine 4'-phosphoryl)serine
O-phosphopantetheine-L-serine
OPpantSer
PSI-MOD
Phosphopantetheine
MOD:00159
Unimod has DiffFormula C 11 H 20 N 2 O 6 P 1 S 1 From DeltaMass: Average Mass: 339
O-phosphopantetheine-L-serine
A protein modification that effectively converts an L-serine residue to O-phosphopantetheine-L-serine.
DeltaMass:0
PubMed:10320345
PubMed:10997907
PubMed:12057197
PubMed:12869567
PubMed:4568609
RESID:AA0150
Unimod:49#S
(2R)-2-hydroxy-3,3-dimethyl-4-[(2S)-2-amino-2-carboxyethyl]phosphonato-N-(3-oxo-3-[(2-sulfanylethyl)amino]propyl)butanamide
4'-Phosphopantetheine
MOD_RES O-(pantetheine 4'-phosphoryl)serine
O-phosphopantetheine-L-serine
OPpantSer
Phosphopantetheine
Phosphopantetheine
A protein modification that effectively converts an L-asparagine residue to an N4-glycosyl-L-asparagine.
N
natural
N4GlycoAsn
PSI-MOD
MOD:00160
N4-glycosyl-L-asparagine
A protein modification that effectively converts an L-asparagine residue to an N4-glycosyl-L-asparagine.
PubMed:111247
PubMed:1694179
PubMed:5490222
RESID:AA0151#var
N4GlycoAsn
A protein modification that effectively converts an L-cysteine residue to S-glucosylated L-cysteine.
162.14
C 6 H 10 N 0 O 5 S 0
162.05283
C 9 H 15 N 1 O 6 S 1
265.28
265.062
C
natural
Unimod:41
uniprot.ptm:PTM-0626
(2R)-2-amino-3-[(beta-D-glucopyranosyl)sulfanyl]propanoic acid
CARBOHYD S-linked (Glc) cysteine
S-(beta-D-glucopyranosyl)cysteine
S-glucosyl-L-cysteine
S-glycosyl-cysteine
SGlcCys
PSI-MOD
Hex
Hexose
MOD:00161
S-glucosyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-glucosylated L-cysteine.
PubMed:1145128
PubMed:15279557
PubMed:5286858
RESID:AA0152
Unimod:41#C
(2R)-2-amino-3-[(beta-D-glucopyranosyl)sulfanyl]propanoic acid
CARBOHYD S-linked (Glc) cysteine
S-(beta-D-glucopyranosyl)cysteine
S-glucosyl-L-cysteine
S-glycosyl-cysteine
SGlcCys
Hex
Hexose
A protein modification that effectively converts an L-lysine residue to O5-glucosylgalactosyl-L-hydroxylysine.
340.28
C 12 H 20 N 0 O 11
340.10056
C 18 H 32 N 2 O 12
468.46
468.19553
K
natural
Unimod:393
(2S,5R)-2,6-diamino-5-[2-O-(alpha-D-glucopyranosyl)-beta-D-galactopyranosyloxy]hexanoic acid
5-(2-O-alpha-D-glucopyranosyl-beta-D-galactopyranosyl)oxy-L-lysine
O5-glucosylgalactosyl-L-hydroxylysine
OGlcGal5HyLys
PSI-MOD
Glucosylgalactosyl
glucosylgalactosyl hydroxylysine
MOD:00162
Secondary to RESID:AA0028.
O5-glucosylgalactosyl-L-hydroxylysine
A protein modification that effectively converts an L-lysine residue to O5-glucosylgalactosyl-L-hydroxylysine.
PubMed:15149698
PubMed:4288358
PubMed:4319110
RESID:AA0153
Unimod:393
(2S,5R)-2,6-diamino-5-[2-O-(alpha-D-glucopyranosyl)-beta-D-galactopyranosyloxy]hexanoic acid
5-(2-O-alpha-D-glucopyranosyl-beta-D-galactopyranosyl)oxy-L-lysine
O5-glucosylgalactosyl-L-hydroxylysine
OGlcGal5HyLys
Glucosylgalactosyl
glucosylgalactosyl hydroxylysine
A protein modification that effectively converts an L-serine residue to O-(N-acetylaminogalactosyl)-L-serine.
203.19
C 8 H 13 N 1 O 5
203.07938
C 11 H 18 N 2 O 7
290.27
290.1114
S
natural
uniprot.ptm:PTM-0564
(2S)-2-amino-3-(2-acetamido-2-deoxy-alpha-D-galactopyranosyloxy)propanoic acid
CARBOHYD O-linked (GalNAc) serine
O-(N-acetylamino)galactosyl-L-serine
O3-(N-acetylgalactosaminyl)serine
OGalNAcSer
mucin type O-glycosylserine
PSI-MOD
HexNAc
MOD:00163
O-(N-acetylamino)galactosyl-L-serine
A protein modification that effectively converts an L-serine residue to O-(N-acetylaminogalactosyl)-L-serine.
PubMed:115869
PubMed:16005634
PubMed:3086323
PubMed:8948436
PubMed:9092502
RESID:AA0154
(2S)-2-amino-3-(2-acetamido-2-deoxy-alpha-D-galactopyranosyloxy)propanoic acid
CARBOHYD O-linked (GalNAc) serine
O-(N-acetylamino)galactosyl-L-serine
O3-(N-acetylgalactosaminyl)serine
OGalNAcSer
mucin type O-glycosylserine
HexNAc
A protein modification that effectively converts an L-asparagine residue to O-(N-acetylaminogalactosyl)-L-threonine.
203.19
C 8 H 13 N 1 O 5
203.07938
C 12 H 20 N 2 O 7
304.3
304.12704
T
natural
uniprot.ptm:PTM-0567
(2S,3R)-2-amino-3-(2-acetamido-2-deoxy-alpha-D-galactopyranosyloxy)butanoic acid
CARBOHYD O-linked (GalNAc) threonine
CARBOHYD O-linked (HexNAc)
O-(N-acetylamino)galactosyl-L-threonine
O3-(N-acetylgalactosaminyl)threonine
OGalNAcThr
mucin type O-glycosylthreonine
PSI-MOD
HexNAc
MOD:00164
O-(N-acetylamino)galactosyl-L-threonine
A protein modification that effectively converts an L-asparagine residue to O-(N-acetylaminogalactosyl)-L-threonine.
PubMed:16005634
PubMed:1997327
PubMed:3086323
PubMed:8948436
PubMed:9092502
RESID:AA0155
(2S,3R)-2-amino-3-(2-acetamido-2-deoxy-alpha-D-galactopyranosyloxy)butanoic acid
CARBOHYD O-linked (GalNAc) threonine
CARBOHYD O-linked (HexNAc)
O-(N-acetylamino)galactosyl-L-threonine
O3-(N-acetylgalactosaminyl)threonine
OGalNAcThr
mucin type O-glycosylthreonine
HexNAc
A protein modification that effectively converts an L-tryptophan residue to 1'-mannosyl-L-tryptophan.
162.14
C 6 H 10 N 0 O 5
162.05283
C 17 H 20 N 2 O 6
348.36
348.13214
W
natural
uniprot.ptm:PTM-0535
(2S)-2-amino-3-(1-D-mannopyranosyloxy-1H-indol-3-yl)propanoic acid
1'-glycosyl-L-tryptophan
1'-mannosyl-L-tryptophan
CARBOHYD N-linked (Man) tryptophan
N-mannosyl-tryptophan
N1'ManTrp
N1-mannosyl-tryptophan
PSI-MOD
MOD:00165
1'-mannosyl-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to 1'-mannosyl-L-tryptophan.
PubMed:1482345
PubMed:16150691
RESID:AA0156
(2S)-2-amino-3-(1-D-mannopyranosyloxy-1H-indol-3-yl)propanoic acid
1'-glycosyl-L-tryptophan
1'-mannosyl-L-tryptophan
CARBOHYD N-linked (Man) tryptophan
N-mannosyl-tryptophan
N1'ManTrp
N1-mannosyl-tryptophan
A protein modification that effectively converts an L-tyrosine residue to O4'-glucosyl-tyrosine.
162.14
C 6 H 10 N 0 O 5
162.05283
C 15 H 19 N 1 O 7
325.32
325.11615
Y
natural
Unimod:41
uniprot.ptm:PTM-0575
(2S)-2-amino-3-(4-alpha-D-glucopyranosyloxy)phenylpropanoic acid
CARBOHYD O-linked (Glc) tyrosine
O4'-glucosyl-L-tyrosine
O4'-glycosyl-L-tyrosine
O4GlcTyr
PSI-MOD
Hex
Hexose
MOD:00166
O4'-glucosyl-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to O4'-glucosyl-tyrosine.
PubMed:15279557
PubMed:3181138
RESID:AA0157
Unimod:41#Y
(2S)-2-amino-3-(4-alpha-D-glucopyranosyloxy)phenylpropanoic acid
CARBOHYD O-linked (Glc) tyrosine
O4'-glucosyl-L-tyrosine
O4'-glycosyl-L-tyrosine
O4GlcTyr
Hex
Hexose
A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylphosphatidylinositolethanolamine.
123.05
C 2 H 6 N 1 O 3 P 1
123.00853
C 6 H 13 N 3 O 6 P 1
254.16
254.0542
N
natural
C-term
uniprot.ptm:PTM-0137
GPIAsn
LIPID GPI-anchor amidated asparagine
N-asparaginyl-glycosylphosphatidylinositolethanolamine
PSI-MOD
MOD:00167
N-asparaginyl-glycosylphosphatidylinositolethanolamine
A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylphosphatidylinositolethanolamine.
PubMed:1824714
PubMed:8276756
RESID:AA0158
GPIAsn
LIPID GPI-anchor amidated asparagine
N-asparaginyl-glycosylphosphatidylinositolethanolamine
A protein modification that effectively converts an L-aspartic acid residue to N-(aspart-1-yl)-glycosylphosphatidylinositolethanolamine.
123.05
C 2 H 6 N 1 O 3 P 1
123.00853
C 6 H 12 N 2 O 7 P 1
255.14
255.03821
D
natural
C-term
uniprot.ptm:PTM-0138
GPIAsp
LIPID GPI-anchor amidated aspartate
N-aspartyl-glycosylphosphatidylinositolethanolamine
PSI-MOD
MOD:00168
N-aspartyl-glycosylphosphatidylinositolethanolamine
A protein modification that effectively converts an L-aspartic acid residue to N-(aspart-1-yl)-glycosylphosphatidylinositolethanolamine.
PubMed:7120400
RESID:AA0159
GPIAsp
LIPID GPI-anchor amidated aspartate
N-aspartyl-glycosylphosphatidylinositolethanolamine
A protein modification that effectively converts an L-cysteine residue to N-cysteinyl-glycosylphosphatidylinositolethanolamine.
123.05
C 2 H 6 N 1 O 3 P 1 S 0
123.00853
C 5 H 12 N 2 O 5 P 1 S 1
243.19
243.02045
C
natural
C-term
uniprot.ptm:PTM-0140
GPICys
LIPID GPI-anchor amidated cysteine
N-cysteinyl-glycosylphosphatidylinositolethanolamine
PSI-MOD
MOD:00169
N-cysteinyl-glycosylphosphatidylinositolethanolamine
A protein modification that effectively converts an L-cysteine residue to N-cysteinyl-glycosylphosphatidylinositolethanolamine.
PubMed:2897081
RESID:AA0160
GPICys
LIPID GPI-anchor amidated cysteine
N-cysteinyl-glycosylphosphatidylinositolethanolamine
A protein modification that effectively converts a glycine residue to N-glycyl-glycosylphosphatidylinositolethanolamine.
123.05
C 2 H 6 N 1 O 3 P 1
123.00853
C 4 H 10 N 2 O 5 P 1
197.11
197.03273
G
natural
C-term
uniprot.ptm:PTM-0141
GPIGly
LIPID GPI-anchor amidated glycine
N-glycyl-glycosylphosphatidylinositolethanolamine
PSI-MOD
MOD:00170
N-glycyl-glycosylphosphatidylinositolethanolamine
A protein modification that effectively converts a glycine residue to N-glycyl-glycosylphosphatidylinositolethanolamine.
PubMed:2341397
RESID:AA0161
GPIGly
LIPID GPI-anchor amidated glycine
N-glycyl-glycosylphosphatidylinositolethanolamine
A protein modification that effectively converts an L-serine residue to N-seryl-glycosylphosphatidylinositolethanolamine.
123.05
C 2 H 6 N 1 O 3 P 1
123.00853
C 5 H 12 N 2 O 6 P 1
227.13
227.0433
S
natural
C-term
uniprot.ptm:PTM-0142
GPISer
LIPID GPI-anchor amidated serine
N-seryl-glycosylphosphatidylinositolethanolamine
PSI-MOD
MOD:00171
N-seryl-glycosylphosphatidylinositolethanolamine
A protein modification that effectively converts an L-serine residue to N-seryl-glycosylphosphatidylinositolethanolamine.
PubMed:2111324
PubMed:8448158
RESID:AA0162
GPISer
LIPID GPI-anchor amidated serine
N-seryl-glycosylphosphatidylinositolethanolamine
A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylphosphatidylinositolethanolamine.
123.05
C 2 H 6 N 1 O 3 P 1
123.00853
C 5 H 12 N 2 O 5 P 1
211.13
211.04839
A
natural
C-term
uniprot.ptm:PTM-0136
GPIAla
LIPID GPI-anchor amidated alanine
N-alanyl-glycosylphosphatidylinositolethanolamine
PSI-MOD
MOD:00172
N-alanyl-glycosylphosphatidylinositolethanolamine
A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylphosphatidylinositolethanolamine.
PubMed:7682556
PubMed:7744038
RESID:AA0163
GPIAla
LIPID GPI-anchor amidated alanine
N-alanyl-glycosylphosphatidylinositolethanolamine
A protein modification that effectively converts an L-threonine residue to N-threonyl-glycosylphosphatidylinositolethanolamine.
123.05
C 2 H 6 N 1 O 3 P 1
123.00853
C 6 H 14 N 2 O 6 P 1
241.16
241.05894
T
hypothetical
C-term
uniprot.ptm:PTM-0143
GPIThr
LIPID GPI-anchor amidated threonine
N-threonyl-glycosylphosphatidylinositolethanolamine
PSI-MOD
MOD:00173
N-threonyl-glycosylphosphatidylinositolethanolamine
A protein modification that effectively converts an L-threonine residue to N-threonyl-glycosylphosphatidylinositolethanolamine.
RESID:AA0164
GPIThr
LIPID GPI-anchor amidated threonine
N-threonyl-glycosylphosphatidylinositolethanolamine
A protein modification that effectively converts a glycine residue to N-glycyl-glycosylsphingolipidinositolethanolamine.
123.05
C 2 H 6 N 1 O 3 P 1
123.00853
C 4 H 10 N 2 O 5 P 1
197.11
197.03273
G
hypothetical
C-term
uniprot.ptm:PTM-0146
GSIGly
LIPID GPI-like-anchor amidated glycine
N-glycyl-glycosylsphingolipidinositolethanolamine
PSI-MOD
MOD:00174
N-glycyl-glycosylsphingolipidinositolethanolamine
A protein modification that effectively converts a glycine residue to N-glycyl-glycosylsphingolipidinositolethanolamine.
PubMed:12626404
PubMed:8404891
RESID:AA0165
GSIGly
LIPID GPI-like-anchor amidated glycine
N-glycyl-glycosylsphingolipidinositolethanolamine
A protein modification that effectively converts an L-serine residue to N-seryl-glycosylsphingolipidinositolethanolamine.
123.05
C 2 H 6 N 1 O 3 P 1
123.00853
C 5 H 12 N 2 O 6 P 1
227.13
227.0433
S
natural
C-term
uniprot.ptm:PTM-0147
GSISer
LIPID GPI-like-anchor amidated serine
N-seryl-glycosylsphingolipidinositolethanolamine
PSI-MOD
MOD:00175
N-seryl-glycosylsphingolipidinositolethanolamine
A protein modification that effectively converts an L-serine residue to N-seryl-glycosylsphingolipidinositolethanolamine.
PubMed:12626404
PubMed:2721485
PubMed:8269952
RESID:AA0166
GSISer
LIPID GPI-like-anchor amidated serine
N-seryl-glycosylsphingolipidinositolethanolamine
A protein modification that effectively converts an L-serine residue to O-(phosphoribosyl dephospho-coenzyme A)-L-serine.
881.63
C 26 H 42 N 7 O 19 P 3 S 1
881.1469
C 29 H 47 N 8 O 21 P 3 S 1
968.71
968.17896
S
natural
Unimod:395
uniprot.ptm:PTM-0389
MOD_RES O-(phosphoribosyl dephospho-coenzyme A)serine
O-(phosphoribosyl dephospho-coenzyme A)-L-serine
O3-(phosphate-5-ribosyl-alpha-2-adenosine-5-diphosphate pantetheine)-L-serine
O3-(phosphoribosyl dephospho-coenzyme A)-L-serine
O3-2'-(5''-phosphoribosyl-3'-dephosphocoenzyme A)-L-serine
OPRibdPCoASer
PSI-MOD
PhosphoribosyldephosphoCoA
phosphoribosyl dephospho-coenzyme A
MOD:00176
pRibodePcoA
O-(phosphoribosyl dephospho-coenzyme A)-L-serine
A protein modification that effectively converts an L-serine residue to O-(phosphoribosyl dephospho-coenzyme A)-L-serine.
PubMed:10924139
PubMed:11052675
PubMed:179809
PubMed:180526
PubMed:368065
RESID:AA0167
Unimod:395#S
MOD_RES O-(phosphoribosyl dephospho-coenzyme A)serine
O-(phosphoribosyl dephospho-coenzyme A)-L-serine
O3-(phosphate-5-ribosyl-alpha-2-adenosine-5-diphosphate pantetheine)-L-serine
O3-(phosphoribosyl dephospho-coenzyme A)-L-serine
O3-2'-(5''-phosphoribosyl-3'-dephosphocoenzyme A)-L-serine
OPRibdPCoASer
PhosphoribosyldephosphoCoA
phosphoribosyl dephospho-coenzyme A
A protein modification that effectively converts an L-argininine residue to omega-N-(ADP-ribosyl)-L-arginine.
541.3
C 15 H 21 N 5 O 13 P 2
541.0611
C 21 H 33 N 9 O 14 P 2
697.49
697.16223
R
natural
Unimod:213
uniprot.ptm:PTM-0053
(S)-2-amino-5-([imino([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)methyl]amino)pentanoic acid
ADPRibArg
MOD_RES ADP-ribosylarginine
N(omega)-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-arginine
N(omega)-alpha-D-ribofuranosyl-L-arginine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
N-(ADP-ribosyl)- (on Arginine)
omega-N-(ADP-ribosyl)-L-arginine
PSI-MOD
ADP Ribose addition
ADP-Ribosyl
MOD:00177
From DeltaMass: Average Mass: 541.
omega-N-(ADP-ribosyl)-L-arginine
A protein modification that effectively converts an L-argininine residue to omega-N-(ADP-ribosyl)-L-arginine.
DeltaMass:0
PubMed:15842200
PubMed:209022
PubMed:3090031
PubMed:3923473
PubMed:6582062
RESID:AA0168
Unimod:213#R
(S)-2-amino-5-([imino([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)methyl]amino)pentanoic acid
ADPRibArg
MOD_RES ADP-ribosylarginine
N(omega)-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-arginine
N(omega)-alpha-D-ribofuranosyl-L-arginine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
N-(ADP-ribosyl)- (on Arginine)
omega-N-(ADP-ribosyl)-L-arginine
ADP Ribose addition
ADP-Ribosyl
A protein modification that effectively converts an L-cysteine residue to S-(ADP-ribosyl)-L-cysteine.
541.3
C 15 H 21 N 5 O 13 P 2 S 0
541.0611
C 18 H 26 N 6 O 14 P 2 S 1
644.44
644.0703
C
natural
Unimod:213
uniprot.ptm:PTM-0055
(R)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]sulfanyl)propanoic acid
ADPRibCys
MOD_RES ADP-ribosylcysteine
S-(ADP-ribosyl)- (on Cysteine)
S-(ADP-ribosyl)-L-cysteine
S-L-cysteine alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
S-alpha-D-ribofuranosyl-L-cysteine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
PSI-MOD
ADP Ribose addition
ADP-Ribosyl
MOD:00178
From DeltaMass: Average Mass: 541.
S-(ADP-ribosyl)-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-(ADP-ribosyl)-L-cysteine.
DeltaMass:0
PubMed:15842200
PubMed:3863818
RESID:AA0169
Unimod:213#C
(R)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]sulfanyl)propanoic acid
ADPRibCys
MOD_RES ADP-ribosylcysteine
S-(ADP-ribosyl)- (on Cysteine)
S-(ADP-ribosyl)-L-cysteine
S-L-cysteine alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
S-alpha-D-ribofuranosyl-L-cysteine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
ADP Ribose addition
ADP-Ribosyl
A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-glycerylphosphorylethanolamine.
197.13
C 5 H 12 N 1 O 5 P 1
197.0453
C 10 H 19 N 2 O 8 P 1
326.24
326.0879
E
natural
Unimod:396
uniprot.ptm:PTM-0403
(S)-2-amino-5-[2-([([2,3-dihydroxypropyl]oxy)(hydroxy)phosphoryl]oxy)ethyl]amino-5-oxopentanoic acid
5-L-glutamyl glycerylphosphorylethanolamine
5GlyceroPEtAGlu
L-glutamyl 5-glycerophosphoethanolamine
L-glutamyl 5-glycerophosphorylethanolamine
L-glutamyl 5-glycerylphosphorylethanolamine
MOD_RES 5-glutamyl glycerylphosphorylethanolamine
PSI-MOD
GlycerylPE
glycerylphosphorylethanolamine
MOD:00179
glycerylPE
L-glutamyl 5-glycerylphosphorylethanolamine
A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-glycerylphosphorylethanolamine.
PubMed:2511205
PubMed:2569467
PubMed:9662537
RESID:AA0170
Unimod:396#E
(S)-2-amino-5-[2-([([2,3-dihydroxypropyl]oxy)(hydroxy)phosphoryl]oxy)ethyl]amino-5-oxopentanoic acid
5-L-glutamyl glycerylphosphorylethanolamine
5GlyceroPEtAGlu
L-glutamyl 5-glycerophosphoethanolamine
L-glutamyl 5-glycerophosphorylethanolamine
L-glutamyl 5-glycerylphosphorylethanolamine
MOD_RES 5-glutamyl glycerylphosphorylethanolamine
GlycerylPE
glycerylphosphorylethanolamine
A protein modification that effectively converts an L-cysteine residue to S-sulfo-L-cysteine.
80.06
C 0 H 0 N 0 O 3 S 1
79.95682
C 3 H 5 N 1 O 4 S 2
183.2
182.966
C
natural
Unimod:40
(2R)-2-amino-3-(sulfosulfanyl)propanoic acid
2-amino-3-(sulfothio)propanoic acid
3-(sulfosulfanyl)-L-alanine
S-sulfo-L-cysteine
S-sulfocysteine
SSulfCys
cysteine sulfate thioester
cysteine-S-sulfonic acid
PSI-MOD
O-Sulfonation
Sulfo
MOD:00180
S-sulfo-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-sulfo-L-cysteine.
PubMed:12876326
PubMed:14752058
PubMed:643076
RESID:AA0171
Unimod:40#C
(2R)-2-amino-3-(sulfosulfanyl)propanoic acid
2-amino-3-(sulfothio)propanoic acid
3-(sulfosulfanyl)-L-alanine
S-sulfo-L-cysteine
S-sulfocysteine
S-sulfocysteine
SSulfCys
cysteine sulfate thioester
cysteine-S-sulfonic acid
O-Sulfonation
Sulfo
A protein modification that effectively converts an L-tyrosine residue to O4'-sulfo-L-tyrosine.
80.06
C 0 H 0 N 0 O 3 S 1
79.95682
C 9 H 9 N 1 O 5 S 1
243.23
243.02014
Y
natural
Unimod:40
uniprot.ptm:PTM-0286
(S)-2-amino-3-(4-sulfooxyphenyl)propanoic acid
2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-sulfate
MOD_RES Sulfotyrosine
O4'-sulfo-L-tyrosine
O4-sulfotyrosine
OSulfTyr
Sulphation (of O of Tyrosine)
Tyrosinyl Sulphate
sulfationy
tyrosine sulfate
tyrosine-O-sulfonic acid
tyrosine-O-sulphonic acid
PSI-MOD
O-Sulfonation
Sulfo
MOD:00181
From DeltaMass: Average Mass: 80 Average Mass Change:80 PubMed:9624161.
O4'-sulfo-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to O4'-sulfo-L-tyrosine.
DeltaMass:88
OMSSA:114
PubMed:10226369
PubMed:14752058
PubMed:2303439
PubMed:3778455
PubMed:3801003
RESID:AA0172
Unimod:40#Y
(S)-2-amino-3-(4-sulfooxyphenyl)propanoic acid
2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-sulfate
MOD_RES Sulfotyrosine
O4'-sulfo-L-tyrosine
O4-sulfotyrosine
OSulfTyr
Sulphation (of O of Tyrosine)
Tyrosinyl Sulphate
sulfationy
tyrosine sulfate
tyrosine-O-sulfonic acid
tyrosine-O-sulphonic acid
O-Sulfonation
Sulfo
A protein modification that effectively converts an L-histidine residue to L-bromohistidine.
78.9
Br 1 C 0 H -1 N 0 O 0
77.910515
Br 1 C 6 H 6 N 3 O 1
216.04
214.96942
H
natural
Unimod:340
uniprot.ptm:PTM-0089
Br1His
L-bromohistidine
MOD_RES Bromohistidine
PSI-MOD
Bromo
bromination
MOD:00182
L-bromohistidine
A protein modification that effectively converts an L-histidine residue to L-bromohistidine.
PubMed:2076468
PubMed:9033387
RESID:AA0173
Unimod:340#H
Br1His
L-bromohistidine
MOD_RES Bromohistidine
Bromo
bromination
A protein modification that effectively converts an L-phenylalanine residue to L-2'-bromophenylalanine.
78.9
Br 1 C 0 H -1 N 0 O 0
77.910515
Br 1 C 9 H 8 N 1 O 1
226.07
224.97893
F
natural
(S)-2-amino-3-(2-bromophenyl)propanoic acid
2'BrPhe
L-2'-bromophenylalanine
L-o-bromination of Phe with 79Br
o-bromophenylalanine
ortho-bromophenylalanine
PSI-MOD
Bromo
bromination
MOD:00183
From DeltaMass: Average Mass: 78 Average Mass Change:78 References:Yoshino,K et.al. Biochemistry Vol. 30 pg 6203-9 (1991) Identifidation of a novel amino acid, o-bromo-L-phenylananine, in egg-associated peptides that activate spermatozoa.
L-2'-bromophenylalanine
A protein modification that effectively converts an L-phenylalanine residue to L-2'-bromophenylalanine.
DeltaMass:83
PubMed:2059627
PubMed:2076468
PubMed:9033387
RESID:AA0174
(S)-2-amino-3-(2-bromophenyl)propanoic acid
2'BrPhe
L-2'-bromophenylalanine
L-o-bromination of Phe with 79Br
o-bromophenylalanine
ortho-bromophenylalanine
Bromo
bromination
A protein modification that effectively converts an L-phenylalanine residue to L-3'-bromophenylalanine.
78.9
Br 1 C 0 H -1 N 0 O 0
77.910515
Br 1 C 9 H 8 N 1 O 1
226.07
224.97893
F
natural
(S)-2-amino-3-(3-bromophenyl)propanoic acid
3'BrPhe
L-3'-bromophenylalanine
m-bromophenylalanine
meta-bromophenylalanine
PSI-MOD
Bromo
bromination
MOD:00184
L-3'-bromophenylalanine
A protein modification that effectively converts an L-phenylalanine residue to L-3'-bromophenylalanine.
PubMed:2076468
PubMed:9033387
RESID:AA0175
(S)-2-amino-3-(3-bromophenyl)propanoic acid
3'BrPhe
L-3'-bromophenylalanine
m-bromophenylalanine
meta-bromophenylalanine
Bromo
bromination
A protein modification that effectively converts an L-phenylalanine residue to L-4'-bromophenylalanine.
78.9
Br 1 C 0 H -1 N 0 O 0
77.910515
Br 1 C 9 H 8 N 1 O 1
226.07
224.97893
F
natural
(2S)-2-amino-3-(4-bromophenyl)propanoic acid
4'BrPhe
L-4'-bromophenylalanine
p-bromophenylalanine
para-bromophenylalanine
PSI-MOD
Bromo
bromination
MOD:00185
L-4'-bromophenylalanine
A protein modification that effectively converts an L-phenylalanine residue to L-4'-bromophenylalanine.
PubMed:2076468
PubMed:9033387
RESID:AA0176
(2S)-2-amino-3-(4-bromophenyl)propanoic acid
4'BrPhe
L-4'-bromophenylalanine
p-bromophenylalanine
para-bromophenylalanine
Bromo
bromination
A protein modification that effectively substitutes an L-tyrosine residue with 3,3',5-triiodo-L-thyronine.
469.79
C 6 H 1 I 3 N 0 O 1
469.71616
C 15 H 10 I 3 N 1 O 3
632.96
632.7795
Y
natural
Unimod:397
uniprot.ptm:PTM-0295
(S)-2-amino-3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]propanoic acid
3',3'',5'-triiodo-L-thyronine
3,3',5-triiodo-L-thyronine
3,5,3'-Triiodothyronine (from Tyrosine)
3,5,3'-triiodo-L-thyronine
4-(4-hydroxy-3-iodophenoxy)-3,5-diiodo-L-phenylalanine
I3Thy
MOD_RES Triiodothyronine
O-(4-hydroxy-3-iodophenyl)-3,5-diiodo-L-tyrosine
T3
liothyronine
PSI-MOD
Triiodothyronine
triiodo
MOD:00186
From DeltaMass: Average Mass: 470.
3,3',5-triiodo-L-thyronine
A protein modification that effectively substitutes an L-tyrosine residue with 3,3',5-triiodo-L-thyronine.
ChEBI:18258
DeltaMass:0
RESID:AA0177
Unimod:397
(S)-2-amino-3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]propanoic acid
3',3'',5'-triiodo-L-thyronine
3,3',5-triiodo-L-thyronine
3,5,3'-Triiodothyronine (from Tyrosine)
3,5,3'-triiodo-L-thyronine
4-(4-hydroxy-3-iodophenoxy)-3,5-diiodo-L-phenylalanine
I3Thy
MOD_RES Triiodothyronine
O-(4-hydroxy-3-iodophenyl)-3,5-diiodo-L-tyrosine
T3
liothyronine
Triiodothyronine
triiodo
A protein modification that effectively substitutes an L-tyrosine residue with L-thyroxine.
595.68
C 6 H 0 I 4 N 0 O 1
595.6128
C 15 H 9 I 4 N 1 O 3
758.86
758.67615
Y
natural
Unimod:398
uniprot.ptm:PTM-0294
(S)-2-amino-3-[4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodophenyl]propanoic acid
3',3'',5',5''-tetraiodo-L-thyronine
3,3',5,5'-tetraiodo-L-thyronine
3,5,3',5'-tetraiodo-L-thyronine
4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodo-L-phenylalanine
I4Thy
L-thyroxine
MOD_RES Thyroxine
O-(4-hydroxy-3,5-diiodophenyl)-3,5-diiodo-L-tyrosine
T4
PSI-MOD
Thyroxine
tetraiodo
MOD:00187
L-thyroxine
A protein modification that effectively substitutes an L-tyrosine residue with L-thyroxine.
ChEBI:18332
PubMed:6704086
RESID:AA0178
Unimod:398
(S)-2-amino-3-[4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodophenyl]propanoic acid
3',3'',5',5''-tetraiodo-L-thyronine
3,3',5,5'-tetraiodo-L-thyronine
3,5,3',5'-tetraiodo-L-thyronine
4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodo-L-phenylalanine
I4Thy
L-thyroxine
MOD_RES Thyroxine
O-(4-hydroxy-3,5-diiodophenyl)-3,5-diiodo-L-tyrosine
T4
Thyroxine
tetraiodo
A protein modification that effectively converts an L-tryptophan residue to 6'-bromo-L-tryptophan.
78.9
Br 1 C 0 H -1 N 0 O 0
77.910515
Br 1 C 11 H 9 N 2 O 1
265.11
263.98984
W
natural
Unimod:398
uniprot.ptm:PTM-0051
(2S)-2-amino-3-(6-bromo-1H-indol-3-yl)propanoic acid
6'-BrTrp
6'-bromo-L-tryptophan
MOD_RES 6'-bromotryptophan
PSI-MOD
Bromo
bromination
MOD:00188
6'-bromo-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to 6'-bromo-L-tryptophan.
PubMed:12118011
PubMed:9030520
PubMed:9033387
PubMed:9434739
RESID:AA0179
Unimod:340#W
(2S)-2-amino-3-(6-bromo-1H-indol-3-yl)propanoic acid
6'-BrTrp
6'-bromo-L-tryptophan
MOD_RES 6'-bromotryptophan
Bromo
bromination
A protein modification that effectively converts an L-serine residue to dehydroalanine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 3 H 3 N 1 O 1
69.06
69.02146
S
natural
Unimod:23
uniprot.ptm:PTM-0006
2,3-didehydroalanine
2-aminoacrylic acid
2-aminopropenoic acid
4-methylidene-imidazole-5-one (MIO) active site
Dha
Dha(Ser)
MOD_RES 2,3-didehydroalanine (Ser)
anhydroserine
beta-elim-s
dehydro
dehydroalanine
phospholosss
PSI-MOD
Dehydrated
MOD:00189
dehydroalanine (Ser)
A protein modification that effectively converts an L-serine residue to dehydroalanine.
DeltaMass:0
OMSSA:140
OMSSA:164
OMSSA:96
PubMed:10220322
PubMed:1547888
PubMed:1815586
PubMed:2914619
PubMed:7947813
PubMed:8239649
RESID:AA0181#SER
Unimod:23#S
2,3-didehydroalanine
2-aminoacrylic acid
2-aminopropenoic acid
4-methylidene-imidazole-5-one (MIO) active site
Dha
Dha(Ser)
MOD_RES 2,3-didehydroalanine (Ser)
anhydroserine
beta-elim-s
dehydro
dehydroalanine
phospholosss
Dehydrated
A protein modification that effectively converts an L-threonine residue to dehydrobutyrine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 4 H 5 N 1 O 1
83.09
83.03712
T
natural
Unimod:23
uniprot.ptm:PTM-0007
(2Z)-2-aminobut-2-enoic acid
(Z)-2-amino-2-butenoic acid
(Z)-2-aminobutenoic acid
(Z)-dehydrobutyrine
2,3-didehydrobutyrine
3-methyldehydroalanine
Dehydroamino butyric acid
Dhb
Dhb(Thr)
MOD_RES 2,3-didehydrobutyrine
alpha,beta-dehydroaminobutyric acid
anhydrothreonine
beta-elim-t
dehydro
methyl-dehydroalanine
phospholosst
PSI-MOD
Dehydrated
Dehydration
MOD:00190
dehydrobutyrine (Thr)
A protein modification that effectively converts an L-threonine residue to dehydrobutyrine.
DeltaMass:0
OMSSA:141
OMSSA:164
OMSSA:97
PubMed:1547888
PubMed:3769923
RESID:AA0182
Unimod:23#T
(2Z)-2-aminobut-2-enoic acid
(Z)-2-amino-2-butenoic acid
(Z)-2-aminobutenoic acid
(Z)-dehydrobutyrine
2,3-didehydrobutyrine
3-methyldehydroalanine
Dehydroamino butyric acid
Dhb
Dhb(Thr)
MOD_RES 2,3-didehydrobutyrine
alpha,beta-dehydroaminobutyric acid
anhydrothreonine
beta-elim-t
dehydro
methyl-dehydroalanine
phospholosst
Dehydrated
Dehydrated
Dehydration
A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine.
-2.02
C 0 H -2 N 0 O 0
-2.01565
C 9 H 7 N 1 O 2
161.16
161.04768
Y
natural
uniprot.ptm:PTM-0002
(2Z)-2-amino-3-(4-hydroxyphenyl)prop-2-enoic acid
(Z)-2,3-didehydrogenated tyrosine
(Z)-2,3-didehydrotyrosine
MOD_RES (Z)-2,3-didehydrotyrosine
Z-dHTyr
amino-(para-hydroxybenzylidenyl)acetic acid
cis-dehydrotyrosine
green fluorescent protein chromophore
para-hydroxybenzylidene-imidazolidinone chromophore
red fluorescent protein chromophore
PSI-MOD
2-amino-3-oxo-butanoic_acid
Didehydro
MOD:00191
incidental to RESID:AA0184; incidental to RESID:AA0187; incidental to RESID:AA0188; incidental to RESID:AA0189; incidental to RESID:AA0378; incidental to RESID:AA0379; incidental to RESID:AA0380; incidental to RESID:AA0381
(Z)-2,3-didehydrotyrosine
A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine.
PubMed:1347277
PubMed:9631087
RESID:AA0183
(2Z)-2-amino-3-(4-hydroxyphenyl)prop-2-enoic acid
(Z)-2,3-didehydrogenated tyrosine
(Z)-2,3-didehydrotyrosine
MOD_RES (Z)-2,3-didehydrotyrosine
Z-dHTyr
amino-(para-hydroxybenzylidenyl)acetic acid
cis-dehydrotyrosine
green fluorescent protein chromophore
para-hydroxybenzylidene-imidazolidinone chromophore
red fluorescent protein chromophore
2-amino-3-oxo-butanoic_acid
Didehydro
A protein modification that effectively crosslinks an L-serine residue and a glycine residue to form L-serine 5-imidazolinone glycine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 5 H 6 N 2 O 2
126.11
126.04293
G, S
natural
uniprot.ptm:PTM-0049
(2-[(1R)-1-amino-2-hydroxyethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2-[1-amino-2-hydroxyethyl]-1-carboxymethyl-1-imidazolin-5-one
4-methylidene-imidazole-5-one (MIO) active site
CROSSLNK 5-imidazolinone (Ser-Gly)
L-serine 5-imidazolinone glycine
green fluorescent protein chromophore
para-hydroxybenzylidene-imidazolidinone chromophore
seryl-5-imidazolinone glycine
PSI-MOD
MOD:00192
Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365.
L-serine 5-imidazolinone glycine
A protein modification that effectively crosslinks an L-serine residue and a glycine residue to form L-serine 5-imidazolinone glycine.
ChEBI:21393
PubMed:1347277
PubMed:9631087
RESID:AA0184
(2-[(1R)-1-amino-2-hydroxyethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2-[1-amino-2-hydroxyethyl]-1-carboxymethyl-1-imidazolin-5-one
4-methylidene-imidazole-5-one (MIO) active site
CROSSLNK 5-imidazolinone (Ser-Gly)
L-serine 5-imidazolinone glycine
green fluorescent protein chromophore
para-hydroxybenzylidene-imidazolidinone chromophore
seryl-5-imidazolinone glycine
A protein modification that effectively converts an L-cysteine residue to L-oxoalanine.
-18.08
C 0 H -2 N 0 O 1 S -1
-17.992805
C 3 H 3 N 1 O 2
85.06
85.01638
C
natural
Unimod:402
uniprot.ptm:PTM-0034
(S)-2-amino-3-oxopropanoic acid
2-amino-3-oxopropionic acid
L-3-oxoalanine
L-amino-malonic acid semialdehyde
L-aminomalonaldehydic acid
MOD_RES 3-oxoalanine (Cys)
Oxala(Cys)
PSI-MOD
C(alpha)-formylglycine
L-serinesemialdehyde
MOD:00193
L-3-oxoalanine (Cys)
A protein modification that effectively converts an L-cysteine residue to L-oxoalanine.
DeltaMass:350
PubMed:14563551
PubMed:7628016
PubMed:8681943
PubMed:9478923
RESID:AA0185#CYS
Unimod:402#C
(S)-2-amino-3-oxopropanoic acid
2-amino-3-oxopropionic acid
L-3-oxoalanine
L-amino-malonic acid semialdehyde
L-aminomalonaldehydic acid
MOD_RES 3-oxoalanine (Cys)
Oxala(Cys)
C(alpha)-formylglycine
L-serinesemialdehyde
A protein modification that effectively converts an L-serine residue to an amino-terminal lactic acid.
-15.02
C 0 H -1 N -1 O 0
-15.010899
C 3 H 5 O 2
73.07
73.02895
S
N-term
Unimod:403
uniprot.ptm:PTM-0163
(2R)-2-hydroxypropanoic acid
2-hydroxypropionic acid
Lac(Ser)
MOD_RES Lactic acid
alpha-hydroxypropionic acid
lactic acid
PSI-MOD
Ser->LacticAcid
lactic acid from N-term Ser
MOD:00194
lactic acid
A protein modification that effectively converts an L-serine residue to an amino-terminal lactic acid.
PubMed:7607233
RESID:AA0186
Unimod:403#S
(2R)-2-hydroxypropanoic acid
2-hydroxypropionic acid
Lac(Ser)
MOD_RES Lactic acid
alpha-hydroxypropionic acid
lactic acid
Ser->LacticAcid
lactic acid from N-term Ser
A protein modification that effectively crosslinks an L-alanine residue and a glycine residue to form L-alanine 5-imidazolinone glycine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 5 H 6 N 2 O 1
110.12
110.04801
A, G
natural
uniprot.ptm:PTM-0045
(2-[(1S)-1-aminoethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2-[1-aminoethyl]-1-carboxymethyl-1-imidazolin-5-one
4-methylidene-imidazole-5-one active site
CROSSLNK 5-imidazolinone (Ala-Gly)
L-alanine 5-imidazolinone glycine
XLNK-1Ala-NGly(Imidazole)
alanyl-5-imidazolinone glycine
para-hydroxybenzylidene-imidazolidinone chromophore
PSI-MOD
MOD:00195
Cross-link 2; carboxamidine; incidental to RESID:AA0181; incidental to RESID:AA0183; incidental to RESID:AA0365.
L-alanine 5-imidazolinone glycine
A protein modification that effectively crosslinks an L-alanine residue and a glycine residue to form L-alanine 5-imidazolinone glycine.
PubMed:10220322
RESID:AA0187
(2-[(1S)-1-aminoethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2-[1-aminoethyl]-1-carboxymethyl-1-imidazolin-5-one
4-methylidene-imidazole-5-one active site
CROSSLNK 5-imidazolinone (Ala-Gly)
L-alanine 5-imidazolinone glycine
XLNK-1Ala-NGly(Imidazole)
alanyl-5-imidazolinone glycine
para-hydroxybenzylidene-imidazolidinone chromophore
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form L-cysteine 5-imidazolinone glycine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 5 H 6 N 2 O 1 S 1
142.18
142.02008
C, G
natural
uniprot.ptm:PTM-0047
(2-[(1R)-1-amino-2-sulfanylethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2-[1-amino-2-sulfanylethyl]-1-carboxymethyl-1-imidazolin-5-one
4-methylidene-imidazole-5-one (MIO) active site
CROSSLNK 5-imidazolinone (Cys-Gly)
L-cysteine 5-imidazolinone glycine
XLNK-1Cys-NGly(Imidazole)
cysteinyl-5-imidazolinone glycine
para-hydroxybenzylidene-imidazolidinone chromophore
PSI-MOD
MOD:00196
Cross-link 2; carboxamidine; incidental to RESID:AA0181; incidental to RESID:AA0183; incidental to RESID:AA0365.
L-cysteine 5-imidazolinone glycine
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form L-cysteine 5-imidazolinone glycine.
PubMed:1537807
RESID:AA0188
(2-[(1R)-1-amino-2-sulfanylethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2-[1-amino-2-sulfanylethyl]-1-carboxymethyl-1-imidazolin-5-one
4-methylidene-imidazole-5-one (MIO) active site
CROSSLNK 5-imidazolinone (Cys-Gly)
L-cysteine 5-imidazolinone glycine
XLNK-1Cys-NGly(Imidazole)
cysteinyl-5-imidazolinone glycine
para-hydroxybenzylidene-imidazolidinone chromophore
A protein modification that effectively crosslinks an L-glutamine residue and a glycine residue to form 2-imino-glutamine 5-imidazolinone glycine.
-20.03
C 0 H -4 N 0 O -1
-20.026215
C 7 H 7 N 3 O 2
165.15
165.05383
G, Q
natural
uniprot.ptm:PTM-0013
2,N-didehydroglutaminyl-5-imidazolinone glycine
2-(3-carbamoyl-1-imino-propyl)-1-carboxymethyl-1-imidazolin-5-one
2-imino-glutamine 5-imidazolinone glycine
CROSSLNK 2-iminomethyl-5-imidazolinone (Gln-Gly)
[2-(3-carbamoyl-1-imino-propyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
[2-(4-amino-4-oxobutanimidoyl)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid
fluorescent protein FP583 chromophore
para-hydroxybenzylidene-imidazolidinone chromophore
red fluorescent protein chromophore
PSI-MOD
MOD:00197
Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365.
2-imino-glutamine 5-imidazolinone glycine
A protein modification that effectively crosslinks an L-glutamine residue and a glycine residue to form 2-imino-glutamine 5-imidazolinone glycine.
PubMed:11050230
PubMed:11209050
RESID:AA0189
2,N-didehydroglutaminyl-5-imidazolinone glycine
2-(3-carbamoyl-1-imino-propyl)-1-carboxymethyl-1-imidazolin-5-one
2-imino-glutamine 5-imidazolinone glycine
CROSSLNK 2-iminomethyl-5-imidazolinone (Gln-Gly)
[2-(3-carbamoyl-1-imino-propyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
[2-(4-amino-4-oxobutanimidoyl)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid
fluorescent protein FP583 chromophore
para-hydroxybenzylidene-imidazolidinone chromophore
red fluorescent protein chromophore
A protein modification that effectively converts an L-alanine residue to D-alanine.
0.0
C 0 H 0 N 0 O 0
0.0
C 3 H 5 N 1 O 1
71.08
71.03712
A
natural
uniprot.ptm:PTM-0112
(R)-2-aminopropanoic acid
D-Ala(Ala)
D-alanine
MOD_RES D-alanine (Ala)
PSI-MOD
MOD:00198
D-alanine (Ala)
A protein modification that effectively converts an L-alanine residue to D-alanine.
PubMed:15023056
PubMed:7287302
PubMed:7961627
RESID:AA0191#ALA
(R)-2-aminopropanoic acid
D-Ala(Ala)
D-alanine
MOD_RES D-alanine (Ala)
A protein modification that effectively converts an L-isoleucine residue to a D-allo-isoleucine.
0.0
C 0 H 0 N 0 O 0
0.0
C 6 H 11 N 1 O 1
113.16
113.08406
I
natural
uniprot.ptm:PTM-0114
(2R,3S)-2-amino-3-methylpentanoic acid
2-azanyl-3-methylpentanoic acid
3-methyl-norvaline
D-Ile
D-allo-isoleucine
D-threo-isoleucine
MOD_RES D-allo-isoleucine
allo-D-isoleucine
alpha-amino-beta-methylvaleric acid
PSI-MOD
MOD:00199
D-allo-isoleucine
A protein modification that effectively converts an L-isoleucine residue to a D-allo-isoleucine.
ChEBI:30007
PubMed:8223491
RESID:AA0192
(2R,3S)-2-amino-3-methylpentanoic acid
2-azanyl-3-methylpentanoic acid
3-methyl-norvaline
D-Ile
D-allo-isoleucine
D-threo-isoleucine
MOD_RES D-allo-isoleucine
allo-D-isoleucine
alpha-amino-beta-methylvaleric acid
A protein modification that effectively converts an L-methionine residue to D-methionine.
0.0
C 0 H 0 N 0 O 0 S 0
0.0
C 5 H 9 N 1 O 1 S 1
131.19
131.04048
M
natural
uniprot.ptm:PTM-0120
(2R)-2-amino-4-(methylsulfanyl)butanoic acid
2-amino-4-(methylthio)butanoic acid
2-amino-4-(methylthio)butyric acid
D-Met
D-methionine
MOD_RES D-methionine
PSI-MOD
MOD:00200
D-methionine
A protein modification that effectively converts an L-methionine residue to D-methionine.
ChEBI:29984
PubMed:16033333
PubMed:2542051
RESID:AA0193
(2R)-2-amino-4-(methylsulfanyl)butanoic acid
2-amino-4-(methylthio)butanoic acid
2-amino-4-(methylthio)butyric acid
D-Met
D-methionine
MOD_RES D-methionine
A protein modification that effectively converts an L-phenylalanine residue to D-phenylalanine.
0.0
C 0 H 0 N 0 O 0
0.0
C 9 H 9 N 1 O 1
147.18
147.06842
F
natural
uniprot.ptm:PTM-0121
(R)-2-amino-3-phenylpropanoic acid
D-Phe
D-phenylalanine
MOD_RES D-phenylalanine
PSI-MOD
MOD:00201
D-phenylalanine
A protein modification that effectively converts an L-phenylalanine residue to D-phenylalanine.
ChEBI:29996
PubMed:1548227
PubMed:1644179
PubMed:2597281
RESID:AA0194
(R)-2-amino-3-phenylpropanoic acid
D-Phe
D-phenylalanine
MOD_RES D-phenylalanine
A protein modification that effectively converts an L-serine residue to D-serine.
0.0
C 0 H 0 N 0 O 0
0.0
C 3 H 5 N 1 O 2
87.08
87.03203
S
natural
uniprot.ptm:PTM-0308
(R)-2-amino-3-hydroxypropanoic acid
D-Ser(Ser)
D-serine
MOD_RES D-serine (Ser)
PSI-MOD
MOD:00202
D-serine (Ser)
A protein modification that effectively converts an L-serine residue to D-serine.
PubMed:7973665
RESID:AA0195#SER
(R)-2-amino-3-hydroxypropanoic acid
D-Ser(Ser)
D-serine
MOD_RES D-serine (Ser)
A protein modification that effectively converts an L-asparagine residue to D-asparagine.
0.0
C 0 H 0 N 0 O 0
0.0
C 4 H 6 N 2 O 2
114.1
114.04293
N
natural
uniprot.ptm:PTM-0115
(R)-2-amino-4-butanediamic acid
D-Asn
D-alpha-aminosuccinamic acid
D-asparagine
D-aspartic acid beta-amide
MOD_RES D-asparagine
PSI-MOD
MOD:00203
D-asparagine
A protein modification that effectively converts an L-asparagine residue to D-asparagine.
ChEBI:29957
PubMed:1859408
RESID:AA0196
(R)-2-amino-4-butanediamic acid
D-Asn
D-alpha-aminosuccinamic acid
D-asparagine
D-aspartic acid beta-amide
MOD_RES D-asparagine
A protein modification that effectively converts an L-leucine residue to D-leucine.
0.0
C 0 H 0 N 0 O 0
0.0
C 6 H 11 N 1 O 1
113.16
113.08406
L
natural
uniprot.ptm:PTM-0119
(2R)-2-amino-4-methylpentanoic acid
D-Leu
D-leucine
MOD_RES D-leucine
alpha-aminoisocaproic acid
PSI-MOD
MOD:00204
D-leucine
A protein modification that effectively converts an L-leucine residue to D-leucine.
ChEBI:30005
PubMed:10461743
PubMed:12135762
PubMed:1358533
PubMed:1548227
RESID:AA0197
(2R)-2-amino-4-methylpentanoic acid
D-Leu
D-leucine
MOD_RES D-leucine
alpha-aminoisocaproic acid
A protein modification that effectively converts an L-tryptophan residue to D-tryptophan.
0.0
C 0 H 0 N 0 O 0
0.0
C 11 H 10 N 2 O 1
186.21
186.07932
W
natural
uniprot.ptm:PTM-0123
(R)-2-amino-3-(1H-indol-3-yl)propanoic acid
D-Trp
D-tryptophan
MOD_RES D-tryptophan
alpha-amino-beta-(3-indolyl)propionoic acid
PSI-MOD
MOD:00205
D-tryptophan
A protein modification that effectively converts an L-tryptophan residue to D-tryptophan.
ChEBI:29955
PubMed:8910408
RESID:AA0198
(R)-2-amino-3-(1H-indol-3-yl)propanoic acid
D-Trp
D-tryptophan
MOD_RES D-tryptophan
alpha-amino-beta-(3-indolyl)propionoic acid
A protein modification that effectively converts an L-glutamic acid residue to L-isoglutamyl-polyglycine.
E
natural
uniprot.ptm:PTM-0394
L-isoglutamyl-polyglycine
MOD_RES 5-glutamyl polyglycine
gamma-glutamylpolyglycine
PSI-MOD
MOD:00206
L-isoglutamyl-polyglycine
A protein modification that effectively converts an L-glutamic acid residue to L-isoglutamyl-polyglycine.
ChEBI:21343
PubMed:10074368
PubMed:16368691
PubMed:7992051
RESID:AA0201
L-isoglutamyl-polyglycine
MOD_RES 5-glutamyl polyglycine
gamma-glutamylpolyglycine
A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl-polyglutamic acid, forming an isopeptide bond with a polyglutamic acid.
E
natural
uniprot.ptm:PTM-0395
L-isoglutamyl-polyglutamic acid
gamma-glutamylpolyglutamic acid
PSI-MOD
MOD:00207
L-isoglutamyl-polyglutamic acid
A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl-polyglutamic acid, forming an isopeptide bond with a polyglutamic acid.
PubMed:10747868
PubMed:1680872
RESID:AA0202
L-isoglutamyl-polyglutamic acid
gamma-glutamylpolyglutamic acid
A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphoadenosine through a phosphodiester bond to form O4'-(phospho-5'-adenosine)-L-tyrosine.
329.21
C 10 H 12 N 5 O 6 P 1
329.05252
C 19 H 21 N 6 O 8 P 1
492.38
492.11584
Y
natural
Unimod:405
uniprot.ptm:PTM-0332
(2S)-2-amino-3-[4-(5'-adenosine phosphonoxy)phenyl]propanoic acid
5'-adenylic-O-tyrosine
MOD_RES O-AMP-tyrosine
O-5'-Adenosylation ( of Tyrosine)
O4'-(phospho-5'-adenosine)-L-tyrosine
O4'-L-tyrosine 5'-adenosine phosphodiester
OAMPTyr
hydrogen 5'-adenylate tyrosine ester
PSI-MOD
AMP binding site
Phosphoadenosine
MOD:00208
From DeltaMass: Average Mass: 329.
O4'-(phospho-5'-adenosine)-L-tyrosine
A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphoadenosine through a phosphodiester bond to form O4'-(phospho-5'-adenosine)-L-tyrosine.
DeltaMass:0
PubMed:5543675
RESID:AA0203
Unimod:405#Y
(2S)-2-amino-3-[4-(5'-adenosine phosphonoxy)phenyl]propanoic acid
5'-adenylic-O-tyrosine
MOD_RES O-AMP-tyrosine
O-5'-Adenosylation ( of Tyrosine)
O4'-(phospho-5'-adenosine)-L-tyrosine
O4'-L-tyrosine 5'-adenosine phosphodiester
OAMPTyr
hydrogen 5'-adenylate tyrosine ester
AMP binding site
Phosphoadenosine
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-D-cysteine.
-64.04
C -1 H -4 N 0 O -3 S 0
-64.016045
C 5 H 7 N 2 O 1 S 1
143.18
143.02791
C, S
C-term
uniprot.ptm:PTM-0268
(2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid
(S,Z)-S-(2-aminovinyl)cysteine
CROSSLNK S-(2-aminovinyl)-D-cysteine (Ser-Cys)
S-(2-aminovinyl)-D-cysteine
XLNK-(D)SCys-VinAm
PSI-MOD
MOD:00209
Cross-link 2.
S-(2-aminovinyl)-D-cysteine (Cys-Ser)
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-D-cysteine.
PubMed:3181159
PubMed:3769923
RESID:AA0204#SER
(2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid
(S,Z)-S-(2-aminovinyl)cysteine
CROSSLNK S-(2-aminovinyl)-D-cysteine (Ser-Cys)
S-(2-aminovinyl)-D-cysteine
XLNK-(D)SCys-VinAm
A protein modification that effectively monooxygenates an L-cysteine residue to L-cysteine sulfenic acid.
16.0
C 0 H 0 N 0 O 1 S 0
15.994915
C 3 H 5 N 1 O 2 S 1
119.14
119.0041
C
natural
Unimod:35
uniprot.ptm:PTM-0107
(2R)-2-amino-3-(hydroxysulfanyl)propanoic acid
(2R)-2-amino-3-(oxido-lambda(4)-sulfanyl)propanoic acid [tautomer]
2-amino-2-carboxyethanesulfenic acid
2-amino-3-sulfinylpropanoic acid [tautomer]
3-sulfenoalanine
ACT_SITE Cysteine sulfenic acid (-SOH) intermediate
CysOH
L-cysteine sulfenic acid
MOD_RES Cysteine sulfenic acid (-SOH)
S-hydroxycysteine
S-oxocysteine [tautomer]
S-oxycysteine [tautomer]
Sulfenic Acid (from Cysteine)
cysteine S-oxide [tautomer]
cysteine sulfoxide [tautomer]
cysteine sulphenic acid
mod193
PSI-MOD
Oxidation
MOD:00210
From DeltaMass: Average Mass: 16 Average Mass Change:16 Notes:Green et al. in J. B. C. 270, 18209-18211 (1995) quote Kim and Raines in Eur. J. Biochem. 224, 109-114 (1994). Kim and Raines using ESI-MS and sulfhydryl group titration found that bovine seminal ribonuclease contains a single oxidized sulfhydryl group, which cannot participate in a disulfide bond. This form of cysteine is called sulfenic acid (-SOH).
L-cysteine sulfenic acid
A protein modification that effectively monooxygenates an L-cysteine residue to L-cysteine sulfenic acid.
DeltaMass:41
OMSSA:193
PubMed:10964927
PubMed:2501303
PubMed:8756456
PubMed:9214307
PubMed:9586994
PubMed:9587003
RESID:AA0205
Unimod:35#C
(2R)-2-amino-3-(hydroxysulfanyl)propanoic acid
(2R)-2-amino-3-(oxido-lambda(4)-sulfanyl)propanoic acid [tautomer]
2-amino-2-carboxyethanesulfenic acid
2-amino-3-sulfinylpropanoic acid [tautomer]
3-sulfenoalanine
ACT_SITE Cysteine sulfenic acid (-SOH) intermediate
CysOH
L-cysteine sulfenic acid
MOD_RES Cysteine sulfenic acid (-SOH)
S-hydroxycysteine
S-oxocysteine [tautomer]
S-oxycysteine [tautomer]
Sulfenic Acid (from Cysteine)
cysteine S-oxide [tautomer]
cysteine sulfoxide [tautomer]
cysteine sulphenic acid
mod193
Oxidation
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a thioester bond to form S-glycyl-L-cysteine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 5 H 7 N 2 O 2 S 1
159.18
159.02283
C, G
C-term
uniprot.ptm:PTM-0429
(2R)-2-amino-3-[(aminoacetyl)sulfanyl]propanoic acid
1-(cystein-S-yl)-glycinate
ACT_SITE Glycyl thioester intermediate
S-(2-amino-1-oxoethyl)cysteine
S-(glycyl)-L-cysteine
XLNK-SCys-1Gly
glycine cysteine thioester
PSI-MOD
MOD:00211
Cross-link 2. For the modification of a C-terminal glycine by formation of a thioester bond with free L-cysteine see MOD:01777 [JSG].
S-(glycyl)-L-cysteine (Cys-Gly)
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a thioester bond to form S-glycyl-L-cysteine.
ChEBI:22050
PubMed:3306404
RESID:AA0206
(2R)-2-amino-3-[(aminoacetyl)sulfanyl]propanoic acid
1-(cystein-S-yl)-glycinate
ACT_SITE Glycyl thioester intermediate
S-(2-amino-1-oxoethyl)cysteine
S-(glycyl)-L-cysteine
XLNK-SCys-1Gly
glycine cysteine thioester
A protein modification that effectively converts an L-cysteine residue to S-4-hydroxycinnamyl-L-cysteine.
146.14
C 9 H 6 N 0 O 2 S 0
146.03677
C 12 H 11 N 1 O 3 S 1
249.28
249.04596
C
natural
Unimod:407
uniprot.ptm:PTM-0414
(2R)-2-amino-3-([(2E)-3-(4-hydroxyphenyl)prop-2-enoyl]sulfanyl)propanoic acid
MOD_RES S-(4-hydroxycinnamyl)cysteine
S-4-hydroxycinnamyl-L-cysteine
S-para-coumaryl-L-cysteine
cinnamate cysteine thioester
PSI-MOD
Hydroxycinnamyl
hydroxycinnamyl
MOD:00212
S-4-hydroxycinnamyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-4-hydroxycinnamyl-L-cysteine.
PubMed:7947803
PubMed:7981196
RESID:AA0207
Unimod:407
(2R)-2-amino-3-([(2E)-3-(4-hydroxyphenyl)prop-2-enoyl]sulfanyl)propanoic acid
MOD_RES S-(4-hydroxycinnamyl)cysteine
S-4-hydroxycinnamyl-L-cysteine
S-para-coumaryl-L-cysteine
cinnamate cysteine thioester
Hydroxycinnamyl
hydroxycinnamyl
A protein modification that effectively cross-links an L-serine residue to the polymer chondroitin sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide.
S
natural
chondroitin 4-sulfate (chondroitin sulfate A)
chondroitin 6-sulfate (chondroitin sulfate C)
chondroitin sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine
poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate-D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine; poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-6-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine
PSI-MOD
MOD:00213
chondroitin sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine
A protein modification that effectively cross-links an L-serine residue to the polymer chondroitin sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide.
PubMed:1794445
PubMed:1898736
PubMed:3472204
RESID:AA0208
chondroitin 4-sulfate (chondroitin sulfate A)
chondroitin 6-sulfate (chondroitin sulfate C)
chondroitin sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine
poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate-D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine; poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-6-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine
A protein modification that effectively cross-links an L-serine residue to the polymer dermatan 4-sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide.
S
natural
beta-heparin
chondroitin sulfate B
dermatan 4-sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine
poly[beta-1,4-L-idopyranuronosyl-alpha-1,3-(2-acetamido-2-deoxy-4-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine
PSI-MOD
MOD:00214
dermatan 4-sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine
A protein modification that effectively cross-links an L-serine residue to the polymer dermatan 4-sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide.
PubMed:2914936
PubMed:3472204
RESID:AA0209
beta-heparin
chondroitin sulfate B
dermatan 4-sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine
poly[beta-1,4-L-idopyranuronosyl-alpha-1,3-(2-acetamido-2-deoxy-4-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine
A protein modification that effectively cross-links an L-serine residue to the polymer heparan sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide.
S
natural
heparan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine
heparin
heparitin sulfate
poly[alpha-1,4-(2-sulfate D-glucopyranuronosyl)-beta-1,4-(2-sulfamino-2-deoxy-6-sulfate D-glucosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine
PSI-MOD
MOD:00215
heparan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine
A protein modification that effectively cross-links an L-serine residue to the polymer heparan sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide.
PubMed:3472204
RESID:AA0210
heparan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine
heparin
heparitin sulfate
poly[alpha-1,4-(2-sulfate D-glucopyranuronosyl)-beta-1,4-(2-sulfamino-2-deoxy-6-sulfate D-glucosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-serine
A protein modification that effectively converts an L-lysine residue to N6-formyl-L-lysine.
28.01
C 1 H 0 N 0 O 1
27.994915
C 7 H 12 N 2 O 2
156.19
156.08987
K
natural
Unimod:122
uniprot.ptm:PTM-0192
(2S)-2-amino-6-(formylamino)hexanoic acid
MOD_RES N6-formyllysine
N(zeta)-formyllysine
N6-formyl-L-lysine
N6-formylated L-lysine
N6FoLys
epsilon-formyllysine
formylk
PSI-MOD
Formyl
Formylation
MOD:00216
N6-formyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-formyl-L-lysine.
OMSSA:43
PubMed:15799070
RESID:AA0211
Unimod:122#K
(2S)-2-amino-6-(formylamino)hexanoic acid
MOD_RES N6-formyllysine
N(zeta)-formyllysine
N6-formyl-L-lysine
N6-formylated L-lysine
N6FoLys
epsilon-formyllysine
formylk
Formyl
Formylation
A protein modification that effectively converts an L-proline residue to O4-arabinosyl-L-hydroxyproline.
148.11
C 5 H 8 N 0 O 5
148.03717
C 10 H 15 N 1 O 6
245.23
245.08994
P
natural
Unimod:408
uniprot.ptm:PTM-0545
(2S,4R)-4-(beta-L-arabinofuranosyloxy)pyrrolidine-2-carboxylic acid
4-(beta-L-arabinofuranosyloxy)proline
4-Glycosyloxy- (pentosyl,C5) (of Proline)
O4-arabinosyl-L-hydroxyproline
O4-glycosyl-hydroxyproline
OAra4HyPro
beta-arabinofuranosyl-4-hydroxyproline
PSI-MOD
Glycosyl
glycosyl-L-hydroxyproline
MOD:00217
secondary to RESID:AA0030; From DeltaMass: Average Mass: 147.
O4-arabinosyl-L-hydroxyproline
A protein modification that effectively converts an L-proline residue to O4-arabinosyl-L-hydroxyproline.
DeltaMass:0
PubMed:666730
PubMed:7852316
RESID:AA0212
Unimod:408
(2S,4R)-4-(beta-L-arabinofuranosyloxy)pyrrolidine-2-carboxylic acid
4-(beta-L-arabinofuranosyloxy)proline
4-Glycosyloxy- (pentosyl,C5) (of Proline)
O4-arabinosyl-L-hydroxyproline
O4-glycosyl-hydroxyproline
OAra4HyPro
beta-arabinofuranosyl-4-hydroxyproline
Glycosyl
glycosyl-L-hydroxyproline
A protein modification that effectively crosslinks an L-serine residue and the 5'-end of RNA through a phosphodiester to form O4'-(phospho-5'-RNA)-L-serine.
S
natural
uniprot.ptm:PTM-0227
(S)-2-amino-3-(5'-ribonucleic acid phosphonoxy)propanoic acid
MOD_RES O-(5'-phospho-RNA)-serine
O-(phospho-5'-RNA)-L-serine
O3-(phospho-5'-RNA)-L-serine
O3-L-serine 5'-RNA phosphodiester
PSI-MOD
MOD:00218
O-(phospho-5'-RNA)-L-serine
A protein modification that effectively crosslinks an L-serine residue and the 5'-end of RNA through a phosphodiester to form O4'-(phospho-5'-RNA)-L-serine.
PubMed:1705009
RESID:AA0213
(S)-2-amino-3-(5'-ribonucleic acid phosphonoxy)propanoic acid
MOD_RES O-(5'-phospho-RNA)-serine
O-(phospho-5'-RNA)-L-serine
O3-(phospho-5'-RNA)-L-serine
O3-L-serine 5'-RNA phosphodiester
A protein modification that effectively converts an L-arginine residue to L-citrulline.
0.98
C 0 H -1 N -1 O 1
0.984016
C 6 H 11 N 3 O 2
157.17
157.08513
R
natural
Unimod:7
uniprot.ptm:PTM-0092
(S)-2-amino-5-(carbamoylamino)pentanoic acid
2-amino-5-(aminocarbonyl)aminopentanoic acid
Cit
Citrulline
L-citrulline
MOD_RES Citrulline
N5-(aminocarbonyl)ornithine
N5-carbamoylornithine
N5-carbamylornithine
alpha-amino-delta-ureidovaleric acid
citrullinationr
delta-ureidonorvaline
PSI-MOD
Deamidated
Deamidation
MOD:00219
This modification is not the result of deamidation, instead the guanidino group is replaced with an ureido group.
L-citrulline
A protein modification that effectively converts an L-arginine residue to L-citrulline.
DeltaMass:0
OMSSA:33
PubMed:2466844
RESID:AA0214
Unimod:7#R
(S)-2-amino-5-(carbamoylamino)pentanoic acid
2-amino-5-(aminocarbonyl)aminopentanoic acid
Cit
Citrulline
L-citrulline
MOD_RES Citrulline
N5-(aminocarbonyl)ornithine
N5-carbamoylornithine
N5-carbamylornithine
alpha-amino-delta-ureidovaleric acid
citrullinationr
delta-ureidonorvaline
Deamidated
Deamidated
Deamidation
A protein modification that effectively converts an L-arginine residue to a 4-hydroxy-L-arginine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 6 H 12 N 4 O 2
172.19
172.09602
R
natural
uniprot.ptm:PTM-0042
(2S,4Xi)-2-amino-5-[(diaminomethylidene)amino]-4-hydroxypentanoic acid
2-amino-5-(carbamimidamido)-4-hydroxypentanoic acid [tautomer]
2-amino-5-[(aminoiminomethyl)amino]-4-hydroxypentanoic acid [tautomer]
2-amino-5-guanidino-4-hydroxypentanoic acid
4-hydroxy-L-arginine
4-hydroxylated L-arginine
4HyArg
C(gamma)-hydroxyarginine
MOD_RES 4-hydroxyarginine
gamma-hydroxyarginine
PSI-MOD
MOD:00220
4-hydroxy-L-arginine
A protein modification that effectively converts an L-arginine residue to a 4-hydroxy-L-arginine.
PubMed:10966817
PubMed:7650037
RESID:AA0215
(2S,4Xi)-2-amino-5-[(diaminomethylidene)amino]-4-hydroxypentanoic acid
2-amino-5-(carbamimidamido)-4-hydroxypentanoic acid [tautomer]
2-amino-5-[(aminoiminomethyl)amino]-4-hydroxypentanoic acid [tautomer]
2-amino-5-guanidino-4-hydroxypentanoic acid
4-hydroxy-L-arginine
4-hydroxylated L-arginine
4HyArg
C(gamma)-hydroxyarginine
MOD_RES 4-hydroxyarginine
gamma-hydroxyarginine
A protein modification that effectively crosslinks L-aspartic acid and L-cysteine residues via an isopeptide bond to form N-(L-isoaspartyl)-L-cysteine.
-17.03
C 0 H -3 N -1 O 0 S 0
-17.026548
C 7 H 9 N 2 O 3 S 1
201.22
201.03339
C, N
natural
N-term
uniprot.ptm:PTM-0151
(S)-2-amino-4-((R)-1-carboxy-2-sulfanylethyl)amino-4-oxobutanoic acid
2-(3-amino-3-carboxypropanoyl)amino-3-mercaptopropanoic acid
2-amino-N4-(1-carboxy-2-mercaptoethyl)butanediamic acid
CROSSLNK Isoaspartyl cysteine isopeptide (Cys-Asn)
N-(L-isoaspartyl)-L-cysteine
N-beta-aspartylcysteine
N-isoaspartyl cysteine
PSI-MOD
MOD:00221
Cross-link 2.
N-(L-isoaspartyl)-L-cysteine
A protein modification that effectively crosslinks L-aspartic acid and L-cysteine residues via an isopeptide bond to form N-(L-isoaspartyl)-L-cysteine.
PubMed:8286361
RESID:AA0216
(S)-2-amino-4-((R)-1-carboxy-2-sulfanylethyl)amino-4-oxobutanoic acid
2-(3-amino-3-carboxypropanoyl)amino-3-mercaptopropanoic acid
2-amino-N4-(1-carboxy-2-mercaptoethyl)butanediamic acid
CROSSLNK Isoaspartyl cysteine isopeptide (Cys-Asn)
N-(L-isoaspartyl)-L-cysteine
N-beta-aspartylcysteine
N-isoaspartyl cysteine
A protein modification that effectively converts an L-tryptophan residue to 2'-alpha-mannosyl-L-tryptophan.
162.14
C 6 H 10 N 0 O 5
162.05283
C 17 H 20 N 2 O 6
348.36
348.13214
W
natural
Unimod:41
uniprot.ptm:PTM-0505
(2S)-2-amino-3-(2-beta-D-mannopyranosyl-1H-indol-3-yl)propanoic acid
2'-mannosyl-L-tryptophan
2'-tryptophan C-mannoside
C2'ManTrp
CARBOHYD C-linked (Man) tryptophan
PSI-MOD
Hex
Hexose
MOD:00222
2'-alpha-mannosyl-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to 2'-alpha-mannosyl-L-tryptophan.
PubMed:15279557
PubMed:7547911
PubMed:7947762
RESID:AA0217
Unimod:41#W
(2S)-2-amino-3-(2-beta-D-mannopyranosyl-1H-indol-3-yl)propanoic acid
2'-mannosyl-L-tryptophan
2'-tryptophan C-mannoside
C2'ManTrp
CARBOHYD C-linked (Man) tryptophan
Hex
Hexose
A protein modification that effectively converts an L-lysine residue to N6-mureinyl-L-lysine.
K
natural
uniprot.ptm:PTM-0195
MOD_RES N6-murein peptidoglycan lysine
N6-[(2R,6S)-2-(N-(N-mureinyl-(R)-alanyl)-(S)-glutamyl)amino-6-amino-6-carboxy-1-oxohex-1-yl]lysine
N6-mureinyl-L-lysine
PSI-MOD
MOD:00223
N6-mureinyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-mureinyl-L-lysine.
PubMed:4261992
RESID:AA0218
MOD_RES N6-murein peptidoglycan lysine
N6-[(2R,6S)-2-(N-(N-mureinyl-(R)-alanyl)-(S)-glutamyl)amino-6-amino-6-carboxy-1-oxohex-1-yl]lysine
N6-mureinyl-L-lysine
A protein modification that effectively converts an L-aspartic acid residue to 1-chondroitin sulfate-L-aspartic acid ester
D
C-term
uniprot.ptm:PTM-0334
1-aspartic acid ester with 6-chondroitin 4-sulfate
1-chondroitin sulfate-L-aspartic acid ester
MOD_RES Aspartate 1-(chondroitin 4-sulfate)-ester
poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate D-galactosyl)]beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate-6-(1-L-aspartyl)-D-galactose)
protein-glycosaminoglycan-protein cross-link
PSI-MOD
MOD:00224
1-chondroitin sulfate-L-aspartic acid ester
A protein modification that effectively converts an L-aspartic acid residue to 1-chondroitin sulfate-L-aspartic acid ester
PubMed:1898736
RESID:AA0219
1-aspartic acid ester with 6-chondroitin 4-sulfate
1-chondroitin sulfate-L-aspartic acid ester
MOD_RES Aspartate 1-(chondroitin 4-sulfate)-ester
poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate D-galactosyl)]beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetamido-2-deoxy-4-sulfate-6-(1-L-aspartyl)-D-galactose)
protein-glycosaminoglycan-protein cross-link
A protein modification that effectively converts an L-cysteine residue to S-(6-FMN)-L-cysteine.
454.33
C 17 H 19 N 4 O 9 P 1 S 0
454.08896
C 20 H 24 N 5 O 10 P 1 S 1
557.47
557.09814
C
natural
Unimod:409
uniprot.ptm:PTM-0271
(R)-2-amino-3-[6-riboflavin 5'-dihydrogen phosphate]sulfanylpropanoic acid
6-[S-cysteinyl]FMN
6-[S-cysteinyl]flavin mononucleotide
MOD_RES S-6-FMN cysteine
S-(6-FMN)-L-cysteine
S6FMNCys
PSI-MOD
FMNH
flavin mononucleotide
MOD:00225
S-(6-FMN)-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-(6-FMN)-L-cysteine.
PubMed:10869173
PubMed:1551870
PubMed:620783
RESID:AA0220
Unimod:409#C
(R)-2-amino-3-[6-riboflavin 5'-dihydrogen phosphate]sulfanylpropanoic acid
6-[S-cysteinyl]FMN
6-[S-cysteinyl]flavin mononucleotide
MOD_RES S-6-FMN cysteine
S-(6-FMN)-L-cysteine
S6FMNCys
FMNH
flavin mononucleotide
A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FAD)-L-histidine.
783.54
C 27 H 31 N 9 O 15 P 2
783.1415
C 33 H 38 N 12 O 16 P 2
920.68
920.2004
H
natural
Unimod:50
uniprot.ptm:PTM-0288
(S)-2-amino-3-(1-[8alpha riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid
1'-(8alpha-FAD)-L-histidine
8alpha-(N(epsilon)-histidyl)FAD
8alpha-(N1'-histidyl)FAD
MOD_RES Tele-8alpha-FAD histidine
N theta and N pi-(8alpha-Flavin) (on Histidine)
N(tau)-(8alpha-FAD)-histidine
Nt8aFADHis
tele-(8alpha-FAD)-histidine
PSI-MOD
8alpha-N3-histidyl FAD
FAD
Flavin adenine dinucleotide
MOD:00226
From DeltaMass: Average Mass: 784
1'-(8alpha-FAD)-L-histidine
A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FAD)-L-histidine.
DeltaMass:0
PubMed:10585424
PubMed:1396672
PubMed:4339951
PubMed:9261083
RESID:AA0221
Unimod:50#H
(S)-2-amino-3-(1-[8alpha riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid
1'-(8alpha-FAD)-L-histidine
8alpha-(N(epsilon)-histidyl)FAD
8alpha-(N1'-histidyl)FAD
MOD_RES Tele-8alpha-FAD histidine
N theta and N pi-(8alpha-Flavin) (on Histidine)
N(tau)-(8alpha-FAD)-histidine
Nt8aFADHis
tele-(8alpha-FAD)-histidine
8alpha-N3-histidyl FAD
FAD
Flavin adenine dinucleotide
A protein modification that effectively converts an L-arginine residue to omega-N-phospho-L-arginine.
79.98
C 0 H 1 N 0 O 3 P 1
79.96633
C 6 H 13 N 4 O 4 P 1
236.17
236.06744
R
natural
Unimod:21
uniprot.ptm:PTM-0250
(2S)-2-amino-5-(N'-phosphonocarbamimidamido)pentanoic acid
(2S)-2-amino-5-([amino(phosphonoamino)methylidene]amino)pentanoic acid
MOD_RES Phosphoarginine
N(gamma)-phosphoarginine
N(omega)-phosphono-L-arginine
N5-[imino(phosphonoamino)methyl]-L-ornithine
PArg
alpha-amino-delta-phosphonoguanidinovaleric acid
omega-N-phospho-L-arginine
phosphoarginine
PSI-MOD
Phospho
Phosphorylation
MOD:00227
omega-N-phospho-L-arginine
A protein modification that effectively converts an L-arginine residue to omega-N-phospho-L-arginine.
PubMed:8300603
RESID:AA0222
Unimod:21#R
(2S)-2-amino-5-(N'-phosphonocarbamimidamido)pentanoic acid
(2S)-2-amino-5-([amino(phosphonoamino)methylidene]amino)pentanoic acid
MOD_RES Phosphoarginine
N(gamma)-phosphoarginine
N(omega)-phosphono-L-arginine
N5-[imino(phosphonoamino)methyl]-L-ornithine
PArg
alpha-amino-delta-phosphonoguanidinovaleric acid
omega-N-phospho-L-arginine
phosphoarginine
Phospho
Phosphorylation
A protein modification that effectively converts an L-cysteine residue to S-diphytanylglycerol diether-L-cysteine.
635.16
C 43 H 86 N 0 O 2 S 0
634.6628
C 46 H 91 N 1 O 3 S 1
738.3
737.672
C
natural
Unimod:410
uniprot.ptm:PTM-0273
(2R)-2-amino-3-([(2S)-2,3-bis(3,7,11,15-tetramethylhexadecanyloxy)propyl]sulfanyl)propanoic acid
LIPID S-archaeol cysteine
S-(diphytanylglyceryl)-L-cysteine
S-[2',3'-bis(phytanyloxy)propyl]cysteine
S-archaeol cysteine
SPhyt2GlyceroCys
PSI-MOD
Archaeol
S-diphytanylglycerol diether
MOD:00228
incidental to RESID:AA0043.
S-diphytanylglycerol diether-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-diphytanylglycerol diether-L-cysteine.
PubMed:7797461
PubMed:8195126
RESID:AA0223
Unimod:410
(2R)-2-amino-3-([(2S)-2,3-bis(3,7,11,15-tetramethylhexadecanyloxy)propyl]sulfanyl)propanoic acid
LIPID S-archaeol cysteine
S-(diphytanylglyceryl)-L-cysteine
S-[2',3'-bis(phytanyloxy)propyl]cysteine
S-archaeol cysteine
SPhyt2GlyceroCys
Archaeol
S-diphytanylglycerol diether
A protein modification that effectively converts two L-cysteine residues to form alpha-1-microglobulin-Ig alpha complex chromophore.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 6 H 8 N 2 O 2 S 2
204.26
204.00272
C, C
natural
BINDING Multimeric 3-hydroxykynurenine chromophore (covalent)
alpha-1-microglobulin-Ig alpha complex chromophore
PSI-MOD
MOD:00229
Cross-link 2.
alpha-1-microglobulin-Ig alpha complex chromophore
A protein modification that effectively converts two L-cysteine residues to form alpha-1-microglobulin-Ig alpha complex chromophore.
PubMed:11058759
PubMed:11877257
PubMed:7506257
PubMed:7535251
RESID:AA0224
BINDING Multimeric 3-hydroxykynurenine chromophore (covalent)
alpha-1-microglobulin-Ig alpha complex chromophore
A protein modification that effectively converts two L-cysteine residues, two L-histidine residues and a two-iron two-sulfur cluster to bis-L-cysteinyl bis-L-histidino diiron disulfide.
171.78
C 0 Fe 2 H -4 N 0 O 0 S 2
171.78381
2-
C 18 Fe 2 H 20 N 8 O 4 S 4
652.34
651.92
C, C, H, H
natural
METAL Iron-sulfur (2Fe-2S)
METAL Iron-sulfur (2Fe-2S); via pros nitrogen
Rieske iron-sulfur cofactor
bis-L-cysteinyl bis-L-histidino diiron disulfide
di-mu-sulfido(bis-S-cysteinyliron)(bis-N3'-histidinoiron)
PSI-MOD
MOD:00230
Cross-link 4.
bis-L-cysteinyl bis-L-histidino diiron disulfide
A protein modification that effectively converts two L-cysteine residues, two L-histidine residues and a two-iron two-sulfur cluster to bis-L-cysteinyl bis-L-histidino diiron disulfide.
PubMed:2765515
PubMed:9651245
RESID:AA0225
METAL Iron-sulfur (2Fe-2S)
METAL Iron-sulfur (2Fe-2S); via pros nitrogen
Rieske iron-sulfur cofactor
bis-L-cysteinyl bis-L-histidino diiron disulfide
di-mu-sulfido(bis-S-cysteinyliron)(bis-N3'-histidinoiron)
A protein modification that effectively converts six L-cysteine residues and a six-iron six-sulfur cluster to hexakis-L-cysteinyl hexairon hexasulfide.
521.38
C 0 Fe 6 H -6 N 0 O 0 S 6
521.3956
1-
C 18 Fe 6 H 24 N 6 O 6 S 12
1140.22
1139.4508
C, C, C, C, C, C
hypothetical
hexa-mu3-sulfido-hexakis(S-cysteinyliron)
hexa-mu3-sulfido-hexakis(cysteinato-kappaS)-hexairon
hexakis-L-cysteinyl hexairon hexasulfide
prismane iron-sulfur cofactor
PSI-MOD
MOD:00231
Cross-link 6. This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
hexakis-L-cysteinyl hexairon hexasulfide
A protein modification that effectively converts six L-cysteine residues and a six-iron six-sulfur cluster to hexakis-L-cysteinyl hexairon hexasulfide.
PubMed:1311311
PubMed:1318833
RESID:AA0226
hexa-mu3-sulfido-hexakis(S-cysteinyliron)
hexa-mu3-sulfido-hexakis(cysteinato-kappaS)-hexairon
hexakis-L-cysteinyl hexairon hexasulfide
prismane iron-sulfur cofactor
A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form N6-(phospho-5'-adenosine)-L-lysine.
329.21
C 10 H 12 N 5 O 6 P 1
329.05252
C 16 H 24 N 7 O 7 P 1
457.38
457.1475
K
natural
Unimod:405
(2S)-2-amino-6-(5'-adenosine phosphonamino)hexanoic acid
5'-adenylic-N6-L-lysine
ACT_SITE N6-AMP-lysine intermediate
AMP Lysyl
L-lysine monoanhydride with 5'-adenylic acid
N(zeta)-5'-adenylic-L-lysine
N6-(phospho-5'-adenosine)-L-lysine
N6-L-lysine 5'-adenosine phosphoramidester
N6AMPLys
epsilon-5'-adenylic-L-lysine
PSI-MOD
AMP binding site
Phosphoadenosine
MOD:00232
N6-(phospho-5'-adenosine)-L-lysine
A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form N6-(phospho-5'-adenosine)-L-lysine.
DeltaMass:316
PubMed:3882425
PubMed:4944632
RESID:AA0227
Unimod:405#K
(2S)-2-amino-6-(5'-adenosine phosphonamino)hexanoic acid
5'-adenylic-N6-L-lysine
ACT_SITE N6-AMP-lysine intermediate
AMP Lysyl
L-lysine monoanhydride with 5'-adenylic acid
N(zeta)-5'-adenylic-L-lysine
N6-(phospho-5'-adenosine)-L-lysine
N6-L-lysine 5'-adenosine phosphoramidester
N6AMPLys
epsilon-5'-adenylic-L-lysine
AMP binding site
Phosphoadenosine
A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoguanosine through a phosphoramide ester bond to form N6-(phospho-5'-guanosine)-L-lysine.
345.21
C 10 H 12 N 5 O 7 P 1
345.04742
C 16 H 24 N 7 O 8 P 1
473.38
473.1424
K
natural
Unimod:413
(2S)-2-amino-6-(5'-guanosine phosphonamino)hexanoic acid
5'-guanylic-N6-L-lysine
5'phos Guanosyl
ACT_SITE N6-GMP-lysine intermediate
L-lysine monoanhydride with 5'-guanylic acid
N(zeta)-5'-guanylic-lysine
N6-(5'-guanylyl)-lysine
N6-(phospho-5'-guanosine)-L-lysine
N6-L-lysine 5'-guanosine phosphoramidester
N6GMPLys
epsilon-5'-guanylic-L-lysine
lysine guanosine-5'-monophosphate
PSI-MOD
Phosphoguanosine
phospho-guanosine
MOD:00233
From DeltaMass: Average Mass: 345 Formula:C10H12O5N7P1 Monoisotopic Mass Change:345.047 Average Mass Change:345.209 References:PE Sciex
N6-(phospho-5'-guanosine)-L-lysine
A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoguanosine through a phosphoramide ester bond to form N6-(phospho-5'-guanosine)-L-lysine.
DeltaMass:304
PubMed:6092377
PubMed:6264433
RESID:AA0228
Unimod:413#K
(2S)-2-amino-6-(5'-guanosine phosphonamino)hexanoic acid
5'-guanylic-N6-L-lysine
5'phos Guanosyl
ACT_SITE N6-GMP-lysine intermediate
L-lysine monoanhydride with 5'-guanylic acid
N(zeta)-5'-guanylic-lysine
N6-(5'-guanylyl)-lysine
N6-(phospho-5'-guanosine)-L-lysine
N6-L-lysine 5'-guanosine phosphoramidester
N6GMPLys
epsilon-5'-guanylic-L-lysine
lysine guanosine-5'-monophosphate
Phosphoguanosine
phospho-guanosine
A protein modification that effectively converts an L-cysteine residue to S-glutathionyl-L-cysteine.
305.3
C 10 H 15 N 3 O 6 S 1
305.06815
C 13 H 20 N 4 O 7 S 2
408.44
408.07733
C
natural
Unimod:55
uniprot.ptm:PTM-0311
(2S)-2-amino-3-((2S)-2-((4R)-4-amino-4-carboxyl-1-oxobutyl)amino-3-(carboxylmethyl)amino-3-oxo-propyl)dithio-propanoic acid
Glutathionation
L-cysteine glutathione disulfide
L-gamma-glutamyl-L-cysteinyl-glycine (2-1')-disulfide with L-cysteine
MOD_RES S-glutathionyl cysteine
N-(N-gamma-glutamyl-cystinyl)-glycine
SGltCys
cysteinyl glutathione
glutathionec
PSI-MOD
Glutathione
glutathione disulfide
MOD:00234
From DeltaMass: Average Mass: 305
Glutamyl-transpeptidase cleaves glutathione into cysteinylglycine (Cys-Gly) and a Glu residue. [PubMed: 28537416]
L-cysteine glutathione disulfide
A protein modification that effectively converts an L-cysteine residue to S-glutathionyl-L-cysteine.
ChEBI:21264
DeltaMass:0
OMSSA:51
PubMed:3083866
PubMed:8344916
RESID:AA0229
Unimod:55
(2S)-2-amino-3-((2S)-2-((4R)-4-amino-4-carboxyl-1-oxobutyl)amino-3-(carboxylmethyl)amino-3-oxo-propyl)dithio-propanoic acid
Glutathionation
L-cysteine glutathione disulfide
L-gamma-glutamyl-L-cysteinyl-glycine (2-1')-disulfide with L-cysteine
MOD_RES S-glutathionyl cysteine
N-(N-gamma-glutamyl-cystinyl)-glycine
SGltCys
cysteinyl glutathione
glutathionec
Glutathione
glutathione disulfide
A protein modification that effectively converts an L-cysteine residue to S-nitrosyl-L-cysteine.
29.0
C 0 H -1 N 1 O 1 S 0
28.990164
C 3 H 4 N 2 O 2 S 1
132.14
131.99934
C
natural
Unimod:275
uniprot.ptm:PTM-0280
(2R)-2-amino-3-nitrososulfanyl-propanoic acid
L-cysteine nitrite ester
MOD_RES S-nitrosocysteine
S-nitrosocysteine
S-nitrosyl-L-cysteine
SNOCys
PSI-MOD
Nitrosyl
S-nitrosylation
MOD:00235
S-nitrosyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-nitrosyl-L-cysteine.
PubMed:10442087
PubMed:11562475
PubMed:15688001
PubMed:8626764
PubMed:8637569
RESID:AA0230
Unimod:275
(2R)-2-amino-3-nitrososulfanyl-propanoic acid
L-cysteine nitrite ester
MOD_RES S-nitrosocysteine
S-nitrosocysteine
S-nitrosyl-L-cysteine
SNOCys
Nitrosyl
S-nitrosylation
A protein modification that effectively converts an L-asparagine residue to N4-(ADP-ribosyl)-L-asparagine.
541.3
C 15 H 21 N 5 O 13 P 2
541.0611
C 19 H 27 N 7 O 15 P 2
655.41
655.10406
N
natural
Unimod:213
uniprot.ptm:PTM-0054
(S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-4-oxobutanoic acid
MOD_RES ADP-ribosylasparagine
N4-(ADP-ribosyl)-L-asparagine
N4-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-asparagine
N4-alpha-D-ribofuranosyl-L-asparagine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
PSI-MOD
ADP Ribose addition
ADP-Ribosyl
MOD:00236
N4-(ADP-ribosyl)-L-asparagine
A protein modification that effectively converts an L-asparagine residue to N4-(ADP-ribosyl)-L-asparagine.
PubMed:15842200
PubMed:2498316
RESID:AA0231
Unimod:213#N
(S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-4-oxobutanoic acid
MOD_RES ADP-ribosylasparagine
N4-(ADP-ribosyl)-L-asparagine
N4-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-asparagine
N4-alpha-D-ribofuranosyl-L-asparagine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
ADP Ribose addition
ADP-Ribosyl
A protein modification that effectively converts an L-aspartic acid residue to L-beta-methylthioaspartic acid.
46.09
C 1 H 2 N 0 O 0 S 1
45.98772
C 5 H 7 N 1 O 3 S 1
161.18
161.01466
D
natural
Unimod:39
uniprot.ptm:PTM-0032
(2R,3Xi)-2-amino-3-(methylsulfanyl)butanedioic acid
3-(methylthio)-L-aspartic acid
3-carboxy-S-methyl-cysteine
3-methylthio-aspartic acid
3MeSAsp
MOD_RES 3-methylthioaspartic acid
beta-Methylthio-aspartic acid
beta-methylthio-aspartic acid
bmethylthiold
methythiold
PSI-MOD
Beta-methylthiolation
Methylthio
MOD:00237
L-beta-methylthioaspartic acid
A protein modification that effectively converts an L-aspartic acid residue to L-beta-methylthioaspartic acid.
ChEBI:73599
DeltaMass:61
OMSSA:13
OMSSA:26
PubMed:15473684
PubMed:8844851
RESID:AA0232
Unimod:39#D
(2R,3Xi)-2-amino-3-(methylsulfanyl)butanedioic acid
3-(methylthio)-L-aspartic acid
3-carboxy-S-methyl-cysteine
3-methylthio-aspartic acid
3MeSAsp
MOD_RES 3-methylthioaspartic acid
beta-Methylthio-aspartic acid
beta-methylthio-aspartic acid
bmethylthiold
methythiold
Beta-methylthiolation
Methylthio
A protein modification that effectively cross-links an L-lysine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 5'-(N6-L-lysine)-L-topaquinone.
11.97
C 0 H -4 N 0 O 1
11.963614
C 15 H 17 N 3 O 4
303.32
303.12192
K, Y
natural
uniprot.ptm:PTM-0171
1-[(S)-5-amino-5-carboxypentyl]amino-2-[(S)-2-amino-2-carboxyethyl]-2,6-cyclohexadien-4,5-dione
2'-(L-lys-N6-yl)-L-4',5'-topaquinone
2'-(L-lysine)-L-tyrosyl-4',5'-quinone
CROSSLNK Lysine tyrosylquinone (Lys-Tyr)
CROSSLNK Lysine tyrosylquinone (Tyr-Lys)
LTQ
lysyl oxidase cofactor
PSI-MOD
MOD:00238
Cross-link 2; secondary to RESID:AA0147.
5'-(N6-L-lysine)-L-topaquinone
A protein modification that effectively cross-links an L-lysine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 5'-(N6-L-lysine)-L-topaquinone.
PubMed:8688089
RESID:AA0233
1-[(S)-5-amino-5-carboxypentyl]amino-2-[(S)-2-amino-2-carboxyethyl]-2,6-cyclohexadien-4,5-dione
2'-(L-lys-N6-yl)-L-4',5'-topaquinone
2'-(L-lysine)-L-tyrosyl-4',5'-quinone
CROSSLNK Lysine tyrosylquinone (Lys-Tyr)
CROSSLNK Lysine tyrosylquinone (Tyr-Lys)
LTQ
lysyl oxidase cofactor
A protein modification that effectively converts an L-cysteine residue to S-methyl-L-cysteine.
14.03
C 1 H 2 N 0 O 0 S 0
14.01565
C 4 H 7 N 1 O 1 S 1
117.17
117.02483
C
natural
Unimod:34
uniprot.ptm:PTM-0636
(R)-2-amino-3-(methylsulfanyl)propanoic acid
ACT_SITE S-methylcysteine intermediate
L-3-(methylthio)alanine
MOD_RES S-methylcysteine
S-methyl-L-cysteine
S-methylated L-cysteine
SMeCys
PSI-MOD
Methyl
Methylation
MOD:00239
S-methyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-methyl-L-cysteine.
PubMed:10660523
PubMed:11875433
PubMed:1339288
RESID:AA0234
Unimod:34#C
(R)-2-amino-3-(methylsulfanyl)propanoic acid
ACT_SITE S-methylcysteine intermediate
L-3-(methylthio)alanine
MOD_RES S-methylcysteine
S-methyl-L-cysteine
S-methylated L-cysteine
SMeCys
Methyl
Methylation
A protein modification that effectively converts an L-lysine residue to 4-hydroxy-L-lysine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 6 H 12 N 2 O 2
144.17
144.08987
K
artifact
uniprot.ptm:PTM-0664
(2S,4R)-2,6-diamino-4-hydroxyhexanoic acid
4-hydroxy-L-lysine
4-hydroxylated L-lysine
4HyLys
L-threo-gamma-hydroxylysine
MOD_RES 4-hydroxylysine
alpha,epsilon-diamino-gamma-hydroxycaproic acid
PSI-MOD
MOD:00240
This modification was not structurally confirmed. Later 5-hydroxy-L-lysine was found at a homologous position in the same protein from closely related species. This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
4-hydroxy-L-lysine
A protein modification that effectively converts an L-lysine residue to 4-hydroxy-L-lysine.
ChEBI:141495
PubMed:4005040
RESID:AA0235
(2S,4R)-2,6-diamino-4-hydroxyhexanoic acid
4-hydroxy-L-lysine
4-hydroxylated L-lysine
4HyLys
L-threo-gamma-hydroxylysine
MOD_RES 4-hydroxylysine
alpha,epsilon-diamino-gamma-hydroxycaproic acid
A protein modification that effectively converts an L-asparagine residue to N4-hydroxymethyl-L-asparagine.
30.03
C 1 H 2 N 0 O 1
30.010565
C 5 H 8 N 2 O 3
144.13
144.0535
N
artifact
Unimod:414
(2S)-2-amino-4-[(hydroxymethyl)amino]-4-oxobutanoic acid
2-amino-N4-hydroxymethylbutanediamic acid
N(gamma)-hydroxymethylasparagine
N4-hydroxymethyl-L-asparagine
N4-hydroxymethylasparagine
beta-hydroxymethylasparagine
PSI-MOD
Hydroxymethyl
hydroxymethyl
MOD:00241
N4-methyl-L-asparagine, see MOD:0079, was found at a homologous position of the same protein in a closely related species. Since the peptide containing this modification was obtained by enzymatic cleavage, not cyanogen bromide cleavage, it could have experienced oxidation of the following methionine residue, leading to the erroneous attribution of a mass of 29 for the modification rather than 14. comment: This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
N4-hydroxymethyl-L-asparagine
A protein modification that effectively converts an L-asparagine residue to N4-hydroxymethyl-L-asparagine.
RESID:AA0236
Unimod:414
(2S)-2-amino-4-[(hydroxymethyl)amino]-4-oxobutanoic acid
2-amino-N4-hydroxymethylbutanediamic acid
N(gamma)-hydroxymethylasparagine
N4-hydroxymethyl-L-asparagine
N4-hydroxymethylasparagine
beta-hydroxymethylasparagine
Hydroxymethyl
hydroxymethyl
A protein modification that effectively converts an L-serine residue to O-(ADP-ribosyl)-L-serine.
541.3
C 15 H 21 N 5 O 13 P 2
541.0611
C 18 H 26 N 6 O 15 P 2
628.38
628.09314
S
natural
Unimod:213
uniprot.ptm:PTM-0056
(S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-propanoic acid
MOD_RES ADP-ribosylserine
O-(ADP-ribosyl)-L-serine
O3-(ADP-ribosyl)-L-serine
O3-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-serine
O3-alpha-D-ribofuranosyl-L-serine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
OADPRibSer
PSI-MOD
ADP Ribose addition
ADP-Ribosyl
MOD:00242
O-(ADP-ribosyl)-L-serine
A protein modification that effectively converts an L-serine residue to O-(ADP-ribosyl)-L-serine.
PubMed:15842200
PubMed:3141412
RESID:AA0237
Unimod:213#S
(S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-propanoic acid
MOD_RES ADP-ribosylserine
O-(ADP-ribosyl)-L-serine
O3-(ADP-ribosyl)-L-serine
O3-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-serine
O3-alpha-D-ribofuranosyl-L-serine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
OADPRibSer
ADP Ribose addition
ADP-Ribosyl
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 6 H 6 N 2 O 2 S 1
170.19
170.015
C, S
natural
uniprot.ptm:PTM-0376
2-(1-azanyl-2-sulfanylethyl)-4-oxazolecarboxylic acid
2-[(1R)-1-amino-2-sulfanylethyl]-1,3-oxazole-4-carboxylic acid
CROSSLNK Oxazole-4-carboxylic acid (Cys-Ser)
L-cysteine oxazole-4-carboxylic acid
PSI-MOD
MOD:00243
Cross-link 2.
L-cysteine oxazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid.
PubMed:8183941
PubMed:8895467
RESID:AA0238
2-(1-azanyl-2-sulfanylethyl)-4-oxazolecarboxylic acid
2-[(1R)-1-amino-2-sulfanylethyl]-1,3-oxazole-4-carboxylic acid
CROSSLNK Oxazole-4-carboxylic acid (Cys-Ser)
L-cysteine oxazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazoline-4-carboxylic acid.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 6 H 8 N 2 O 2 S 1
172.2
172.03065
C, S
natural
uniprot.ptm:PTM-0381
(4S)-2-[(1R)-1-amino-2-sulfanylethyl]-4,5-dihydro-1,3-oxazole-4-carboxylic acid
2-[1-azanyl-2-sulfanylethyl]-4,5-dihydro-1,3-oxazole-4-carboxylic acid
CROSSLNK Oxazoline-4-carboxylic acid (Cys-Ser)
L-cysteine oxazoline-4-carboxylic acid
PSI-MOD
MOD:00244
Cross-link 2.
L-cysteine oxazoline-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazoline-4-carboxylic acid.
PubMed:1880060
RESID:AA0239
(4S)-2-[(1R)-1-amino-2-sulfanylethyl]-4,5-dihydro-1,3-oxazole-4-carboxylic acid
2-[1-azanyl-2-sulfanylethyl]-4,5-dihydro-1,3-oxazole-4-carboxylic acid
CROSSLNK Oxazoline-4-carboxylic acid (Cys-Ser)
L-cysteine oxazoline-4-carboxylic acid
A protein modification that effectively crosslinks a glycine residue and an L-serine residue to form glycine oxazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1
-20.026215
C 5 H 4 N 2 O 2
124.1
124.027275
G, S
natural
uniprot.ptm:PTM-0377
2-aminomethyl-1,3-oxazole-4-carboxylic acid
2-azanylmethyl-1,3-oxazole-4-carboxylic acid
CROSSLNK Oxazole-4-carboxylic acid (Gly-Ser)
glycine oxazole-4-carboxylic acid
PSI-MOD
MOD:00245
Cross-link 2.
glycine oxazole-4-carboxylic acid
A protein modification that effectively crosslinks a glycine residue and an L-serine residue to form glycine oxazole-4-carboxylic acid.
PubMed:8183941
PubMed:8895467
RESID:AA0240
2-aminomethyl-1,3-oxazole-4-carboxylic acid
2-azanylmethyl-1,3-oxazole-4-carboxylic acid
CROSSLNK Oxazole-4-carboxylic acid (Gly-Ser)
glycine oxazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form glycine thiazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 5 H 4 N 2 O 1 S 1
140.16
140.00444
C, G
natural
uniprot.ptm:PTM-0378
2-(aminomethyl)-1,3-thiazole-4-carboxylic acid
2-(azanylmethyl)-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Gly-Cys)
glycine thiazole-4-carboxylic acid
PSI-MOD
MOD:00246
Cross-link 2.
glycine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form glycine thiazole-4-carboxylic acid.
ChEBI:21276
PubMed:8183941
PubMed:8895467
RESID:AA0241
2-(aminomethyl)-1,3-thiazole-4-carboxylic acid
2-(azanylmethyl)-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Gly-Cys)
glycine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-serine thiazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 6 H 6 N 2 O 2 S 1
170.19
170.015
C, S
natural
uniprot.ptm:PTM-0363
2-[(1S)-1-amino-2-hydroxyethyl]-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-hydroxyethyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Ser-Cys)
L-serine thiazole-4-carboxylic acid
PSI-MOD
MOD:00247
Cross-link 2.
L-serine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-serine thiazole-4-carboxylic acid.
PubMed:8183941
PubMed:8895467
RESID:AA0242
2-[(1S)-1-amino-2-hydroxyethyl]-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-hydroxyethyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Ser-Cys)
L-serine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 12 H 10 N 2 O 1 S 1
230.29
230.05139
C, F
natural
uniprot.ptm:PTM-0375
2-[(1S)-1-amino-2-phenylethyl]-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-phenylethyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Phe-Cys)
L-phenylalanine thiazole-4-carboxylic acid
PSI-MOD
MOD:00248
Cross-link 2.
L-phenylalanine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazole-4-carboxylic acid.
PubMed:1880060
RESID:AA0243
2-[(1S)-1-amino-2-phenylethyl]-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-phenylethyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Phe-Cys)
L-phenylalanine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks two L-cysteine residues to form L-cysteine thiazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 6 H 6 N 2 O 1 S 2
186.25
185.99216
C, C
natural
uniprot.ptm:PTM-0360
2-[(1S)-1-amino-2-sulfanylethyl]-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-sulfanylethyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Cys-Cys)
L-cysteine thiazole-4-carboxylic acid
PSI-MOD
MOD:00249
Cross-link 2.
L-cysteine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks two L-cysteine residues to form L-cysteine thiazole-4-carboxylic acid.
PubMed:1880060
RESID:AA0244
2-[(1S)-1-amino-2-sulfanylethyl]-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-sulfanylethyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Cys-Cys)
L-cysteine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to form L-lysine thiazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 9 H 13 N 3 O 1 S 1
211.28
211.07793
C, K
hypothetical
2-[(1S)-1,5-diaminopentyl]-1,3-thiazole-4-carboxylic acid
2-[1,5-bis(azanyl)pentyl]-1,3-thiazole-4-carboxylic acid
L-lysine thiazole-4-carboxylic acid
PSI-MOD
MOD:00250
Cross-link 2. Lysine is now thought not to be encoded in the peptide sequence modified to produce GE2270. See RESID:AA0470. This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
L-lysine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to form L-lysine thiazole-4-carboxylic acid.
PubMed:1880060
RESID:AA0245
2-[(1S)-1,5-diaminopentyl]-1,3-thiazole-4-carboxylic acid
2-[1,5-bis(azanyl)pentyl]-1,3-thiazole-4-carboxylic acid
L-lysine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-serine residue and the 5'-end of DNA through a phosphodiester bond to form O-(phospho-5'-DNA)-L-serine.
S
natural
uniprot.ptm:PTM-0226
(S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)propanoic acid
ACT_SITE O-(5'-phospho-DNA)-serine intermediate
MOD_RES O-(5'-phospho-DNA)-serine
O-(phospho-5'-DNA)-L-serine
O3-(phospho-5'-DNA)-L-serine
O3-L-serine 5'-DNA phosphodiester
PSI-MOD
MOD:00251
O-(phospho-5'-DNA)-L-serine
A protein modification that effectively crosslinks an L-serine residue and the 5'-end of DNA through a phosphodiester bond to form O-(phospho-5'-DNA)-L-serine.
PubMed:7142163
PubMed:7265205
RESID:AA0246
(S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)propanoic acid
ACT_SITE O-(5'-phospho-DNA)-serine intermediate
MOD_RES O-(5'-phospho-DNA)-serine
O-(phospho-5'-DNA)-L-serine
O3-(phospho-5'-DNA)-L-serine
O3-L-serine 5'-DNA phosphodiester
A protein modification that effectively cross-links an L-threonine residue to the polymer keratan sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide.
T
natural
keratan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-threonine
keratosulfate
poly[beta-1,4-(2-acetamido-2-deoxy-6-sulfate D-glucosyl)-beta-1,3-D-galactosyl]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-threonine
PSI-MOD
MOD:00252
keratan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-threonine
A protein modification that effectively cross-links an L-threonine residue to the polymer keratan sulfate by a D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl tetrasaccharide.
PubMed:1417734
PubMed:3472204
RESID:AA0247
keratan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-threonine
keratosulfate
poly[beta-1,4-(2-acetamido-2-deoxy-6-sulfate D-glucosyl)-beta-1,3-D-galactosyl]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-threonine
A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide).
1572.02
C 40 H 47 Mo 1 N 20 O 26 P 4 S 4 Se 0
1572.9857
C 43 H 52 Mo 1 N 21 O 27 P 4 S 4 Se 1
1722.07
1723.9395
U
natural
Unimod:415
PSI-MOD
MOD:00253
L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (Sec)
A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide).
PubMed:14235557
PubMed:2211698
PubMed:8052647
PubMed:9036855
RESID:AA0248#SEC
Unimod:415
A protein modification that effectively crosslinks an L-tyrosine residue and the 5'-end of RNA through a phosphodiester to form O4'-(phospho-5'-RNA)-L-tyrosine.
Y
natural
uniprot.ptm:PTM-0229
(S)-2-amino-3-[4-(5'-ribonucleic acid phosphonoxy)phenyl]propanoic acid
MOD_RES O-(5'-phospho-RNA)-tyrosine
O4'-(phospho-5'-RNA)-L-tyrosine
O4'-L-tyrosine 5'-RNA phosphodiester
PSI-MOD
MOD:00254
O4'-(phospho-5'-RNA)-L-tyrosine
A protein modification that effectively crosslinks an L-tyrosine residue and the 5'-end of RNA through a phosphodiester to form O4'-(phospho-5'-RNA)-L-tyrosine.
PubMed:1702164
PubMed:209034
PubMed:217003
PubMed:6264310
RESID:AA0249
(S)-2-amino-3-[4-(5'-ribonucleic acid phosphonoxy)phenyl]propanoic acid
MOD_RES O-(5'-phospho-RNA)-tyrosine
O4'-(phospho-5'-RNA)-L-tyrosine
O4'-L-tyrosine 5'-RNA phosphodiester
A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3-(3'-L-histidyl)-L-tyrosine.
-2.02
C 0 H -2 N 0 O 0
-2.01565
C 15 H 14 N 4 O 3
298.3
298.1066
H, Y
natural
uniprot.ptm:PTM-0027
(2S,3R)-2-amino-3-(5-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)-3-(4-hydroxyphenyl)propanoic acid
3-(3'-L-histidyl)-L-tyrosine
3-(N3'-histidyl)tyrosine
3-(pi-histidyl)tyrosine
3-(pros-histidyl)tyrosine
CROSSLNK 3'-histidyl-3-tyrosine (His-Tyr)
beta-(N(delta)-histidyl)tyrosine
beta-(N3'-histidyl)tyrosine
PSI-MOD
MOD:00255
Cross-link 2.
3-(3'-L-histidyl)-L-tyrosine
A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3-(3'-L-histidyl)-L-tyrosine.
PubMed:9144772
RESID:AA0250
(2S,3R)-2-amino-3-(5-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)-3-(4-hydroxyphenyl)propanoic acid
3-(3'-L-histidyl)-L-tyrosine
3-(N3'-histidyl)tyrosine
3-(pi-histidyl)tyrosine
3-(pros-histidyl)tyrosine
CROSSLNK 3'-histidyl-3-tyrosine (His-Tyr)
beta-(N(delta)-histidyl)tyrosine
beta-(N3'-histidyl)tyrosine
A protein modification that dioxygenates an L-methionine residue to L-methionine sulfone.
32.0
C 0 H 0 N 0 O 2 S 0
31.989828
C 5 H 9 N 1 O 3 S 1
163.19
163.03032
M
natural
Unimod:425
uniprot.ptm:PTM-0175
(2S)-2-amino-4-(methylsulfonyl)butanoic acid
L-methionine S,S-dioxide
L-methionine sulfone
MOD_RES Methionine sulfone
MetO2
MethionylSulphone
Oxidation of Methionine (to Sulphone)
S,S-dioxymethionine
suphonem
PSI-MOD
Dioxidation
dihydroxy
MOD:00256
DeltaMass gives the formula C 5 H 9 N 3 O 1 S 1 with mass 163
L-methionine sulfone
A protein modification that dioxygenates an L-methionine residue to L-methionine sulfone.
DeltaMass:205
OMSSA:115
PubMed:12686488
PubMed:7786407
PubMed:7791219
PubMed:9252331
RESID:AA0251
Unimod:425#M
(2S)-2-amino-4-(methylsulfonyl)butanoic acid
L-methionine S,S-dioxide
L-methionine sulfone
MOD_RES Methionine sulfone
MetO2
MethionylSulphone
Oxidation of Methionine (to Sulphone)
S,S-dioxymethionine
suphonem
Dioxidation
dihydroxy
A protein modification that effectively converts an L-cysteine residue to dipyrrolylmethanemethyl-L-cysteine.
418.4
C 20 H 22 N 2 O 8 S 0
418.1376
C 23 H 27 N 3 O 9 S 1
521.54
521.1468
C
natural
Unimod:416
uniprot.ptm:PTM-0421
(2S)-3-[5-[4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methyl-4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid
3-[5-(3-acetic acid-4-propanoic acid-1-pyrrol-2-yl)methyl-3-acetic acid-4-propanoic acid-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid
MOD_RES S-(dipyrrolylmethanemethyl)cysteine
dipyrrole cofactor
dipyrrolylmethanemethyl-L-cysteine
dipyrrolylmethyl-L-cysteine
dipyrromethane cofactor
pyrromethane cofactor
PSI-MOD
Dipyrrolylmethanemethyl
dipyrrolylmethanemethyl
MOD:00257
dipyrrolylmethanemethyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to dipyrrolylmethanemethyl-L-cysteine.
PubMed:3042456
PubMed:3196304
PubMed:3421931
PubMed:8727319
RESID:AA0252
Unimod:416
(2S)-3-[5-[4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methyl-4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid
3-[5-(3-acetic acid-4-propanoic acid-1-pyrrol-2-yl)methyl-3-acetic acid-4-propanoic acid-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid
MOD_RES S-(dipyrrolylmethanemethyl)cysteine
dipyrrole cofactor
dipyrrolylmethanemethyl-L-cysteine
dipyrrolylmethyl-L-cysteine
dipyrromethane cofactor
pyrromethane cofactor
Dipyrrolylmethanemethyl
dipyrrolylmethanemethyl
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form S-(2-aminovinyl)-3-methyl-D-cysteine.
-64.04
C -1 H -4 N 0 O -3 S 0
-64.016045
C 6 H 9 N 2 O 1 S 1
157.21
157.04356
C, T
natural
C-term
uniprot.ptm:PTM-0267
(2S,3S)-2-amino-3-[((Z)-2-aminoethenyl)sulfanyl]butanoic acid
2-amino-3-[(2-aminovinyl)sulfanyl]butanoic acid
CROSSLNK S-(2-aminovinyl)-3-methyl-D-cysteine (Thr-Cys)
S-(2-aminovinyl)-3-methyl-D-cysteine
decarboxylated methyllanthionine
PSI-MOD
MOD:00258
Cross-link 2.
S-(2-aminovinyl)-3-methyl-D-cysteine
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form S-(2-aminovinyl)-3-methyl-D-cysteine.
PubMed:9119018
RESID:AA0253
(2S,3S)-2-amino-3-[((Z)-2-aminoethenyl)sulfanyl]butanoic acid
2-amino-3-[(2-aminovinyl)sulfanyl]butanoic acid
CROSSLNK S-(2-aminovinyl)-3-methyl-D-cysteine (Thr-Cys)
S-(2-aminovinyl)-3-methyl-D-cysteine
decarboxylated methyllanthionine
A protein modification that effectively crosslinks an L-tyrosine residue and the 5'-end of DNA through a phosphodiester bond to form O4'-(phospho-5'-DNA)-L-tyrosine.
Y
natural
uniprot.ptm:PTM-0228
(S)-2-amino-3-[4-(5'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid
ACT_SITE O-(5'-phospho-DNA)-tyrosine intermediate
MOD_RES O-(5'-phospho-DNA)-tyrosine
O4'-(phospho-5'-DNA)-L-tyrosine
O4'-L-tyrosine 5'-DNA phosphodiester
PSI-MOD
MOD:00259
O4'-(phospho-5'-DNA)-L-tyrosine
A protein modification that effectively crosslinks an L-tyrosine residue and the 5'-end of DNA through a phosphodiester bond to form O4'-(phospho-5'-DNA)-L-tyrosine.
PubMed:1861973
PubMed:2940511
PubMed:3684578
RESID:AA0254
(S)-2-amino-3-[4-(5'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid
ACT_SITE O-(5'-phospho-DNA)-tyrosine intermediate
MOD_RES O-(5'-phospho-DNA)-tyrosine
O4'-(phospho-5'-DNA)-L-tyrosine
O4'-L-tyrosine 5'-DNA phosphodiester
A protein modification that effectively crosslinks an L-threonine residue and the 5'-end of DNA through a phosphodiester bond to form O-(phospho-5'-DNA)-L-threonine.
78.97
C 0 H 0 N 0 O 3 P 1
78.9585
C 4 H 7 N 1 O 5 P 1
180.08
180.00618
T
natural
(S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)butanoic acid
O-(phospho-5'-DNA)-L-threonine
O3-(phospho-5'-DNA)-L-threonine
O3-L-threonine 5'-DNA phosphodiester
PSI-MOD
MOD:00260
O-(phospho-5'-DNA)-L-threonine
A protein modification that effectively crosslinks an L-threonine residue and the 5'-end of DNA through a phosphodiester bond to form O-(phospho-5'-DNA)-L-threonine.
PubMed:3081736
RESID:AA0255
(S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)butanoic acid
O-(phospho-5'-DNA)-L-threonine
O3-(phospho-5'-DNA)-L-threonine
O3-L-threonine 5'-DNA phosphodiester
A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphouridine through a phosphodiester bond to form O4'-(phospho-5'-uridine)-L-tyrosine.
306.17
C 9 H 11 N 2 O 8 P 1
306.0253
C 18 H 20 N 3 O 10 P 1
469.34
469.08862
Y
natural
Unimod:417
uniprot.ptm:PTM-0333
(S)-2-amino-3-[4-(5'-uridine phosphonoxy)phenyl]propanoic acid
5'-uridylic-O-tyrosine
MOD_RES O-UMP-tyrosine
O-Uridinylylation (of Tyrosine)
O4'-(phospho-5'-uridine)-L-tyrosine
O4'-L-tyrosine 5'-uridine phosphodiester
OUMPTyr
hydrogen 5'-uridylate tyrosine ester
PSI-MOD
PhosphoUridine
uridine phosphodiester
MOD:00261
From DeltaMass: Average Mass: 306.
O4'-(phospho-5'-uridine)-L-tyrosine
A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphouridine through a phosphodiester bond to form O4'-(phospho-5'-uridine)-L-tyrosine.
DeltaMass:0
PubMed:11467524
PubMed:2885322
RESID:AA0256
Unimod:417#Y
(S)-2-amino-3-[4-(5'-uridine phosphonoxy)phenyl]propanoic acid
5'-uridylic-O-tyrosine
MOD_RES O-UMP-tyrosine
O-Uridinylylation (of Tyrosine)
O4'-(phospho-5'-uridine)-L-tyrosine
O4'-L-tyrosine 5'-uridine phosphodiester
OUMPTyr
hydrogen 5'-uridylate tyrosine ester
PhosphoUridine
uridine phosphodiester
A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and a free L-tyrosine.
-17.01
C 0 H -1 N 0 O -1
-17.00274
C 14 H 16 N 2 O 5
292.29
292.10593
E, Y
natural
C-term
(S,S)-2-(2-aminopentanedio-1-yl)amino-3-(4-hydoxyphenyl)propanoic acid
L-glutamyl L-tyrosine
N-(L-glutamyl)-L-tyrosine
SITE Involved in polymerization
PSI-MOD
MOD:00262
Cross-link 2.
N-(L-glutamyl)-L-tyrosine
A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and a free L-tyrosine.
ChEBI:21477
PubMed:6387372
PubMed:8093886
RESID:AA0257
(S,S)-2-(2-aminopentanedio-1-yl)amino-3-(4-hydoxyphenyl)propanoic acid
L-glutamyl L-tyrosine
N-(L-glutamyl)-L-tyrosine
SITE Involved in polymerization
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoviolobilin.
586.69
C 33 H 38 N 4 O 6 S 0
586.2791
C 36 H 43 N 5 O 7 S 1
689.83
689.2883
C
natural
Unimod:387
(4S)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-4,5-dihydro-2,7,13,17-tetramethyl-(21H,22H,24H)-biladiene-bc-1,19-dione
BINDING Phycoviolobilin chromophore (covalent; via 1 link)
PBV
PVB
PXB
S-phycobiliviolin-L-cysteine
S-phycoviolobilin-L-cysteine
cryptobiliviolin
cryptoviolin
cryptoviolobilin
PSI-MOD
Phycocyanobilin
phycocyanobilin
MOD:00263
S-phycoviolobilin-L-cysteine
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoviolobilin.
PubMed:2106585
PubMed:3208761
RESID:AA0258
Unimod:387
(4S)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-4,5-dihydro-2,7,13,17-tetramethyl-(21H,22H,24H)-biladiene-bc-1,19-dione
BINDING Phycoviolobilin chromophore (covalent; via 1 link)
PBV
PVB
PXB
S-phycobiliviolin-L-cysteine
S-phycoviolobilin-L-cysteine
cryptobiliviolin
cryptoviolin
cryptoviolobilin
Phycocyanobilin
phycocyanobilin
A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycoerythrobilin.
586.69
C 33 H 38 N 4 O 6 S 0
586.2791
C 39 H 48 N 6 O 8 S 2
792.97
792.2975
C, C
natural
(2S,3R,16R)-3,18-bis-[(R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione
3,18-bis-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,3,15,16-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-biladiene-ab-8,12-dipropanoic acid
BINDING Phycoerythrobilin chromophore (covalent; via 2 links)
PEB
phycoerythrobilin biscysteine adduct
phycoerythrobilin-bis-L-cysteine
PSI-MOD
MOD:00264
Cross-link 2.
phycoerythrobilin-bis-L-cysteine
A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycoerythrobilin.
PubMed:3208761
PubMed:3838747
RESID:AA0259
(2S,3R,16R)-3,18-bis-[(R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione
3,18-bis-[1-((2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,3,15,16-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-biladiene-ab-8,12-dipropanoic acid
BINDING Phycoerythrobilin chromophore (covalent; via 2 links)
PEB
phycoerythrobilin biscysteine adduct
phycoerythrobilin-bis-L-cysteine
A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycourobilin.
586.69
C 33 H 38 N 4 O 6 S 0
586.2791
C 39 H 48 N 6 O 8 S 2
792.97
792.2975
C, C
natural
3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-2,7,13,17-tetramethyl-1,19-dioxo-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-8,12-dipropanoic acid
3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-1,19(4H,16H)-dione
BINDING Phycourobilin chromophore (covalent; via 2 links)
PUB
phycourobilin biscysteine adduct
phycourobilin-bis-L-cysteine
PSI-MOD
MOD:00265
Cross-link 2.
phycourobilin-bis-L-cysteine
A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycourobilin.
PubMed:3208761
PubMed:3838665
PubMed:3838747
PubMed:8876649
RESID:AA0260
3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-2,7,13,17-tetramethyl-1,19-dioxo-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-8,12-dipropanoic acid
3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-1,19(4H,16H)-dione
BINDING Phycourobilin chromophore (covalent; via 2 links)
PUB
phycourobilin biscysteine adduct
phycourobilin-bis-L-cysteine
A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and one or more free L-glutamic acid molecules to form N-(L-glutamyl)-poly-L-glutamic acid.
E
natural
C-term
PSI-MOD
MOD:00266
N-L-glutamyl-poly-L-glutamic acid
A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and one or more free L-glutamic acid molecules to form N-(L-glutamyl)-poly-L-glutamic acid.
PubMed:2570347
PubMed:328274
RESID:AA0261
A protein modification that effectively dioxygenates an L-cysteine residue to L-cysteine sulfinic acid.
32.0
C 0 H 0 N 0 O 2 S 0
31.989828
C 3 H 5 N 1 O 3 S 1
135.14
134.99901
C
natural
Unimod:425
uniprot.ptm:PTM-0108
(2R)-2-amino-3-sulfinopropanoic acid
2-amino-2-carboxyethanesulfinic acid
2-amino-3-(dioxido-lambda(6)-sulfanyl)propanoic acid [tautomer]
2-amino-3-sulfonylpropanoic acid [tautomer]
3-sulfinoalanine
3-sulphinoalanine
CysO2H
L-cysteine sulfinic acid
MOD_RES Cysteine sulfinic acid (-SO2H)
S-cysteinesulfinic acid
S-sulfinocysteine
cysteine sulphinic acid
cysteine-S,S-dioxide [tautomer]
sulfinicacid
PSI-MOD
Dioxidation
dihydroxy
MOD:00267
"Hyun Ae Woo, et. al., Science 300 (5619), 653-656"
L-cysteine sulfinic acid
A protein modification that effectively dioxygenates an L-cysteine residue to L-cysteine sulfinic acid.
ChEBI:16345
OMSSA:162
PubMed:12686488
PubMed:9252331
PubMed:9586994
RESID:AA0262
Unimod:425#C
(2R)-2-amino-3-sulfinopropanoic acid
2-amino-2-carboxyethanesulfinic acid
2-amino-3-(dioxido-lambda(6)-sulfanyl)propanoic acid [tautomer]
2-amino-3-sulfonylpropanoic acid [tautomer]
3-sulfinoalanine
3-sulphinoalanine
CysO2H
L-cysteine sulfinic acid
MOD_RES Cysteine sulfinic acid (-SO2H)
S-cysteinesulfinic acid
S-sulfinocysteine
cysteine sulphinic acid
cysteine-S,S-dioxide [tautomer]
sulfinicacid
Dioxidation
dihydroxy
A protein modification that effectively converts an L-tyrosine residue to L-3',4',5'-trihydroxyphenylalanine.
32.0
C 0 H 0 N 0 O 2
31.989828
C 9 H 9 N 1 O 4
195.17
195.05316
Y
natural
Unimod:425
uniprot.ptm:PTM-0667
(S)-2-amino-3-(3,4,5-trihydroxyphenyl)propanoic acid
3,4,6-Trihydroxy-Phenylalanine (from Tyrosine) (TOPA)
35Hy2Tyr
L-3',4',5'-trihydroxyphenylalanine
L-3,4,5-TOPA
MOD_RES 3',4',5'-trihydroxyphenylalanine
PSI-MOD
Dioxidation
dihydroxy
MOD:00268
From DeltaMass: Average Mass: 32
L-3',4',5'-trihydroxyphenylalanine
A protein modification that effectively converts an L-tyrosine residue to L-3',4',5'-trihydroxyphenylalanine.
ChEBI:141811
DeltaMass:0
PubMed:12686488
PubMed:12771378
PubMed:8554314
PubMed:9252331
PubMed:9434739
RESID:AA0263
Unimod:425#Y
(S)-2-amino-3-(3,4,5-trihydroxyphenyl)propanoic acid
3,4,6-Trihydroxy-Phenylalanine (from Tyrosine) (TOPA)
35Hy2Tyr
L-3',4',5'-trihydroxyphenylalanine
L-3,4,5-TOPA
MOD_RES 3',4',5'-trihydroxyphenylalanine
Dioxidation
dihydroxy
A protein modification that effectively converts an L-serine residue to O-(sn-1-glycerophosphoryl)-L-serine.
154.06
C 3 H 7 N 0 O 5 P 1
154.00311
C 6 H 12 N 1 O 7 P 1
241.14
241.03514
S
natural
Unimod:419
uniprot.ptm:PTM-0230
(2S)-2-amino-3-[(2Xi)-2,3-dihydroxypropyl]phosphonoxypropanoic acid
MOD_RES O-(sn-1-glycerophosphoryl)serine
O-(sn-1-glycerophosphoryl)-L-serine
O3-(sn-1-glycerophosphoryl)-L-serine
O3-2,3-dihydroxypropyl hydrogen phosphate-L-serine ester
O3-L-serine glyceryl-1-phosphodiester
alpha-glycerophosphoryl serine
glycerophosphoserine
PSI-MOD
Glycerophospho
glycerophospho
MOD:00269
O-(sn-1-glycerophosphoryl)-L-serine
A protein modification that effectively converts an L-serine residue to O-(sn-1-glycerophosphoryl)-L-serine.
PubMed:8645220
RESID:AA0264
Unimod:419#S
(2S)-2-amino-3-[(2Xi)-2,3-dihydroxypropyl]phosphonoxypropanoic acid
MOD_RES O-(sn-1-glycerophosphoryl)serine
O-(sn-1-glycerophosphoryl)-L-serine
O3-(sn-1-glycerophosphoryl)-L-serine
O3-2,3-dihydroxypropyl hydrogen phosphate-L-serine ester
O3-L-serine glyceryl-1-phosphodiester
alpha-glycerophosphoryl serine
glycerophosphoserine
Glycerophospho
glycerophospho
A protein modification that effectively converts a glycine residue to an internal 1-thioglycine.
16.06
C 0 H 0 N 0 O -1 S 1
15.977156
C 2 H 3 N 1 S 1
73.11
72.99862
G
natural
uniprot.ptm:PTM-0004
1-thioglycine
2-amino-1-sulfanylethanone
MOD_RES 1-thioglycine
S(O)Gly
aminoethanethioic O-acid
aminoethanethioic acid
aminoethanethionic acid
aminothioacetic acid
PSI-MOD
Carboxy->Thiocarboxy
thiocarboxylic acid
MOD:00270
This modification occurs naturally in two forms. At an interior peptide location it exists as aminoethanethionic acid (or aminoethanethioic O-acid). At the carboxyl-terminal it exists as aminoethanethiolic acid (or aminoethanethioic S-acid).
1-thioglycine (internal)
A protein modification that effectively converts a glycine residue to an internal 1-thioglycine.
PubMed:11463785
PubMed:9367957
RESID:AA0265#INT
1-thioglycine
2-amino-1-sulfanylethanone
MOD_RES 1-thioglycine
S(O)Gly
aminoethanethioic O-acid
aminoethanethioic acid
aminoethanethionic acid
aminothioacetic acid
Carboxy->Thiocarboxy
thiocarboxylic acid
A protein modification that effectively results from forming an adduct between two cysteine residues, the C-3' of a tyrosine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
614.48
C 34 Fe 1 H 30 N 4 O 4 S 0
614.1616
C 49 Fe 1 H 49 N 7 O 8 S 2
983.94
983.24335
C, C, Y
natural
(10S,11S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-10-(2-hydroxy-5-[(S)-2-amino-2-carboxy]ethylphenyl)-3,8,13,17-tetramethyl-21H,23H-10,11-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
BINDING Heme (covalent; via 3 links)
bis(S-cysteinyl)-(tyros-3'-yl)-heme
heme P460-bis-L-cysteine-L-tyrosine
PSI-MOD
MOD:00271
Cross-link 3.
heme P460-bis-L-cysteine-L-tyrosine
A protein modification that effectively results from forming an adduct between two cysteine residues, the C-3' of a tyrosine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
PubMed:8325841
PubMed:9095195
RESID:AA0266
(10S,11S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-10-(2-hydroxy-5-[(S)-2-amino-2-carboxy]ethylphenyl)-3,8,13,17-tetramethyl-21H,23H-10,11-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
BINDING Heme (covalent; via 3 links)
bis(S-cysteinyl)-(tyros-3'-yl)-heme
heme P460-bis-L-cysteine-L-tyrosine
A protein modification that effectively crosslinks an L-threonine residue and 5'-phosphoadenosine through a phosphodiester bond to form O-(phospho-5'-adenosine)-L-threonine.
329.21
C 10 H 12 N 5 O 6 P 1
329.05252
C 14 H 19 N 6 O 8 P 1
430.31
430.1002
T
natural
Unimod:405
uniprot.ptm:PTM-0393
(2S,3R)-2-amino-3-(5'-adenosine phosphonoxy)butanoic acid
5'-adenylic-O3-L-threonine
ACT_SITE O-AMP-threonine intermediate
L-threonine monoanhydride with 5'-adenylic acid
MOD_RES O-AMP-threonine
O(gamma)-5'-adenylic-L-threonine
O-(phospho-5'-adenosine)-L-threonine
O3-(phospho-5'-adenosine)-L-threonine
O3-L-threonine 5'-adenosine phosphodiester
beta-5'-adenylic-L-threonine
PSI-MOD
AMP binding site
Phosphoadenosine
MOD:00272
O-(phospho-5'-adenosine)-L-threonine
A protein modification that effectively crosslinks an L-threonine residue and 5'-phosphoadenosine through a phosphodiester bond to form O-(phospho-5'-adenosine)-L-threonine.
PubMed:2989287
PubMed:8917428
RESID:AA0267
Unimod:405#T
(2S,3R)-2-amino-3-(5'-adenosine phosphonoxy)butanoic acid
5'-adenylic-O3-L-threonine
ACT_SITE O-AMP-threonine intermediate
L-threonine monoanhydride with 5'-adenylic acid
MOD_RES O-AMP-threonine
O(gamma)-5'-adenylic-L-threonine
O-(phospho-5'-adenosine)-L-threonine
O3-(phospho-5'-adenosine)-L-threonine
O3-L-threonine 5'-adenosine phosphodiester
beta-5'-adenylic-L-threonine
AMP binding site
Phosphoadenosine
A protein modification that effectively converts four L-cysteine residues, two L-glutamic acid residues, an L-histidine residue and a four-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide.
360.5
C 0 Fe 4 H -7 N 0 O 3 S 3
360.58594
C 28 Fe 4 H 34 N 9 O 14 S 7
1168.43
1167.7667
C, C, C, C, E, E, H
natural
4Fe-2S-3O cluster
METAL Iron-oxo-sulfur (4Fe-2O-2S)
METAL Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group
METAL Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen
hybrid four iron cluster 2
mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O5-glutamato 2-iron-3,4-bis-(S-cysteinyl iron)
tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide
PSI-MOD
prismane iron-sulfur cofactor
MOD:00273
Cross-link 7; secondary to RESID:AA0269.
tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide
A protein modification that effectively converts four L-cysteine residues, two L-glutamic acid residues, an L-histidine residue and a four-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide.
PubMed:12764602
RESID:AA0268
4Fe-2S-3O cluster
METAL Iron-oxo-sulfur (4Fe-2O-2S)
METAL Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group
METAL Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen
hybrid four iron cluster 2
mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O5-glutamato 2-iron-3,4-bis-(S-cysteinyl iron)
tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide
prismane iron-sulfur cofactor
A protein modification that effectively replaces the hydrogen atom of a cysteine sulfanyl group with a sulfanyl group, forming a disulfanyl group, and converting an L-cysteine residue to L-cysteine persulfide.
32.06
C 0 H 0 N 0 O 0 S 1
31.97207
C 3 H 5 N 1 O 1 S 2
135.2
134.98126
C
natural
Unimod:421
uniprot.ptm:PTM-0106
(R)-2-amino-3-disulfanylpropanoic acid
2-amino-3-disulfanylpropanoic acid
2-amino-3-hydrodisulfidopropanoic acid
2-amino-3-hydropersulfidopropanoic acid
2-amino-3-persulfhydrylpropanoic acid
3-(thiosulfeno)-alanine
3-disulfanylalanine
ACT_SITE Cysteine persulfide intermediate
L-cysteine persulfide
MOD_RES Cysteine persulfide
S-mercaptocysteine
S-sulfanylcysteine
thiocysteine
PSI-MOD
Sulfide
persulfide
MOD:00274
L-cysteine persulfide
A protein modification that effectively replaces the hydrogen atom of a cysteine sulfanyl group with a sulfanyl group, forming a disulfanyl group, and converting an L-cysteine residue to L-cysteine persulfide.
ChEBI:28839
PubMed:15096637
PubMed:4276457
PubMed:8161529
RESID:AA0269
Unimod:421
(R)-2-amino-3-disulfanylpropanoic acid
2-amino-3-disulfanylpropanoic acid
2-amino-3-hydrodisulfidopropanoic acid
2-amino-3-hydropersulfidopropanoic acid
2-amino-3-persulfhydrylpropanoic acid
3-(thiosulfeno)-alanine
3-disulfanylalanine
ACT_SITE Cysteine persulfide intermediate
L-cysteine persulfide
MOD_RES Cysteine persulfide
S-mercaptocysteine
S-sulfanylcysteine
thiocysteine
Sulfide
persulfide
A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3'-(1'-L-histidyl)-L-tyrosine.
-2.02
C 0 H -2 N 0 O 0
-2.01565
C 15 H 14 N 4 O 3
298.3
298.1066
H, Y
natural
uniprot.ptm:PTM-0003
(2S)-2-amino-3-[1-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenyl)-1H-imidazol-4-yl]propanoic acid
3'-(1'-L-histidyl)-L-tyrosine
3'-(N(epsilon)-histidyl)tyrosine
3'-(N1'-histidyl)tyrosine
3'-(tau-histidyl)tyrosine
3'-(tele-histidyl)tyrosine
CROSSLNK 1'-histidyl-3'-tyrosine (His-Tyr)
PSI-MOD
MOD:00275
Cross-link 2.
3'-(1'-L-histidyl)-L-tyrosine
A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3'-(1'-L-histidyl)-L-tyrosine.
ChEBI:19837
PubMed:10338009
RESID:AA0270
(2S)-2-amino-3-[1-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenyl)-1H-imidazol-4-yl]propanoic acid
3'-(1'-L-histidyl)-L-tyrosine
3'-(N(epsilon)-histidyl)tyrosine
3'-(N1'-histidyl)tyrosine
3'-(tau-histidyl)tyrosine
3'-(tele-histidyl)tyrosine
CROSSLNK 1'-histidyl-3'-tyrosine (His-Tyr)
A protein modification that effectively results from forming an adduct between two cysteine residues, a lysine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
614.48
C 34 Fe 1 H 30 N 4 O 4 S 0
614.1616
C 46 Fe 1 H 52 N 8 O 7 S 2
948.94
948.27496
C, C, K
natural
(19S,20S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-20-([(S)-5-amino-5-carboxypentyl]amino)-3,8,13,17-tetramethyl-21H,23H-19,20-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
BINDING Heme (covalent; via 3 links)
bis(S-cysteinyl)-N6-lysino-heme
heme P460-bis-L-cysteine-L-lysine
PSI-MOD
MOD:00276
Cross-link 3.
heme P460-bis-L-cysteine-L-lysine
A protein modification that effectively results from forming an adduct between two cysteine residues, a lysine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
PubMed:12709052
PubMed:9237682
RESID:AA0271
(19S,20S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-20-([(S)-5-amino-5-carboxypentyl]amino)-3,8,13,17-tetramethyl-21H,23H-19,20-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
BINDING Heme (covalent; via 3 links)
bis(S-cysteinyl)-N6-lysino-heme
heme P460-bis-L-cysteine-L-lysine
A protein modification that effectively converts an L-arginine residue to 5-methyl-L-arginine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 7 H 14 N 4 O 1
170.22
170.11676
R
natural
uniprot.ptm:PTM-0050
(2S,5S)-2-amino-5-carbamimidamidohexanoic acid
2-amino-5-guanidinohexanoic acid
5-methyl-L-arginine
5-methylated L-arginine
C5Me1Arg
MOD_RES 5-methylarginine
delta-methylarginine
PSI-MOD
4-methylarginine
Methyl
Methylation
MOD:00277
5-methyl-L-arginine
A protein modification that effectively converts an L-arginine residue to 5-methyl-L-arginine.
PubMed:10660523
PubMed:11875433
PubMed:9367957
RESID:AA0272
(2S,5S)-2-amino-5-carbamimidamidohexanoic acid
2-amino-5-guanidinohexanoic acid
5-methyl-L-arginine
5-methylated L-arginine
C5Me1Arg
MOD_RES 5-methylarginine
delta-methylarginine
4-methylarginine
Methyl
Methylation
A protein modification that effectively converts an L-glutamine residue to 2-methyl-L-glutamine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 6 H 10 N 2 O 2
142.16
142.07423
Q
natural
uniprot.ptm:PTM-0016
(S)-2-amino-2-methylpentanediamic acid
2-methyl-L-glutamine
2-methylated L-glutamine
2-methylglutamine
C2MeGln
MOD_RES 2-methylglutamine
alpha-methylglutamine
PSI-MOD
Methyl
Methylation
MOD:00278
2-methyl-L-glutamine
A protein modification that effectively converts an L-glutamine residue to 2-methyl-L-glutamine.
PubMed:10660523
PubMed:11875433
PubMed:9367957
RESID:AA0273
(S)-2-amino-2-methylpentanediamic acid
2-methyl-L-glutamine
2-methylated L-glutamine
2-methylglutamine
C2MeGln
MOD_RES 2-methylglutamine
alpha-methylglutamine
Methyl
Methylation
A protein modification that effectively converts an L-cysteine residue to N-pyruvic acid 2-iminyl-L-cysteine.
70.05
C 3 H 2 N 0 O 2 S 0
70.00548
C 6 H 8 N 1 O 3 S 1
174.19
174.02249
C
natural
N-term
Unimod:422
uniprot.ptm:PTM-0224
(R)-2-(1-carboxy-2-sulfanylethanimino)propanoic acid
MOD_RES N-pyruvate 2-iminyl-cysteine
N-pyruvic acid 2-iminyl-L-cysteine
PSI-MOD
N-pyruvic acid 2-iminyl
PyruvicAcidIminyl
MOD:00279
N-pyruvic acid 2-iminyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to N-pyruvic acid 2-iminyl-L-cysteine.
PubMed:1388164
RESID:AA0274
Unimod:422#C
(R)-2-(1-carboxy-2-sulfanylethanimino)propanoic acid
MOD_RES N-pyruvate 2-iminyl-cysteine
N-pyruvic acid 2-iminyl-L-cysteine
N-pyruvic acid 2-iminyl
PyruvicAcidIminyl
A protein modification that effectively converts an L-valine residue to N-pyruvic acid 2-iminyl-L-valine.
70.05
C 3 H 2 N 0 O 2
70.00548
C 8 H 12 N 1 O 3
170.19
170.08171
V
natural
N-term
Unimod:422
uniprot.ptm:PTM-0225
(S)-2-(1-carboxy-2-methylpropanimino)propanoic acid
MOD_RES N-pyruvate 2-iminyl-valine
N-pyruvic acid 2-iminyl-L-valine
PSI-MOD
N-pyruvic acid 2-iminyl
PyruvicAcidIminyl
MOD:00280
N-pyruvic acid 2-iminyl-L-valine
A protein modification that effectively converts an L-valine residue to N-pyruvic acid 2-iminyl-L-valine.
PubMed:2071591
RESID:AA0275
Unimod:422#V
(S)-2-(1-carboxy-2-methylpropanimino)propanoic acid
MOD_RES N-pyruvate 2-iminyl-valine
N-pyruvic acid 2-iminyl-L-valine
N-pyruvic acid 2-iminyl
PyruvicAcidIminyl
A protein modification that effectively results from forming an adduct between the pros nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
616.5
C 34 Fe 1 H 32 N 4 O 4
616.1773
C 40 Fe 1 H 39 N 7 O 5
753.64
753.2362
H
natural
2-[1-(N3'-histidyl)ethyl]protoporphyrin IX
3'-heme-L-histidine
BINDING Heme (covalent; via pros nitrogen)
N(delta)-histidyl heme
N(pi)-histidyl heme
N3'-histidyl heme
[7-ethenyl-12-((S)-1-[((R)-2-amino-2-carboxyethyl)-3H-imidazol-3-yl]ethyl)-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
pros-histidyl heme
PSI-MOD
MOD:00281
3'-heme-L-histidine
A protein modification that effectively results from forming an adduct between the pros nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
PubMed:12119398
PubMed:12429096
PubMed:12486054
PubMed:9712585
RESID:AA0276
2-[1-(N3'-histidyl)ethyl]protoporphyrin IX
3'-heme-L-histidine
BINDING Heme (covalent; via pros nitrogen)
N(delta)-histidyl heme
N(pi)-histidyl heme
N3'-histidyl heme
[7-ethenyl-12-((S)-1-[((R)-2-amino-2-carboxyethyl)-3H-imidazol-3-yl]ethyl)-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
pros-histidyl heme
A protein modification that effectively converts an L-cysteine residue to S-selenyl-L-cysteine.
78.97
C 0 H 0 N 0 O 0 S 0 Se 1
79.91652
C 3 H 5 N 1 O 1 S 1 Se 1
182.11
182.9257
C
hypothetical
Unimod:423
uniprot.ptm:PTM-0282
(R)-2-amino-3-(selanylsulfanyl)propanoic acid
2-amino-3-hydroselenosulfidopropanoic acid
2-amino-3-hydroselenylsulfidopropanoic acid
2-amino-3-hydroselenylthiopropanoic acid
ACT_SITE S-selanylcysteine intermediate
MOD_RES S-selenylcysteine
S-selanyl-L-cysteine
S-selanylcysteine
S-selenylcysteine
PSI-MOD
Delta:Se(1)
cysteine perselenide
selenyl
MOD:00282
S-selenyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-selenyl-L-cysteine.
PubMed:10430865
PubMed:10966817
PubMed:11827487
PubMed:12716131
PubMed:14594807
RESID:AA0277
Unimod:423#C
(R)-2-amino-3-(selanylsulfanyl)propanoic acid
2-amino-3-hydroselenosulfidopropanoic acid
2-amino-3-hydroselenylsulfidopropanoic acid
2-amino-3-hydroselenylthiopropanoic acid
ACT_SITE S-selanylcysteine intermediate
MOD_RES S-selenylcysteine
S-selanyl-L-cysteine
S-selanylcysteine
S-selenylcysteine
Delta:Se(1)
cysteine perselenide
selenyl
A protein modification that effectively converts an L-lysine residue to an N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine.
K
natural
uniprot.ptm:PTM-0198
(alpha)- ([([(5S)-5-amino-5-carboxypentyl]amino)propyl][(methyl)amino])-(omega)-methyl poly[propane-1,3-diyl(methylimino)]
MOD_RES N6-poly(methylaminopropyl)lysine
N6-[3-([(omega)-(dimethyl)aminopropyl-poly(3-[methylamino]propyl)]amino)propyl]lysine
N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine
lysine derivative Lys(x)
silaffin polycationic lysine derivative
PSI-MOD
MOD:00283
N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine
A protein modification that effectively converts an L-lysine residue to an N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine.
PubMed:10550045
PubMed:11349130
RESID:AA0278
(alpha)- ([([(5S)-5-amino-5-carboxypentyl]amino)propyl][(methyl)amino])-(omega)-methyl poly[propane-1,3-diyl(methylimino)]
MOD_RES N6-poly(methylaminopropyl)lysine
N6-[3-([(omega)-(dimethyl)aminopropyl-poly(3-[methylamino]propyl)]amino)propyl]lysine
N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine
lysine derivative Lys(x)
silaffin polycationic lysine derivative
A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
612.47
C 34 Fe 1 H 28 N 4 O 4
612.146
C 43 Fe 1 H 40 N 6 O 10
856.67
856.2155
D, E
hypothetical
1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester
BINDING Heme (covalent; via 2 links)
[13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-7,12-diethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
dihydroxyheme-L-aspartate ester-L-glutamate ester
peroxidase heme cofactor
PSI-MOD
MOD:00284
Cross-link 2.
dihydroxyheme-L-aspartate ester-L-glutamate ester
A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
PubMed:10447690
RESID:AA0279
1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester
BINDING Heme (covalent; via 2 links)
[13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-7,12-diethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
dihydroxyheme-L-aspartate ester-L-glutamate ester
peroxidase heme cofactor
A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, a methionine residue (forming a sulfonium ether), and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
613.47
C 34 Fe 1 H 29 N 4 O 4 S 0
613.15326
1+
C 48 Fe 1 H 50 N 7 O 11 S 1
988.87
988.2633
D, E, M
natural
1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester 2-methionine sulfonium
BINDING Heme (covalent; via 3 links)
[13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-12-[(S)-(3-amino-3-carboxy)propylsulfoniumethyl]-7-ethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium
myeloperoxidase heme cofactor
PSI-MOD
MOD:00285
Cross-link 3.
dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium
A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, a methionine residue (forming a sulfonium ether), and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
PubMed:10447690
PubMed:10480885
PubMed:1320128
PubMed:7840679
RESID:AA0280
1,5-bishydroxymethyl protoporphyrin IX 1-glutamate ester 5-aspartate ester 2-methionine sulfonium
BINDING Heme (covalent; via 3 links)
[13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-12-[(S)-(3-amino-3-carboxy)propylsulfoniumethyl]-7-ethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium
myeloperoxidase heme cofactor
A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide).
1572.02
C 40 H 47 Mo 1 N 20 O 26 P 4 S 4
1572.9857
C 43 H 52 Mo 1 N 21 O 27 P 4 S 5
1675.15
1675.995
C
hypothetical
Unimod:424
2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide
L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide)
bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-cystein-S-yl-molybdenum
PSI-MOD
MolybdopterinGD
molybdenum bis(molybdopterin guanine dinucleotide)
MOD:00286
L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide)
A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide).
RESID:AA0281
Unimod:424#C
2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide
L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide)
bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-cystein-S-yl-molybdenum
MolybdopterinGD
molybdenum bis(molybdopterin guanine dinucleotide)
A protein modification that effectively converts an L-proline residue to a (2S,3R,4S)-3,4-dihydroxyproline.
32.0
C 0 H 0 N 0 O 2
31.989828
C 5 H 7 N 1 O 3
129.12
129.04259
P
natural
Unimod:425
uniprot.ptm:PTM-0306
(2S,3R,4S)-3,4-dihydroxyproline
(2S,3R,4S)-3,4-dihydroxypyrrolidine-2-carboxylic acid
2,3-trans-3,4-cis-3,4-dihydroxy-L-proline
2-alpha-3-beta-4-beta-3,4-dihydroxyproline
3,4-Dihydroxylation (of Proline)
3,4-dihydroxylated L-proline
34Hy2Pro
MOD_RES (3R,4S)-3,4-dihydroxyproline
trans-2,3-cis-3,4-dihydroxy-L-proline
PSI-MOD
Dioxidation
dihydroxy
MOD:00287
From DeltaMass: Average Mass: 32.
(2S,3R,4S)-3,4-dihydroxyproline
A protein modification that effectively converts an L-proline residue to a (2S,3R,4S)-3,4-dihydroxyproline.
ChEBI:141803
DeltaMass:0
PubMed:12686488
RESID:AA0282
Unimod:425#P
(2S,3R,4S)-3,4-dihydroxyproline
(2S,3R,4S)-3,4-dihydroxypyrrolidine-2-carboxylic acid
2,3-trans-3,4-cis-3,4-dihydroxy-L-proline
2-alpha-3-beta-4-beta-3,4-dihydroxyproline
3,4-Dihydroxylation (of Proline)
3,4-dihydroxylated L-proline
34Hy2Pro
MOD_RES (3R,4S)-3,4-dihydroxyproline
trans-2,3-cis-3,4-dihydroxy-L-proline
Dioxidation
dihydroxy
A protein modification that effectively doubly cross-links an L-glutamic acid residue and an L-tyrosine residue with a carbon-carbon bond and a carbon-nitrogen bond to form pyrroloquinoline quinone.
37.92
C 0 H -10 N 0 O 3
37.906494
C 14 H 6 N 2 O 8
330.21
330.01242
E, Y
natural
uniprot.ptm:PTM-0263
2,4,6-tricarboxylic-pyrrolo[2,3-5,6]quinoline 8,9-quinone
2,7,9-tricarboxy-1H-pyrrolo(2,3-f)quinoline-4,5-dione
4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-5,6]quinoline-2,7,9-tricarboxylic acid
CROSSLNK Pyrroloquinoline quinone (Glu-Tyr)
coenzyme PQQ
methoxatin
pyrroloquinoline quinone
PSI-MOD
MOD:00288
Cross-link 2.
pyrroloquinoline quinone
A protein modification that effectively doubly cross-links an L-glutamic acid residue and an L-tyrosine residue with a carbon-carbon bond and a carbon-nitrogen bond to form pyrroloquinoline quinone.
ChEBI:18315
PubMed:1310505
PubMed:7665488
RESID:AA0283
2,4,6-tricarboxylic-pyrrolo[2,3-5,6]quinoline 8,9-quinone
2,7,9-tricarboxy-1H-pyrrolo(2,3-f)quinoline-4,5-dione
4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-5,6]quinoline-2,7,9-tricarboxylic acid
CROSSLNK Pyrroloquinoline quinone (Glu-Tyr)
coenzyme PQQ
methoxatin
pyrroloquinoline quinone
A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide.
347.59
C 0 Fe 4 H -4 N 0 O 0 S 4
347.59784
2-
C 15 Fe 4 H 18 N 6 O 4 S 7
794.15
793.6843
C, C, C, H
natural
METAL Iron-sulfur (4Fe-4S)
METAL Iron-sulfur (4Fe-4S); via tele nitrogen
tetra-mu3-sulfidotris(S-cysteinyliron)(N1'-histidinoiron)
tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide
PSI-MOD
MOD:00289
Cross-link 4.
tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide
A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide.
PubMed:9836629
RESID:AA0284
METAL Iron-sulfur (4Fe-4S)
METAL Iron-sulfur (4Fe-4S); via tele nitrogen
tetra-mu3-sulfidotris(S-cysteinyliron)(N1'-histidinoiron)
tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide
A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide.
347.59
C 0 Fe 4 H -4 N 0 O 0 S 4
347.59784
2-
C 15 Fe 4 H 18 N 6 O 4 S 7
794.15
793.6843
C, C, C, H
natural
METAL Iron-sulfur (4Fe-4S)
METAL Iron-sulfur (4Fe-4S); via pros nitrogen
tetra-mu3-sulfidotris(S-cysteinyliron)(N3'-histidinoiron)
tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide
PSI-MOD
MOD:00290
Cross-link 4.
tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide
A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide.
PubMed:7854413
RESID:AA0285
METAL Iron-sulfur (4Fe-4S)
METAL Iron-sulfur (4Fe-4S); via pros nitrogen
tetra-mu3-sulfidotris(S-cysteinyliron)(N3'-histidinoiron)
tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide
A protein modification that effectively converts three L-cysteine residues, an L-aspartic acid residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-aspartato tetrairon tetrasulfide.
347.59
C 0 Fe 4 H -4 N 0 O 0 S 4
347.59784
2-
C 13 Fe 4 H 16 N 4 O 6 S 7
772.09
771.65234
C, C, C, D
natural
METAL Iron-sulfur (4Fe-4S)
tetra-mu3-sulfidotris(S-cysteinyliron)(O4-aspartatoiron)
tris-L-cysteinyl L-aspartato tetrairon tetrasulfide
PSI-MOD
MOD:00291
Cross-link 4.
tris-L-cysteinyl L-aspartato tetrairon tetrasulfide
A protein modification that effectively converts three L-cysteine residues, an L-aspartic acid residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-aspartato tetrairon tetrasulfide.
PubMed:7819255
PubMed:9283079
RESID:AA0286
METAL Iron-sulfur (4Fe-4S)
tetra-mu3-sulfidotris(S-cysteinyliron)(O4-aspartatoiron)
tris-L-cysteinyl L-aspartato tetrairon tetrasulfide
A protein modification that effectively converts an L-lysine residue to N6-pyruvic acid 2-iminyl-L-lysine.
70.05
C 3 H 2 N 0 O 2
70.00548
C 9 H 14 N 2 O 3
198.22
198.10045
K
natural
Unimod:422
(2S)-2-amino-6-([1-carboxyethylidene]amino)hexanoic acid
ACT_SITE Schiff-base intermediate with substrate
N6-pyruvic acid 2-iminyl-L-lysine
PSI-MOD
N-pyruvic acid 2-iminyl
PyruvicAcidIminyl
MOD:00292
N6-pyruvic acid 2-iminyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-pyruvic acid 2-iminyl-L-lysine.
PubMed:1463470
PubMed:7853400
PubMed:9047371
RESID:AA0287
Unimod:422#K
(2S)-2-amino-6-([1-carboxyethylidene]amino)hexanoic acid
ACT_SITE Schiff-base intermediate with substrate
N6-pyruvic acid 2-iminyl-L-lysine
N-pyruvic acid 2-iminyl
PyruvicAcidIminyl
A protein modification that effectively converts three L-cysteine residues, an L-serine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-serinyl tetrairon tetrasulfide.
347.59
C 0 Fe 4 H -4 N 0 O 0 S 4
347.59784
2-
C 12 Fe 4 H 16 N 4 O 5 S 7
744.08
743.6574
C, C, C, S
hypothetical
tetra-mu3-sulfidotris(S-cysteinyliron)(O3-serinyliron)
tris-L-cysteinyl L-serinyl tetrairon tetrasulfide
PSI-MOD
MOD:00293
Cross-link 4.
tris-L-cysteinyl L-serinyl tetrairon tetrasulfide
A protein modification that effectively converts three L-cysteine residues, an L-serine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-serinyl tetrairon tetrasulfide.
RESID:AA0288
tetra-mu3-sulfidotris(S-cysteinyliron)(O3-serinyliron)
tris-L-cysteinyl L-serinyl tetrairon tetrasulfide
A protein modification that effectively converts two L-cysteine residues, an L-histidine residues, an L-serine residue and a four-iron four-sulfur cluster to bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide.
347.59
C 0 Fe 4 H -4 N 0 O 0 S 4
347.59784
2-
C 15 Fe 4 H 18 N 6 O 5 S 6
778.09
777.70715
C, C, H, S
hypothetical
METAL Iron-sulfur (4Fe-4S)
METAL Iron-sulfur (4Fe-4S); via pros nitrogen
bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide
tetra-mu3-sulfidobis(S-cysteinyliron)(N3'-histidinoiron)(O3-serinyliron)
PSI-MOD
MOD:00294
Cross-link 4.
bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide
A protein modification that effectively converts two L-cysteine residues, an L-histidine residues, an L-serine residue and a four-iron four-sulfur cluster to bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide.
RESID:AA0289
METAL Iron-sulfur (4Fe-4S)
METAL Iron-sulfur (4Fe-4S); via pros nitrogen
bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide
tetra-mu3-sulfidobis(S-cysteinyliron)(N3'-histidinoiron)(O3-serinyliron)
A protein modification that effectively converts an L-serine residue to O-octanoyl-L-serine.
126.2
C 8 H 14 N 0 O 1
126.10446
C 11 H 19 N 1 O 3
213.28
213.13649
S
natural
Unimod:426
uniprot.ptm:PTM-0239
(2S)-2-amino-3-(octanoyloxy)propanoic acid
L-serine octanoate ester
LIPID O-octanoyl serine
O-octanoyl-L-serine
O-octanoylated L-serine
O3-octanoyl-L-serine
OOctSer
PSI-MOD
Octanoyl
octanoyl
MOD:00295
O-octanoyl-L-serine
A protein modification that effectively converts an L-serine residue to O-octanoyl-L-serine.
PubMed:10604470
PubMed:12716131
RESID:AA0290
Unimod:426#S
(2S)-2-amino-3-(octanoyloxy)propanoic acid
L-serine octanoate ester
LIPID O-octanoyl serine
O-octanoyl-L-serine
O-octanoylated L-serine
O3-octanoyl-L-serine
OOctSer
Octanoyl
octanoyl
A protein modification that effectively converts an L-serine residue to O-D-glucuronosyl-L-serine.
176.12
C 6 H 8 N 0 O 6
176.03209
C 9 H 13 N 1 O 8
263.2
263.06412
S
natural
Unimod:54
uniprot.ptm:PTM-0577
(2S)-2-amino-3-(beta-D-glucopyranuronosyl)propanoic acid
CARBOHYD O-linked (GlcA) serine
O-D-glucuronosyl-L-serine
O3-D-glucuronosyl-L-serine
PSI-MOD
Glucuronyl
N-glucuronylation
MOD:00296
O-D-glucuronosyl-L-serine
A protein modification that effectively converts an L-serine residue to O-D-glucuronosyl-L-serine.
PubMed:10858503
PubMed:12716131
PubMed:7398618
RESID:AA0291
Unimod:54#S
(2S)-2-amino-3-(beta-D-glucopyranuronosyl)propanoic acid
CARBOHYD O-linked (GlcA) serine
O-D-glucuronosyl-L-serine
O3-D-glucuronosyl-L-serine
Glucuronyl
N-glucuronylation
A protein modification that effectively converts four L-cysteine residues, two L-glutamic acid residues, an L-histidine residue and a three-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide.
363.35
C 0 Fe 3 H -7 N 0 Ni 1 O 3 S 3
362.58633
C 28 Fe 3 H 34 N 9 Ni 1 O 14 S 7
1171.28
1169.7672
C, C, C, C, E, E, H
artifact
Ni-3Fe-2S-3O cluster
carbon monoxide dehydrogenase nickel-iron cofactor
hybrid nickel-triiron cluster
mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O5-glutamato 2-nickel-3,4-bis-(S-cysteinyl iron)
tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide
PSI-MOD
MOD:00297
Cross-link 7; secondary to RESID:AA0269. This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide
A protein modification that effectively converts four L-cysteine residues, two L-glutamic acid residues, an L-histidine residue and a three-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide.
RESID:AA0292
Ni-3Fe-2S-3O cluster
carbon monoxide dehydrogenase nickel-iron cofactor
hybrid nickel-triiron cluster
mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O5-glutamato 2-nickel-3,4-bis-(S-cysteinyl iron)
tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide
A protein modification that effectively converts four L-cysteine residues, an L-glutamic acid residue, an L-histidine residue, an L-serine residue and a one-nickel three-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide.
363.35
C 0 Fe 3 H -7 N 0 Ni 1 O 3 S 3
362.58633
C 26 Fe 3 H 32 N 9 Ni 1 O 13 S 7
1129.24
1127.7566
C, C, C, C, E, H, S
artifact
Ni-3Fe-2S-3O cluster
carbon monoxide dehydrogenase nickel-iron cofactor
hybrid nickel-triiron cluster
mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O3-serinyl 2-nickel-3,4-bis-(S-cysteinyl iron)
tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide
PSI-MOD
MOD:00298
Cross-link 7; secondary to RESID:AA0269. This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide
A protein modification that effectively converts four L-cysteine residues, an L-glutamic acid residue, an L-histidine residue, an L-serine residue and a one-nickel three-iron three-sulfur three-oxygen cluster to tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide.
PubMed:2550436
RESID:AA0293
Ni-3Fe-2S-3O cluster
carbon monoxide dehydrogenase nickel-iron cofactor
hybrid nickel-triiron cluster
mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-O5-glutamato 1-iron-S5-cysteine persulfido-O3-serinyl 2-nickel-3,4-bis-(S-cysteinyl iron)
tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide
A protein modification that effectively crosslinks an L-asparagine residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine and the release of ammonia.
-17.03
C 0 H -3 N -1 O 0
-17.026548
C 10 H 15 N 3 O 3
225.25
225.11134
K, N
natural
uniprot.ptm:PTM-0153
(2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid
CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn)
N(epsilon)-(beta-aspartyl)lysine
N-(beta-Aspartyl)-Lysine (Crosslink)
N6-(L-isoaspartyl)-L-lysine
XLNK-4Asp-N6Lys(Asn)
beta-(N6-lysyl)aspartyl acid
isoaspartyl N6-lysine
PSI-MOD
MOD:00299
Cross-link 2.
N6-(L-isoaspartyl)-L-lysine (Asn)
A protein modification that effectively crosslinks an L-asparagine residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine and the release of ammonia.
ChEBI:21862
DeltaMass:0
PubMed:11000116
PubMed:6503713
RESID:AA0294
(2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid
CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn)
N(epsilon)-(beta-aspartyl)lysine
N-(beta-Aspartyl)-Lysine (Crosslink)
N6-(L-isoaspartyl)-L-lysine
XLNK-4Asp-N6Lys(Asn)
beta-(N6-lysyl)aspartyl acid
isoaspartyl N6-lysine
A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl-5-poly(ADP-ribose).
E
natural
Unimod:213
(S)-2-amino-5-poly[2'-adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with 1alpha-D-ribofuranosyl]oxy-5-oxopentanoic acid
L-glutamyl-5-poly(ADP-ribose)
L-isoglutamyl-poly(ADP-ribose)
MOD_RES PolyADP-ribosyl glutamic acid
O-ADP-ribosylation (on Glutamate or C terminus)
PSI-MOD
ADP Ribose addition
ADP-Ribosyl
MOD:00300
L-glutamyl-5-poly(ADP-ribose)
A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl-5-poly(ADP-ribose).
DeltaMass:0
PubMed:11246023
PubMed:15842200
PubMed:8533153
RESID:AA0295
Unimod:213#E
(S)-2-amino-5-poly[2'-adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with 1alpha-D-ribofuranosyl]oxy-5-oxopentanoic acid
L-glutamyl-5-poly(ADP-ribose)
L-isoglutamyl-poly(ADP-ribose)
MOD_RES PolyADP-ribosyl glutamic acid
O-ADP-ribosylation (on Glutamate or C terminus)
ADP Ribose addition
ADP-Ribosyl
A protein modification that effectively converts an L-serine residue to O-(N-acetylglucosamine-1-phosphoryl)-L-serine.
283.17
C 8 H 14 N 1 O 8 P 1
283.04572
C 11 H 19 N 2 O 10 P 1
370.25
370.07773
S
natural
Unimod:428
uniprot.ptm:PTM-0586
(2S)-2-amino-3-[([(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy][hydroxy]phosphoryl)oxy]propanoic acid
CARBOHYD O-linked (GalNAcP) serine
O-(N-acetylglucosamine-1-phosphoryl)-L-serine
O-GlcNAc-1-phosphorylation (of Serine)
O-beta(N-acetyl-glucosamine-alpha1-phosphate)serine
O3-(N-acetylglucosamine-1-phosphoryl)-L-serine
O3-L-serine 2-(acetylamino)-2-deoxy-D-glucopyranose 1-phosphodiester
PSI-MOD
N-acetylglucosamine-1-phosphoryl
PhosphoHexNAc
MOD:00301
O-(N-acetylglucosamine-1-phosphoryl)-L-serine
A protein modification that effectively converts an L-serine residue to O-(N-acetylglucosamine-1-phosphoryl)-L-serine.
DeltaMass:0
PubMed:6438439
PubMed:6993483
PubMed:8631906
RESID:AA0296
Unimod:428
(2S)-2-amino-3-[([(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy][hydroxy]phosphoryl)oxy]propanoic acid
CARBOHYD O-linked (GalNAcP) serine
O-(N-acetylglucosamine-1-phosphoryl)-L-serine
O-GlcNAc-1-phosphorylation (of Serine)
O-beta(N-acetyl-glucosamine-alpha1-phosphate)serine
O3-(N-acetylglucosamine-1-phosphoryl)-L-serine
O3-L-serine 2-(acetylamino)-2-deoxy-D-glucopyranose 1-phosphodiester
N-acetylglucosamine-1-phosphoryl
PhosphoHexNAc
A protein modification that effectively converts an L-serine residue to O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine.
242.12
C 6 H 11 N 0 O 8 P 1
242.01915
C 9 H 16 N 1 O 10 P 1
329.2
329.05118
S
natural
Unimod:429
uniprot.ptm:PTM-0594
CARBOHYD O-linked (Man1P) serine
O-(D-mannose-1-phosphoryl)-L-serine
O-(alpha-D-mannosyl-1-phosphoryl)-L-serine
O-[alpha-D-mannopyranosyloxy(hydroxy)phosphoryl]-L-serine
O3-(D-mannose-1-phosphoryl)-L-serine
O3-L-serine alpha-D-mannopyranose 1-phosphodiester
PSI-MOD
PhosphoHex
phosphoglycosyl-D-mannose-1-phosphoryl
MOD:00302
O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine
A protein modification that effectively converts an L-serine residue to O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine.
PubMed:10037765
PubMed:15649890
RESID:AA0297
Unimod:429
CARBOHYD O-linked (Man1P) serine
O-(D-mannose-1-phosphoryl)-L-serine
O-(alpha-D-mannosyl-1-phosphoryl)-L-serine
O-[alpha-D-mannopyranosyloxy(hydroxy)phosphoryl]-L-serine
O3-(D-mannose-1-phosphoryl)-L-serine
O3-L-serine alpha-D-mannopyranose 1-phosphodiester
PhosphoHex
phosphoglycosyl-D-mannose-1-phosphoryl
A protein modification that effectively converts seven L-histidinine residues and a four-copper one-sulfur one-hydroxide cluster to heptakis-L-histidino tetracopper mu4-sulfide hydroxide.
296.19
C 0 Cu 4 H -6 N 0 O 1 S 1
293.63843
C 42 Cu 4 H 43 N 21 O 8 S 1
1256.19
1253.0508
H, H, H, H, H, H, H
natural
heptakis-L-histidino tetracopper mu4-sulfide hydroxide
mu4-sulfido bis(bis-N1'-histidino copper)(N1'-histidino-N3'-histidino copper)(N3'-histidino hydroxide copper)
nitrous oxide reductase nosZ CuZ cluster
pentakis-L-N1'-histidino-bis-L-N3'-histidino tetracopper sulfide hydroxide
PSI-MOD
MOD:00303
Cross-link 7.
heptakis-L-histidino tetracopper mu4-sulfide hydroxide
A protein modification that effectively converts seven L-histidinine residues and a four-copper one-sulfur one-hydroxide cluster to heptakis-L-histidino tetracopper mu4-sulfide hydroxide.
PubMed:11024061
PubMed:11041839
RESID:AA0298
heptakis-L-histidino tetracopper mu4-sulfide hydroxide
mu4-sulfido bis(bis-N1'-histidino copper)(N1'-histidino-N3'-histidino copper)(N3'-histidino hydroxide copper)
nitrous oxide reductase nosZ CuZ cluster
pentakis-L-N1'-histidino-bis-L-N3'-histidino tetracopper sulfide hydroxide
A protein modification that effectively converts an L-leucine residue to L-leucine methyl ester.
14.03
C 1 H 2 N 0 O 0
14.01565
C 7 H 14 N 1 O 2
144.19
144.10245
L
natural
C-term
Unimod:34
uniprot.ptm:PTM-0167
2-amino-4-methylpentanoic methyl ester
L-leucine methyl ester
MOD_RES Leucine methyl ester
OMeLeu
alpha-aminoisocaproic methyl ester
methyl (2S)-2-amino-4-methylpentanoate
methyl L-leucinate
methyl esterified L-leucine
PSI-MOD
Methyl
Methylation
MOD:00304
incidental to RESID:AA0039
L-leucine methyl ester
A protein modification that effectively converts an L-leucine residue to L-leucine methyl ester.
PubMed:10191253
PubMed:11875433
PubMed:8206937
RESID:AA0299
Unimod:34#C-term
2-amino-4-methylpentanoic methyl ester
L-leucine methyl ester
MOD_RES Leucine methyl ester
OMeLeu
alpha-aminoisocaproic methyl ester
methyl (2S)-2-amino-4-methylpentanoate
methyl L-leucinate
methyl esterified L-leucine
Methyl
Methylation
A protein modification that effectively converts six L-cysteine residues, an L-serine residue and a eight-iron seven-sulfur cluster to hexakis-L-cysteinyl L-serinyl octairon heptasulfide.
663.12
C 0 Fe 8 H -8 N 0 O 0 S 7
663.223
3-
C 21 Fe 8 H 27 N 7 O 8 S 13
1369.03
1368.3102
C, C, C, C, C, C, S
natural
Cys6Ser-[8Fe7S]
METAL Iron-sulfur (8Fe-7S)
hexakis-L-cysteinyl L-serinyl octairon heptasulfide
nitrogenase P-cluster
PSI-MOD
MOD:00305
Cross-link 7; incidental to RESID:AA0141.
hexakis-L-cysteinyl L-serinyl octairon heptasulfide
A protein modification that effectively converts six L-cysteine residues, an L-serine residue and a eight-iron seven-sulfur cluster to hexakis-L-cysteinyl L-serinyl octairon heptasulfide.
PubMed:10525412
PubMed:12215645
PubMed:9063865
RESID:AA0300
Cys6Ser-[8Fe7S]
METAL Iron-sulfur (8Fe-7S)
hexakis-L-cysteinyl L-serinyl octairon heptasulfide
nitrogenase P-cluster
Natural or modified residues with a mass of 113.084064 Da.
0.0
C 0 H 0 N 0 O 0
0.0
C 6 H 11 N 1 O 1
113.16
113.08406
X
L-isoleucine or L-leucine
Xle
PSI-MOD
MOD:00306
residues isobaric at 113.084064 Da
Natural or modified residues with a mass of 113.084064 Da.
PubMed:10523135
RESID:AA0301
L-isoleucine or L-leucine
Xle
A protein modification that effectively cyclizes an L-asparagine residue to form a carboxyl-terminal L-aspartimide.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 4 H 5 N 2 O 2
113.1
113.0351
N
natural
C-term
Unimod:23
(3S)-3-amino-2,5-pyrrolidinedione
2-amino-butanimide
ASI
L-2-aminosuccinimide
L-asparaginimide
L-aspartimide
Succinimide formation from asparagine
alpha-aminosuccinimide
PSI-MOD
Dehydrated
Dehydration
L-3-aminosuccinimide
MOD:00307
From DeltaMass: Average Mass: -17 Average Mass Change:-17 References:Clarke, S., Lability of Aspargine and Aspartic Acid Residues in Protein and Peptides, in: Stability of Protein Pharmaceuticals : Chemical and Physical Paths of Protein Degradation, Part A (T.J. Ahern and M.C. Manning, eds.), 1992,Plenum Press, New York, pp.1-29Xie, M.; Vander Velde, D.; Morton, M.; Borchardt, R.T.; Schowen,R.L.: pH-Induced Change in the Rate-Determining Step for the Hydrolysis of the Asp/Asn-Derived Cyclic-Imide Intermediate in Protein Degradation. (1996) J. Am. Chem. Soc. 118: 8955-8956.
L-aspartimide
A protein modification that effectively cyclizes an L-asparagine residue to form a carboxyl-terminal L-aspartimide.
DeltaMass:18
PubMed:12771378
PubMed:2378679
PubMed:7662664
PubMed:7988548
PubMed:9309583
RESID:AA0302
Unimod:23#N
(3S)-3-amino-2,5-pyrrolidinedione
2-amino-butanimide
ASI
L-2-aminosuccinimide
L-asparaginimide
L-aspartimide
Succinimide formation from asparagine
alpha-aminosuccinimide
Dehydrated
Dehydration
L-3-aminosuccinimide
A protein modification that effectively cyclizes an L-glutamine residue to form a carboxyl-terminal L-glutamimide.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 5 H 7 N 2 O 2
127.12
127.05075
Q
hypothetical
C-term
Unimod:23
(3S)-3-aminopiperidine-2,6-dione
2-aminopentanimide
3-amino-2,6-piperidinedione
L-glutamimide
alpha-aminoglutarimide
PSI-MOD
Dehydrated
Dehydration
MOD:00308
L-glutamimide
A protein modification that effectively cyclizes an L-glutamine residue to form a carboxyl-terminal L-glutamimide.
PubMed:12771378
PubMed:14593103
RESID:AA0303
Unimod:23#Q
(3S)-3-aminopiperidine-2,6-dione
2-aminopentanimide
3-amino-2,6-piperidinedione
L-glutamimide
alpha-aminoglutarimide
Dehydrated
Dehydration
A protein modification that effectively converts an L-aspartic acid residue to L-beta-carboxyaspartic acid.
44.01
C 1 H 0 N 0 O 2
43.98983
C 5 H 5 N 1 O 5
159.1
159.01677
D
hypothetical
Unimod:299
(2S)-2-aminoethane-1,1,2-tricarboxylic acid
2-amino-3-carboxybutanedioic acid
3-carboxy-L-aspartic acid
3-carboxyaspartic acid
3CbxAsp
beta-carboxyaspartic acid
gammacarboxyld
PSI-MOD
Carboxy
Carboxylation
MOD:00309
References to this modification as a gamma-carboxylation are in error [JSG].
L-beta-carboxyaspartic acid
A protein modification that effectively converts an L-aspartic acid residue to L-beta-carboxyaspartic acid.
OMSSA:47
PubMed:6390094
PubMed:7138832
PubMed:7457858
PubMed:8135347
RESID:AA0304
Unimod:299#D
(2S)-2-aminoethane-1,1,2-tricarboxylic acid
2-amino-3-carboxybutanedioic acid
3-carboxy-L-aspartic acid
3-carboxyaspartic acid
3CbxAsp
beta-carboxyaspartic acid
gammacarboxyld
Carboxy
Carboxy
Carboxylation
A protein modification that effectively converts an L-arginine residue to N5-methyl-L-arginine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 7 H 14 N 4 O 1
170.22
170.11676
R
hypothetical
uniprot.ptm:PTM-0185
(2S)-2-amino-5-(N-methylcarbamimidamido)pentanoic acid
MOD_RES N5-methylarginine
N5-carbamimidoyl-N5-methyl-L-ornithine
N5-methyl-L-arginine
N5-methylated L-arginine
N5Me1Arg
delta-N-methylarginine
PSI-MOD
Methyl
Methylation
MOD:00310
N5-methyl-L-arginine
A protein modification that effectively converts an L-arginine residue to N5-methyl-L-arginine.
PubMed:11875433
PubMed:9792625
PubMed:9873020
RESID:AA0305
(2S)-2-amino-5-(N-methylcarbamimidamido)pentanoic acid
MOD_RES N5-methylarginine
N5-carbamimidoyl-N5-methyl-L-ornithine
N5-methyl-L-arginine
N5-methylated L-arginine
N5Me1Arg
delta-N-methylarginine
Methyl
Methylation
A protein modification that effectively converts an L-cysteine residue to L-cysteine coenzyme A disulfide.
765.52
C 21 H 34 N 7 O 16 P 3 S 1
765.09955
C 24 H 39 N 8 O 17 P 3 S 2
868.66
868.10876
C
hypothetical
Unimod:281
(2R)-2-amino-3-(2-((3-(((2R)-2,4-dihydroxy-3,3-dimethyl-1-oxobutyl)amino)-1-oxopropyl)amino)ethyl)dithio-propanoic acid 4'-ester with adenosine 5'-(trihydrogen diphosphate) 3'-(dihydrogen phosphate)
L-cysteine coenzyme A disulfide
SCoACys
coenzyme A L-cysteine mixed disulfide
PSI-MOD
CoenzymeA
Cysteine modified Coenzyme A
MOD:00311
DeltaMass gives no formula with mass as 454.
L-cysteine coenzyme A disulfide
A protein modification that effectively converts an L-cysteine residue to L-cysteine coenzyme A disulfide.
DeltaMass:0
PubMed:1734967
RESID:AA0306
Unimod:281#C
(2R)-2-amino-3-(2-((3-(((2R)-2,4-dihydroxy-3,3-dimethyl-1-oxobutyl)amino)-1-oxopropyl)amino)ethyl)dithio-propanoic acid 4'-ester with adenosine 5'-(trihydrogen diphosphate) 3'-(dihydrogen phosphate)
L-cysteine coenzyme A disulfide
SCoACys
coenzyme A L-cysteine mixed disulfide
CoenzymeA
Cysteine modified Coenzyme A
A protein modification that effectively converts an L-cysteine residue to S-myristoyl-L-cysteine.
210.36
C 14 H 26 N 0 O 1 S 0
210.19836
C 17 H 31 N 1 O 2 S 1
313.5
313.20755
C
hypothetical
Unimod:45
(R)-2-amino-3-(tetradecanoylsulfanyl)propanoic acid
LIPID S-myristoyl cysteine
S-(C14:1 aliphatic acyl)cysteine
S-myristoyl-L-cysteine
S-myristoylated L-cysteine
SMyrCys
tetradecanoate cysteine thioester
PSI-MOD
Myristoyl
Myristoylation
MOD:00312
S-myristoyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-myristoyl-L-cysteine.
PubMed:10026218
PubMed:10080938
PubMed:8824274
RESID:AA0307
Unimod:45#C
(R)-2-amino-3-(tetradecanoylsulfanyl)propanoic acid
LIPID S-myristoyl cysteine
S-(C14:1 aliphatic acyl)cysteine
S-myristoyl-L-cysteine
S-myristoylated L-cysteine
SMyrCys
tetradecanoate cysteine thioester
Myristoyl
Myristoylation
A protein modification that effectively converts an L-cysteine residue to S-palmitoleyl-L-cysteine.
236.4
C 16 H 28 N 0 O 1 S 0
236.21402
C 19 H 33 N 1 O 2 S 1
339.54
339.2232
C
hypothetical
Unimod:431
uniprot.ptm:PTM-0645
(R)-2-amino-3-((Z)-9-hexadecenoylsulfanyl)propanoic acid
S-palmitoleyl-L-cysteine
S-palmitoleylated L-cysteine
SPamD1Cys
cis-9-hexadecenoate cysteine thioester
mod187
PSI-MOD
Palmitoleyl
palmitoleyl
MOD:00313
S-palmitoleyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-palmitoleyl-L-cysteine.
OMSSA:187
PubMed:8294460
RESID:AA0308
Unimod:431#C
(R)-2-amino-3-((Z)-9-hexadecenoylsulfanyl)propanoic acid
S-palmitoleyl-L-cysteine
S-palmitoleylated L-cysteine
SPamD1Cys
cis-9-hexadecenoate cysteine thioester
mod187
Palmitoleyl
palmitoleyl
A protein modification that effectively converts a glycine residue to glycine cholesterol ester.
368.65
C 27 H 44 N 0 O 0
368.3443
C 29 H 48 N 1 O 2
442.71
442.3685
G
natural
C-term
Unimod:432
uniprot.ptm:PTM-0090
LIPID Cholesterol glycine ester
cholesteryl glycinate
glycine cholest-5-en-3beta-ol ester
glycine cholesterol ester
hedgehog lipophilic adduct
PSI-MOD
C-cholesterol
cholesterol ester
MOD:00314
Incidental to RESID:AA0060. Unimod origin corrected [JSG].
glycine cholesterol ester
A protein modification that effectively converts a glycine residue to glycine cholesterol ester.
ChEBI:143135
PubMed:11111088
PubMed:8824192
RESID:AA0309
Unimod:432#C-term
LIPID Cholesterol glycine ester
cholesteryl glycinate
glycine cholest-5-en-3beta-ol ester
glycine cholesterol ester
hedgehog lipophilic adduct
C-cholesterol
cholesterol ester
A protein modification that effectively converts five L-cysteine residues, an L-histidine residue and a one-nickel four-iron five-sulfur cluster to pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide.
436.33
C 0 Fe 4 H -6 N 0 Ni 1 O 0 S 5
435.4885
C 21 Fe 4 H 26 N 8 Ni 1 O 6 S 10
1089.16
1087.5934
C, C, C, C, C, H
natural
METAL Nickel-iron-sulfur (Ni-4Fe-5S)
METAL Nickel-iron-sulfur (Ni-4Fe-5S); via tele nitrogen
Ni-4Fe-5S cluster
carbon monoxide dehydrogenase nickel-iron cofactor
mu-1:2kappaS-sulfido-mu3-1:3:5kappaS-sulfido-mu3-2:3:4kappaS-sulfido-mu3-2:4:5kappaS-sulfido-mu3-3:4:5kappaS-sulfido-N1'-histidino-S-cysteinyl-1-iron-S-cysteinyl-2-nickel-3,4,5-tris-(S-cysteinyl iron)
pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide
PSI-MOD
MOD:00315
Cross-link 6.
pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide
A protein modification that effectively converts five L-cysteine residues, an L-histidine residue and a one-nickel four-iron five-sulfur cluster to pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide.
PubMed:11509720
PubMed:2550436
RESID:AA0310
METAL Nickel-iron-sulfur (Ni-4Fe-5S)
METAL Nickel-iron-sulfur (Ni-4Fe-5S); via tele nitrogen
Ni-4Fe-5S cluster
carbon monoxide dehydrogenase nickel-iron cofactor
mu-1:2kappaS-sulfido-mu3-1:3:5kappaS-sulfido-mu3-2:3:4kappaS-sulfido-mu3-2:4:5kappaS-sulfido-mu3-3:4:5kappaS-sulfido-N1'-histidino-S-cysteinyl-1-iron-S-cysteinyl-2-nickel-3,4,5-tris-(S-cysteinyl iron)
pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide
A protein modification that effectively converts an L-asparagine residue to N4,N4-dimethyl-L-asparagine.
28.05
C 2 H 4 N 0 O 0
28.0313
C 6 H 10 N 2 O 2
142.16
142.07423
N
hypothetical
Unimod:36
uniprot.ptm:PTM-0182
(2S)-2-amino-4-(dimethylamino)-4-oxobutanoic acid
2-amino-N4,N4-dimethylbutanediamic acid
MOD_RES N4,N4-dimethylasparagine
N(gamma),N(gamma)-dimethylasparagine
N4,N4-dimethyl-L-asparagine
N4,N4-dimethylated L-asparagine
N4Me2Asn
PSI-MOD
Dimethyl
beta-dimethylasparagine
di-Methylation
MOD:00316
N4,N4-dimethyl-L-asparagine
A protein modification that effectively converts an L-asparagine residue to N4,N4-dimethyl-L-asparagine.
PubMed:12964758
PubMed:14570711
PubMed:8783012
RESID:AA0311
Unimod:36#N
(2S)-2-amino-4-(dimethylamino)-4-oxobutanoic acid
2-amino-N4,N4-dimethylbutanediamic acid
MOD_RES N4,N4-dimethylasparagine
N(gamma),N(gamma)-dimethylasparagine
N4,N4-dimethyl-L-asparagine
N4,N4-dimethylated L-asparagine
N4Me2Asn
Dimethyl
beta-dimethylasparagine
di-Methylation
A protein modification that effectively converts an L-lysine residue to N6-3,4-didehydroretinylidene-L-lysine.
264.41
C 20 H 24 N 0 O 0
264.1878
C 26 H 36 N 2 O 1
392.59
392.28278
K
natural
Unimod:433
(S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohexa-1,3-dien-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid
N6-(3,4-didehydroretinylidene)-L-lysine
N6-3-dehydroretinal-L-lysine
N6-3-dehydroretinyl-lysine
PSI-MOD
3,4-didehydroretinylidene
Didehydroretinylidene
MOD:00317
N6-3,4-didehydroretinylidene-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-3,4-didehydroretinylidene-L-lysine.
PubMed:10717661
PubMed:3257009
PubMed:4056688
RESID:AA0312
Unimod:433#K
(S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohexa-1,3-dien-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid
N6-(3,4-didehydroretinylidene)-L-lysine
N6-3-dehydroretinal-L-lysine
N6-3-dehydroretinyl-lysine
3,4-didehydroretinylidene
Didehydroretinylidene
A protein modification that effectively cross-links an L-cysteine residue and an L-tryptophan residue by a thioether bond to form 4'-(S-L-cysteinyl)-L-tryptophyl quinone.
27.97
C 0 H -4 N 0 O 2 S 0
27.958529
C 14 H 11 N 3 O 4 S 1
317.32
317.04703
C, W
natural
uniprot.ptm:PTM-0041
(2R)-2-amino-3-[(3-[(2S)-2-amino-2-carboxyethyl]-6,7-dioxo-6,7-dihydro-1H-indol-4-yl)sulfanyl]propanoic acid
3-(2-amino-2-carboxyethyl)-4-[2-amino-2-carboxyethyl]sulfanyl-6,7-indolinedione
4'-(L-cystein-S-yl)-L-tryptophyl quinone
4-(S-cysteinyl)tryptophan-6,7-dione
CROSSLNK 4'-cysteinyl-tryptophylquinone (Cys-Trp)
CTQ
cysteine tryptophylquinone
PSI-MOD
MOD:00318
Cross-link 2; secondary to RESID:AA0148.
4'-(S-L-cysteinyl)-L-tryptophyl quinone
A protein modification that effectively cross-links an L-cysteine residue and an L-tryptophan residue by a thioether bond to form 4'-(S-L-cysteinyl)-L-tryptophyl quinone.
PubMed:11555656
PubMed:11717396
RESID:AA0313
(2R)-2-amino-3-[(3-[(2S)-2-amino-2-carboxyethyl]-6,7-dioxo-6,7-dihydro-1H-indol-4-yl)sulfanyl]propanoic acid
3-(2-amino-2-carboxyethyl)-4-[2-amino-2-carboxyethyl]sulfanyl-6,7-indolinedione
4'-(L-cystein-S-yl)-L-tryptophyl quinone
4-(S-cysteinyl)tryptophan-6,7-dione
CROSSLNK 4'-cysteinyl-tryptophylquinone (Cys-Trp)
CTQ
cysteine tryptophylquinone
A protein modification that effectively cross-links an L-cysteine residue and an L-aspartic acid residue by a thioether bond to form 2-(S-L-cysteinyl)-L-aspartic acid.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 7 H 8 N 2 O 4 S 1
216.21
216.02048
C, D
natural
uniprot.ptm:PTM-0025
(2R,3S)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanedioic acid
(2R,3S,6R)-2,6-diamino-3-carboxy-4-thiaheptanedioic acid
3-(L-cystein-S-yl)-L-aspartic acid
3-carboxy-L-lanthionine
CROSSLNK 3-cysteinyl-aspartic acid (Cys-Asp)
PSI-MOD
MOD:00319
Cross-link 2.
3-(S-L-cysteinyl)-L-aspartic acid
A protein modification that effectively cross-links an L-cysteine residue and an L-aspartic acid residue by a thioether bond to form 2-(S-L-cysteinyl)-L-aspartic acid.
PubMed:11555656
PubMed:11717396
RESID:AA0314
(2R,3S)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanedioic acid
(2R,3S,6R)-2,6-diamino-3-carboxy-4-thiaheptanedioic acid
3-(L-cystein-S-yl)-L-aspartic acid
3-carboxy-L-lanthionine
CROSSLNK 3-cysteinyl-aspartic acid (Cys-Asp)
A protein modification that effectively cross-links an L-cysteine residue and an L-glutamic acid residue by a thioether bond to form 4-(S-L-cysteinyl)-L-glutamic acid.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 8 H 10 N 2 O 4 S 1
230.24
230.03613
C, E
natural
uniprot.ptm:PTM-0040
(2S,3S,7R)-2,7-diamino-4-carboxy-5-thiaoctanedioic acid
(2S,4S)-2-amino-4-[(R)-2-amino-2-carboxyethyl]sulfanylpentanedioic acid
4-(L-cystein-S-yl)-L-glutamic acid
CROSSLNK 4-cysteinyl-glutamic acid (Cys-Glu)
PSI-MOD
MOD:00320
Cross-link 2.
4-(S-L-cysteinyl)-L-glutamic acid
A protein modification that effectively cross-links an L-cysteine residue and an L-glutamic acid residue by a thioether bond to form 4-(S-L-cysteinyl)-L-glutamic acid.
ChEBI:20293
PubMed:11555656
PubMed:11717396
RESID:AA0315
(2S,3S,7R)-2,7-diamino-4-carboxy-5-thiaoctanedioic acid
(2S,4S)-2-amino-4-[(R)-2-amino-2-carboxyethyl]sulfanylpentanedioic acid
4-(L-cystein-S-yl)-L-glutamic acid
CROSSLNK 4-cysteinyl-glutamic acid (Cys-Glu)
A protein modification that effectively converts an L-aspartic acid residue to cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester.
294.39
C 17 H 26 N 0 O 4
294.1831
C 21 H 31 N 1 O 7
409.48
409.21005
D
natural
Unimod:434
uniprot.ptm:PTM-0091
(7Z,14Xi)-14-[(S)-3-amino-3-carboxy-propanoyl]oxy-10,13-dioxo-7-heptadecenoic acid
LIPID Cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester
barley lipid transfer protein modification
cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester
PSI-MOD
CHDH
cis-14-hydroxy-10,13-dioxo-7-heptadecenoic ester
MOD:00321
cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester
A protein modification that effectively converts an L-aspartic acid residue to cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester.
PubMed:11435437
PubMed:7949339
RESID:AA0316
Unimod:434#D
(7Z,14Xi)-14-[(S)-3-amino-3-carboxy-propanoyl]oxy-10,13-dioxo-7-heptadecenoic acid
LIPID Cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester
barley lipid transfer protein modification
cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester
CHDH
cis-14-hydroxy-10,13-dioxo-7-heptadecenoic ester
A protein modification that effectively converts an L-histidine residue to tele-methyl-L-histidine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 7 H 9 N 3 O 1
151.17
151.07455
H
natural
uniprot.ptm:PTM-0290
(S)-2-amino-3-(1-methyl-1H-imidazol-4-yl)propanoic acid
1'-methyl-L-histidine
MOD_RES Tele-methylhistidine
N(epsilon)-methylhistidine
N(tau)-methylhistidine
NteleMeHis
tele-methylated L-histidine
tele-methylhistidine
PSI-MOD
3-methylhistidine
4-methyl-histidine
Methyl
Methylation
MOD:00322
1'-methyl-L-histidine
A protein modification that effectively converts an L-histidine residue to tele-methyl-L-histidine.
PubMed:10601317
PubMed:11474090
PubMed:11875433
PubMed:6692818
PubMed:8076
PubMed:8645219
RESID:AA0317
(S)-2-amino-3-(1-methyl-1H-imidazol-4-yl)propanoic acid
1'-methyl-L-histidine
MOD_RES Tele-methylhistidine
N(epsilon)-methylhistidine
N(tau)-methylhistidine
NteleMeHis
tele-methylated L-histidine
tele-methylhistidine
3-methylhistidine
4-methyl-histidine
Methyl
Methylation
A protein modification that effectively converts an L-lysine residue to L-lysine methyl ester.
14.03
C 1 H 2 N 0 O 0
14.01565
C 7 H 15 N 2 O 2
159.21
159.11336
K
natural
C-term
Unimod:34
uniprot.ptm:PTM-0170
2,6-diaminohexanoic methyl ester
L-lysine methyl ester
MOD_RES Lysine methyl ester
OMeLys
alpha,epsilon-diaminocaproic methyl ester
methyl (S)-2,6-diaminohexanoate
methyl L-lysinate
methyl esterified L-lysine
PSI-MOD
Methyl
Methylation
MOD:00323
L-lysine methyl ester
A protein modification that effectively converts an L-lysine residue to L-lysine methyl ester.
PubMed:10973948
PubMed:11875433
RESID:AA0318
Unimod:34#C-term
2,6-diaminohexanoic methyl ester
L-lysine methyl ester
MOD_RES Lysine methyl ester
OMeLys
alpha,epsilon-diaminocaproic methyl ester
methyl (S)-2,6-diaminohexanoate
methyl L-lysinate
methyl esterified L-lysine
Methyl
Methylation
A protein modification that effectively converts an L-serine residue to L-serinyl molybdenum bis(molybdopterin guanine dinucleotide).
1588.01
C 40 H 47 Mo 1 N 20 O 27 P 4 S 4
1588.9807
C 43 H 52 Mo 1 N 21 O 29 P 4 S 4
1675.09
1676.0127
S
natural
2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide
L-serinyl molybdenum bis(molybdopterin guanine dinucleotide)
bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-O3-serinyl-molybdenum oxide
PSI-MOD
MOD:00324
L-serinyl molybdenum bis(molybdopterin guanine dinucleotide)
A protein modification that effectively converts an L-serine residue to L-serinyl molybdenum bis(molybdopterin guanine dinucleotide).
PubMed:8658132
PubMed:8658134
RESID:AA0319
2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide
L-serinyl molybdenum bis(molybdopterin guanine dinucleotide)
bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-O3-serinyl-molybdenum oxide
A protein modification that effectively converts an L-asparagine residue to L-beta-methylthioasparagine.
46.09
C 1 H 2 N 0 O 0 S 1
45.98772
C 5 H 8 N 2 O 2 S 1
160.19
160.03065
N
hypothetical
Unimod:39
(2R,3Xi)-2-amino-3-(methylsulfanyl)-4-butanediamic acid
2,4-diamino-3-(methylsulfanyl)-4-oxobutanoic acid
3-(methylthio)-L-asparagine
3-carboxamido-S-methyl-cysteine
beta-(methylthio)asparagine
PSI-MOD
Beta-methylthiolation
Methylthio
MOD:00325
This modification was predicted for ribosomal protein S12 in Bacillus subtilis when the sequence in the original version of the genome was reported to have asparagine rather than aspartic acid at the position of the methylthioaspartic acid modification (see MOD:00237). Two groups independently confirmed that the genome sequence was incorrect. The sequence in the revised genome has aspartic acid at that position. This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
L-beta-methylthioasparagine
A protein modification that effectively converts an L-asparagine residue to L-beta-methylthioasparagine.
RESID:AA0320
Unimod:39#N
(2R,3Xi)-2-amino-3-(methylsulfanyl)-4-butanediamic acid
2,4-diamino-3-(methylsulfanyl)-4-oxobutanoic acid
3-(methylthio)-L-asparagine
3-carboxamido-S-methyl-cysteine
beta-(methylthio)asparagine
Beta-methylthiolation
Methylthio
A protein modification that effectively converts an L-lysine residue to L-pyrrolysine (not known as a natural, post-translational modification process).
109.13
C 6 H 7 N 1 O 1
109.052765
C 12 H 19 N 3 O 2
237.3
237.14772
K
artifact
Unimod:435
(2S)-2-amino-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]aminohexanoic acid
2-azanyl-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]azanylhexanoic acid
L-pyrrolysine
N6-(4-methyl-1,2-didehydropyrrolidine-5-carboxyl)-L-lysine
N6-(4-methyl-delta-1-pyrroline-5-carboxyl)-L-lysine
N6-([(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl)-L-lysine
NON_STD Pyrrolysine
Pyl(Lys)
monomethylamine methyltransferase cofactor lysine adduct
PSI-MOD
MOD:00326
This entry is for the artifactual formation of L-pyrrolysine from lysine. For encoded L-pyrrolysine, use MOD:01187 [JSG].
L-pyrrolysine (Lys)
A protein modification that effectively converts an L-lysine residue to L-pyrrolysine (not known as a natural, post-translational modification process).
PubMed:11435424
PubMed:12029131
PubMed:12029132
PubMed:15314242
PubMed:16096277
RESID:AA0321#LYS
Unimod:435#K
(2S)-2-amino-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]aminohexanoic acid
2-azanyl-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]azanylhexanoic acid
L-pyrrolysine
N6-(4-methyl-1,2-didehydropyrrolidine-5-carboxyl)-L-lysine
N6-(4-methyl-delta-1-pyrroline-5-carboxyl)-L-lysine
N6-([(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl)-L-lysine
NON_STD Pyrrolysine
Pyl(Lys)
monomethylamine methyltransferase cofactor lysine adduct
A protein modification that effectively converts an L-tryptophan residue to a 3-hydroxy-L-tryptophan.
16.0
C 0 H 0 N 0 O 1
15.994915
C 11 H 10 N 2 O 2
202.21
202.07423
W
hypothetical
uniprot.ptm:PTM-0031
(2S,3S)-2-amino-3-hydroxy-3-(1H-indol-3-yl)propanoic acid
3-hydroxy-L-tryptophan
3-hydroxylated L-tryptophan
3-hydroxytryptophan
3HyTrp
MOD_RES 3-hydroxytryptophan
beta-hydroxytryptophan
PSI-MOD
MOD:00327
3-hydroxy-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to a 3-hydroxy-L-tryptophan.
ChEBI:141794
PubMed:10024453
PubMed:11457355
RESID:AA0322
(2S,3S)-2-amino-3-hydroxy-3-(1H-indol-3-yl)propanoic acid
3-hydroxy-L-tryptophan
3-hydroxylated L-tryptophan
3-hydroxytryptophan
3HyTrp
MOD_RES 3-hydroxytryptophan
beta-hydroxytryptophan
A protein modification that effectively crosslinks an L-tyrosine residue and the 3'-end of DNA through a phosphodiester bond to form O4'-(phospho-3'-DNA)-L-tyrosine.
Y
natural
(S)-2-amino-3-[4-(3'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid
ACT_SITE O-(3'-phospho-DNA)-tyrosine intermediate
O4'-(phospho-3'-DNA)-L-tyrosine
O4'-L-tyrosine 3'-DNA phosphodiester
PSI-MOD
MOD:00328
O4'-(phospho-3'-DNA)-L-tyrosine
A protein modification that effectively crosslinks an L-tyrosine residue and the 3'-end of DNA through a phosphodiester bond to form O4'-(phospho-3'-DNA)-L-tyrosine.
PubMed:2211714
RESID:AA0323
(S)-2-amino-3-[4-(3'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid
ACT_SITE O-(3'-phospho-DNA)-tyrosine intermediate
O4'-(phospho-3'-DNA)-L-tyrosine
O4'-L-tyrosine 3'-DNA phosphodiester
A protein modification that effectively results from forming an adduct between a glutamic acid residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
614.48
C 34 Fe 1 H 30 N 4 O 4
614.1616
C 39 Fe 1 H 37 N 5 O 7
743.6
743.2042
E
natural
Unimod:436
5-hydroxymethyl protoporphyrin IX 5-glutamate ester
BINDING Heme (covalent; via 1 link)
[3-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-7,12-diethenyl-8,13,17-trimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
cytochrome P450 CYP4A family heme cofactor
hydroxyheme-L-glutamate ester
PSI-MOD
Hydroxyheme
hydroxyheme
MOD:00329
hydroxyheme-L-glutamate ester
A protein modification that effectively results from forming an adduct between a glutamic acid residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
PubMed:11139583
PubMed:11821421
PubMed:11980497
RESID:AA0324
Unimod:436#E
5-hydroxymethyl protoporphyrin IX 5-glutamate ester
BINDING Heme (covalent; via 1 link)
[3-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-7,12-diethenyl-8,13,17-trimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
cytochrome P450 CYP4A family heme cofactor
hydroxyheme-L-glutamate ester
Hydroxyheme
hydroxyheme
A protein modification that effectively converts an L-histidine residue to a (phospho-5'-guanosine)-L-histidine.
345.21
C 10 H 12 N 5 O 7 P 1
345.04742
C 16 H 19 N 8 O 8 P 1
482.35
482.10635
H
natural
Unimod:413
(2S)-2-amino-3-(1-(5'-adenosine phosphono)imidazol-4-yl)propanoic acid
1'-(phospho-5'-guanosine)-L-histidine
ACT_SITE GMP-histidine intermediate
L-histidine 5'-guanosine phosphoramidester
L-histidine monoanhydride with 5'-guanylic acid
N(tau)-5'-guanylic-L-histidine
N1'-guanylylated histidine
tele-5'-guanylic-L-histidine
PSI-MOD
Phosphoguanosine
phospho-guanosine
MOD:00330
(phospho-5'-guanosine)-L-histidine
A protein modification that effectively converts an L-histidine residue to a (phospho-5'-guanosine)-L-histidine.
PubMed:10529169
PubMed:10869342
PubMed:7559521
RESID:AA0325
Unimod:413#H
(2S)-2-amino-3-(1-(5'-adenosine phosphono)imidazol-4-yl)propanoic acid
1'-(phospho-5'-guanosine)-L-histidine
ACT_SITE GMP-histidine intermediate
L-histidine 5'-guanosine phosphoramidester
L-histidine monoanhydride with 5'-guanylic acid
N(tau)-5'-guanylic-L-histidine
N1'-guanylylated histidine
tele-5'-guanylic-L-histidine
Phosphoguanosine
phospho-guanosine
A protein modification that effectively converts four L-cysteine residues and a three-iron four-sulfur cluster to tetrakis-L-cysteinyl triiron tetrasulfide.
291.74
C 0 Fe 3 H -4 N 0 O 0 S 4
291.66345
3-
C 12 Fe 3 H 16 N 4 O 4 S 8
704.3
703.7002
C, C, C, C
hypothetical
bis[bis-L-cysteinyl iron disulfido]iron
di-mu-1:2kappaS-sulfido di-mu-2:3kappaS-sulfido iron bis(bis-S-cysteinyliron)
tetra-mu-sulfido tetrakis-S-L-cysteinyl triiron
tetrakis-L-cysteinyl linear [3Fe-4S] cluster
tetrakis-L-cysteinyl triiron tetrasulfide
tetrakis-L-cysteinyl triiron tetrasulfide D2 cluster
PSI-MOD
MOD:00331
Cross-link 4.
tetrakis-L-cysteinyl triiron tetrasulfide
A protein modification that effectively converts four L-cysteine residues and a three-iron four-sulfur cluster to tetrakis-L-cysteinyl triiron tetrasulfide.
PubMed:11592901
PubMed:11941493
PubMed:2511202
PubMed:6094558
RESID:AA0326
bis[bis-L-cysteinyl iron disulfido]iron
di-mu-1:2kappaS-sulfido di-mu-2:3kappaS-sulfido iron bis(bis-S-cysteinyliron)
tetra-mu-sulfido tetrakis-S-L-cysteinyl triiron
tetrakis-L-cysteinyl linear [3Fe-4S] cluster
tetrakis-L-cysteinyl triiron tetrasulfide
tetrakis-L-cysteinyl triiron tetrasulfide D2 cluster
A protein modification that effectively converts an L-arginine residue to N4-glucosyl-arginine.
162.14
C 6 H 10 N 0 O 5
162.05283
C 12 H 22 N 4 O 6
318.33
318.15393
R
natural
Unimod:41
uniprot.ptm:PTM-0515
(2S)-2-amino-5-(beta-D-glucopyranosyl[imino(methylamino)methyl]amino)pentanoic acid
CARBOHYD N-linked (Glc) arginine
NG-beta-D-glucosylarginine
omega-N-(beta-D-glucosyl)-L-arginine
omega-N-glucosyl-L-arginine
omega-N-glycosyl-L-arginine
PSI-MOD
Hex
Hexose
MOD:00332
omega-N-glucosyl-L-arginine
A protein modification that effectively converts an L-arginine residue to N4-glucosyl-arginine.
PubMed:15279557
PubMed:8521968
PubMed:9536051
RESID:AA0327
Unimod:41#R
(2S)-2-amino-5-(beta-D-glucopyranosyl[imino(methylamino)methyl]amino)pentanoic acid
CARBOHYD N-linked (Glc) arginine
NG-beta-D-glucosylarginine
omega-N-(beta-D-glucosyl)-L-arginine
omega-N-glucosyl-L-arginine
omega-N-glycosyl-L-arginine
Hex
Hexose
A protein modification that effectively converts an L-asparagine residue to (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine.
386.3
C 13 H 19 N 6 O 6 P 1
386.11038
C 17 H 26 N 8 O 9 P 1
517.42
517.156
N
natural
C-term
Unimod:437
uniprot.ptm:PTM-0335
(3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine
5'-O-[(3-aminopropoxy)(L-aspart-1-ylamino)phosphoryl]adenosine
9-(5'-O-[(3-aminopropoxy)(L-aspart-1-ylamino)phosphoryl]-beta-D-ribofuranosyl)adenine
MOD_RES Aspartic acid 1-[(3-aminopropyl)(5'-adenosyl)phosphono]amide
N-(aspart-1-yl)-O-(3-aminopropyl)-O-(5'-adenosyl)phosphoramide
microcin C7 asparagine modification
PSI-MOD
(3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5-adenosine
C-Asn-deriv
MOD:00333
Unimod origin shown as C-term [JSG].
(3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine
A protein modification that effectively converts an L-asparagine residue to (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine.
PubMed:7559516
PubMed:7835418
PubMed:8183363
RESID:AA0328
Unimod:437#C-term
(3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine
5'-O-[(3-aminopropoxy)(L-aspart-1-ylamino)phosphoryl]adenosine
9-(5'-O-[(3-aminopropoxy)(L-aspart-1-ylamino)phosphoryl]-beta-D-ribofuranosyl)adenine
MOD_RES Aspartic acid 1-[(3-aminopropyl)(5'-adenosyl)phosphono]amide
N-(aspart-1-yl)-O-(3-aminopropyl)-O-(5'-adenosyl)phosphoramide
microcin C7 asparagine modification
(3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5-adenosine
C-Asn-deriv
A protein modification that effectively results from forming an adduct between the tele nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
616.5
C 34 Fe 1 H 32 N 4 O 4
616.1773
C 40 Fe 1 H 39 N 7 O 5
753.64
753.2362
H
hypothetical
Unimod:390
(S)-[7-ethenyl-12-[1-((2-amino-2-carboxyethyl)-1H-imidazol-1-yl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
1'-heme-L-histidine
2-[1-(N1'-histidyl)ethyl]protoporphyrin IX
BINDING Heme (covalent; via tele nitrogen)
N(epsilon)-histidyl heme
N(tau)-histidyl heme
N1'-histidyl heme
tele-histidyl heme
PSI-MOD
Heme
heme
MOD:00334
1'-heme-L-histidine
A protein modification that effectively results from forming an adduct between the tele nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.
PubMed:12033922
PubMed:12121092
RESID:AA0329
Unimod:390#H
(S)-[7-ethenyl-12-[1-((2-amino-2-carboxyethyl)-1H-imidazol-1-yl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate
1'-heme-L-histidine
2-[1-(N1'-histidyl)ethyl]protoporphyrin IX
BINDING Heme (covalent; via tele nitrogen)
N(epsilon)-histidyl heme
N(tau)-histidyl heme
N1'-histidyl heme
tele-histidyl heme
Heme
heme
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2S,3S,2'R)-3-methyllanthionine sulfoxide.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 7 H 10 N 2 O 3 S 1
202.23
202.04121
C, T
natural
uniprot.ptm:PTM-0069
(2S,3S,4Xi,6R)-2,6-diamino-3-methyl-4-oxo-4-thiaheptanedioic acid
(2S,3S,SXi)-2-amino-3-([(R)-2-amino-2-carboxyethyl]sulfinyl)butanoic acid
3-methyl-L-lanthionine S-oxide
3-methyl-L-lanthionine sulfoxide
CROSSLNK Beta-methyllanthionine sulfoxide (Thr-Cys)
S-oxy-3-methyllanthionine
PSI-MOD
MOD:00335
Cross-link 2.
(2S,3S,2'R)-3-methyllanthionine sulfoxide
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2S,3S,2'R)-3-methyllanthionine sulfoxide.
PubMed:7737178
PubMed:9219543
RESID:AA0330
(2S,3S,4Xi,6R)-2,6-diamino-3-methyl-4-oxo-4-thiaheptanedioic acid
(2S,3S,SXi)-2-amino-3-([(R)-2-amino-2-carboxyethyl]sulfinyl)butanoic acid
3-methyl-L-lanthionine S-oxide
3-methyl-L-lanthionine sulfoxide
CROSSLNK Beta-methyllanthionine sulfoxide (Thr-Cys)
S-oxy-3-methyllanthionine
A protein modification that effectively converts three L-cysteine residues, an L-aspartic acid residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-aspartato diiron disulfide.
171.78
C 0 Fe 2 H -4 N 0 O 0 S 2
171.78381
2-
C 13 Fe 2 H 16 N 4 O 6 S 5
596.28
595.8383
C, C, C, D
hypothetical
METAL Iron-sulfur (2Fe-2S)
di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-O4-aspartatoiron)
tris-L-cysteinyl L-aspartato diiron disulfide
PSI-MOD
MOD:00336
Cross-link 4.
tris-L-cysteinyl L-aspartato diiron disulfide
A protein modification that effectively converts three L-cysteine residues, an L-aspartic acid residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-aspartato diiron disulfide.
PubMed:10968624
PubMed:1312028
PubMed:7947772
RESID:AA0331
METAL Iron-sulfur (2Fe-2S)
di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-O4-aspartatoiron)
tris-L-cysteinyl L-aspartato diiron disulfide
A protein modification that effectively converts an L-cysteine residue to S-carbamoyl-L-cysteine.
43.02
C 1 H 1 N 1 O 1 S 0
43.005814
C 4 H 6 N 2 O 2 S 1
146.16
146.015
C
natural
Unimod:5
uniprot.ptm:PTM-0649
(R)-2-amino-3-(carbamoylsulfanyl)propanoic acid
2-amino-3-(aminocarbonyl)sulfanylpropanoic acid
2-amino-3-(aminocarbonyl)thiopropanoic acid
MOD_RES S-carbamoylcysteine
S-(aminocarbonyl)cysteine
S-carbamoyl-L-cysteine
S-carbamoylcysteine
S-carbamylcysteine
S-cysteinyl carbamate ester
SCbmCys
alpha-amino-beta-carbamylthiopropionic acid
beta-carbamylthioalanine
PSI-MOD
MOD:00337
S-carbamoyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-carbamoyl-L-cysteine.
PubMed:12586941
PubMed:240389
RESID:AA0332
Unimod:5#C
(R)-2-amino-3-(carbamoylsulfanyl)propanoic acid
2-amino-3-(aminocarbonyl)sulfanylpropanoic acid
2-amino-3-(aminocarbonyl)thiopropanoic acid
MOD_RES S-carbamoylcysteine
S-(aminocarbonyl)cysteine
S-carbamoyl-L-cysteine
S-carbamoylcysteine
S-carbamylcysteine
S-cysteinyl carbamate ester
SCbmCys
alpha-amino-beta-carbamylthiopropionic acid
beta-carbamylthioalanine
A protein modification that effectively converts an L-cysteine residue to S-cyano-L-cysteine.
25.01
C 1 H -1 N 1 O 0 S 0
24.995249
C 4 H 4 N 2 O 1 S 1
128.15
128.00444
C
natural
Unimod:438
uniprot.ptm:PTM-0650
(2R)-2-amino-3-thiocyanatopropanoic acid
MOD_RES S-cyanocysteine
S-cyano-L-cysteine
S-cyanocysteine
alpha-amino-beta-thiocyanatopropionic acid
beta-thiocyanatoalanine
serine thiocyanic acid ester
PSI-MOD
Cyano
cyano
MOD:00338
S-cyano-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-cyano-L-cysteine.
PubMed:12586941
PubMed:4808702
RESID:AA0333
Unimod:438#C
(2R)-2-amino-3-thiocyanatopropanoic acid
MOD_RES S-cyanocysteine
S-cyano-L-cysteine
S-cyanocysteine
alpha-amino-beta-thiocyanatopropionic acid
beta-thiocyanatoalanine
serine thiocyanic acid ester
Cyano
cyano
A protein modification that effectively converts an L-cysteine residue to L-cysteinyl hydrogenase diiron subcluster.
342.87
C 5 Fe 2 H -1 N 2 O 5 S 2
342.78693
C 8 Fe 2 H 4 N 3 O 6 S 3
446.01
445.7961
C
natural
Unimod:439
1,7-biscarbonyl-1-(cystein-S-yl)-8-oxo-4-aza-2lambda(3),6 lambda(3)-dithia-1,7-diferratricyclo[4.2.0.0(2,7)]octane-1,7-dicarbonitrile
L-cysteinyl hydrogenase diiron subcluster
METAL Diiron subcluster
mu-carbonyl-dicarbonyl-1kappaC,2kappaC-dicyanido-1kappaC,2kappaC-cysteinato-1kS-1,2-azadimethanthiol-1kS,2kS'-diiron
PSI-MOD
Diironsubcluster
hydrogenase diiron subcluster
MOD:00339
incidental to RESID:AA0140.
L-cysteinyl hydrogenase diiron subcluster
A protein modification that effectively converts an L-cysteine residue to L-cysteinyl hydrogenase diiron subcluster.
PubMed:10694885
PubMed:9836629
RESID:AA0334
Unimod:439#C
1,7-biscarbonyl-1-(cystein-S-yl)-8-oxo-4-aza-2lambda(3),6 lambda(3)-dithia-1,7-diferratricyclo[4.2.0.0(2,7)]octane-1,7-dicarbonitrile
L-cysteinyl hydrogenase diiron subcluster
METAL Diiron subcluster
mu-carbonyl-dicarbonyl-1kappaC,2kappaC-dicyanido-1kappaC,2kappaC-cysteinato-1kS-1,2-azadimethanthiol-1kS,2kS'-diiron
Diironsubcluster
hydrogenase diiron subcluster
A protein modification that effectively converts an L-cysteine residue to S-amidino-L-cysteine.
42.04
C 1 H 2 N 2 O 0 S 0
42.021797
C 4 H 7 N 3 O 1 S 1
145.18
145.03099
C
natural
Unimod:440
(2R)-2-amino-3-(carbamimidoylsulfanyl)propanoic acid
2-amino-3-amidinosulfanylpropanoic acid
2-amino-3-amidinothiopropanoic acid
ACT_SITE Amidino-cysteine intermediate
S-amidino-L-cysteine
S-amidinocysteine
alpha-amino-beta-amidinothiopropionic acid
beta-(S-isothiourea)alanine
beta-amidinothioalanine
PSI-MOD
Amidino
amidino
MOD:00340
S-amidino-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-amidino-L-cysteine.
PubMed:9148748
RESID:AA0335
Unimod:440#C
(2R)-2-amino-3-(carbamimidoylsulfanyl)propanoic acid
2-amino-3-amidinosulfanylpropanoic acid
2-amino-3-amidinothiopropanoic acid
ACT_SITE Amidino-cysteine intermediate
S-amidino-L-cysteine
S-amidinocysteine
alpha-amino-beta-amidinothiopropionic acid
beta-(S-isothiourea)alanine
beta-amidinothioalanine
Amidino
amidino
A protein modification that effectively converts an L-isoleucine residue to N-methyl-L-isoleucine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 7 H 13 N 1 O 1
127.19
127.09972
I
hypothetical
uniprot.ptm:PTM-0215
(2S,3S)-2-methylamino-3-methylpentanoic acid
MOD_RES N-methylisoleucine
N-methyl-L-isoleucine
N-methylated L-isoleucine
N-methylisoleucine
NMe1Ile
PSI-MOD
Methyl
Methylation
MOD:00341
Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG].
N-methyl-L-isoleucine
A protein modification that effectively converts an L-isoleucine residue to N-methyl-L-isoleucine.
PubMed:11875433
RESID:AA0336
(2S,3S)-2-methylamino-3-methylpentanoic acid
MOD_RES N-methylisoleucine
N-methyl-L-isoleucine
N-methylated L-isoleucine
N-methylisoleucine
NMe1Ile
Methyl
Methylation
A protein modification that effectively converts an L-leucine residue to N-methyl-L-leucine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 7 H 13 N 1 O 1
127.19
127.09972
L
hypothetical
uniprot.ptm:PTM-0216
(S)-2-methylamino-4-methylpentanoic acid
2-(methylamino)-4-methyl-valeric acid
MOD_RES N-methylleucine
N-methyl-L-leucine
N-methylated L-leucine
N-methylleucine
NMe1Leu
PSI-MOD
Methyl
Methylation
MOD:00342
Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG].
N-methyl-L-leucine
A protein modification that effectively converts an L-leucine residue to N-methyl-L-leucine.
PubMed:11875433
RESID:AA0337
(S)-2-methylamino-4-methylpentanoic acid
2-(methylamino)-4-methyl-valeric acid
MOD_RES N-methylleucine
N-methyl-L-leucine
N-methylated L-leucine
N-methylleucine
NMe1Leu
Methyl
Methylation
A protein modification that effectively converts an L-tyrosine residue to N-methyl-L-tyrosine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 10 H 11 N 1 O 2
177.2
177.07898
Y
hypothetical
uniprot.ptm:PTM-0220
(2S)-3-(4-hydroxyphenyl)-2-(methylamino)propanoic acid
MOD_RES N-methyltyrosine
N-methyl Tyrosinyl
N-methyl-L-tyrosine
N-methylated L-tyrosine
N-methyltyrosine
NMe1Tyr
PSI-MOD
Methyl
MOD:00343
Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG].
N-methyl-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to N-methyl-L-tyrosine.
DeltaMass:0
RESID:AA0338
(2S)-3-(4-hydroxyphenyl)-2-(methylamino)propanoic acid
MOD_RES N-methyltyrosine
N-methyl Tyrosinyl
N-methyl-L-tyrosine
N-methylated L-tyrosine
N-methyltyrosine
NMe1Tyr
Methyl
A protein modification that effectively converts a glycine residue to N-palmitoylglycine.
238.41
C 16 H 30 N 0 O 1 S 0
238.22966
C 18 H 34 N 1 O 2
296.47
296.25894
G
natural
N-term
uniprot.ptm:PTM-0223
(hexadecanamido)acetic acid
(hexadecanoylamino)acetic acid
(hexadecanoylamino)ethanoic acid
LIPID N-palmitoyl glycine
N-(1-oxohexadecyl)glycine
N-hexadecanoylated glycine
N-palmitoyl-glycine
N-palmitoylated glycine
NPamGly
PSI-MOD
MOD:00344
incidental to RESID:AA0060
N-palmitoylglycine
A protein modification that effectively converts a glycine residue to N-palmitoylglycine.
PubMed:12574119
RESID:AA0339
(hexadecanamido)acetic acid
(hexadecanoylamino)acetic acid
(hexadecanoylamino)ethanoic acid
LIPID N-palmitoyl glycine
N-(1-oxohexadecyl)glycine
N-hexadecanoylated glycine
N-palmitoyl-glycine
N-palmitoylated glycine
NPamGly
A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-phenylalanine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 12 H 12 N 2 O 2 S 1
248.3
248.06195
C, F
natural
uniprot.ptm:PTM-0012
(2R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylpropanoic acid
(2R,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid
2-(L-cystein-S-yl)-L-phenylalanine
CROSSLNK 2-cysteinyl-L-phenylalanine (Cys-Phe)
alpha-(L-cystein-S-yl)-L-phenylalanine
PSI-MOD
MOD:00345
Cross-link 2.
2-(S-L-cysteinyl)-L-phenylalanine
A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-phenylalanine.
PubMed:12696888
PubMed:3936839
RESID:AA0340
(2R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylpropanoic acid
(2R,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid
2-(L-cystein-S-yl)-L-phenylalanine
CROSSLNK 2-cysteinyl-L-phenylalanine (Cys-Phe)
alpha-(L-cystein-S-yl)-L-phenylalanine
A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-phenylalanine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 12 H 12 N 2 O 2 S 1
248.3
248.06195
C, F
natural
uniprot.ptm:PTM-0011
(2S)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylpropanoic acid
(2S,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid
2-(L-cystein-S-yl)-D-phenylalanine
CROSSLNK 2-cysteinyl-D-phenylalanine (Cys-Phe)
alpha-(L-cystein-S-yl)-D-phenylalanine
PSI-MOD
MOD:00346
Cross-link 2.
2-(S-L-cysteinyl)-D-phenylalanine
A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-phenylalanine.
PubMed:12696888
PubMed:3936839
RESID:AA0341
(2S)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylpropanoic acid
(2S,5R)-2,5-diamino-3-thia-2-phenylmethylhexanedioic acid
2-(L-cystein-S-yl)-D-phenylalanine
CROSSLNK 2-cysteinyl-D-phenylalanine (Cys-Phe)
alpha-(L-cystein-S-yl)-D-phenylalanine
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-allo-threonine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 7 H 10 N 2 O 3 S 1
202.23
202.04121
C, T
natural
uniprot.ptm:PTM-0010
(2R,5S,6R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiaheptanoic acid
(2S,3R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid
2-(L-cystein-S-yl)-D-allo-threonine
CROSSLNK 2-cysteinyl-D-allo-threonine (Cys-Thr)
alpha-(L-cystein-S-yl)-D-allo-threonine
PSI-MOD
MOD:00347
Cross-link 2.
2-(S-L-cysteinyl)-D-allo-threonine
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-allo-threonine.
PubMed:12696888
PubMed:3936839
RESID:AA0342
(2R,5S,6R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiaheptanoic acid
(2S,3R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid
2-(L-cystein-S-yl)-D-allo-threonine
CROSSLNK 2-cysteinyl-D-allo-threonine (Cys-Thr)
alpha-(L-cystein-S-yl)-D-allo-threonine
A protein modification that effectively converts an L-alanine residue to N-carbamoyl-L-alanine.
43.02
C 1 H 1 N 1 O 1
43.005814
C 4 H 7 N 2 O 2
115.11
115.05075
A
natural
N-term
uniprot.ptm:PTM-0374
(S)-2-(carbamoylamino)propanoic acid
2-ureidopropanoic acid
MOD_RES N-carbamoylalanine
N-carbamoyl-L-alanine
N-carbamylalanine
N2CbmAla
PSI-MOD
MOD:00348
N-carbamoyl-L-alanine
A protein modification that effectively converts an L-alanine residue to N-carbamoyl-L-alanine.
PubMed:12203680
RESID:AA0343
(S)-2-(carbamoylamino)propanoic acid
2-ureidopropanoic acid
MOD_RES N-carbamoylalanine
N-carbamoyl-L-alanine
N-carbamylalanine
N2CbmAla
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form 4-amino-3-isothiazolidinone-L-serine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 6 H 8 N 2 O 3 S 1
188.2
188.02556
C, S
natural
uniprot.ptm:PTM-0037
(2S)-2-[(4R)-4-amino-3-oxo-1,2-thiazolidin-2-yl]-3-hydroxypropanoic acid
2-(4-amino-3-oxo-isothiazolidin-2-yl)-3-hydroxy-propanoic acid
4-amino-3-isothiazolidinone-L-serine
CROSSLNK N,N-(cysteine-1,S-diyl)serine (Cys-Ser)
N,N-(L-cysteine-1,S-diyl)-L-serine
serine-cysteine sulfenyl amide cross-link
serine-cysteine sulphenyl amide cross-link
PSI-MOD
MOD:00349
Cross-link 2.
4-amino-3-isothiazolidinone-L-serine
A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form 4-amino-3-isothiazolidinone-L-serine.
PubMed:12802338
PubMed:12802339
RESID:AA0344
(2S)-2-[(4R)-4-amino-3-oxo-1,2-thiazolidin-2-yl]-3-hydroxypropanoic acid
2-(4-amino-3-oxo-isothiazolidin-2-yl)-3-hydroxy-propanoic acid
4-amino-3-isothiazolidinone-L-serine
CROSSLNK N,N-(cysteine-1,S-diyl)serine (Cys-Ser)
N,N-(L-cysteine-1,S-diyl)-L-serine
serine-cysteine sulfenyl amide cross-link
serine-cysteine sulphenyl amide cross-link
A protein modification that effectively attaches an L-threonine residue to murein peptidoglycan by a pentaglycine linker peptide.
T
natural
C-term
uniprot.ptm:PTM-0246
(2R,6S)-2-(N-mureinyl-(R)-alanyl-(S)-isoglutamyl)amino-6-(threonyl-pentaglycyl)amino-pimeloyl-(S)-alanyl-(S)-alanine
L-threonyl-pentaglycyl-murein peptidoglycan
MOD_RES Pentaglycyl murein peptidoglycan amidated threonine
PSI-MOD
MOD:00350
L-threonyl-pentaglycyl-murein peptidoglycan
A protein modification that effectively attaches an L-threonine residue to murein peptidoglycan by a pentaglycine linker peptide.
PubMed:10754567
PubMed:1638631
RESID:AA0345
(2R,6S)-2-(N-mureinyl-(R)-alanyl-(S)-isoglutamyl)amino-6-(threonyl-pentaglycyl)amino-pimeloyl-(S)-alanyl-(S)-alanine
L-threonyl-pentaglycyl-murein peptidoglycan
MOD_RES Pentaglycyl murein peptidoglycan amidated threonine
A protein modification that effectively converts a glycine residue to N-glycyl-1-(phosphatidyl)ethanolamine.
699.99
C 39 H 74 N 1 O 7 P 1
699.52026
C 41 H 78 N 2 O 9 P 1
774.05
773.5445
G
natural
C-term
uniprot.ptm:PTM-0249
(R)-1-hexadecanoyloxy-2-((Z)-9-octadecenoyloxy)-3-[2-(aminoacetylamino)ethyloxyphospho]propane
LIPID Phosphatidylethanolamine amidated glycine
N-glycyl-1-(phosphatidyl)ethanolamine
N-glycyl-1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine
PSI-MOD
MOD:00351
N-glycyl-1-(phosphatidyl)ethanolamine
A protein modification that effectively converts a glycine residue to N-glycyl-1-(phosphatidyl)ethanolamine.
PubMed:11100732
RESID:AA0346
(R)-1-hexadecanoyloxy-2-((Z)-9-octadecenoyloxy)-3-[2-(aminoacetylamino)ethyloxyphospho]propane
LIPID Phosphatidylethanolamine amidated glycine
N-glycyl-1-(phosphatidyl)ethanolamine
N-glycyl-1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine
A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-omega-hydroxyceramide ester.
761.31
C 50 H 96 N 0 O 4
760.73083
C 55 H 104 N 2 O 6
889.44
888.7894
Q
natural
uniprot.ptm:PTM-0236
(S)-2-amino-5-[30-((2S,3R,4E)-1,3-dihydroxyicos-4-en-2-ylamino)-30-oxotriacontan-1-yloxy]-5-oxopentanoic acid
2-[30-(isoglutamyloxy)triacontanoyl]icosasphingosine
L-glutamyl 5-omega-hydroxyceramide ester
LIPID Omega-hydroxyceramide glutamate ester
PSI-MOD
MOD:00352
L-glutamyl 5-omega-hydroxyceramide ester
A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-omega-hydroxyceramide ester.
PubMed:10411887
PubMed:9651377
RESID:AA0347
(S)-2-amino-5-[30-((2S,3R,4E)-1,3-dihydroxyicos-4-en-2-ylamino)-30-oxotriacontan-1-yloxy]-5-oxopentanoic acid
2-[30-(isoglutamyloxy)triacontanoyl]icosasphingosine
L-glutamyl 5-omega-hydroxyceramide ester
LIPID Omega-hydroxyceramide glutamate ester
A protein modification that effectively cross-links an L-tryptophan residue with an L-tyrosine residue by a carbon-carbon bond, and cross-links the L-tyrosine residue to an L-methionine residue by a thioether bond to form S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium.
-3.02
C 0 H -3 N 0 O 0 S 0
-3.024024
1+
C 25 H 25 N 4 O 4 S 1
477.56
477.1591
M, W, Y
natural
uniprot.ptm:PTM-0328
5'-(6'-tryptophyl)-tyrosin-3'-yl-methionin-S-ium
S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium
PSI-MOD
MOD:00353
Cross-link 3.
S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium
A protein modification that effectively cross-links an L-tryptophan residue with an L-tyrosine residue by a carbon-carbon bond, and cross-links the L-tyrosine residue to an L-methionine residue by a thioether bond to form S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium.
PubMed:12172540
PubMed:16285713
RESID:AA0348
5'-(6'-tryptophyl)-tyrosin-3'-yl-methionin-S-ium
S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium
A protein modification that effectively converts an L-threonine residue to O-(riboflavin phosphoryl)-L-threonine.
438.33
C 17 H 19 N 4 O 8 P 1
438.09406
C 21 H 26 N 5 O 10 P 1
539.44
539.1417
T
natural
Unimod:442
uniprot.ptm:PTM-0126
(2S,3R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)butanoic acid
MOD_RES FMN phosphoryl threonine
O-(riboflavin phosphoryl)-L-threonine
O3-threonyl FMN
O3-threonyl flavin mononucleotide
OFMNThr
PSI-MOD
FMN
O3-(riboflavin phosphoryl)
MOD:00354
O-(riboflavin phosphoryl)-L-threonine
A protein modification that effectively converts an L-threonine residue to O-(riboflavin phosphoryl)-L-threonine.
PubMed:10587447
PubMed:11163785
PubMed:11248234
RESID:AA0349
Unimod:442#T
(2S,3R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)butanoic acid
MOD_RES FMN phosphoryl threonine
O-(riboflavin phosphoryl)-L-threonine
O3-threonyl FMN
O3-threonyl flavin mononucleotide
OFMNThr
FMN
O3-(riboflavin phosphoryl)
A protein modification that effectively converts an L-serine residue to O-(riboflavin phosphoryl)-L-serine.
438.33
C 17 H 19 N 4 O 8 P 1
438.09406
C 20 H 24 N 5 O 10 P 1
525.41
525.1261
S
natural
Unimod:442
uniprot.ptm:PTM-0125
(R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)propanoic acid
MOD_RES FMN phosphoryl serine
O-(riboflavin phosphoryl)-L-serine
O3-seryl FMN
O3-seryl flavin mononucleotide
OFMNSer
PSI-MOD
FMN
O3-(riboflavin phosphoryl)
MOD:00355
O-(riboflavin phosphoryl)-L-serine
A protein modification that effectively converts an L-serine residue to O-(riboflavin phosphoryl)-L-serine.
RESID:AA0350
Unimod:442#S
(R)-2-amino-3-(riboflavin 5'-hydrogen phosphonoxy)propanoic acid
MOD_RES FMN phosphoryl serine
O-(riboflavin phosphoryl)-L-serine
O3-seryl FMN
O3-seryl flavin mononucleotide
OFMNSer
FMN
O3-(riboflavin phosphoryl)
A protein modification that effectively converts an L-cysteine residue to S-(4a-FMN)-L-cysteine.
456.35
C 17 H 21 N 4 O 9 P 1 S 0
456.1046
C 20 H 26 N 5 O 10 P 1 S 1
559.49
559.1138
C
natural
Unimod:443
uniprot.ptm:PTM-0270
(R)-2-amino-3-(4a-riboflavin 5'-dihydrogen phosphate)sulfanylpropanoic acid
4a-(S-cysteinyl)FMN
4a-(S-cysteinyl)flavin mononucleotide
MOD_RES S-4a-FMN cysteine
S-(4a-FMN)-L-cysteine
S4aFMNCys
PSI-MOD
FMNC
S-(4a-FMN)
MOD:00356
S-(4alpha-FMN)-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-(4a-FMN)-L-cysteine.
PubMed:12668455
PubMed:12846567
PubMed:7692961
RESID:AA0351
Unimod:443#C
(R)-2-amino-3-(4a-riboflavin 5'-dihydrogen phosphate)sulfanylpropanoic acid
4a-(S-cysteinyl)FMN
4a-(S-cysteinyl)flavin mononucleotide
MOD_RES S-4a-FMN cysteine
S-(4a-FMN)-L-cysteine
S4aFMNCys
FMNC
S-(4a-FMN)
A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FMN)-L-histidine.
454.33
C 17 H 19 N 4 O 9 P 1
454.08896
C 23 H 26 N 7 O 10 P 1
591.47
591.1479
H
natural
Unimod:409
uniprot.ptm:PTM-0289
(S)-2-amino-3-(1-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid
1'-(8alpha-FMN)-L-histidine
8alpha-(N(epsilon)-histidyl)FMN
8alpha-(N1'-histidyl)FMN
MOD_RES Tele-8alpha-FMN histidine
N(tau)-(8alpha-FMN)-histidine
Ntele8aFMNHis
tele-(8alpha-FMN)-histidine
PSI-MOD
FMNH
flavin mononucleotide
MOD:00357
1'-(8alpha-FMN)-L-histidine
A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FMN)-L-histidine.
PubMed:11902668
PubMed:8611516
RESID:AA0352
Unimod:409#H
(S)-2-amino-3-(1-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid
1'-(8alpha-FMN)-L-histidine
8alpha-(N(epsilon)-histidyl)FMN
8alpha-(N1'-histidyl)FMN
MOD_RES Tele-8alpha-FMN histidine
N(tau)-(8alpha-FMN)-histidine
Ntele8aFMNHis
tele-(8alpha-FMN)-histidine
FMNH
flavin mononucleotide
A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FMN)-L-histidine.
454.33
C 17 H 19 N 4 O 9 P 1
454.08896
C 23 H 26 N 7 O 10 P 1
591.47
591.1479
H
hypothetical
Unimod:409
(S)-2-amino-3-(3-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid
3'-(8alpha-FMN)-L-histidine
8alpha-(N(delta)-histidyl)FMN
8alpha-(N3'-histidyl)FMN
N(pi)-(8alpha-FMN)-histidine
Npros8aFMNHis
pros-(8alpha-FMN)-histidine
PSI-MOD
FMNH
flavin mononucleotide
MOD:00358
In a later publication, PubMed:19438211, the authors changed the enzyme activity, the connection from a histidine nitrogen to a cysteine sulfur, and the identity of the flavin from FMN to FAD. They now believe the modification is S-(8alpha-FAD)-L-cysteine, see MOD:00152. This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
3'-(8alpha-FMN)-L-histidine
A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FMN)-L-histidine.
PubMed:12417325
RESID:AA0353
Unimod:409#H
(S)-2-amino-3-(3-[8alpha riboflavin 5'-dihydrogen phosphate]imidazol-4-yl)propanoic acid
3'-(8alpha-FMN)-L-histidine
8alpha-(N(delta)-histidyl)FMN
8alpha-(N3'-histidyl)FMN
N(pi)-(8alpha-FMN)-histidine
Npros8aFMNHis
pros-(8alpha-FMN)-histidine
FMNH
flavin mononucleotide
A protein modification that effectively converts an L-arginine residue to N2-acetyl-L-arginine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 8 H 15 N 4 O 2
199.23
199.1195
R
natural
N-term
uniprot.ptm:PTM-0180
(S)-2-acetamido-5-carbamimidamidopentanoic acid
2-acetamido-5-guanidinopentanoic acid
2-acetylamino-5-guanidinopentanoic acid
AcArg
MOD_RES N2-acetylarginine
N(alpha)-acetylarginine
N2-acetyl-L-arginine
N2-acetylated L-arginine
acetylarginine
alpha-acetylamino-delta-guanidinovaleric acid
PSI-MOD
MOD:00359
N2-acetyl-L-arginine
A protein modification that effectively converts an L-arginine residue to N2-acetyl-L-arginine.
PubMed:12883043
PubMed:1894641
RESID:AA0354
(S)-2-acetamido-5-carbamimidamidopentanoic acid
2-acetamido-5-guanidinopentanoic acid
2-acetylamino-5-guanidinopentanoic acid
AcArg
MOD_RES N2-acetylarginine
N(alpha)-acetylarginine
N2-acetyl-L-arginine
N2-acetylated L-arginine
acetylarginine
alpha-acetylamino-delta-guanidinovaleric acid
A protein modification that effectively converts an L-cysteine residue to L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide.
922.07
C 19 Cu 1 H 24 Mo 1 N 8 O 15 P 2 S 3
922.83484
C 22 Cu 1 H 29 Mo 1 N 9 O 16 P 2 S 4
1025.2
1025.844
C
natural
Unimod:444
L-cysteinyl copper sulfido molybdopterin cytosine dinucleotide
[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with cytosine)methyl-6-oxo-3,4-dimercapto-pteridino[6,7-5,6]pyranoato-S3,S4]-cysteinyl-S-copper-mu-sulfido-molybdenum hydroxide oxide
cysteinyl copper mu-sulfido Mo-pterin cytosine dinucleotide
PSI-MOD
CuSMo
copper sulfido molybdopterin cytosine dinuncleotide
MOD:00360
L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide
A protein modification that effectively converts an L-cysteine residue to L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide.
PubMed:12475995
RESID:AA0355
Unimod:444#C
L-cysteinyl copper sulfido molybdopterin cytosine dinucleotide
[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with cytosine)methyl-6-oxo-3,4-dimercapto-pteridino[6,7-5,6]pyranoato-S3,S4]-cysteinyl-S-copper-mu-sulfido-molybdenum hydroxide oxide
cysteinyl copper mu-sulfido Mo-pterin cytosine dinucleotide
CuSMo
copper sulfido molybdopterin cytosine dinuncleotide
A protein modification that effectively converts three L-cysteine residues, an S-adenosylmethionine and a four-iron four-sulfur cluster to tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide.
747.03
C 15 Fe 4 H 19 N 6 O 5 S 5
746.7424
1-
C 24 Fe 4 H 34 N 9 O 8 S 8
1056.45
1055.7699
C, C, C
natural
METAL Iron-sulfur (4Fe-4S-S-AdoMet)
tetra-mu3-sulfido(S-adenosylmethion-N,O-diyliron)tris(S-cysteinyliron)
tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide
PSI-MOD
MOD:00361
Cross-link 3.
tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide
A protein modification that effectively converts three L-cysteine residues, an S-adenosylmethionine and a four-iron four-sulfur cluster to tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide.
PubMed:11222759
PubMed:14704425
RESID:AA0356
METAL Iron-sulfur (4Fe-4S-S-AdoMet)
tetra-mu3-sulfido(S-adenosylmethion-N,O-diyliron)tris(S-cysteinyliron)
tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide
A protein modification that effectively converts three L-cysteine residues, an L-arginine residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-arginyl diiron disulfide.
172.79
C 0 Fe 2 H -3 N 0 O 0 S 2
172.79164
2-
C 15 Fe 2 H 24 N 7 O 4 S 5
638.39
637.9203
C, C, C, R
natural
METAL Iron-sulfur (2Fe-2S)
di-mu-sulfido(N(eta1)-arginyl-S-cysteinyliron)(bis-S-cysteinyliron)
tris-L-cysteinyl L-arginyl diiron disulfide
PSI-MOD
MOD:00362
Cross-link 4.
tris-L-cysteinyl L-arginyl diiron disulfide
A protein modification that effectively converts three L-cysteine residues, an L-arginine residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-arginyl diiron disulfide.
PubMed:14704425
RESID:AA0357
METAL Iron-sulfur (2Fe-2S)
di-mu-sulfido(N(eta1)-arginyl-S-cysteinyliron)(bis-S-cysteinyliron)
tris-L-cysteinyl L-arginyl diiron disulfide
A protein modification that effectively cross-links an L-cysteine residue and an L-selenocysteine residues to form L-cysteinyl-L-selenocystine.
-2.02
C 0 H -2 N 0 O 0 S 0 Se 0
-2.01565
C 6 H 8 N 2 O 2 S 1 Se 1
251.17
251.94717
C, U
natural
uniprot.ptm:PTM-0109
(R,R)-2-amino-3-[3-(2-aminopropanoic acid)sulfanyl]selanylpropanoic acid
CROSSLNK Cysteinyl-selenocysteine (Cys-Sec)
CROSSLNK Cysteinyl-selenocysteine (Sec-Cys)
L-cysteinyl-L-selenocysteine
PSI-MOD
MOD:00363
Cross-link 2.
L-cysteinyl-L-selenocysteine (Cys-Sec)
A protein modification that effectively cross-links an L-cysteine residue and an L-selenocysteine residues to form L-cysteinyl-L-selenocystine.
PubMed:12911312
RESID:AA0358#SEC
(R,R)-2-amino-3-[3-(2-aminopropanoic acid)sulfanyl]selanylpropanoic acid
CROSSLNK Cysteinyl-selenocysteine (Cys-Sec)
CROSSLNK Cysteinyl-selenocysteine (Sec-Cys)
L-cysteinyl-L-selenocysteine
A protein modification that effectively converts an L-lysine residue to 5-hydroxy-N6,N6,N6-trimethyl-L-lysine.
59.09
C 3 H 7 N 0 O 1
59.04914
1+
C 9 H 19 N 2 O 2
187.26
187.1441
K
natural
Unimod:445
uniprot.ptm:PTM-0186
(2R,5Xi)-5-amino-5-carboxy-2-hydroxy-N,N,N-trimethylpentan-1-aminium
(2Xi,5S)-5-amino-5-carboxy-2-hydroxy-N,N,N-trimethylpentanaminium
(2Xi,5S)-5-azanyl-5-carboxy-2-hydroxy-N,N,N-trimethylpentanazanium
5-hydroxy-N(zeta)-trimethyllysine
5-hydroxy-N6,N6,N6-trimethyl-L-lysine
5-hydroxy-N6,N6,N6-trimethyllysin-N6-ium
5-hydroxy-N6,N6,N6-trimethyllysine cation
5-hydroxylated N6,N6,N6-trimethylated L-lysine
5HyN6Me3Lys
MOD_RES N6,N6,N6-trimethyl-5-hydroxylysine
alpha-amino-epsilon-dimethylamino-delta-hydroxycaproic acid
delta-hydroxy-epsilon-N,N,N-trimethyllysine
lysine derivative Lys(z)
PSI-MOD
5-hydroxy-N6,N6,N6-trimethyl
Hydroxytrimethyl
MOD:00364
Incidental to RESID:AA0278; secondary to RESID:AA0028; secondary to RESID:AA0074.
5-hydroxy-N6,N6,N6-trimethyl-L-lysine
A protein modification that effectively converts an L-lysine residue to 5-hydroxy-N6,N6,N6-trimethyl-L-lysine.
PubMed:11349130
PubMed:14661085
RESID:AA0359
Unimod:445#K
(2R,5Xi)-5-amino-5-carboxy-2-hydroxy-N,N,N-trimethylpentan-1-aminium
(2Xi,5S)-5-amino-5-carboxy-2-hydroxy-N,N,N-trimethylpentanaminium
(2Xi,5S)-5-azanyl-5-carboxy-2-hydroxy-N,N,N-trimethylpentanazanium
5-hydroxy-N(zeta)-trimethyllysine
5-hydroxy-N6,N6,N6-trimethyl-L-lysine
5-hydroxy-N6,N6,N6-trimethyllysin-N6-ium
5-hydroxy-N6,N6,N6-trimethyllysine cation
5-hydroxylated N6,N6,N6-trimethylated L-lysine
5HyN6Me3Lys
MOD_RES N6,N6,N6-trimethyl-5-hydroxylysine
alpha-amino-epsilon-dimethylamino-delta-hydroxycaproic acid
delta-hydroxy-epsilon-N,N,N-trimethyllysine
lysine derivative Lys(z)
5-hydroxy-N6,N6,N6-trimethyl
Hydroxytrimethyl
A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue by an isopeptide bond to form N-(L-isoglutamyl)-glycine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 7 H 9 N 2 O 3
169.16
169.06131
E, G
natural
N-term
uniprot.ptm:PTM-0157
(S)-2-amino-5-(carboxymethyl)amino-5-oxopentanoic acid
2-amino-N5-(carboxymethyl)-pentanediamic acid
CROSSLNK Isoglutamyl glycine isopeptide (Gly-Glu)
N-(L-isoglutamyl)-glycine
N-gamma-glutamylglycine
isoglutamyl glycine
PSI-MOD
MOD:00365
Cross-link 2.
N-(L-isoglutamyl)-glycine
A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue by an isopeptide bond to form N-(L-isoglutamyl)-glycine.
PubMed:14531691
RESID:AA0360
(S)-2-amino-5-(carboxymethyl)amino-5-oxopentanoic acid
2-amino-N5-(carboxymethyl)-pentanediamic acid
CROSSLNK Isoglutamyl glycine isopeptide (Gly-Glu)
N-(L-isoglutamyl)-glycine
N-gamma-glutamylglycine
isoglutamyl glycine
A protein modification that effectively converts an L-serine residue to O-sulfo-L-serine.
80.06
C 0 H 0 N 0 O 3 S 1
79.95682
C 3 H 5 N 1 O 5 S 1
167.13
166.98885
S
natural
Unimod:40
uniprot.ptm:PTM-0284
(2S)-2-amino-3-(sulfooxy)propanoic acid
2-amino-3-hydroxypropanoic acid 3-sulfate
MOD_RES Sulfoserine
O-sulfo-L-serine
O3-sulfonoserine
O3-sulfoserine
serine sulfate ester
PSI-MOD
O-Sulfonation
Sulfo
MOD:00366
O-sulfo-L-serine
A protein modification that effectively converts an L-serine residue to O-sulfo-L-serine.
PubMed:14752058
RESID:AA0361
Unimod:40#S
(2S)-2-amino-3-(sulfooxy)propanoic acid
2-amino-3-hydroxypropanoic acid 3-sulfate
MOD_RES Sulfoserine
O-sulfo-L-serine
O3-sulfonoserine
O3-sulfoserine
serine sulfate ester
O-Sulfonation
Sulfo
A protein modification that effectively converts an L-threonine residue to O-sulfo-L-threonine.
80.06
C 0 H 0 N 0 O 3 S 1
79.95682
C 4 H 7 N 1 O 5 S 1
181.16
181.00449
T
natural
Unimod:40
uniprot.ptm:PTM-0285
(2S,3R)-2-amino-3-(sulfooxy)butanoic acid
2-amino-3-hydroxybutanoic acid 3-sulfate
MOD_RES Sulfothreonine
O-sulfo-L-threonine
O3-sulfonothreonine
O3-sulfothreonine
threonine sulfate ester
PSI-MOD
O-Sulfonation
Sulfo
MOD:00367
O-sulfo-L-threonine
A protein modification that effectively converts an L-threonine residue to O-sulfo-L-threonine.
PubMed:14752058
RESID:AA0362
Unimod:40#T
(2S,3R)-2-amino-3-(sulfooxy)butanoic acid
2-amino-3-hydroxybutanoic acid 3-sulfate
MOD_RES Sulfothreonine
O-sulfo-L-threonine
O3-sulfonothreonine
O3-sulfothreonine
threonine sulfate ester
O-Sulfonation
Sulfo
A protein modification that effectively converts an L-methionine residue to N-carboxy-L-methionine.
44.01
C 1 H 0 N 0 O 2 S 0
43.98983
C 6 H 10 N 1 O 3 S 1
176.21
176.03813
M
hypothetical
N-term
Unimod:299
(S)-2-carboxyamino-4-(methylsulfanyl)butanoic acid
2-carbamic-4-(methylsulfanyl)butanoic acid
2-carbamic-4-(methylthio)butanoic acid
N-carboxy-L-methionine
N-carboxymethionine
PSI-MOD
Carboxy
Carboxylation
MOD:00368
At least three protein crystallographic structures have been reported with this modification. However, no chemical evidence for this modification is provided, there were no reports of this modification before these crystallographic reports, and there is no metabolic explanation for the conversion of a formyl group to a carboxy group. There is confusion in its description, and misnaming is common. This modification is probably a misidentification of N-(dihydroxymethyl)methionine, the hydrated form of N-formylmethionine. See MOD:01446 [JSG].
N-carboxy-L-methionine
A protein modification that effectively converts an L-methionine residue to N-carboxy-L-methionine.
PubMed:10368287
PubMed:11120890
PubMed:12595263
PubMed:8312270
RESID:AA0363
Unimod:299#M
(S)-2-carboxyamino-4-(methylsulfanyl)butanoic acid
2-carbamic-4-(methylsulfanyl)butanoic acid
2-carbamic-4-(methylthio)butanoic acid
N-carboxy-L-methionine
N-carboxymethionine
Carboxy
Carboxylation
A protein modification that effectively converts an L-serine residue to O-acetyl-L-serine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 5 H 7 N 1 O 3
129.12
129.04259
S
natural
Unimod:1
uniprot.ptm:PTM-0232
(2S)-3-(acetyloxy)-2-aminopropanoic acid
MOD_RES O-acetylserine
O-acetyl-L-serine
O-acetylated L-serine
O-acetylserine
OAcSer
serine acetate ester
PSI-MOD
Acetyl
Acetylation
MOD:00369
incidental to RESID:AA0051
O-acetyl-L-serine
A protein modification that effectively converts an L-serine residue to O-acetyl-L-serine.
ChEBI:17981
PubMed:11857757
PubMed:11999733
PubMed:12175151
PubMed:14730666
PubMed:15350136
PubMed:16731519
PubMed:489587
PubMed:7309355
RESID:AA0364
Unimod:1#S
(2S)-3-(acetyloxy)-2-aminopropanoic acid
MOD_RES O-acetylserine
O-acetyl-L-serine
O-acetylated L-serine
O-acetylserine
OAcSer
serine acetate ester
Acetyl
Acetylation
A protein modification that effectively converts an L-tyrosine residue to (E)-2,3-didehydrotyrosine.
-2.02
C 0 H -2 N 0 O 0
-2.01565
C 9 H 7 N 1 O 2
161.16
161.04768
Y
natural
uniprot.ptm:PTM-0001
(2E)-2-amino-3-(4-hydroxyphenyl)prop-2-enoic acid
(E)-2,3-didehydrogenated tyrosine
(E)-2,3-didehydrotyrosine
E-dHTyr
MOD_RES (E)-2,3-didehydrotyrosine
amino-(para-hydroxybenzylidenyl)acetic acid
blue non-fluorescent pocilloporin chromophore
para-hydroxybenzylidene-imidazolidinone chromophore
trans-dehydrotyrosine
PSI-MOD
2-amino-3-oxo-butanoic_acid
Didehydro
MOD:00370
incidental to RESID:AA0184; incidental to RESID:AA0187; incidental to RESID:AA0188; incidental to RESID:AA0189; incidental to RESID:AA0378; incidental to RESID:AA0379; incidental to RESID:AA0380; incidental to RESID:AA0381
(E)-2,3-didehydrotyrosine
A protein modification that effectively converts an L-tyrosine residue to (E)-2,3-didehydrotyrosine.
PubMed:12623015
RESID:AA0365
(2E)-2-amino-3-(4-hydroxyphenyl)prop-2-enoic acid
(E)-2,3-didehydrogenated tyrosine
(E)-2,3-didehydrotyrosine
E-dHTyr
MOD_RES (E)-2,3-didehydrotyrosine
amino-(para-hydroxybenzylidenyl)acetic acid
blue non-fluorescent pocilloporin chromophore
para-hydroxybenzylidene-imidazolidinone chromophore
trans-dehydrotyrosine
2-amino-3-oxo-butanoic_acid
Didehydro
A protein modification that effectively converts two L-aspartic acid residues, three L-glutamic acid residues, an L-histidine residue, and a one-calcium, four-iron, four-oxygen cluster to bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide.
317.78
C 0 Ca 1 H -6 Mn 4 N 0 O 4
317.6475
C 29 Ca 1 H 32 Mn 4 N 8 O 20
1072.44
1071.8881
D, D, E, E, E, H
hypothetical
4Mn-Ca-4O cluster
bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide
mu3-1:2:3kappaO-oxido-mu3-1:3:4kappaO-oxido-mu3-2:3:4kappaO-oxido-mu4-1:2:4:5kappaO-oxido-N1'-histidino-O5-glutamato 2-manganese-O5,O5-glutamato 3-manganese-O4-aspartato 4-manganese-O4-aspartato-O5-glutamato 5-manganese
photosystem II catalytic cluster
PSI-MOD
MOD:00371
Cross-link 6.
bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide
A protein modification that effectively converts two L-aspartic acid residues, three L-glutamic acid residues, an L-histidine residue, and a one-calcium, four-iron, four-oxygen cluster to bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide.
PubMed:14764885
RESID:AA0366
4Mn-Ca-4O cluster
bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide
mu3-1:2:3kappaO-oxido-mu3-1:3:4kappaO-oxido-mu3-2:3:4kappaO-oxido-mu4-1:2:4:5kappaO-oxido-N1'-histidino-O5-glutamato 2-manganese-O5,O5-glutamato 3-manganese-O4-aspartato 4-manganese-O4-aspartato-O5-glutamato 5-manganese
photosystem II catalytic cluster
A protein modification that effectively cross-links two L-tyrosine residues with a carbon-carbon bond to form 3'-(3'-L-tyrosinyl)-L-tyrosine.
-2.02
C 0 H -2 N 0 O 0
-2.01565
C 18 H 16 N 2 O 4
324.34
324.111
Y, Y
natural
(2S,2'S)-3,3'-(6,6'-dihydroxybiphenyl-3,3'-diyl)bis(2-aminopropanoic acid)
3'-(L-tyros-3'-yl)-L-tyrosine
3,3'-BiTyr (Crosslink)
6,6'-dihydroxy-(1,1'-biphenyl)-3,3'-bis(2-aminopropanoic acid)
alpha,alpha'-diamino-6,6'-dihydroxy-(1,1'-biphenyl)-3,3'-dipropanoic acid
bityrosine
o,o-dityrosine
PSI-MOD
MOD:00372
Cross-link 2; From DeltaMass: Average Mass: -2.
3'-(3'-L-tyrosinyl)-L-tyrosine
A protein modification that effectively cross-links two L-tyrosine residues with a carbon-carbon bond to form 3'-(3'-L-tyrosinyl)-L-tyrosine.
DeltaMass:0
PubMed:14249161
PubMed:637884
PubMed:8702710
PubMed:8937563
RESID:AA0367
(2S,2'S)-3,3'-(6,6'-dihydroxybiphenyl-3,3'-diyl)bis(2-aminopropanoic acid)
3'-(L-tyros-3'-yl)-L-tyrosine
3,3'-BiTyr (Crosslink)
6,6'-dihydroxy-(1,1'-biphenyl)-3,3'-bis(2-aminopropanoic acid)
alpha,alpha'-diamino-6,6'-dihydroxy-(1,1'-biphenyl)-3,3'-dipropanoic acid
bityrosine
o,o-dityrosine
A protein modification that effectively cross-links L-tyrosine residues with an ether bond to form 3'-(O4'-L-tyrosinyl)-L-tyrosine.
-2.02
C 0 H -2 N 0 O 0
-2.01565
C 18 H 16 N 2 O 4
324.34
324.111
Y, Y
natural
uniprot.ptm:PTM-0155
(2S)-2-amino-3-[3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-4-hydroxyphenyl]propanoic acid
2-amino-3-[4-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenoxy)phenyl]propanoic acid
3'-(L-tyros-O4'-yl)-L-tyrosine
CROSSLNK Isodityrosine (Tyr-Tyr)
IsodiTyr (Crosslink)
O-(5-(2-amino-2-carboxyethyl)-2-hydroxyphenyl)-L-tyrosine
isodityrosine
PSI-MOD
MOD:00373
Cross-link 2; secondary to RESID:AA0146; From DeltaMass: Average Mass: -2.
3'-(O4'-L-tyrosinyl)-L-tyrosine
A protein modification that effectively cross-links L-tyrosine residues with an ether bond to form 3'-(O4'-L-tyrosinyl)-L-tyrosine.
DeltaMass:0
PubMed:12719529
PubMed:7115340
PubMed:8702710
RESID:AA0368
(2S)-2-amino-3-[3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-4-hydroxyphenyl]propanoic acid
2-amino-3-[4-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenoxy)phenyl]propanoic acid
3'-(L-tyros-O4'-yl)-L-tyrosine
CROSSLNK Isodityrosine (Tyr-Tyr)
IsodiTyr (Crosslink)
O-(5-(2-amino-2-carboxyethyl)-2-hydroxyphenyl)-L-tyrosine
isodityrosine
A protein modification that effectively converts an L-arginine residue to 3,4-dihydroxy-L-arginine.
32.0
C 0 H 0 N 0 O 2
31.989828
C 6 H 12 N 4 O 3
188.19
188.09094
R
natural
Unimod:425
uniprot.ptm:PTM-0022
(2S,3Xi,4Xi)-2-amino-5-carbamimidamido-3,4-dihydroxypentanoic acid
2-amino-5-guanidino-3,4-dihydroxypentanoic acid
3,4-dihydroxy-L-arginine
3,4-dihydroxylated L-arginine
34Hy2Arg
MOD_RES 3,4-dihydroxyarginine
beta,gamma-dihydroxyarginine
PSI-MOD
Dioxidation
dihydroxy
MOD:00374
3,4-dihydroxy-L-arginine
A protein modification that effectively converts an L-arginine residue to 3,4-dihydroxy-L-arginine.
ChEBI:141829
PubMed:10978343
PubMed:12686488
RESID:AA0369
Unimod:425#R
(2S,3Xi,4Xi)-2-amino-5-carbamimidamido-3,4-dihydroxypentanoic acid
2-amino-5-guanidino-3,4-dihydroxypentanoic acid
3,4-dihydroxy-L-arginine
3,4-dihydroxylated L-arginine
34Hy2Arg
MOD_RES 3,4-dihydroxyarginine
beta,gamma-dihydroxyarginine
Dioxidation
dihydroxy
A protein modification that effectively converts an L-lysine residue to 4,5-dihydroxy-L-lysine.
32.0
C 0 H 0 N 0 O 2
31.989828
C 6 H 12 N 2 O 3
160.17
160.0848
K
natural
Unimod:425
uniprot.ptm:PTM-0036
(2S,4Xi,5Xi)-2,6-diamino-4,5-dihydroxyhexanoic acid
4,5-dihydroxy-L-lysine
4,5-dihydroxylated L-lysine
45Hy2Lys
MOD_RES 4,5-dihydroxylysine
alpha,epsilon-diamino-delta,gamma-dihydroxycaproic acid
delta,gamma-dihydroxylysine
PSI-MOD
Dioxidation
dihydroxy
MOD:00375
4,5-dihydroxy-L-lysine
A protein modification that effectively converts an L-lysine residue to 4,5-dihydroxy-L-lysine.
PubMed:10978343
PubMed:12686488
RESID:AA0370
Unimod:425#K
(2S,4Xi,5Xi)-2,6-diamino-4,5-dihydroxyhexanoic acid
4,5-dihydroxy-L-lysine
4,5-dihydroxylated L-lysine
45Hy2Lys
MOD_RES 4,5-dihydroxylysine
alpha,epsilon-diamino-delta,gamma-dihydroxycaproic acid
delta,gamma-dihydroxylysine
Dioxidation
dihydroxy
A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form 1'-(phospho-5'-adenosine)-L-histidine.
329.21
C 10 H 12 N 5 O 6 P 1
329.05252
C 16 H 19 N 8 O 7 P 1
466.35
466.11142
H
natural
Unimod:405
(2S)-2-amino-3-[1-(5'-adenosine phosphono)imidazol-4-yl]propanoic acid
1'-(phospho-5'-adenosine)-L-histidine
ACT_SITE Tele-AMP-histidine intermediate
L-histidine 5'-adenosine phosphoramidester
L-histidine monoanhydride with 5'-adenylic acid
N(tau)-5'-adenylic-L-histidine
N1'-adenylylated histidine
tele-5'-adenylic-L-histidine
PSI-MOD
AMP binding site
Phosphoadenosine
MOD:00376
1'-(phospho-5'-adenosine)-L-histidine
A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form 1'-(phospho-5'-adenosine)-L-histidine.
PubMed:15182206
PubMed:9323207
RESID:AA0371
Unimod:405#H
(2S)-2-amino-3-[1-(5'-adenosine phosphono)imidazol-4-yl]propanoic acid
1'-(phospho-5'-adenosine)-L-histidine
ACT_SITE Tele-AMP-histidine intermediate
L-histidine 5'-adenosine phosphoramidester
L-histidine monoanhydride with 5'-adenylic acid
N(tau)-5'-adenylic-L-histidine
N1'-adenylylated histidine
tele-5'-adenylic-L-histidine
AMP binding site
Phosphoadenosine
A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphouridine through a phosphoramide ester bond to form 1'-(phospho-5'-uridine)-L-histidine.
306.17
C 9 H 11 N 2 O 8 P 1
306.0253
C 15 H 18 N 5 O 9 P 1
443.31
443.08423
H
natural
Unimod:417
uniprot.ptm:PTM-0500
(S)-2-amino-3-[1-(5'-uridine phosphono)imidazol-4-yl]propanoic acid
1'-(phospho-5'-uridine)-L-histidine
ACT_SITE Tele-UMP-histidine intermediate
L-histidine 5'-uridine phosphoramidester
L-histidine monoanhydride with 5'-uridylic acid
MOD_RES O-UMP-histidine
N(tau)-5'-uridylic-L-histidine
N1'-uridylylated histidine
tele-5'-uridylic-L-histidine
PSI-MOD
PhosphoUridine
uridine phosphodiester
MOD:00377
1'-(phospho-5'-uridine)-L-histidine
A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphouridine through a phosphoramide ester bond to form 1'-(phospho-5'-uridine)-L-histidine.
PubMed:11467524
PubMed:321007
PubMed:380639
PubMed:8794735
RESID:AA0372
Unimod:417#H
(S)-2-amino-3-[1-(5'-uridine phosphono)imidazol-4-yl]propanoic acid
1'-(phospho-5'-uridine)-L-histidine
ACT_SITE Tele-UMP-histidine intermediate
L-histidine 5'-uridine phosphoramidester
L-histidine monoanhydride with 5'-uridylic acid
MOD_RES O-UMP-histidine
N(tau)-5'-uridylic-L-histidine
N1'-uridylylated histidine
tele-5'-uridylic-L-histidine
PhosphoUridine
uridine phosphodiester
A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl semialdehyde.
-16.0
C 0 H 0 N 0 O -1
-15.994915
C 4 H 5 N 1 O 2
99.09
99.03203
D
natural
Unimod:447
uniprot.ptm:PTM-0064
(S)-2-amino-4-oxobutanoic acid
L-aminosuccinaldehydic acid
L-aminosuccinic acid semialdehyde
L-aspartate-beta-semialdehyde
L-aspartic beta-semialdehyde
L-aspartyl aldehyde
L-beta-formylalanine
MOD_RES Aspartyl aldehyde
aspartyl 4-semialdehyde
aspartyl aldehyde
PSI-MOD
Deoxy
reduction
MOD:00378
L-aspartyl semialdehyde
A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl semialdehyde.
PubMed:1093385
PubMed:14235557
PubMed:15237995
RESID:AA0373
Unimod:447#D
(S)-2-amino-4-oxobutanoic acid
L-aminosuccinaldehydic acid
L-aminosuccinic acid semialdehyde
L-aspartate-beta-semialdehyde
L-aspartic beta-semialdehyde
L-aspartyl aldehyde
L-beta-formylalanine
MOD_RES Aspartyl aldehyde
aspartyl 4-semialdehyde
aspartyl aldehyde
Deoxy
reduction
A protein modification that effectively converts an L-serine residue to L-serine microcin E492 siderophore ester.
831.69
C 36 H 37 N 3 O 20
831.197
C 39 H 43 N 4 O 23
935.78
935.2318
S
natural
C-term
Unimod:448
uniprot.ptm:PTM-0276
L-serine microcin E492 siderophore ester
MOD_RES Serine microcin E492 siderophore ester
N-[5-(6-O-seryl-beta-glucosyl)-2,3-dihydroxybenzoyl]-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)seryl]seryl]serine
PSI-MOD
Microcin
microcin E492 siderophore ester from serine
MOD:00379
Unimod origin corrected [JSG].
L-serine microcin E492 siderophore ester
A protein modification that effectively converts an L-serine residue to L-serine microcin E492 siderophore ester.
PubMed:15102848
RESID:AA0374
Unimod:448#C-term
L-serine microcin E492 siderophore ester
MOD_RES Serine microcin E492 siderophore ester
N-[5-(6-O-seryl-beta-glucosyl)-2,3-dihydroxybenzoyl]-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)seryl]seryl]serine
Microcin
microcin E492 siderophore ester from serine
A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide).
1572.02
C 40 H 47 Mo 1 N 20 O 26 P 4 S 4
1572.9857
C 44 H 52 Mo 1 N 21 O 29 P 4 S 4
1687.1
1688.0127
D
natural
Unimod:424
2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide
L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide)
bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-aspartyl-molybdenum
nitrate reductase A aspartyl Mo-bisMGD cofactor
phosphoric acid 4-(2-amino-4-oxo-3,4,5,6,-tetrahydro-pteridin-6-yl)-2-hydroxy-3,4-dimercapto-but-3-en-yl ester guanylate ester
PSI-MOD
MolybdopterinGD
molybdenum bis(molybdopterin guanine dinucleotide)
MOD:00380
L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide)
A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide).
PubMed:12910261
PubMed:14725769
RESID:AA0375
Unimod:424#D
2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide
L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide)
bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-aspartyl-molybdenum
nitrate reductase A aspartyl Mo-bisMGD cofactor
phosphoric acid 4-(2-amino-4-oxo-3,4,5,6,-tetrahydro-pteridin-6-yl)-2-hydroxy-3,4-dimercapto-but-3-en-yl ester guanylate ester
MolybdopterinGD
molybdenum bis(molybdopterin guanine dinucleotide)
A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide).
1691.97
C 40 H 47 N 20 O 26 P 4 S 5 Se 0 W 1
1691.0034
C 43 H 52 N 21 O 27 P 4 S 5 Se 1 W 1
1842.02
1841.957
U
natural
PSI-MOD
MOD:00381
L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (Sec)
A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide).
PubMed:11372198
PubMed:12220497
RESID:AA0376#SEC
A protein modification that effectively crosslinks an L-methionyl-L-tyrosine dipeptide to form 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 14 H 15 N 2 O 2 S 1
275.35
275.08542
M, Y
hypothetical
N-term
3-(2-methylsulfanyl)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one
3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-amino-3,6-didehydropyrazin-2-ol
3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one
GFP-like chromoprotein asFP595 chromophore
L-methionyl-L-tyrosyl-2-keto-5-iminopiperazine
PSI-MOD
MOD:00382
carboxamidine; cross-link 1. This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one
A protein modification that effectively crosslinks an L-methionyl-L-tyrosine dipeptide to form 3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one.
PubMed:10852900
PubMed:11259412
PubMed:15491166
RESID:AA0377
3-(2-methylsulfanyl)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one
3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-amino-3,6-didehydropyrazin-2-ol
3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one
GFP-like chromoprotein asFP595 chromophore
L-methionyl-L-tyrosyl-2-keto-5-iminopiperazine
A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue to form 2-imino-glutamic acid 5-imidazolinone glycine.
-20.03
C 0 H -4 N 0 O -1
-20.026215
C 7 H 6 N 2 O 3
166.14
166.03784
E, G
hypothetical
uniprot.ptm:PTM-0014
2,N-didehydroglutamyl-5-imidazolinone glycine
2-(3-carboxy-1-iminopropyl)-1-carboxymethyl-1-imidazolin-5-one
2-imino-glutamic acid 5-imidazolinone glycine
2-imino-glutamyl-5-imidazolinone glycine
4-[1-(carboxymethyl)-5-oxo-4,5-dihydro-1H-imidazol-2-yl]-4-iminobutanoic acid
CROSSLNK 2-iminomethyl-5-imidazolinone (Glu-Gly)
[2-(3-carboxy-1-iminopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
para-hydroxybenzylidene-imidazolidinone chromophore
PSI-MOD
MOD:00383
Cross-link 2; carboxamidine; cross-link 1; incidental to RESID:AA0183; incidental to RESID:AA0365.
2-imino-glutamic acid 5-imidazolinone glycine
A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue to form 2-imino-glutamic acid 5-imidazolinone glycine.
PubMed:11682051
RESID:AA0378
2,N-didehydroglutamyl-5-imidazolinone glycine
2-(3-carboxy-1-iminopropyl)-1-carboxymethyl-1-imidazolin-5-one
2-imino-glutamic acid 5-imidazolinone glycine
2-imino-glutamyl-5-imidazolinone glycine
4-[1-(carboxymethyl)-5-oxo-4,5-dihydro-1H-imidazol-2-yl]-4-iminobutanoic acid
CROSSLNK 2-iminomethyl-5-imidazolinone (Glu-Gly)
[2-(3-carboxy-1-iminopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
para-hydroxybenzylidene-imidazolidinone chromophore
A protein modification that effectively crosslinks an L-methionine residue and a glycine residue to form 2-imino-methionine 5-imidazolinone glycine.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 7 H 8 N 2 O 1 S 1
168.21
168.03574
G, M
natural
uniprot.ptm:PTM-0015
(2-[1-imino-3-(methylsulfanyl)propyl]-5-oxo-4,5-dihydro-imidazol-1-yl)acetic acid
(2-[3-(methylsulfanyl)propanimidoyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2,N-didehydromethionyl-5-imidazolinone glycine
2-[1-imino-3-(methylsulfanyl)propyl]-1-carboxymethyl-1-imidazolin-5-one
2-imino-methionine 5-imidazolinone glycine
2-imino-methionyl-5-imidazolinone glycine
CROSSLNK 2-iminomethyl-5-imidazolinone (Met-Gly)
GFP-like chromoprotein asFP595 chromophore
para-hydroxybenzylidene-imidazolidinone chromophore
red fluorescent protein eqFP611 chromophore
PSI-MOD
MOD:00384
Cross-link 2; carboxamidine; cross-link 1; incidental to RESID:AA0183; incidental to RESID:AA0365.
2-imino-methionine 5-imidazolinone glycine
A protein modification that effectively crosslinks an L-methionine residue and a glycine residue to form 2-imino-methionine 5-imidazolinone glycine.
PubMed:10852900
PubMed:12185250
PubMed:12909624
PubMed:15542608
RESID:AA0379
(2-[1-imino-3-(methylsulfanyl)propyl]-5-oxo-4,5-dihydro-imidazol-1-yl)acetic acid
(2-[3-(methylsulfanyl)propanimidoyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2,N-didehydromethionyl-5-imidazolinone glycine
2-[1-imino-3-(methylsulfanyl)propyl]-1-carboxymethyl-1-imidazolin-5-one
2-imino-methionine 5-imidazolinone glycine
2-imino-methionyl-5-imidazolinone glycine
CROSSLNK 2-iminomethyl-5-imidazolinone (Met-Gly)
GFP-like chromoprotein asFP595 chromophore
para-hydroxybenzylidene-imidazolidinone chromophore
red fluorescent protein eqFP611 chromophore
A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue to form L-asparagine 5-imidazolinone glycine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 6 H 7 N 3 O 2
153.14
153.05383
G, N
hypothetical
uniprot.ptm:PTM-0046
(2-[(1S)-1,3-diamino-3-oxopropyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2-[(S)-1,3-diamino-3-oxopropyl]-1-carboxymethyl-1-imidazolin-5-one
CROSSLNK 5-imidazolinone (Asn-Gly)
L-asparagine 5-imidazolinone glycine
Zoanthus sp. fluorescent protein FP506 chromophore
[2-(1,3-diamino-3-oxopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
asparaginyl-5-imidazolinone glycine
para-hydroxybenzylidene-imidazolidinone chromophore
PSI-MOD
MOD:00385
Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365.
L-asparagine 5-imidazolinone glycine
A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue to form L-asparagine 5-imidazolinone glycine.
PubMed:10504696
RESID:AA0380
(2-[(1S)-1,3-diamino-3-oxopropyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2-[(S)-1,3-diamino-3-oxopropyl]-1-carboxymethyl-1-imidazolin-5-one
CROSSLNK 5-imidazolinone (Asn-Gly)
L-asparagine 5-imidazolinone glycine
Zoanthus sp. fluorescent protein FP506 chromophore
[2-(1,3-diamino-3-oxopropyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
asparaginyl-5-imidazolinone glycine
para-hydroxybenzylidene-imidazolidinone chromophore
A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form L-lysine 5-imidazolinone glycine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 8 H 13 N 3 O 1
167.21
167.10587
G, K
hypothetical
uniprot.ptm:PTM-0048
(2-[(1S)-1,5-diaminopentyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2-[(S)-1,5-diaminopentanyl]-1-carboxymethyl-1-imidazolin-5-one
Anemonia majano fluorescent protein FP486 chromophore
CROSSLNK 5-imidazolinone (Lys-Gly)
L-lysine 5-imidazolinone glycine
[2-(1,5-diaminopentanyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
lysyl-5-imidazolinone glycine
para-hydroxybenzylidene-imidazolidinone chromophore
PSI-MOD
MOD:00386
Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365.
L-lysine 5-imidazolinone glycine
A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form L-lysine 5-imidazolinone glycine.
PubMed:10504696
RESID:AA0381
(2-[(1S)-1,5-diaminopentyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2-[(S)-1,5-diaminopentanyl]-1-carboxymethyl-1-imidazolin-5-one
Anemonia majano fluorescent protein FP486 chromophore
CROSSLNK 5-imidazolinone (Lys-Gly)
L-lysine 5-imidazolinone glycine
[2-(1,5-diaminopentanyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
lysyl-5-imidazolinone glycine
para-hydroxybenzylidene-imidazolidinone chromophore
A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form 2-tetrahydropyridinyl-5-imidazolinone glycine.
-37.06
C 0 H -7 N -1 O -1
-37.052765
C 8 H 9 N 2 O 1
149.17
149.07149
G, K
natural
N-term
uniprot.ptm:PTM-0018
2-(3,4,5,6-tetrahydropyridin-2-yl)-1-carboxymethyl-1-imidazolin-5-one
2-(tetrahydropyrid-2-yl)-5-imidazolinone glycine
2-tetrahydropyridinyl-5-imidazolinone glycine
CROSSLNK 2-tetrahydro-2-pyridyl-5-imidazolinone (Lys-Gly)
Zoanthus sp. fluorescent protein zFP538 chromophore
[5-oxo-2-(3,4,5,6-tetrahydropyridin-2-yl)-4,5-dihydro-1H-imidazol-1-yl]acetic acid
para-hydroxybenzylidene-imidazolidinone chromophore
PSI-MOD
MOD:00387
Cross-link 2; carboxamidine; incidental to RESID:AA0183; incidental to RESID:AA0365.
2-tetrahydropyridinyl-5-imidazolinone glycine
A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form 2-tetrahydropyridinyl-5-imidazolinone glycine.
PubMed:10504696
PubMed:15628861
RESID:AA0382
2-(3,4,5,6-tetrahydropyridin-2-yl)-1-carboxymethyl-1-imidazolin-5-one
2-(tetrahydropyrid-2-yl)-5-imidazolinone glycine
2-tetrahydropyridinyl-5-imidazolinone glycine
CROSSLNK 2-tetrahydro-2-pyridyl-5-imidazolinone (Lys-Gly)
Zoanthus sp. fluorescent protein zFP538 chromophore
[5-oxo-2-(3,4,5,6-tetrahydropyridin-2-yl)-4,5-dihydro-1H-imidazol-1-yl]acetic acid
[5-oxo-2-(3,4,5,6-tetrahydropyridin-2-yl)-4,5-dihydro-1H-imidazol-1-yl]acetic acid
para-hydroxybenzylidene-imidazolidinone chromophore
A protein modification that effectively attaches an L-alanine residue to murein peptidoglycan by a pentaglycine linker peptide.
A
hypothetical
C-term
uniprot.ptm:PTM-0245
(2R,6S)-2-(N-mureinyl-(R)-alanyl-(S)-isoglutamyl)amino-6-(alanyl-pentaglycyl)amino-pimeloyl-(S)-alanyl-(S)-alanine
L-alanyl-pentaglycyl-murein peptidoglycan
MOD_RES Pentaglycyl murein peptidoglycan amidated alanine
PSI-MOD
MOD:00388
L-alanyl-pentaglycyl-murein peptidoglycan
A protein modification that effectively attaches an L-alanine residue to murein peptidoglycan by a pentaglycine linker peptide.
PubMed:8163519
RESID:AA0383
(2R,6S)-2-(N-mureinyl-(R)-alanyl-(S)-isoglutamyl)amino-6-(alanyl-pentaglycyl)amino-pimeloyl-(S)-alanyl-(S)-alanine
L-alanyl-pentaglycyl-murein peptidoglycan
MOD_RES Pentaglycyl murein peptidoglycan amidated alanine
A protein modification that effectively converts an L-proline residue to N-formyl-L-proline.
28.01
C 1 H 0 N 0 O 1
27.994915
C 6 H 8 N 1 O 2
126.14
126.055504
P
hypothetical
N-term
Unimod:122
(2S)-1-formylpyrrolidine-2-carboxylic acid
1-formyl-2-pyrrolidinecarboxylic acid
1-formylproline
N-formyl-L-proline
N-formylated L-proline
NFoPro
PSI-MOD
MOD:00389
CAUTION - observations of this modification can be attributed to unintended artifactual production, or to spurious peptide MS identification. This modification is probably not a natural post-translational modification [JSG].
N-formyl-L-proline
A protein modification that effectively converts an L-proline residue to N-formyl-L-proline.
PubMed:12051774
PubMed:5464655
RESID:AA0384
Unimod:122#N-term
(2S)-1-formylpyrrolidine-2-carboxylic acid
1-formyl-2-pyrrolidinecarboxylic acid
1-formylproline
N-formyl-L-proline
N-formylated L-proline
NFoPro
A protein modification that effectively converts an L-serine residue to O-decanoyl-L-serine.
154.25
C 10 H 18 N 0 O 1
154.13576
C 13 H 23 N 1 O 3
241.33
241.1678
S
natural
Unimod:449
uniprot.ptm:PTM-0234
(2S)-2-amino-3-(decanoyloxy)propanoic acid
L-serine decanoate ester
LIPID O-decanoyl serine
O-decanoyl-L-serine
O-decanoylated L-serine
O3-decanoyl-L-serine
ODecSer
PSI-MOD
Decanoyl
lipid
MOD:00390
O-decanoyl-L-serine
A protein modification that effectively converts an L-serine residue to O-decanoyl-L-serine.
PubMed:12630926
RESID:AA0385
Unimod:449#S
(2S)-2-amino-3-(decanoyloxy)propanoic acid
L-serine decanoate ester
LIPID O-decanoyl serine
O-decanoyl-L-serine
O-decanoylated L-serine
O3-decanoyl-L-serine
ODecSer
Decanoyl
lipid
A protein modification that effectively converts an L-threonine residue to O-octanoyl-L-threonine.
126.2
C 8 H 14 N 0 O 1
126.10446
C 12 H 21 N 1 O 3
227.3
227.15215
T
natural
Unimod:426
uniprot.ptm:PTM-0240
(2S)-2-amino-3-(octanoyloxy)butanoic acid
L-threonine octanoate ester
LIPID O-octanoyl threonine
O-octanoyl-L-threonine
O-octanoylated L-threonine
O3-octanoyl-L-threonine
OOctThr
PSI-MOD
Octanoyl
octanoyl
MOD:00391
O-octanoyl-L-threonine
A protein modification that effectively converts an L-threonine residue to O-octanoyl-L-threonine.
PubMed:11546772
PubMed:12716131
RESID:AA0386
Unimod:426#T
(2S)-2-amino-3-(octanoyloxy)butanoic acid
L-threonine octanoate ester
LIPID O-octanoyl threonine
O-octanoyl-L-threonine
O-octanoylated L-threonine
O3-octanoyl-L-threonine
OOctThr
Octanoyl
octanoyl
A protein modification that effectively converts an L-threonine residue to O-decanoyl-L-threonine.
154.25
C 10 H 18 N 0 O 1
154.13576
C 14 H 25 N 1 O 3
255.36
255.18344
T
natural
Unimod:449
uniprot.ptm:PTM-0235
(2S)-2-amino-3-(decanoyloxy)propanoic acid
L-threonine decanoate ester
LIPID O-decanoyl threonine
O-decanoyl-L-threonine
O-decanoylated L-threonine
O3-decanoyl-L-threonine
ODecThr
PSI-MOD
Decanoyl
lipid
MOD:00392
O-decanoyl-L-threonine
A protein modification that effectively converts an L-threonine residue to O-decanoyl-L-threonine.
PubMed:11546772
RESID:AA0387
Unimod:449#T
(2S)-2-amino-3-(decanoyloxy)propanoic acid
L-threonine decanoate ester
LIPID O-decanoyl threonine
O-decanoyl-L-threonine
O-decanoylated L-threonine
O3-decanoyl-L-threonine
ODecThr
Decanoyl
lipid
A protein modification that effectively replaces a hydroxyl group hydrogen with a methyl group to produce either an ether from an alcohol or an ester from an acid.
OMeRes
PSI-MOD
MOD:00393
O-methylated residue
A protein modification that effectively replaces a hydroxyl group hydrogen with a methyl group to produce either an ether from an alcohol or an ester from an acid.
PubMed:18688235
OMeRes
A protein modification that effectively replaces one hydrogen atom with one acetyl group.
42.04
C 2 H 2 O 1
42.010567
X
artifact
Unimod:1
Ac1Res
Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac)
PSI-MOD
Acetyl
Acetylation
MOD:00394
Amino hydrogens are replaced to produce amides; hydroxyl hydrogens are replaced to produce esters; and hydrosulfanyl (thiol) hydrogens are replaced to produce sulfanyl esters (thiol esters). From DeltaMass: Average Mass: 42
monoacetylated residue
A protein modification that effectively replaces one hydrogen atom with one acetyl group.
DeltaMass:0
PubMed:11857757
PubMed:11999733
PubMed:12175151
PubMed:14730666
PubMed:15350136
Unimod:1
Ac1Res
Acetylation (N terminus, N epsilon of Lysine, O of Serine) (Ac)
Acetyl
Acetylation
A protein modification that crosslinks two residues by formation of a thioester bond between a cysteine thiol and either an alpha-carbonyl, as in S-(L-methionyl-L-cysteine), or a sidechain carbonyl, as in S-(L-isoglutamyl)-L-cysteine.
PSI-MOD
MOD:00395
thioester crosslinked residues
A protein modification that crosslinks two residues by formation of a thioester bond between a cysteine thiol and either an alpha-carbonyl, as in S-(L-methionyl-L-cysteine), or a sidechain carbonyl, as in S-(L-isoglutamyl)-L-cysteine.
PubMed:18688235
A protein modification that effectively replaces a residue hydrogen atom on an oxygen with a carbohydrate-like group through a glycosidic bond.
OGlycoRes
PSI-MOD
MOD:00396
O-glycosylated residue
A protein modification that effectively replaces a residue hydrogen atom on an oxygen with a carbohydrate-like group through a glycosidic bond.
PubMed:18688235
OGlycoRes
A protein modification that is produced by reaction with iodoacetamide, usually replacement of a reactive hydrogen with a methylcarboxamido group.
57.05
C 2 H 3 N 1 O 1
57.021465
X
artifact
Unimod:4
PSI-MOD
Carbamidomethyl
Iodoacetamide derivative
MOD:00397
iodoacetamide derivatized residue
A protein modification that is produced by reaction with iodoacetamide, usually replacement of a reactive hydrogen with a methylcarboxamido group.
PubMed:11327326
PubMed:11510821
PubMed:12422359
Unimod:4
Carbamidomethyl
Iodoacetamide derivative
A protein modification that effectively replaces a hydrogen atom with a carbamoyl (carboxamido) group. Replacement of an amino hydrogen produces a ureido group.
43.02
C 1 H 1 N 1 O 1
43.005814
X
Unimod:5
Carbamylation
PSI-MOD
Carbamyl
Carbamylation
MOD:00398
This modification can be produced by hydrogen cyanate, either used as a reagent or as released by urea degradation in solution [JSG].
carbamoylated residue
A protein modification that effectively replaces a hydrogen atom with a carbamoyl (carboxamido) group. Replacement of an amino hydrogen produces a ureido group.
DeltaMass:56
PubMed:10978403
PubMed:12203680
Unimod:5
Carbamylation
Carbamyl
Carbamylation
A protein modification that is produced by reaction with iodoacetic acid, usually replacement of a reactive hydrogen with a methylcarboxy group.
58.04
C 2 H 2 O 2
58.005478
X
artifact
Unimod:6
Carboxymethyl (on Cysteine)
PSI-MOD
Carboxymethyl
Iodoacetic acid derivative
MOD:00399
From DeltaMass: Average Mass: 58 Abbreviation:CmC Average Mass Change:58 Notes:Cysteine reacts with iodoacetic acid to produce carboxymethyl cysteine.
iodoacetic acid derivatized residue
A protein modification that is produced by reaction with iodoacetic acid, usually replacement of a reactive hydrogen with a methylcarboxy group.
DeltaMass:64
Unimod:6
Carboxymethyl (on Cysteine)
Carboxymethyl
Iodoacetic acid derivative
A protein modification that effectively replaces a carboxamido group with a carboxyl group, with both a gain of oxygen and loss of a nitrogen and a hydrogen.
0.98
H -1 N -1 O 1
0.984016
X
Unimod:7
Deamidation of Asparagine and Glutamine to Aspartate and Glutamate
dNRes
deamidationkq
PSI-MOD
Deamidated
Deamidation
MOD:00400
From DeltaMass: References:Vish Katta.
deamidated residue
A protein modification that effectively replaces a carboxamido group with a carboxyl group, with both a gain of oxygen and loss of a nitrogen and a hydrogen.
DeltaMass:32
OMSSA:4
Unimod:7
Deamidation of Asparagine and Glutamine to Aspartate and Glutamate
dNRes
deamidationkq
Deamidated
Deamidation
A protein modification that is produced by formation of an adduct of a cysteine residue with the Gygi isotope-coded affinity tag d0 reagent.
486.63
C 22 H 38 N 4 O 6 S 1
486.25122
C 25 H 43 N 5 O 7 S 2
589.77
589.2604
C
artifact
Unimod:8
PSI-MOD
Gygi ICAT(TM) d0
ICAT-G
MOD:00401
Gygi ICAT(TM) d0 modified cysteine
A protein modification that is produced by formation of an adduct of a cysteine residue with the Gygi isotope-coded affinity tag d0 reagent.
PubMed:10504701
Unimod:8#C
Gygi ICAT(TM) d0
ICAT-G
A protein modification that is produced by formation of an adduct of a cysteine residue with the Gygi isotope-coded affinity tag d8 reagent.
494.3
C 22 (1)H 30 (2)H 8 N 4 O 6 S 1
494.30142
C 25 (1)H 35 (2)H 8 N 5 O 7 S 2
597.31
597.3106
C
artifact
Unimod:9
PSI-MOD
Gygi ICAT(TM) d8
ICAT-G:2H(8)
MOD:00402
Gygi ICAT(TM) d8 modified cysteine
A protein modification that is produced by formation of an adduct of a cysteine residue with the Gygi isotope-coded affinity tag d8 reagent.
PubMed:10504701
Unimod:9#C
Gygi ICAT(TM) d8
ICAT-G:2H(8)
A protein modification that effectively converts an L-methionine residue to homoserine.
-30.09
C -1 H -2 O 1 S -1
-29.992805
C 4 H 7 N 1 O 2
101.1
101.047676
M
artifact
C-term
Unimod:10
Homoserine formed from Met by CNBr treatment
ctermpephsem
PSI-MOD
Homoserine
Met->Hse
MOD:00403
Usually formed from methionine by reaction with cyanogen bromide, CNBr, which cleaves the peptide at the methionine carboxyl group and the following residue amino group.
homoserine
A protein modification that effectively converts an L-methionine residue to homoserine.
DeltaMass:113
OMSSA:56
Unimod:10#M
Homoserine formed from Met by CNBr treatment
ctermpephsem
Homoserine
Met->Hse
A protein modification that effectively converts an L-methionine residue to homoserine lactone.
-48.1
C -1 H -4 S -1
-48.003372
C 4 H 5 N 1 O 1
83.09
83.03712
M
artifact
C-term
Unimod:11
ctermpephselactm
PSI-MOD
Homoserine lactone
Met->Hsl
MOD:00404
Usually formed from methionine by reaction with cyanogen bromide, CNBr, which cleaves the peptide at the methionine carboxyl group. Under acid conditions the homoserine dehydrates to form the cyclic lactone.
homoserine lactone
A protein modification that effectively converts an L-methionine residue to homoserine lactone.
DeltaMass:90
OMSSA:57
Unimod:11#M
ctermpephselactm
Homoserine lactone
Met->Hsl
A protein modification that is produced by formation of an adduct of a cysteine residue with the Applied Biosystems original isotope-coded affinity tag d8 reagent.
450.28
C 20 (1)H 26 (2)H 8 N 4 O 5 S 1
450.2752
C 23 (1)H 31 (2)H 8 N 5 O 6 S 2
553.28
553.28436
C
artifact
Unimod:12
PSI-MOD
Applied Biosystems original ICAT(TM) d8
ICAT-D:2H(8)
MOD:00405
Applied Biosystems original ICAT(TM) d8 modified cysteine
A protein modification that is produced by formation of an adduct of a cysteine residue with the Applied Biosystems original isotope-coded affinity tag d8 reagent.
Unimod:12#C
Applied Biosystems original ICAT(TM) d8
ICAT-D:2H(8)
A protein modification that is produced by formation of an adduct of a cysteine residue with the Applied Biosystems original isotope-coded affinity tag d0 reagent.
442.22
C 20 (1)H 34 N 4 O 5 S 1
442.225
C 23 (1)H 39 N 5 O 6 S 2
545.23
545.2342
C
artifact
Unimod:13
PSI-MOD
Applied Biosystems original ICAT(TM) d0
ICAT-D
MOD:00406
Applied Biosystems original ICAT(TM) d0 modified cysteine
A protein modification that is produced by formation of an adduct of a cysteine residue with the Applied Biosystems original isotope-coded affinity tag d0 reagent.
Unimod:13#C
Applied Biosystems original ICAT(TM) d0
ICAT-D
A protein modification that effectively replaces a carboxyl group with a carboxy methyl ester group. OBSOLETE because Unimod:14 merged with entry 34, remap to MOD:00599.
MOD:00599
14.03
C 1 H 2
14.01565
X
ResOMe
PSI-MOD
MOD:00407
residue methyl ester
true
A protein modification that effectively replaces a carboxyl group with a carboxy methyl ester group. OBSOLETE because Unimod:14 merged with entry 34, remap to MOD:00599.
PubMed:18688235
ResOMe
A protein modification that effectively replaces a residue amino or imino hydrogen with an acetyl group.
42.04
C 2 H 2 O 1
42.010567
X
N-Acetyl
N-Acetylation
NAcRes
PSI-MOD
MOD:00408
mono N-acetylated residue
A protein modification that effectively replaces a residue amino or imino hydrogen with an acetyl group.
PubMed:18688235
N-Acetyl
N-Acetylation
NAcRes
A protein modification that effectively replaces a residue amino group with a formamido group.
28.01
C 1 O 1
27.994915
X
NFoRes
ntermformyl
ntermpepformyl
PSI-MOD
Formyl
MOD:00409
N-formylated residue
A protein modification that effectively replaces a residue amino group with a formamido group.
OMSSA:44
OMSSA:82
NFoRes
ntermformyl
ntermpepformyl
Formyl
A protein modification that effectively converts an L-cysteine residue to S-(N-isopropylcarboxamidomethyl)-L-cysteine.
99.13
C 5 H 9 N 1 O 1 S 0
99.06841
C 8 H 14 N 2 O 2 S 1
202.27
202.0776
C
artifact
Unimod:17
nipcam
PSI-MOD
N-isopropylcarboxamidomethyl
NIPCAM
MOD:00410
S-(N-isopropylcarboxamidomethyl)-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-(N-isopropylcarboxamidomethyl)-L-cysteine.
OMSSA:84
PubMed:11465505
PubMed:8465942
Unimod:17#C
nipcam
N-isopropylcarboxamidomethyl
NIPCAM
modification from Unimod Isotopic label. OBSOLETE because Unimod:18 is now merged with entry 258 remap to MOD:00581 'single 018 label'
MOD:00581
2.0
(16)O -1 (18)O 1
2.004246
X
artifact
PSI-MOD
MOD:00411
A modification from Unimod:18
O18 label
true
modification from Unimod Isotopic label. OBSOLETE because Unimod:18 is now merged with entry 258 remap to MOD:00581 'single 018 label'
PubMed:18688235
modification from Unimod artifact. OBSOLETE because Unimod entry 19 is now merged with Unimod 35 remap to MOD:00425 'monohydroxylated residue'.
MOD:00425
16.0
O 1
15.994915
X
PSI-MOD
MOD:00412
oxidation
true
modification from Unimod artifact. OBSOLETE because Unimod entry 19 is now merged with Unimod 35 remap to MOD:00425 'monohydroxylated residue'.
PubMed:18688235
A protein modification that is produced by reaction of a cysteine residue with biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine.
414.52
C 18 H 30 N 4 O 5 S 1
414.1937
C 21 H 35 N 5 O 6 S 2
517.66
517.2029
C
artifact
Unimod:20
PSI-MOD
Biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine
PEO-Iodoacetyl-LC-Biotin
MOD:00413
biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine derivatized cysteine
A protein modification that is produced by reaction of a cysteine residue with biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine.
Unimod:20#C
Biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine
PEO-Iodoacetyl-LC-Biotin
A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with one methyl group.
14.03
C 1 H 2 N 0 O 0
14.01565
C 7 H 14 N 4 O 1
170.22
170.11676
R
Unimod:34
Me1Arg
N-methyl Arginyl
methylr
PSI-MOD
Methyl
MOD:00414
From DeltaMass: formula incorrect, N and O reversed
monomethylated L-arginine
A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with one methyl group.
DeltaMass:215
OMSSA:77
Unimod:34#R
Me1Arg
N-methyl Arginyl
methylr
Methyl
modification from Unimod - OBSOLETE because Unimod entry 22 is now merged with entry 21 remap to MOD:00696 'phosphorylated residue'.
MOD:00696
79.98
H 1 O 3 P 1
79.96633
X
artifact
PSI-MOD
MOD:00415
phosphorylation without neutral loss
true
modification from Unimod - OBSOLETE because Unimod entry 22 is now merged with entry 21 remap to MOD:00696 'phosphorylated residue'.
PubMed:18688235
A change resulting in an alteration of the measured molecular mass of a peptide or protein hydroxyl amino acid phosphorylated promptly followed by secondary loss of a neutral trihydrogen phosphate molecular fragment.
-18.02
H -2 O -1
-18.010565
X
artifact
Unimod:23
PSI-MOD
Dehydrated
Dehydration
MOD:00416
O4-phosphotyrosine does not lose phosphate by this mechanism. Unimod does not provide a citation for this particular modification [JSG].
phosphorylation of an hydroxyl amino acid with prompt loss of phosphate
A change resulting in an alteration of the measured molecular mass of a peptide or protein hydroxyl amino acid phosphorylated promptly followed by secondary loss of a neutral trihydrogen phosphate molecular fragment.
Unimod:23
Dehydrated
Dehydration
A protein modification that effectively converts an L-cysteine residue to S-carboxamidoethyl-L-cysteine.
71.08
C 3 H 5 N 1 O 1 S 0
71.03712
C 6 H 10 N 2 O 2 S 1
174.22
174.0463
C
artifact
Unimod:24
PAM-Cys
Propionamide or Acrylamide adduct
S-(3-amino-3-oxopropyl)cysteine
S-carbamoylethyl-L-cysteine
S-propanamide-L-cysteine
propionamidec
PSI-MOD
Acrylamide adduct
Propionamide
MOD:00417
From DeltaMass: References: Anal. Biochem. Vol 216 No. 1 p131 (citation not found) Notes: Residual acrylamide in SDS gels can label free cysteines to produce propionamido-Cys (also known as PAM-Cys)
S-carboxamidoethyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-carboxamidoethyl-L-cysteine.
DeltaMass:72
OMSSA:5
PubMed:1481983
Unimod:24#C
PAM-Cys
Propionamide or Acrylamide adduct
S-(3-amino-3-oxopropyl)cysteine
S-carbamoylethyl-L-cysteine
S-propanamide-L-cysteine
propionamidec
Acrylamide adduct
Propionamide
A protein modification that effectively replaces a hydrogen atom with an (pyridin-3-yl)acetyl group.
119.12
C 7 H 5 N 1 O 1
119.03712
X
artifact
Unimod:25
PSI-MOD
Pyridylacetyl
pyridylacetyl
MOD:00418
Produced by reaction with N-[(pyrid-3-yl)acetyl]oxy-succinimide [JSG].
pyridylacetylated residue
A protein modification that effectively replaces a hydrogen atom with an (pyridin-3-yl)acetyl group.
PubMed:9276974
Unimod:25
Pyridylacetyl
pyridylacetyl
A protein modification that effectively converts an L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid.
40.02
C 2 H 0 N 0 O 1 S 0
39.994915
C 5 H 6 N 1 O 2 S 1
144.17
144.01192
C
artifact
N-term
Unimod:26
(R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid
5-oxothiomorpholine-3-carboxylic acid
Otc
S-carbamoylmethylcysteine cyclization (N-terminus)
PSI-MOD
Pyro-carbamidomethyl
S-carbamoylmethylcysteine cyclization (N-terminus)
MOD:00419
From DeltaMass: A secondary modification affecting peptides with S-carbamoylmethyl-L-cysteine (CamC) at the N-terminus. These exist in enzymatic digests of proteins that have been S-alkylated with iodoacetamide. Cyclization of N-terminal CamC gives a residue of (R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid. Peptides in which this has occurred become more hydrophobic, and lose 17 Da from the N-terminal residue.
(R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid
A protein modification that effectively converts an L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid.
DeltaMass:336
PubMed:12643538
Unimod:26#C
(R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid
5-oxothiomorpholine-3-carboxylic acid
Otc
S-carbamoylmethylcysteine cyclization (N-terminus)
Pyro-carbamidomethyl
S-carbamoylmethylcysteine cyclization (N-terminus)
A protein modification that effectively converts an L-glutamic acid residue to 2-pyrrolidone-5-carboxylic acid.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 5 H 6 N 1 O 2
112.11
112.039856
E
artifact
N-term
Unimod:27
uniprot.ptm:PTM-0262
(2S)-5-oxo-2-pyrrolidinecarboxylic acid
2-oxopyrrolidine-5-carboxylic acid
2-pyrrolidone-5-carboxylic acid
5-oxoproline
5-oxopyrrolidine-2-carboxylic acid
5-pyrrolidone-2-carboxylic acid
MOD_RES Pyrrolidone carboxylic acid (Glu)
PCA
PyrGlu(Glu)
Pyroglutamic Acid formed from Glutamic Acid
ntermpeppyroe
pyroglutamic acid
PSI-MOD
Glu->pyro-Glu
Pyro-glu from E
MOD:00420
From DeltaMass: References: The conversion of glutamic acid to pyroglutamic was reported for the beta-amyloid protein. Miller et al. Arch. Biochem. Biophy. (1993) 301, 41-52 [DeltaMass]. The modification in amyloid protein is probably an artifact of treatment with strong acid under anhydrous conditions. Peptides with N-terminal glutamic acid isolated from single cells of Aplysia neurons show partial conversion to pyroglutamic acid, possibly dependent on a temperature sensitive factor [JSG].
2-pyrrolidone-5-carboxylic acid (Glu)
A protein modification that effectively converts an L-glutamic acid residue to 2-pyrrolidone-5-carboxylic acid.
DeltaMass:16
OMSSA:109
PubMed:10214721
PubMed:1836357
PubMed:3473473
PubMed:8382902
RESID:AA0031#GLU
Unimod:27#E
(2S)-5-oxo-2-pyrrolidinecarboxylic acid
2-oxopyrrolidine-5-carboxylic acid
2-pyrrolidone-5-carboxylic acid
5-oxoproline
5-oxopyrrolidine-2-carboxylic acid
5-pyrrolidone-2-carboxylic acid
MOD_RES Pyrrolidone carboxylic acid (Glu)
PCA
PyrGlu(Glu)
Pyroglutamic Acid formed from Glutamic Acid
ntermpeppyroe
pyroglutamic acid
Glu->pyro-Glu
Pyro-glu from E
A protein modification that effectively replaces a residue hydrogen atom on a carbon with a carbohydrate-like group through a glycosidic bond.
CGlycoRes
PSI-MOD
MOD:00421
C-glycosylated residue
A protein modification that effectively replaces a residue hydrogen atom on a carbon with a carbohydrate-like group through a glycosidic bond.
PubMed:18688235
CGlycoRes
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a morpholine-2-acetyl group.
127.14
C 6 H 9 N 1 O 2
127.06333
X
artifact
N-term
Unimod:29
N-succinimidylmorpholine-2-acetate alpha-amino derivative
PSI-MOD
N-Succinimidyl-2-morpholine acetate
SMA
MOD:00422
The Unimod name "N-Succinimidyl-3-morpholine acetate" appears to have been a typographical error [JSG].
alpha-amino morpholine-2-acetylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a morpholine-2-acetyl group.
PubMed:10446193
Unimod:29#N-term
N-succinimidylmorpholine-2-acetate alpha-amino derivative
N-Succinimidyl-2-morpholine acetate
SMA
A protein modification that effectively substitutes one sodium atom for one hydrogen atom.
21.98
H -1 Na 1
21.981943
X
Unimod:30
Na1Res
Sodium
PSI-MOD
Cation:Na
Sodium adduct
MOD:00423
monosodium salt
A protein modification that effectively substitutes one sodium atom for one hydrogen atom.
DeltaMass:0
Unimod:30
Na1Res
Sodium
Cation:Na
Sodium adduct
A protein modification that effectively converts an L-cysteine residue to S-pyridylethyl-L-cysteine.
105.14
C 7 H 7 N 1
105.057846
C 10 H 12 N 2 O 1 S 1
208.28
208.06703
C
artifact
Unimod:31
PECys
Pyridylethyl Cystenyl
S-pyridinylethyl-L-cysteine
spyridylethylc
vinylpyridine derivatized cysteine residue
PSI-MOD
Pyridylethyl
S-pyridylethylation
MOD:00424
From DeltaMass: Formula:C10H12O2N1S1 (formula incorrect, N and O reversed) Monoisotopic Mass Change:208.067 Average Mass Change:208.286 (mass incorrect, aggregate not delta) References:PE Sciex
S-pyridylethyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-pyridylethyl-L-cysteine.
DeltaMass:253
OMSSA:112
PubMed:11760118
PubMed:626389
PubMed:8297018
PubMed:8783016
Unimod:31#C
PECys
Pyridylethyl Cystenyl
S-pyridinylethyl-L-cysteine
spyridylethylc
vinylpyridine derivatized cysteine residue
Pyridylethyl
S-pyridylethylation
A protein modification that effectively replaces one hydrogen atom with a hydroxyl group.
16.0
O 1
15.994915
X
Unimod:35
Hy1Res
PSI-MOD
Oxidation
Oxidation or Hydroxylation
MOD:00425
monohydroxylated residue
A protein modification that effectively replaces one hydrogen atom with a hydroxyl group.
Unimod:35
Hy1Res
Oxidation
Oxidation or Hydroxylation
A protein modification that effectively replaces a residue hydrogen atom on a sulfur with a carbohydrate-like group through a glycosidic bond.
SGlycoRes
PSI-MOD
MOD:00426
S-glycosylated residue
A protein modification that effectively replaces a residue hydrogen atom on a sulfur with a carbohydrate-like group through a glycosidic bond.
PubMed:18688235
SGlycoRes
A protein modification that effectively replaces a hydrogen atom with a methyl group.
MeRes
Methylation (N terminus, N epsilon of Lysine, O of Serine, Threonine or C terminus, N of Asparagine)
PSI-MOD
MOD:00427
From DeltaMass: Average Mass: 14 Average Mass Change:14 References:Methylation of Asparagine (found in phycobiliproteins) Klotz and Glazer (1987) J. Biol. Chem. 262; 17350-17355
methylated residue
A protein modification that effectively replaces a hydrogen atom with a methyl group.
DeltaMass:36
MeRes
Methylation (N terminus, N epsilon of Lysine, O of Serine, Threonine or C terminus, N of Asparagine)
A protein modification that effectively replaces two hydrogen atoms with two hydroxyl groups.
32.0
C 0 H 0 N 0 O 2
31.989828
X
Unimod:425
Hy2Res
PSI-MOD
Dioxidation
dihydroxy
MOD:00428
dihydroxylated residue
A protein modification that effectively replaces two hydrogen atoms with two hydroxyl groups.
PubMed:12686488
Unimod:425
Hy2Res
Dioxidation
dihydroxy
A protein modification that effectively replaces two hydrogen atoms with two methyl groups.
28.05
C 2 H 4
28.0313
X
Unimod:36
Me2Res
N,N dimethylation (of Arginine or Lysine)
PSI-MOD
Dimethyl
di-Methylation
MOD:00429
For amino-terminal proline residues, dimethylation can effectively only be accomplished with a protonated imino group. This process accounts only for dimethylation and not protonation. The alternative Me2+Res process accounts for both protonation and dimethylation [JSG].
dimethylated residue
A protein modification that effectively replaces two hydrogen atoms with two methyl groups.
DeltaMass:0
PubMed:12964758
PubMed:14570711
Unimod:36
Me2Res
N,N dimethylation (of Arginine or Lysine)
Dimethyl
di-Methylation
A protein modification that effectively replaces three hydrogen atoms with three methyl groups.
42.08
C 3 H 6
42.04695
X
Unimod:37
Me3Res
PSI-MOD
Trimethyl
tri-Methylation
MOD:00430
For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative Me3+Res process accounts for both protonation and trimethylation.
trimethylated residue
A protein modification that effectively replaces three hydrogen atoms with three methyl groups.
PubMed:12590383
PubMed:3145979
PubMed:4304194
PubMed:6778808
PubMed:7093227
PubMed:8453381
Unimod:37
Me3Res
Trimethyl
tri-Methylation
Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral molecular fragment.
NLModRes
PSI-MOD
MOD:00431
modified residue with a secondary neutral loss
Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral molecular fragment.
PubMed:18688235
NLModRes
Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral trihydrogen phosphate molecular fragment.
dPhosModRes
PSI-MOD
MOD:00432
modified residue with neutral loss of phosphate
Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral trihydrogen phosphate molecular fragment.
PubMed:18688235
dPhosModRes
A protein modification that effectively replaces a hydrogen atom with an glucose group through a glycosidic bond.
162.14
C 6 H 10 N 0 O 5
162.05283
X
GlcRes
PSI-MOD
MOD:00433
monoglucosylated residue
A protein modification that effectively replaces a hydrogen atom with an glucose group through a glycosidic bond.
PubMed:18688235
GlcRes
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexose sugar group through a glycosidic bond.
X
natural
Unimod:41
Hex
Hexoses (Fru, Gal, Glc, Man)
O-Glycosyl-
PSI-MOD
Hex
Hexose
MOD:00434
From DeltaMass: Average Mass: 162 Formula:C6 H10 05 Monoisotopic Mass Change:162.053 Average Mass Change:162.143 References:PE Sciex.
hexosylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexose sugar group through a glycosidic bond.
DeltaMass:203
PubMed:15279557
Unimod:41
Hex
Hexoses (Fru, Gal, Glc, Man)
O-Glycosyl-
Hex
Hexose
Covalent modification of a peptide or protein amino acid phosphorylated serine with a secondary loss of a neutral trihydrogen phosphate molecular fragment.
-97.99
C 0 H -3 N 0 O -4 P -1
-97.9769
C 3 H 3 N 1 O 1
69.06
69.02146
MOD:00046
artifact
dPhosOPhosSer
PSI-MOD
MOD:00435
O-phospho-L-serine with neutral loss of phosphate
Covalent modification of a peptide or protein amino acid phosphorylated serine with a secondary loss of a neutral trihydrogen phosphate molecular fragment.
PubMed:18688235
dPhosOPhosSer
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylhexosamine group through a glycosidic bond.
203.19
C 8 H 13 N 1 O 5
203.07938
X
GNO:G29068FM
HexNAc
PSI-MOD
HexNAc
N-Acetylhexosamine
MOD:00436
N-acetylhexosaminylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylhexosamine group through a glycosidic bond.
PubMed:18688235
HexNAc
HexNAc
N-Acetylhexosamine
A protein modification that effectively replaces a hydrogen atom with a farnesyl group.
204.36
C 15 H 24
204.1878
X
natural
Unimod:44
FarnRes
Farnesylation
PSI-MOD
Farnesyl
Farnesylation
MOD:00437
From DeltaMass: Average Mass: 204
farnesylated residue
A protein modification that effectively replaces a hydrogen atom with a farnesyl group.
DeltaMass:0
PubMed:15609361
Unimod:44
FarnRes
Farnesylation
Farnesyl
Farnesylation
A protein modification that effectively replaces a hydrogen atom with a myristoyl group.
210.36
C 14 H 26 O 1
210.19836
X
natural
Unimod:45
C14:0 aliphatic acylated residue
MyrRes
Myristoylation
PSI-MOD
Myristoyl
Myristoylation
MOD:00438
From DeltaMass: Average Mass: 210
myristoylated residue
A protein modification that effectively replaces a hydrogen atom with a myristoyl group.
DeltaMass:0
Unimod:45
C14:0 aliphatic acylated residue
MyrRes
Myristoylation
Myristoyl
Myristoylation
Covalent modification of a peptide or protein amino acid phosphorylated threonine with a secondary loss of a neutral trihydrogen phosphate molecular fragment.
-97.99
C 0 H -3 N 0 O -4 P -1
-97.9769
C 4 H 5 N 1 O 1
83.09
83.03712
MOD:00047
artifact
dPhosOPhosThr
PSI-MOD
MOD:00439
O-phospho-L-threonine with neutral loss of phosphate
Covalent modification of a peptide or protein amino acid phosphorylated threonine with a secondary loss of a neutral trihydrogen phosphate molecular fragment.
PubMed:18688235
dPhosOPhosThr
A protein modification that effectively replaces a hydrogen atom with a palmitoyl group.
238.41
C 16 H 30 O 1
238.22966
X
natural
Hexadecanoylated residue
Palmitoylation
PamRes
PSI-MOD
Palmitoyl
Palmitoylation
MOD:00440
From DeltaMass: Average Mass: 238
palmitoylated residue
A protein modification that effectively replaces a hydrogen atom with a palmitoyl group.
DeltaMass:0
Hexadecanoylated residue
Palmitoylation
PamRes
Palmitoyl
Palmitoylation
A protein modification that effectively replaces a hydrogen atom with a geranylgeranyl group.
272.48
C 20 H 32
272.2504
X
natural
Unimod:48
Geranylgeranylation
GergerRes
PSI-MOD
Geranyl-geranyl
GeranylGeranyl
MOD:00441
From DeltaMass: Average Mass: 272
geranylgeranylated residue
A protein modification that effectively replaces a hydrogen atom with a geranylgeranyl group.
DeltaMass:0
PubMed:15609361
Unimod:48
Geranylgeranylation
GergerRes
Geranyl-geranyl
GeranylGeranyl
Covalent modification of a peptide or protein L-arginine residue to protonated omega-N,omega-N'-dimethylated L-arginine with secondary loss of an N,N'-carbodiimide molecular fragment.
42.04
C 1 H 2 N 2 O 0
42.021797
C 7 H 14 N 2 O 1
142.2
142.11061
R
artifact
dCDI-NNMe2+Arg
PSI-MOD
MOD:00442
protonated omega-N,omega-N'-dimethylated L-arginine with secondary neutral loss of N,N'-carbodiimide
Covalent modification of a peptide or protein L-arginine residue to protonated omega-N,omega-N'-dimethylated L-arginine with secondary loss of an N,N'-carbodiimide molecular fragment.
PubMed:15835918
PubMed:18688235
dCDI-NNMe2+Arg
Covalent modification of a peptide or protein L-arginine residue to protonated omega-N,omega-N-dimethlyated L-arginine with secondary neutral loss of an N,N-dimethylamine molecular fragment.
59.09
C 2 H 7 N 2
59.060925
C 6 H 10 N 3 O 1
140.17
140.08238
R
artifact
dDMA-NoMe2+Arg
PSI-MOD
MOD:00443
protonated omega-N,omega-N-dimethlyated L-arginine with secondary neutral loss of N,N-dimethylamine
Covalent modification of a peptide or protein L-arginine residue to protonated omega-N,omega-N-dimethlyated L-arginine with secondary neutral loss of an N,N-dimethylamine molecular fragment.
PubMed:15835918
PubMed:18688235
dDMA-NoMe2+Arg
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine.
789.32
C 51 H 96 O 5
788.72577
C 54 H 101 N 1 O 6 S 1
892.46
891.735
C
natural
N-term
Unimod:51
ntermpeptripalmitatec
PSI-MOD
N-acyl diglyceride cysteine
Tripalmitate
MOD:00444
N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine.
OMSSA:118
PubMed:10356335
Unimod:51
ntermpeptripalmitatec
N-acyl diglyceride cysteine
Tripalmitate
A protein modification that effectively converts an L-lysine residue to L-homoarginine, such as reaction with O-methylisourea.
42.04
C 1 H 2 N 2
42.021797
C 7 H 14 N 4 O 1
170.22
170.11676
K
artifact
Unimod:52
guanidinationk
PSI-MOD
Guanidination
Guanidinyl
MOD:00445
L-homoarginine
A protein modification that effectively converts an L-lysine residue to L-homoarginine, such as reaction with O-methylisourea.
OMSSA:53
PubMed:11078590
PubMed:11085420
PubMed:11821862
Unimod:52
guanidinationk
Guanidination
Guanidinyl
A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal.
156.22
C 9 H 16 O 2
156.11504
X
artifact
Unimod:53
PSI-MOD
4-hydroxynonenal (HNE)
HNE
MOD:00446
4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG].
4-hydroxynonenal adduct
A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal.
PubMed:11327326
PubMed:15133838
Unimod:53
4-hydroxynonenal (HNE)
HNE
A protein modification that effectively results from forming an adduct with a glucuronic acid either through a carboxyl group amide or ester bond, or through C1-glycosylation.
176.12
C 6 H 8 O 6
176.03209
X
Unimod:54
N-Glucuronyl (N terminus)
PSI-MOD
Glucuronyl
N-glucuronylation
MOD:00447
N-glucuronylated residue
A protein modification that effectively results from forming an adduct with a glucuronic acid either through a carboxyl group amide or ester bond, or through C1-glycosylation.
DeltaMass:0
PubMed:7398618
Unimod:54#N-term
N-Glucuronyl (N terminus)
Glucuronyl
N-glucuronylation
A protein modification that effectively replaces a hydrogen atom with an N-acetylaminoglucose group through a glycosidic bond.
203.19
C 8 H 13 N 1 O 5
203.07938
X
GlcNAcRes
PSI-MOD
HexNAc
MOD:00448
mono-N-acetylaminoglucosylated residue
A protein modification that effectively replaces a hydrogen atom with an N-acetylaminoglucose group through a glycosidic bond.
PubMed:18688235
GlcNAcRes
HexNAc
modification from Unimod Isotopic label
45.03
C 2 (1)H -1 (2)H 3 O 1
45.029396
X
artifact
N-term
Unimod:56
PSI-MOD
Acetate labeling reagent (N-term & K) (heavy form, +3amu)
Acetyl:2H(3)
MOD:00449
acetate labeling reagent (N-term) (heavy form, +3amu)
modification from Unimod Isotopic label
PubMed:11857757
PubMed:11999733
PubMed:12175151
Unimod:56
Acetate labeling reagent (N-term & K) (heavy form, +3amu)
Acetyl:2H(3)
OBSOLETE because this isotopic label from Unimod entry 57 is deprecated
42.01
C 2 (1)H 2 O 1
42.010567
K
artifact
PSI-MOD
MOD:00450
acetate labeling reagent light form (K)
true
OBSOLETE because this isotopic label from Unimod entry 57 is deprecated
PubMed:11857757
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a propanoyl group.
56.06
C 3 H 4 O 1
56.026215
X
artifact
N-term
Unimod:58
PSI-MOD
Propionate labeling reagent light form (N-term & K)
Propionyl
MOD:00451
alpha-amino propanoylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a propanoyl group.
PubMed:11857757
PubMed:11999733
PubMed:12175151
Unimod:58#N-term
Propionate labeling reagent light form (N-term & K)
Propionyl
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(13)C-labeled propanoyl group.
59.04
(13)C 3 H 4 O 1
59.036278
(12)C 6 (13)C 3 H 16 N 2 O 2
187.13
187.13124
X
artifact
N-term
Unimod:59
PSI-MOD
Propionate labeling reagent heavy form (+3amu), N-term & K
Propionyl:13C(3)
MOD:00452
alpha-amino 3x(13)C-labeled propanoylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(13)C-labeled propanoyl group.
PubMed:11857757
PubMed:11999733
PubMed:12175151
Unimod:59#N-term
Propionate labeling reagent heavy form (+3amu), N-term & K
Propionyl:13C(3)
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent light form group.
127.19
C 7 H 13 N 1 O 1
127.09972
X
artifact
Unimod:60
PSI-MOD
GIST-Quat
Quaternary amine labeling reagent light form (N-term & K)
MOD:00453
quaternary amine labeling reagent light form (N-term & K)
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent light form group.
PubMed:11857757
Unimod:60
GIST-Quat
Quaternary amine labeling reagent light form (N-term & K)
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+3amu) form group.
130.12
C 7 (1)H 10 (2)H 3 N 1 O 1
130.11855
C 13 (1)H 22 (2)H 3 N 3 O 2
258.21
258.2135
X
artifact
Unimod:61
PSI-MOD
GIST-Quat:2H(3)
Quaternary amine labeling reagent heavy (+3amu) form, N-term & K
MOD:00454
quaternary amine labeling reagent heavy form (+3amu) (N-term & K)
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+3amu) form group.
PubMed:11857757
Unimod:61
GIST-Quat:2H(3)
Quaternary amine labeling reagent heavy (+3amu) form, N-term & K
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+6amu) form group.
133.14
C 7 H 7 (2)H 6 N 1 O 1
133.13737
X
artifact
Unimod:62
PSI-MOD
GIST-Quat:2H(6)
Quaternary amine labeling reagent heavy form (+6amu), N-term & K
MOD:00455
quaternary amine labeling reagent heavy form (+6amu) (N-term & K)
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+6amu) form group.
PubMed:11857757
Unimod:62
GIST-Quat:2H(6)
Quaternary amine labeling reagent heavy form (+6amu), N-term & K
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+9amu) form group.
136.16
C 7 (1)H 4 (2)H 9 N 1 O 1
136.1562
C 13 (1)H 16 (2)H 9 N 3 O 2
264.25
264.25116
X
artifact
Unimod:63
PSI-MOD
GIST-Quat:2H(9)
Quaternary amine labeling reagent heavy form (+9amu), N-term & K
MOD:00456
quaternary amine labeling reagent heavy form (+9amu) (N-term & K)
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+9amu) form group.
PubMed:11857757
Unimod:63
GIST-Quat:2H(9)
Quaternary amine labeling reagent heavy form (+9amu), N-term & K
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a light succinyl group.
100.03
(12)C 4 (1)H 4 O 3
100.016045
X
natural
N-term
Unimod:64
PSI-MOD
Succinic anhydride labeling reagent light form (N-term)
Succinyl
MOD:00457
4x(12)C, 4x(1)H labeled alpha-amino succinylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a light succinyl group.
PubMed:11857757
PubMed:12175151
Unimod:64#N-term
Succinic anhydride labeling reagent light form (N-term)
Succinyl
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(2)H labeled succinyl group.
104.04
C 4 (2)H 4 O 3
104.04115
X
artifact
N-term
Unimod:65
PSI-MOD
Succinic anhydride labeling reagent, heavy form (+4amu, 4H2), N-term
Succinyl:2H(4)
MOD:00458
4x(2)H labeled alpha-amino succinylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(2)H labeled succinyl group.
PubMed:11857757
PubMed:12175151
Unimod:65#N-term
Succinic anhydride labeling reagent, heavy form (+4amu, 4H2), N-term
Succinyl:2H(4)
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(13)C labeled succinyl group.
104.03
(13)C 4 H 4 O 3
104.029465
X
Unimod:66
PSI-MOD
Succinic anhydride labeling reagent, heavy form (+4amu, 4C13), N-term & K
Succinyl:13C(4)
MOD:00459
4x(13)C labeled alpha-amino succinylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(13)C labeled succinyl group.
PubMed:11857757
PubMed:12175151
Unimod:66#N-term
Succinic anhydride labeling reagent, heavy form (+4amu, 4C13), N-term & K
Succinyl:13C(4)
A protein modification that effectively trioxygenates an L-cysteine residue to L-cysteine sulfonic acid.
48.0
C 0 H 0 N 0 O 3 S 0
47.984745
C 3 H 5 N 1 O 4 S 1
151.14
150.99393
C
artifact
Unimod:345
uniprot.ptm:PTM-0634
(2R)-2-amino-3-sulfopropanoic acid
2-amino-2-carboxyethanesulfonic acid
2-azanyl-3-sulfopropanoic acid
3-sulfoalanine
Cya
CysO3H
Cysteic acid, oxidation of cysteine
L-cysteine sulfonic acid
MOD_RES Cysteine sulfonic acid (-SO3H)
cysteic acid
cysteicacidc
cysteine sulphonic acid
PSI-MOD
Trioxidation
cysteine oxidation to cysteic acid
MOD:00460
From DeltaMass: Notes:Treatment of cysteine by strongly oxidising reagents such as performic acid results in the complete oxidation of the sulphur atom. Such treatment is often carried out prior to amino acid analysis as the resulting cysteic acid is then resistant to acid degradation during the hydrolysis procedure.
L-cysteic acid (L-cysteine sulfonic acid)
A protein modification that effectively trioxygenates an L-cysteine residue to L-cysteine sulfonic acid.
ChEBI:17285
DeltaMass:334
OMSSA:34
PubMed:14678012
PubMed:18306178
PubMed:19522542
PubMed:9252331
RESID:AA0556
Unimod:345#C
(2R)-2-amino-3-sulfopropanoic acid
2-amino-2-carboxyethanesulfonic acid
2-azanyl-3-sulfopropanoic acid
3-sulfoalanine
Cya
CysO3H
Cysteic acid, oxidation of cysteine
L-cysteine sulfonic acid
MOD_RES Cysteine sulfonic acid (-SO3H)
cysteic acid
cysteicacidc
cysteine sulphonic acid
Trioxidation
cysteine oxidation to cysteic acid
A protein modification that effectively substitutes a nitrite (NO2) group for a hydrogen atom.
45.0
H -1 N 1 O 2
44.985077
X
Unimod:354
Nitro (NO2)
PSI-MOD
Nitro
Oxidation to nitro
MOD:00461
Note, this is often misrepresented as the introduction of a nitrate (NO3) group [JSG].
nitrated residue
A protein modification that effectively substitutes a nitrite (NO2) group for a hydrogen atom.
DeltaMass:0
PubMed:8839040
PubMed:9252331
Unimod:354
Nitro (NO2)
Nitro
Oxidation to nitro
A protein modification that effectively converts an L-tryptophan residue to L-kynurenine.
3.99
C -1 O 1
3.994915
C 10 H 10 N 2 O 2
190.2
190.07423
W
artifact
Unimod:351
(2S)-2-amino-4-(2-aminophenyl)-4-oxo-butanoic acid
kynureninw
PSI-MOD
Trp->Kynurenin
tryptophan oxidation to kynurenin
MOD:00462
L-kynurenine
A protein modification that effectively converts an L-tryptophan residue to L-kynurenine.
DeltaMass:357
OMSSA:66
PubMed:11029593
PubMed:9252331
Unimod:351#W
(2S)-2-amino-4-(2-aminophenyl)-4-oxo-butanoic acid
kynureninw
Trp->Kynurenin
tryptophan oxidation to kynurenin
A protein modification that effectively converts an L-tryptophan residue to 3'-hydroxy-L-kynurenine.
19.99
C -1 O 2
19.989828
C 10 H 10 N 2 O 3
206.2
206.06914
W
artifact
Unimod:350
hydroxykynureninw
PSI-MOD
Trp->Hydroxykynurenin
tryptophan oxidation to hydroxykynurenin
MOD:00463
3'-hydroxy-L-kynurenine
A protein modification that effectively converts an L-tryptophan residue to 3'-hydroxy-L-kynurenine.
OMSSA:58
PubMed:9252331
Unimod:350#W
hydroxykynureninw
Trp->Hydroxykynurenin
tryptophan oxidation to hydroxykynurenin
A protein modification that effectively converts an L-tryptophan residue to N'-formyl-L-kynurenine.
32.0
O 2
31.989828
C 11 H 10 N 2 O 3
218.21
218.06914
W
artifact
Unimod:425
Double oxidation of Trp
formylkynureninw
PSI-MOD
Dioxidation
dihydroxy
tryptophan oxidation to formylkynurenin
MOD:00464
From DeltaMass: References:Willy V. Bienvenut, Catherine Déon, Carla Pasquarello, Jennifer M. Campbell, Jean-Charles Sanchez, Marvin L. Vestal, Denis F. Hochstrasser Matrix-assisted laser desorption/ionization-tandemmass spectrometry with high resolution andsensitivity for identification and characterizationof proteins. Proteomics 2002, 2, 868-876 Notes: A double oxidation of tryptophan for which the N-formylkynurenine (+32) structure can be proposed. Many minor peaks accompanying the main peak might also be attributed to other oxidation products of the tryptophan such as kynurenine (+4), an unknown by-product found in all oxidized tryptophan patterns (+13), hydroxytryptophan (+16), 3-hydroxykynurenine (+20) and hydroxy-N-formylkynurenine (+48). See proposed structures at http://www.abrf.org/images/misc/dmass32.jpg.
N'-formyl-L-kynurenine
A protein modification that effectively converts an L-tryptophan residue to N'-formyl-L-kynurenine.
DeltaMass:356
OMSSA:45
PubMed:12124932
PubMed:12686488
PubMed:9252331
Unimod:425#W
Double oxidation of Trp
formylkynureninw
Dioxidation
dihydroxy
tryptophan oxidation to formylkynurenin
A protein modification that effectively converts an L-phenylalanine residue to a dihydroxyphenylalanine.
32.0
O 2
31.989828
C 9 H 9 N 1 O 3
179.17
179.05824
F
artifact
Unimod:425
dihydroxyf
PSI-MOD
Dioxidation
dihydroxy
MOD:00465
Dihydroxyphenyalanines with a 4'-hydroxyl orginate naturally by a monohydroxylation of tyrosine, and not by dihydroxylation of phenylalanine [JSG].
dihydroxyphenylalanine (Phe)
A protein modification that effectively converts an L-phenylalanine residue to a dihydroxyphenylalanine.
OMSSA:39
PubMed:1610822
PubMed:1903612
PubMed:3734192
PubMed:9252331
RESID:AA0146#var
Unimod:425#F
dihydroxyf
Dioxidation
dihydroxy
A protein modification that effectively converts a residue to a glycosylsphingolipidinositolethanolamidated.
GSIRes
PSI-MOD
MOD:00466
glycosylsphingolipidinositolated residue
A protein modification that effectively converts a residue to a glycosylsphingolipidinositolethanolamidated.
PubMed:12626404
PubMed:18688235
PubMed:8404891
GSIRes
A protein modification that effectively substitutes an iminobiotinyl group for a hydrogen atom.
225.31
C 10 H 15 N 3 O 1 S 1
225.09358
X
artifact
Unimod:89
PSI-MOD
Iminobiotin
Iminobiotinylation
MOD:00467
iminobiotinyl modified residue
A protein modification that effectively substitutes an iminobiotinyl group for a hydrogen atom.
PubMed:9750125
Unimod:89
Iminobiotin
Iminobiotinylation
modification from Unimod Isotopic label
338.47
C 16 H 26 N 4 O 2 S 1
338.17764
X
artifact
Unimod:90
PSI-MOD
ESP
ESP-Tag light d0
MOD:00468
ESP-Tag light d0
modification from Unimod Isotopic label
Unimod:90
ESP
ESP-Tag light d0
modification from Unimod Isotopic label
348.24
C 16 (1)H 16 (2)H 10 N 4 O 2 S 1
348.24042
X
artifact
Unimod:91
PSI-MOD
ESP-Tag heavy d10
ESP:2H(10)
MOD:00469
ESP-Tag heavy d10
modification from Unimod Isotopic label
Unimod:91
ESP-Tag heavy d10
ESP:2H(10)
modification from Unimod Chemical derivative
339.45
C 16 H 25 N 3 O 3 S 1
339.16165
X
artifact
Unimod:92
PSI-MOD
NHS-LC-Biotin
MOD:00470
NHS-LC-Biotin
modification from Unimod Chemical derivative
Unimod:92
NHS-LC-Biotin
NHS-LC-Biotin
modification from Unimod Chemical derivative
601.8
C 25 H 39 N 5 O 6 S 3
601.20624
X
artifact
Unimod:93
PSI-MOD
EDT-maleimide-PEO-biotin
MOD:00471
EDT-maleimide-PEO-biotin
modification from Unimod Chemical derivative
Unimod:93
EDT-maleimide-PEO-biotin
EDT-maleimide-PEO-biotin
modification from Unimod Isotopic label
68.04
C 3 (1)H 4 N 2
68.037445
C 9 H 16 N 4 O 1
196.13
196.13242
K
artifact
Unimod:94
PSI-MOD
IMID
IMID d0
MOD:00472
IMID d0
modification from Unimod Isotopic label
PubMed:11746907
URL:http://dx.doi.org/10.1002/rcm.517
Unimod:94
IMID
IMID d0
modification from Unimod Isotopic label
72.06
C 3 (2)H 4 N 2
72.06255
C 9 (1)H 12 (2)H 4 N 4 O 1
200.16
200.15752
K
artifact
Unimod:95
PSI-MOD
IMID d4
IMID:2H(4)
MOD:00473
IMID d4
modification from Unimod Isotopic label
PubMed:11746907
URL:http://dx.doi.org/10.1002/rcm.517
Unimod:95
IMID d4
IMID:2H(4)
A protein modification that effectively converts an L-cysteine residue to S-(1,1,2-(2)H3)-propanamide-L-cysteine.
74.06
C 3 (1)H 2 (2)H 3 N 1 O 1
74.05595
C 6 (1)H 7 (2)H 3 N 2 O 2 S 1
177.07
177.06512
C
artifact
Unimod:97
S-([1,1,2-(2)H3]-3-amino-3-oxopropyl)cysteine
S-([1,1,2-(2)H3]-carbamoylethyl)-L-cysteine
S-([1,1,2-(2)H3]-propanamide)-L-cysteine
PSI-MOD
Acrylamide d3
Propionamide:2H(3)
MOD:00474
S-([1,1,2-(2)H3]-carboxamidoethyl)-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-(1,1,2-(2)H3)-propanamide-L-cysteine.
Unimod:97#C
S-([1,1,2-(2)H3]-3-amino-3-oxopropyl)cysteine
S-([1,1,2-(2)H3]-carbamoylethyl)-L-cysteine
S-([1,1,2-(2)H3]-propanamide)-L-cysteine
Acrylamide d3
Propionamide:2H(3)
A protein modification that effectively converts an L-tyrosine residue to 2-amino-L-tyrosine.
15.02
H 1 N 1
15.010899
C 9 H 10 N 2 O 2
178.19
178.07423
Y
artifact
Unimod:342
PSI-MOD
Amino
Tyrosine oxidation to 2-aminotyrosine
MOD:00475
2-amino-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to 2-amino-L-tyrosine.
PubMed:8839040
PubMed:9252331
Unimod:342#Y
Amino
Tyrosine oxidation to 2-aminotyrosine
A protein modification that effectively replaces a hydrogen atom with an galactose group through a glycosidic bond.
162.14
C 6 H 10 O 5
162.05283
X
natural
GalRes
PSI-MOD
MOD:00476
monogalactosylated residue
A protein modification that effectively replaces a hydrogen atom with an galactose group through a glycosidic bond.
PubMed:18688235
GalRes
A protein modification that effectively converts, by oxidative decarboxylation, an L-proline residue to 2-pyrrolidone with breakage of the peptide chain.
-13.02
C -1 H -1 N 0 O 0
-13.007825
C 4 H 6 N 1 O 1
84.1
84.04494
P
artifact
Unimod:360
PSI-MOD
Pro->Pyrrolidinone
Proline oxidation to pyrrolidinone
MOD:00477
The oxidative decarboxylation of a proline residue results in breaking of the peptide chain, leaving a peptidyl-2-pyrrolidone at the C-terminus. The difference formula, derived from the result in the original citation, has been corrected from the Unimod entry.
2-pyrrolidone
A protein modification that effectively converts, by oxidative decarboxylation, an L-proline residue to 2-pyrrolidone with breakage of the peptide chain.
PubMed:2161657
PubMed:9252331
Unimod:360#P
Pro->Pyrrolidinone
Proline oxidation to pyrrolidinone
A protein modification that effectively converts an L-proline residue to L-glutamyl semialdehyde.
16.0
C 0 H 0 N 0 O 1
15.994915
C 5 H 7 N 1 O 2
113.12
113.047676
P
artifact
Unimod:35
Oxidation of proline to gamma-glutamyl semialdehyde
gamma-glutamyl semialdehyde
glutamyl 5-semialdehyde
glutamyl aldehyde
PSI-MOD
Oxidation
Oxidation or Hydroxylation
MOD:00478
glutamyl semialdehyde (Pro)
A protein modification that effectively converts an L-proline residue to L-glutamyl semialdehyde.
DeltaMass:354
PubMed:11120890
PubMed:2563380
PubMed:9252331
Unimod:35#P
Oxidation of proline to gamma-glutamyl semialdehyde
gamma-glutamyl semialdehyde
glutamyl 5-semialdehyde
glutamyl aldehyde
Oxidation
Oxidation or Hydroxylation
A protein modification that effectively converts an L-arginine residue to L-glutamyl semialdehyde.
-43.07
C -1 H -5 N -3 O 1
-43.053432
C 5 H 7 N 1 O 2
113.12
113.047676
R
artifact
Unimod:344
Oxidation of arginine (to glutamic acid)
PSI-MOD
Arg->GluSA
Arginine oxidation to glutamic semialdehyde
MOD:00479
From DeltaMass: Average Mass: -27 Monoisotopic Mass Change:-27.06 Average Mass Change:-27.07 References:Amici A, Levine, RL, Tsai, L, and Stadtman, ER: Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. Journal of Biological Chemistry 264: 3341-3346 1989.Requena JR, Chao CC, Levine RL, and Stadtman ER: Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proceedings of the National Academy of Sciences USA 98: 69-74 2001.
glutamyl semialdehyde (Arg)
A protein modification that effectively converts an L-arginine residue to L-glutamyl semialdehyde.
DeltaMass:351
PubMed:11120890
PubMed:1680314
PubMed:9252331
Unimod:344#R
Oxidation of arginine (to glutamic acid)
Arg->GluSA
Arginine oxidation to glutamic semialdehyde
modification from Unimod Isotopic label
227.26
C 10 H 17 N 3 O 3
227.12698
C 13 H 22 N 4 O 4 S 1
330.4
330.13617
C
artifact
Unimod:105
icatlight
PSI-MOD
Applied Biosystems cleavable ICAT(TM) light
ICAT-C
MOD:00480
Applied Biosystems cleavable ICAT(TM) light
modification from Unimod Isotopic label
OMSSA:129
URL:http://www.appliedbiosystems.com/products/productdetail.cfm?prod_id=153
Unimod:105#C
icatlight
Applied Biosystems cleavable ICAT(TM) light
ICAT-C
modification from Unimod Isotopic label
236.16
(12)C 1 (13)C 9 H 17 N 3 O 3
236.15718
(12)C 4 (13)C 9 H 22 N 4 O 4 S 1
339.17
339.16638
C
artifact
Unimod:106
icatheavy
PSI-MOD
Applied Biosystems cleavable ICAT(TM) heavy
ICAT-C:13C(9)
MOD:00481
Applied Biosystems cleavable ICAT(TM) heavy
modification from Unimod Isotopic label
OMSSA:130
URL:http://www.appliedbiosystems.com/products/productdetail.cfm?prod_id=153
Unimod:106#C
icatheavy
Applied Biosystems cleavable ICAT(TM) heavy
ICAT-C:13C(9)
A protein modification that effectively converts an L-methionine residue to N-formyl-L-methionine (not known as a natural, post-translational modification process).
28.01
C 1 H 0 N 0 O 1 S 0
27.994915
C 6 H 10 N 1 O 2 S 1
160.21
160.04323
M
artifact
N-term
Unimod:122
uniprot.ptm:PTM-0212
(2S)-2-formylamino-4-(methylsulfanyl)butanoic acid
2-formamido-4-(methylsulfanyl)butanoic acid
2-formylamino-4-(methylthio)butanoic acid
2-formylazanyl-4-(methylsulfanyl)butanoic acid
MOD_RES N-formylmethionine
N-formyl-L-methionine
N-formylated L-methionine
NFoMet
PSI-MOD
MOD:00482
This entry is for the artifactual formation of N-formyl-L-methionine from methionine. For encoded N-formyl-L-methionine, use MOD:00030 [JSG].
N-formyl-L-methionine (Met)
A protein modification that effectively converts an L-methionine residue to N-formyl-L-methionine (not known as a natural, post-translational modification process).
PubMed:11152118
PubMed:2165784
PubMed:3042771
RESID:AA0021#MET
Unimod:122#M
(2S)-2-formylamino-4-(methylsulfanyl)butanoic acid
2-formamido-4-(methylsulfanyl)butanoic acid
2-formylamino-4-(methylthio)butanoic acid
2-formylazanyl-4-(methylsulfanyl)butanoic acid
MOD_RES N-formylmethionine
N-formyl-L-methionine
N-formylated L-methionine
NFoMet
A protein modification that is produced by reaction with N-ethylmaleimide.
125.13
C 6 H 7 N 1 O 2
125.047676
C 9 H 12 N 2 O 3 S 1
228.27
228.05687
C
artifact
Unimod:108
nemc
PSI-MOD
N-ethylmaleimide on cysteines
Nethylmaleimide
MOD:00483
N-ethylmaleimide derivatized cysteine
A protein modification that is produced by reaction with N-ethylmaleimide.
OMSSA:83
PubMed:11813307
PubMed:12777388
Unimod:108#C
nemc
N-ethylmaleimide on cysteines
Nethylmaleimide
modification from Unimod Chemical derivative
354.47
C 16 H 26 N 4 O 3 S 1
354.17258
C 22 H 38 N 6 O 4 S 1
482.64
482.26752
K
artifact
Unimod:112
PSI-MOD
OxLysBiotinRed
Oxidized lysine biotinylated with biotin-LC-hydrazide, reduced
MOD:00484
oxidized lysine biotinylated with biotin-LC-hydrazide, reduced
modification from Unimod Chemical derivative
Unimod:112#K
OxLysBiotinRed
Oxidized lysine biotinylated with biotin-LC-hydrazide, reduced
modification from Unimod Chemical derivative
352.45
C 16 H 24 N 4 O 3 S 1
352.15692
C 22 H 36 N 6 O 4 S 1
480.63
480.25186
K
artifact
Unimod:113
PSI-MOD
OxLysBiotin
Oxidized lysine biotinylated with biotin-LC-hydrazide
MOD:00485
oxidized lysine biotinylated with biotin-LC-hydrazide
modification from Unimod Chemical derivative
Unimod:113#K
OxLysBiotin
Oxidized lysine biotinylated with biotin-LC-hydrazide
modification from Unimod Chemical derivative
371.5
C 16 H 29 N 5 O 3 S 1
371.1991
C 21 H 36 N 6 O 4 S 1
468.62
468.25186
P
artifact
Unimod:114
PSI-MOD
OxProBiotinRed
Oxidized proline biotinylated with biotin-LC-hydrazide, reduced
MOD:00486
oxidized proline biotinylated with biotin-LC-hydrazide, reduced
modification from Unimod Chemical derivative
Unimod:114#C
OxProBiotinRed
Oxidized proline biotinylated with biotin-LC-hydrazide, reduced
modification from Unimod Chemical derivative
369.48
C 16 H 27 N 5 O 3 S 1
369.18347
C 21 H 34 N 6 O 4 S 1
466.6
466.23624
P
artifact
Unimod:115
PSI-MOD
OxProBiotin
Oxidized Proline biotinylated with biotin-LC-hydrazide
MOD:00487
oxidized proline biotinylated with biotin-LC-hydrazide
modification from Unimod Chemical derivative
Unimod:115#C
OxProBiotin
Oxidized Proline biotinylated with biotin-LC-hydrazide
modification from Unimod Chemical derivative
310.41
C 15 H 22 N 2 O 3 S 1
310.1351
C 21 H 34 N 6 O 4 S 1
466.6
466.23624
R
artifact
PSI-MOD
OxArgBiotin
Oxidized arginine biotinylated with biotin-LC-hydrazide
MOD:00488
oxidized arginine biotinylated with biotin-LC-hydrazide
modification from Unimod Chemical derivative
Unimod:116#C
OxArgBiotin
Oxidized arginine biotinylated with biotin-LC-hydrazide
modification from Unimod Chemical derivative
312.43
C 15 H 24 N 2 O 3 S 1
312.15076
C 21 H 36 N 6 O 4 S 1
468.62
468.25186
R
artifact
Unimod:117
PSI-MOD
OxArgBiotinRed
Oxidized arginine biotinylated with biotin-LC-hydrazide, reduced
MOD:00489
oxidized arginine biotinylated with biotin-LC-hydrazide, reduced
modification from Unimod Chemical derivative
Unimod:117#C
OxArgBiotinRed
Oxidized arginine biotinylated with biotin-LC-hydrazide, reduced
modification from Unimod Chemical derivative
490.7
C 20 H 34 N 4 O 4 S 3
490.17422
X
Unimod:118
PSI-MOD
EDT-iodo-PEO-biotin
EDT-iodoacetyl-PEO-biotin
MOD:00490
EDT-iodo-PEO-biotin
modification from Unimod Chemical derivative
Unimod:118
EDT-iodo-PEO-biotin
EDT-iodoacetyl-PEO-biotin
modification from Unimod Chemical derivative
316.38
C 22 H 21 P 1
316.1381
C 25 H 26 N 1 O 1 P 1 S 1
419.52
419.14728
C
artifact
Unimod:119
PSI-MOD
IBTP
Thio Ether Formation - BTP Adduct
MOD:00491
thio ether formation - BTP Adduct
modification from Unimod Chemical derivative
PubMed:11861642
Unimod:119#C
IBTP
Thio Ether Formation - BTP Adduct
A protein modification that crosslinks the N6-amino of a peptidyl lysine with the carboxyl of glycylglycine, the two glycine residues left after tryptic digestion of ubiquitin.
114.1
C 4 H 6 N 2 O 2
114.04293
C 10 H 18 N 4 O 3
242.28
242.1379
K
artifact
Unimod:121
N6-(glycylglycyl)lysine
N6-glycylglycyl-L-lysine
glyglyk
PSI-MOD
GlyGly
ubiquitinylation residue
MOD:00492
ubiquitination signature dipeptidyl lysine
A protein modification that crosslinks the N6-amino of a peptidyl lysine with the carboxyl of glycylglycine, the two glycine residues left after tryptic digestion of ubiquitin.
OMSSA:52
PubMed:11125103
PubMed:12612601
PubMed:12872131
RESID:AA0125#var
Unimod:121#K
N6-(glycylglycyl)lysine
N6-glycylglycyl-L-lysine
glyglyk
GlyGly
ubiquitinylation residue
A protein modification that effectively replaces a hydrogen atom with a formyl group.
28.01
C 1 O 1
27.994915
X
Unimod:122
FoRes
Formylation (CHO)
PSI-MOD
Formyl
Formylation
MOD:00493
From DeltaMass: Average Mass: 28
formylated residue
A protein modification that effectively replaces a hydrogen atom with a formyl group.
DeltaMass:0
PubMed:15799070
Unimod:122
FoRes
Formylation (CHO)
Formyl
Formylation
modification from Unimod Isotopic label
345.78
C 15 Cl 1 H 20 N 1 O 6 S 0
345.0979
C 18 Cl 1 H 25 N 2 O 7 S 1
448.91
448.1071
C
artifact
Unimod:123
PSI-MOD
ICAT-H
N-iodoacetyl, p-chlorobenzyl-12C6-glucamine
MOD:00494
N-iodoacetyl, p-chlorobenzyl-12C6-glucamine
modification from Unimod Isotopic label
PubMed:12185208
Unimod:123#C
ICAT-H
N-iodoacetyl, p-chlorobenzyl-12C6-glucamine
modification from Unimod Isotopic label
351.12
(12)C 9 (13)C 6 Cl 1 H 20 N 1 O 6 S 0
351.11804
(12)C 12 (13)C 6 Cl 1 H 25 N 2 O 7 S 1
454.13
454.12723
C
artifact
Unimod:124
PSI-MOD
ICAT-H:13C(6)
N-iodoacetyl, p-chlorobenzyl-13C6-glucamine
MOD:00495
N-iodoacetyl, p-chlorobenzyl-13C6-glucamine
modification from Unimod Isotopic label
PubMed:12185208
Unimod:124#C
ICAT-H:13C(6)
N-iodoacetyl, p-chlorobenzyl-13C6-glucamine
OBSOLETE because Unimod entry 125 is merged with entry 199, remap to id: MOD:00552
MOD:00552
32.06
C 2 (2)H 4
32.056408
K
artifact
Unimod:125
PSI-MOD
MOD:00496
reductive amination-D
true
OBSOLETE because Unimod entry 125 is merged with entry 199, remap to id: MOD:00552
Unimod:125
modification from Unimod [(35)S]dithiobis(succinimidyl propionate) crosslinking
88.12
C 3 H 4 O 1 S 1
87.99828
C 9 H 16 N 2 O 2 S 1
216.3
216.09325
K
artifact
Unimod:126
PSI-MOD
3,3-Dithio-bis-(sulfosuccinimidyl)propionate
3-sulfanylpropanoyl
Thioacyl
MOD:00497
The name "thioacylation of primary amines" in Unimod was a misdescription [JSG].
3-sulfanylpropanoyl (N-term and Lys)
modification from Unimod [(35)S]dithiobis(succinimidyl propionate) crosslinking
PubMed:957432
Unimod:126
3,3-Dithio-bis-(sulfosuccinimidyl)propionate
3-sulfanylpropanoyl
Thioacyl
A protein modification that effectively substitutes a hydrogen of a residue with a fluorine atom.
X
artifact
FRes
Fluorophenylalanyl
PSI-MOD
Fluoro
fluorophenylalanine replacement of phenylalanine
MOD:00498
fluorinated residue
A protein modification that effectively substitutes a hydrogen of a residue with a fluorine atom.
PubMed:18688235
FRes
Fluorophenylalanyl
Fluoro
fluorophenylalanine replacement of phenylalanine
modification from Unimod Chemical derivative
388.35
C 22 H 14 N 1 O 6
388.08212
C 25 H 19 N 2 O 7 S 1
491.49
491.0913
C
artifact
Unimod:128
PSI-MOD
5-Iodoacetamidofluorescein (Molecular Probe, Eugene, OR)
Fluorescein
MOD:00499
5-iodoacetamidofluorescein
modification from Unimod Chemical derivative
PubMed:3311742
PubMed:3578767
Unimod:128#C
5-Iodoacetamidofluorescein (Molecular Probe, Eugene, OR)
Fluorescein
A protein modification that effectively substitutes one hydrogen atom of a residue with one iodine atom.
125.9
H -1 I 1
125.896645
X
Unimod:129
I1Res
Iodination (of Histidine[C4] or Tyrosine[C3])
PSI-MOD
Iodination
Iodo
MOD:00500
From DeltaMass: Average Mass: 126
monoiodinated residue
A protein modification that effectively substitutes one hydrogen atom of a residue with one iodine atom.
DeltaMass:0
PubMed:15627961
PubMed:2026710
Unimod:129
I1Res
Iodination (of Histidine[C4] or Tyrosine[C3])
Iodination
Iodo
A protein modification that effectively substitutes two hydrogen atoms of a residue with two iodine atoms.
251.79
H -2 I 2
251.79329
X
Unimod:130
I2Res
PSI-MOD
Diiodo
di-Iodination
MOD:00501
From DeltaMass: Average Mass: 252
diiodinated residue
A protein modification that effectively substitutes two hydrogen atoms of a residue with two iodine atoms.
Unimod:130
I2Res
Diiodo
di-Iodination
A protein modification that effectively substitutes three hydrogen atoms of a residue with three iodine atoms.
377.69
H -3 I 3
377.68994
X
artifact
Unimod:131
I3Res
triiodinationy
PSI-MOD
Triiodo
tri-Iodination
MOD:00502
From Unimod. In PubMed:2026710, mono- and diiodination of tyrosine are discussed, but triiodination of tyrosine is not mentioned. In PubMed:15627961, triiodothyronine (see MOD:00186) is discussed, but triiodotyrosine is not mentioned. This modification probably does not exist, and may be a confusion of "tyrosine" for "thyronine", a common error [JSG].
triiodinated residue
A protein modification that effectively substitutes three hydrogen atoms of a residue with three iodine atoms.
OMSSA:116
PubMed:15627961
PubMed:2026710
Unimod:131
I3Res
triiodinationy
Triiodo
tri-Iodination
A protein modification that effectively converts a glycine residue to N-(cis-delta 5)-tetradecaenoylglycine.
208.35
C 14 H 24 N 0 O 1
208.18271
C 16 H 27 N 1 O 2
265.4
265.2042
G
natural
N-term
Unimod:134
N-(C14:1 aliphatic acyl)glycine
myristoleylation (one double bond)
ntermpepmyristoyeylationg
PSI-MOD
(cis-delta 5)-tetradecaenoyl
Myristoleyl
MOD:00503
N-(cis-delta 5)-tetradecaenoylglycine
A protein modification that effectively converts a glycine residue to N-(cis-delta 5)-tetradecaenoylglycine.
OMSSA:78
PubMed:11955007
PubMed:11955008
PubMed:1326520
PubMed:1386601
PubMed:6436247
PubMed:7543369
RESID:AA0059#var
Unimod:134#G
N-(C14:1 aliphatic acyl)glycine
myristoleylation (one double bond)
ntermpepmyristoyeylationg
(cis-delta 5)-tetradecaenoyl
Myristoleyl
A protein modification that effectively converts a glycine residue to N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine.
206.33
C 14 H 22 O 1
206.16707
C 16 H 25 N 1 O 2
263.38
263.18854
G
natural
N-term
Unimod:135
N-(C14:2 aliphatic acyl)glycine
myristoylation-4H (two double bonds)
ntermpepmyristoyl4hg
PSI-MOD
(cis,cis-delta 5, delta 8)-tetradecadienoyl
Myristoyl+Delta:H(-4)
MOD:00504
N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine
A protein modification that effectively converts a glycine residue to N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine.
OMSSA:79
PubMed:11955007
PubMed:11955008
PubMed:1326520
PubMed:1386601
PubMed:6436247
PubMed:7543369
RESID:AA0059#var
Unimod:135#G
N-(C14:2 aliphatic acyl)glycine
myristoylation-4H (two double bonds)
ntermpepmyristoyl4hg
(cis,cis-delta 5, delta 8)-tetradecadienoyl
Myristoyl+Delta:H(-4)
modification from Unimod Isotopic label
104.11
C 7 H 4 O 1
104.026215
X
artifact
Unimod:136
Benzoyl (Bz)
PSI-MOD
Benzoyl
labeling reagent light form (N-term & K)
MOD:00505
From DeltaMass: Average Mass: 104
benzoyl labeling reagent light form (N-term and K)
modification from Unimod Isotopic label
DeltaMass:0
PubMed:15456300
Unimod:136
Benzoyl (Bz)
Benzoyl
labeling reagent light form (N-term & K)
modification from Unimod N-linked glycosylation, Hex(5) HexNAc(2)
1217.09
C 46 H 76 N 2 O 35
1216.4229
C 50 H 82 N 4 O 37
1331.2
1330.4658
N
natural
GNO:G02815KT
Unimod:137
PSI-MOD
Hex(5)HexNAc(2)
N-linked glycan core
MOD:00506
N-linked glycan core N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, Hex(5) HexNAc(2)
PubMed:111247
PubMed:1694179
PubMed:5490222
RESID:AA0151#var
Unimod:137#N
Hex(5)HexNAc(2)
N-linked glycan core
OBSOLETE because redundant, replaced by MOD:01653. Remap to MOD:01653.
MOD:01653
233.29
C 12 H 11 N 1 O 2 S 1
233.05106
X
artifact
Unimod:139
Dansyl (Dns)
PSI-MOD
5-dimethylaminonaphthalene-1-sulfonyl
Dansyl
MOD:00507
From DeltaMass: Average Mass: 233
5-dimethylaminonaphthalene-1-sulfonyl
true
OBSOLETE because redundant, replaced by MOD:01653. Remap to MOD:01653.
DeltaMass:0
Unimod:139
Dansyl (Dns)
5-dimethylaminonaphthalene-1-sulfonyl
Dansyl
OBSOLETE because this is an ion type and is not a biological or chemical modification to a polypeptide, can be handled by PSI-MS CV term, MS:1001229
X
artifact
C-term
Unimod:140
PSI-MOD
ISD a-series (C-Term)
a-type-ion
MOD:00508
Virtual Modification for MS/MS of a-type ions, by decarboxylation of C-terminus as reaction inside the mass spectrometer.
ISD a-series (C-Term)
true
OBSOLETE because this is an ion type and is not a biological or chemical modification to a polypeptide, can be handled by PSI-MS CV term, MS:1001229
PubMed:14588022
Unimod:140
ISD a-series (C-Term)
a-type-ion
modification from Unimod Chemical derivative
41.05
C 2 H 3 N 1
41.02655
X
artifact
Unimod:141
PSI-MOD
Amidine
amidination of lysines or N-terminal amines with methyl acetimidate
MOD:00509
amidination of lysines or N-terminal amines with methyl acetimidate
modification from Unimod Chemical derivative
PubMed:12643539
PubMed:6273432
Unimod:141
Amidine
amidination of lysines or N-terminal amines with methyl acetimidate
modification from Unimod N-linked glycosylation, dHex HexNAc
349.34
C 14 H 23 N 1 O 9
349.13727
C 18 H 29 N 3 O 11
463.44
463.1802
N
natural
GNO:G00194GV
Unimod:142
dHexHexNAcN
PSI-MOD
HexNAc(1)dHex(1)
HexNAc1dHex1
MOD:00510
HexNAc1dHex1 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, dHex HexNAc
OMSSA:183
PubMed:111247
PubMed:1694179
PubMed:5490222
RESID:AA0151#var
Unimod:142
dHexHexNAcN
HexNAc(1)dHex(1)
HexNAc1dHex1
modification from Unimod N-linked glycosylation, HexNAc(2)
406.39
C 16 H 26 N 2 O 10
406.15875
C 20 H 32 N 4 O 12
520.49
520.20166
N
natural
GNO:G27391WQ
Unimod:143
PSI-MOD
HexNAc(2)
HexNAc2
MOD:00511
HexNAc2 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, HexNAc(2)
PubMed:111247
PubMed:1694179
PubMed:5490222
RESID:AA0151#var
Unimod:143
HexNAc(2)
HexNAc2
modification from Unimod N-linked glycosylation, Hex3
486.42
C 18 H 30 O 15
486.15848
C 22 H 36 N 2 O 17
600.53
600.2014
N
natural
GNO:G39365VM
Unimod:144
PSI-MOD
Hex(3)
Hex3
MOD:00512
Hex3 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, Hex3
PubMed:111247
PubMed:1694179
PubMed:5490222
RESID:AA0151#var
Unimod:144
Hex(3)
Hex3
modification from Unimod N-linked glycosylation, dHex(2) HexNAc
495.48
C 20 H 33 N 1 O 13
495.1952
C 24 H 39 N 3 O 15
609.58
609.2381
N
natural
GNO:G74392IM
Unimod:145
PSI-MOD
HexNAc(1)dHex(2)
HexNAc1dHex2
MOD:00513
HexNAc1dHex2 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, dHex(2) HexNAc
PubMed:111247
PubMed:1694179
PubMed:5490222
RESID:AA0151#var
Unimod:145
HexNAc(1)dHex(2)
HexNAc1dHex2
modification from Unimod N-linked glycosylation, dHex Hex HexNAc
511.48
C 20 H 33 N 1 O 14
511.1901
C 24 H 39 N 3 O 16
625.58
625.23303
N
natural
GNO:G54129SE
Unimod:146
PSI-MOD
Hex(1)HexNAc(1)dHex(1)
Hex1HexNAc1dHex1
MOD:00514
Hex1HexNAc1dHex1 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, dHex Hex HexNAc
PubMed:111247
PubMed:1694179
PubMed:5490222
RESID:AA0151#var
Unimod:146
Hex(1)HexNAc(1)dHex(1)
Hex1HexNAc1dHex1
modification from Unimod N-linked glycosylation, dHex HexNAc(2)
552.53
C 22 H 36 N 2 O 14
552.2167
C 26 H 42 N 4 O 16
666.63
666.2596
N
natural
GNO:G06042JP
Unimod:147
PSI-MOD
HexNAc(2)dHex(1)
HexNAc2dHex1
MOD:00515
HexNAc2dHex1 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, dHex HexNAc(2)
PubMed:111247
PubMed:1694179
PubMed:5490222
RESID:AA0151#var
Unimod:147
HexNAc(2)dHex(1)
HexNAc2dHex1
modification from Unimod N-linked glycosylation
568.53
C 22 H 36 N 2 O 15
568.21155
C 26 H 42 N 4 O 17
682.63
682.2545
N
natural
GNO:G58001LT
Unimod:148
PSI-MOD
Hex(1)HexNAc(2)
Hex1HexNAc2
MOD:00516
Hex1HexNAc2 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation
RESID:AA0151#var
Unimod:148
Hex(1)HexNAc(2)
Hex1HexNAc2
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond.
657.6
C 25 H 41 N 2 O 18
657.2354
X
natural
GNO:G17015OC
NeuAc-Hex-HexNAc
PSI-MOD
Hex(1)HexNAc(1)NeuAc(1)
Hex1HexNAc1NeuAc1
MOD:00517
From DeltaMass: Average Mass: 657
Hex1HexNAc1NeuAc1 glycosylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond.
DeltaMass:0
Unimod:149
NeuAc-Hex-HexNAc
Hex(1)HexNAc(1)NeuAc(1)
Hex1HexNAc1NeuAc1
modification from Unimod N-linked glycosylation
698.67
C 28 H 46 N 2 O 18
698.27454
C 32 H 52 N 4 O 20
812.78
812.3175
N
natural
GNO:G90423UY
Unimod:150
PSI-MOD
HexNAc(2)dHex(2)
HexNAc2dHex2
MOD:00518
HexNAc2dHex2 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation
RESID:AA0151#var
Unimod:150
HexNAc(2)dHex(2)
HexNAc2dHex2
modification from Unimod N-linked glycosylation
700.64
C 27 H 44 N 2 O 19
700.25385
C 31 H 50 N 4 O 21
814.75
814.29675
N
natural
GNO:G54968WM
Unimod:151
PSI-MOD
Hex(1)HexNAc(2)Pent(1)
Hex1HexNAc2Pent1
MOD:00519
Hex1HexNAc2Pent1 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation
RESID:AA0151#var
Unimod:151
Hex(1)HexNAc(2)Pent(1)
Hex1HexNAc2Pent1
modification from Unimod N-linked glycosylation
714.67
C 28 H 46 N 2 O 19
714.2695
C 32 H 52 N 4 O 21
828.77
828.3124
N
natural
GNO:G94583DZ
Unimod:152
PSI-MOD
Hex(1)HexNAc(2)dHex(1)
Hex1HexNAc2dHex1
MOD:00520
Hex1HexNAc2dHex1 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation
RESID:AA0151#var
Unimod:152
Hex(1)HexNAc(2)dHex(1)
Hex1HexNAc2dHex1
modification from Unimod N-linked glycosylation
730.67
C 28 H 46 N 2 O 20
730.2644
C 32 H 52 N 4 O 22
844.77
844.3073
N
natural
GNO:G53434XO
Unimod:153
PSI-MOD
Hex(2)HexNAc(2)
Hex2HexNAc2
MOD:00521
Hex2HexNAc2 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation
RESID:AA0151#var
Unimod:153
Hex(2)HexNAc(2)
Hex2HexNAc2
modification from Unimod N-linked glycosylation
821.73
C 31 H 51 N 1 O 24
821.2801
C 35 H 57 N 3 O 26
935.84
935.32306
N
natural
GNO:G64686LL
Unimod:154
PSI-MOD
Hex(3)HexNAc(1)Pent(1)
Hex3HexNAc1Pent1
MOD:00522
Hex3HexNAc1Pent1 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation
RESID:AA0151#var
Unimod:154
Hex(3)HexNAc(1)Pent(1)
Hex3HexNAc1Pent1
modification from Unimod N-linked glycosylation
846.79
C 33 H 54 N 2 O 23
846.3117
C 35 H 57 N 3 O 26
960.89
960.3547
N
natural
GNO:G84825UQ
Unimod:155
PSI-MOD
Hex(1)HexNAc(2)dHex(1)Pent(1)
Hex1HexNAc2dHex1Pent1
MOD:00523
Hex1HexNAc2dHex1Pent1 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation
RESID:AA0151#var
Unimod:155
Hex(1)HexNAc(2)dHex(1)Pent(1)
Hex1HexNAc2dHex1Pent1
modification from Unimod N-linked glycosylation
860.81
C 34 H 56 N 2 O 23
860.3274
C 38 H 62 N 4 O 25
974.92
974.3703
N
natural
GNO:G05460KC
Unimod:156
PSI-MOD
Hex(1)HexNAc(2)dHex(2)
Hex1HexNAc2dHex2
MOD:00524
Hex1HexNAc2dHex2 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation
RESID:AA0151#var
Unimod:156
Hex(1)HexNAc(2)dHex(2)
Hex1HexNAc2dHex2
modification from Unimod N-linked glycosylation
862.79
C 33 H 54 N 2 O 24
862.30664
C 37 H 60 N 4 O 26
976.89
976.34955
N
natural
GNO:G18999EB
Unimod:157
PSI-MOD
Hex(2)HexNAc(2)Pent(1)
Hex2HexNAc2Pent1
MOD:00525
Hex2HexNAc2Pent1 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation
RESID:AA0151#var
Unimod:157
Hex(2)HexNAc(2)Pent(1)
Hex2HexNAc2Pent1
modification from Unimod N-linked glycosylation
876.81
C 34 H 56 N 2 O 24
876.3223
C 38 H 62 N 4 O 26
990.92
990.36523
N
natural
GNO:G93579XB
Unimod:158
PSI-MOD
Hex(2)HexNAc(2)dHex(1)
Hex2HexNAc2dHex1
MOD:00526
Hex2HexNAc2dHex1 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation
RESID:AA0151#var
Unimod:158
Hex(2)HexNAc(2)dHex(1)
Hex2HexNAc2dHex1
modification from Unimod N-linked glycosylation
892.81
C 34 H 56 N 2 O 25
892.3172
C 38 H 62 N 4 O 27
1006.92
1006.36017
N
natural
GNO:G28681TP
Unimod:159
(Hex)3-HexNAc-HexNAc
PSI-MOD
Hex(3)HexNAc(2)
Hex3HexNAc2
MOD:00527
From DeltaMass: Average Mass: 893
Hex3HexNAc2 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation
DeltaMass:0
RESID:AA0151#var
Unimod:159
(Hex)3-HexNAc-HexNAc
Hex(3)HexNAc(2)
Hex3HexNAc2
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond.
947.85
C 36 H 57 N 3 O 26
947.32306
X
natural
GNO:G23729WG
Unimod:160
PSI-MOD
Hex(1)HexNAc(1)NeuAc(2)
Hex1HexNAc1NeuAc2
MOD:00528
Hex1HexNAc1NeuAc2 glycosylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond.
Unimod:160
Hex(1)HexNAc(1)NeuAc(2)
Hex1HexNAc1NeuAc2
modification from Unimod N-linked glycosylation
972.79
C 34 H 57 N 2 O 28 P 1
972.28357
C 38 H 63 N 4 O 30 P 1
1086.89
1086.3264
N
natural
GNO:G88520YF
Unimod:161
PSI-MOD
Hex(3)HexNAc(2)P(1)
Hex3HexNAc2P1
MOD:00529
Hex3HexNAc2P1 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation
RESID:AA0151#var
Unimod:161
Hex(3)HexNAc(2)P(1)
Hex3HexNAc2P1
A protein modification that effectively converts an L-methionine residue to L-selenomethionine.
46.91
C 0 H 0 N 0 S -1 Se 1
47.94445
C 5 H 9 N 1 O 1 Se 1
178.1
178.98494
M
artifact
Unimod:162
Se(S)Met
semetm
PSI-MOD
Delta:S(-1)Se(1)
Selenium replaces sulphur
MOD:00530
L-selenomethionine
A protein modification that effectively converts an L-methionine residue to L-selenomethionine.
OMSSA:113
PubMed:12148805
Unimod:162#M
Se(S)Met
semetm
Delta:S(-1)Se(1)
Selenium replaces sulphur
A protein modification that effectively converts an L-asparagine residue to L-aspartic acid with one (18)O as the result of having been deglycosylated in (18)O water.
2.99
H -1 N -1 (18)O 1
2.988262
C 4 H 5 N 1 (16)O 2 (18)O 1
117.03
117.03119
N
artifact
Unimod:170
PSI-MOD
Delta:H(1)O(-1)18O(1)
glycosylated asparagine 18O labeling
MOD:00531
(18)O labeled deglycosylated asparagine
A protein modification that effectively converts an L-asparagine residue to L-aspartic acid with one (18)O as the result of having been deglycosylated in (18)O water.
PubMed:14435542
Unimod:170
Delta:H(1)O(-1)18O(1)
glycosylated asparagine 18O labeling
modification from Unimod Chemical derivative
159.01
(13)C 6 H 3 N 1 O 2 S 1
159.00858
(12)C 11 (13)C 6 H 13 N 3 O 3 S 1
345.09
345.0879
W
artifact
Unimod:171
PSI-MOD
NBS:13C(6)
Shimadzu NBS-13C
MOD:00532
Shimadzu 13CNBS
modification from Unimod Chemical derivative
PubMed:12845591
Unimod:171
NBS:13C(6)
Shimadzu NBS-13C
modification from Unimod Chemical derivative
152.99
(12)C 6 H 3 N 1 O 2 S 1
152.98845
(12)C 17 H 13 N 3 O 3 S 1
339.07
339.06775
W
artifact
Unimod:172
PSI-MOD
NBS
Shimadzu NBS-12C
MOD:00533
Shimadzu 12CNBS
modification from Unimod Chemical derivative
PubMed:12845591
Unimod:172
NBS
Shimadzu NBS-12C
modification from Unimod Post-translational
218.34
C 15 H 22 O 1
218.16707
X
artifact
Unimod:176
PSI-MOD
BHT
Michael addition of BHT quinone methide to Cysteine and Lysine
MOD:00534
Butylated Hydroxytoluene adduct.
Michael addition of BHT quinone methide to cysteine and lysine
modification from Unimod Post-translational
PubMed:9448752
Unimod:176
BHT
Michael addition of BHT quinone methide to Cysteine and Lysine
modification from Unimod Chemical derivative
87.18
C 4 H 9 N 1 O -1 S 1
87.05066
X
artifact
Unimod:178
PSI-MOD
DAET
phosphorylation to amine thiol
MOD:00535
DAET = 2-(dimethylamino)ethanethiol. The phosphorylation to amine is the beta elimination of phosphate and Michael addition of 2-(dimethylamino)ethanethiol to the site.
phosphorylation to amine thiol
modification from Unimod Chemical derivative
PubMed:12216740
Unimod:178
DAET
phosphorylation to amine thiol
OBSOLETE because Unimod 179 merged with Unimod 447 remap to ??? a protein modification that replaces an L-serine residue with an L-alanine residue
-16.0
O -1
-15.994915
S
artifact
Unimod:179
Ser_Ala
PSI-MOD
MOD:00536
L-serine to L-alanine replacement
true
OBSOLETE because Unimod 179 merged with Unimod 447 remap to ??? a protein modification that replaces an L-serine residue with an L-alanine residue
Unimod:179
Ser_Ala
A protein modification that effectively converts an L-threonine residue to L-alanine.
-30.03
C -1 H -2 O -1
-30.010565
C 3 H 5 N 1 O 1
71.08
71.03712
T
Unimod:659
Thr(Ala)
PSI-MOD
Thr->Ala
Thr->Ala substitution
MOD:00537
This could represent either an engineered replacement or a chemical modification.
L-alanine residue (Thr)
A protein modification that effectively converts an L-threonine residue to L-alanine.
Unimod:659
Thr(Ala)
Thr->Ala
Thr->Ala substitution
Modified amino acid residues groups into isobaric sets at particular mass resolution cut-offs.
PSI-MOD
MOD:00538
protein modification categorized by isobaric sets
Modified amino acid residues groups into isobaric sets at particular mass resolution cut-offs.
PubMed:18688235
OBSOLETE because Unimod 179 merged wth Unimod 447 remap to ??? modification from Unimod O-linked glycosylation
-17.01
H -1 O -1
-17.00274
T
artifact
Unimod:182
PSI-MOD
MOD:00539
threonine reduced to aminobutynate
true
OBSOLETE because Unimod 179 merged wth Unimod 447 remap to ??? modification from Unimod O-linked glycosylation
Unimod:182
A protein modification that effectively converts a residue containing common isotopes to a 9x(13)C labeled residue.
9.03
(12)C -9 (13)C 9
9.030194
X
artifact
Unimod:184
PSI-MOD
13C(9) Silac label
Label:13C(9)
MOD:00540
9x(13)C labeled residue
A protein modification that effectively converts a residue containing common isotopes to a 9x(13)C labeled residue.
PubMed:12716131
Unimod:184
13C(9) Silac label
Label:13C(9)
A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-phosphotyrosine.
89.0
(12)C -9 (13)C 9 H 1 O 3 P 1
88.99652
(13)C 9 H 10 N 1 O 5 P 1
252.06
252.05986
Y
artifact
Unimod:185
PSI-MOD
C13 label (Phosphotyrosine)
Label:13C(9)+Phospho
MOD:00541
9x(13)C labeled L-phosphotyrosine
A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-phosphotyrosine.
PubMed:12716131
Unimod:185
C13 label (Phosphotyrosine)
Label:13C(9)+Phospho
modification from Unimod Chemical derivative
132.12
C 8 H 4 O 2
132.02113
C 14 H 16 N 4 O 3
288.31
288.12225
R
artifact
Unimod:186
PSI-MOD
HPG
Hydroxyphenylglyoxal arginine
MOD:00542
hydroxyphenylglyoxal arginine
modification from Unimod Chemical derivative
PubMed:11698400
PubMed:11914093
Unimod:186
HPG
Hydroxyphenylglyoxal arginine
modification from Unimod Chemical derivative
282.25
C 16 H 10 O 5
282.05283
C 22 H 22 N 4 O 6
438.44
438.15393
R
artifact
Unimod:187
PSI-MOD
2HPG
bis(hydroxphenylglyoxal) arginine
MOD:00543
OH-PGO and PGO react with arginine at a stoichiometry of 2:1 [Unimod].
bis(hydroxyphenylglyoxal) arginine
modification from Unimod Chemical derivative
PubMed:11698400
Unimod:187
2HPG
bis(hydroxphenylglyoxal) arginine
A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C labeled residue.
6.02
(12)C -6 (13)C 6
6.020129
X
artifact
Unimod:188
PSI-MOD
13C(6) Silac label
Label:13C(6)
MOD:00544
6x(13)C labeled residue
A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C labeled residue.
PubMed:12716131
Unimod:188
13C(6) Silac label
Label:13C(6)
OBSOLETE because redundant with MOD:00927. Remap to MOD:00927.
MOD:00927
X
artifact
N-term
PSI-MOD
MOD:00545
deuterated dimethyl labeling (D)
true
OBSOLETE because redundant with MOD:00927. Remap to MOD:00927.
PubMed:14670044
A protein modification that effectively substitutes two (18)O atom for the two (16)O atoms of an alpha-carboxyl (1-carboxyl) group.
4.01
(16)O -2 (18)O 2
4.008493
X
artifact
C-term
Unimod:193
ctermpepdio18
PSI-MOD
Label:18O(2)
O18 label at both C-terminal oxygens
MOD:00546
(18)O label at both C-terminal oxygens
A protein modification that effectively substitutes two (18)O atom for the two (16)O atoms of an alpha-carboxyl (1-carboxyl) group.
OMSSA:88
PubMed:11467524
Unimod:193
ctermpepdio18
Label:18O(2)
O18 label at both C-terminal oxygens
modification from Unimod Chemical derivative used for amino acid analysis
170.17
C 10 H 6 N 2 O 1
170.04802
X
artifact
Unimod:194
PSI-MOD
6-aminoquinolyl-N-hydroxysuccinimidyl carbamate
AccQTag
MOD:00547
6-aminoquinolyl-N-hydroxysuccinimidyl carbamate
modification from Unimod Chemical derivative used for amino acid analysis
PubMed:14997490
Unimod:194
6-aminoquinolyl-N-hydroxysuccinimidyl carbamate
AccQTag
modification from Unimod Chemical derivative
171.26
C 9 H 19 N 2 O 1
171.14973
C 12 H 24 N 3 O 2 S 1
274.4
274.15894
C
artifact
Unimod:195
PSI-MOD
APTA-d0
QAT
MOD:00548
Derivatization of cysteine with 3-acrylamidopropyl)trimethylammonium chloride [JSG].
APTA
modification from Unimod Chemical derivative
PubMed:15283597
Unimod:195
APTA-d0
QAT
modification from Unimod Isotopic label
174.17
C 9 (1)H 16 (2)H 3 N 2 O 1
174.16856
C 12 (1)H 21 (2)H 3 N 3 O 2 S 1
277.18
277.17776
C
artifact
Unimod:196
PSI-MOD
(3-acrylamidopropyl)trimethylammonium
APTA d3
QAT:2H(3)
MOD:00549
Derivatization of cysteine with 3-acrylamidopropyl)trimethylammonium chloride (difference formula correct) [JSG].
APTA d3
modification from Unimod Isotopic label
PubMed:15283597
Unimod:196
(3-acrylamidopropyl)trimethylammonium
APTA d3
QAT:2H(3)
modification from Unimod Chemical derivative
184.28
C 10 H 20 N 2 O 1
184.15756
C 13 H 25 N 3 O 2 S 1
287.42
287.16675
C
artifact
Unimod:197
PSI-MOD
EAPTA d0
EQAT
MOD:00550
EAPTA d0
modification from Unimod Chemical derivative
Unimod:197
EAPTA d0
EQAT
modification from Unimod Isotopic label
189.19
C 10 (1)H 15 (2)H 5 N 2 O 1
189.18895
C 13 (1)H 20 (2)H 5 N 3 O 2 S 1
292.2
292.19812
C
artifact
Unimod:198
PSI-MOD
EAPTA d5
EQAT:2H(5)
MOD:00551
EAPTA d5
modification from Unimod Isotopic label
Unimod:198
EAPTA d5
EQAT:2H(5)
A protein modification that effectively converts a residue containing common isotopes to a 4x(2)H labeled dimethylated residue.
32.06
C 2 (2)H 4
32.056408
X
artifact
Unimod:199
PSI-MOD
DiMethyl-CHD2
Dimethyl:2H(4)
MOD:00552
Supposed to be alpha-amino and Lys-N6 derivatized by C(2)H2O and reduction.
4x(2)H labeled dimethylated residue
A protein modification that effectively converts a residue containing common isotopes to a 4x(2)H labeled dimethylated residue.
PubMed:14670044
Unimod:199
DiMethyl-CHD2
Dimethyl:2H(4)
A protein modification that effectively substitutes a (2-sulfanylethyl)sulfanyl (or thioethylthiol) group for a hydroxy group.
76.18
C 2 H 4 O -1 S 2
75.98053
X
artifact
Unimod:200
1,2-ethanedithiol (EDT)
PSI-MOD
EDT
Ethanedithiol
MOD:00553
From DeltaMass: Average Mass: 93; supposed to be derivatization of serine and threonine.
1,2-ethanedithiol modified residue
A protein modification that effectively substitutes a (2-sulfanylethyl)sulfanyl (or thioethylthiol) group for a hydroxy group.
DeltaMass:0
PubMed:11507762
Unimod:200
1,2-ethanedithiol (EDT)
EDT
Ethanedithiol
OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative
MOD:00548
170.26
C 9 H 18 N 2 O 1
170.1419
C
artifact
Unimod:202
PSI-MOD
MOD:00554
APTA-d0 with no neutral loss
true
OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative
Unimod:202
OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative
MOD:00548
170.26
C 9 H 18 N 2 O 1
170.1419
C
artifact
Unimod:203
PSI-MOD
MOD:00555
APTA-d0 with quaternary amine loss
true
OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative
Unimod:203
OBSOLETE because this modification not supported by any literature that I can find[PMT]
94.11
C 6 H 6 O 1
94.04186
C 12 H 18 N 2 O 2
222.29
222.13683
K
artifact
Unimod:205
PSI-MOD
Acrolein addition +94
Delta:H(6)C(6)O(1)
MOD:00556
acrolein addition +94
true
OBSOLETE because this modification not supported by any literature that I can find[PMT]
Unimod:205
Acrolein addition +94
Delta:H(6)C(6)O(1)
OBSOLETE because this modification not supported by the papers listed or any other that I can find[PMT]
56.06
C 3 H 4 O 1
56.026215
X
artifact
Unimod:206
PSI-MOD
Acrolein addition +56
Delta:H(4)C(3)O(1)
MOD:00557
acrolein addition +56
true
OBSOLETE because this modification not supported by the papers listed or any other that I can find[PMT]
PubMed:10825247
PubMed:15541752
Unimod:206
Acrolein addition +56
Delta:H(4)C(3)O(1)
OBSOLETE because this modification not supported by any literature that I can find[PMT]
38.05
C 3 H 2
38.01565
C 9 H 14 N 2 O 1
166.22
166.11061
K
artifact
Unimod:207
PSI-MOD
Acrolein addition +38
Delta:H(2)C(3)
MOD:00558
acrolein addition +38
true
OBSOLETE because this modification not supported by any literature that I can find[PMT]
Unimod:207
Acrolein addition +38
Delta:H(2)C(3)
OBSOLETE because this modification not supported by any literature that I can find[PMT]
76.1
C 6 H 4
76.0313
C 12 H 16 N 2 O 1
204.27
204.12627
K
artifact
Unimod:208
PSI-MOD
Acrolein addition +76
Delta:H(4)C(6)
MOD:00559
acrolein addition +76
true
OBSOLETE because this modification not supported by any literature that I can find[PMT]
Unimod:208
Acrolein addition +76
Delta:H(4)C(6)
OBSOLETE because this modification not supported by any literature that I can find[PMT]
112.13
C 6 H 8 O 2
112.05243
C 12 H 20 N 2 O 3
240.3
240.1474
K
artifact
Unimod:209
PSI-MOD
Acrolein addition +112
Delta:H(8)C(6)O(2)
MOD:00560
acrolein addition +112
true
OBSOLETE because this modification not supported by any literature that I can find[PMT]
Unimod:209
Acrolein addition +112
Delta:H(8)C(6)O(2)
modification from Unimod Isotopic label
85.11
C 4 H 7 N 1 O 1
85.052765
X
artifact
Unimod:211
PSI-MOD
N-ethyl iodoacetamide-d0
NEIAA
MOD:00561
N-ethyl iodoacetamide-
modification from Unimod Isotopic label
PubMed:12766232
Unimod:211
N-ethyl iodoacetamide-d0
NEIAA
modification from Unimod Isotopic label
90.08
C 4 (1)H 2 (2)H 5 N 1 O 1
90.084145
X
artifact
Unimod:212
PSI-MOD
N-ethyl iodoacetamide-d5
NEIAA:2H(5)
MOD:00562
N-ethyl iodoacetamide-d5
modification from Unimod Isotopic label
PubMed:12766232
Unimod:212
N-ethyl iodoacetamide-d5
NEIAA:2H(5)
A protein modification that effectively replaces a hydrogen atom with an N-acetylaminogalactose group through a glycosidic bond.
203.19
C 8 H 13 N 1 O 5
203.07938
X
GalNAcRes
PSI-MOD
HexNAc
MOD:00563
mono-N-acetylaminogalactosylated residue
A protein modification that effectively replaces a hydrogen atom with an N-acetylaminogalactose group through a glycosidic bond.
PubMed:18688235
GalNAcRes
HexNAc
Modification from Unimod Isotopic label. The Unimod term was extracted when it had not been approved. OBSOLETE because redundant to MOD:01505. Remap to MOD:01505, or one of the child terms MOD:01493 or MOD:01497.
MOD:01505
X
artifact
Unimod:214
PSI-MOD
Representative mass and accurate mass for 116 & 117
iTRAQ4plex
MOD:00564
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
true
Modification from Unimod Isotopic label. The Unimod term was extracted when it had not been approved. OBSOLETE because redundant to MOD:01505. Remap to MOD:01505, or one of the child terms MOD:01493 or MOD:01497.
URL:http://docs.appliedbiosystems.com/pebiodocs/04351918.pdf
Unimod:214
Representative mass and accurate mass for 116 & 117
iTRAQ4plex
modification from Unimod N-linked glycosylation
0.98
H -1 N -1 O 1
0.984016
C 4 H 5 N 1 O 3
115.09
115.02694
N
artifact
Unimod:7
PSI-MOD
Deamidated
Deamidation
MOD:00565
Conversion of glycosylated asparagine residues upon deglycosylation with PGNase F in H2O. CAUTION - the difference formula appears to be based on a partial structure [JSG].
deglycosylated asparagine
modification from Unimod N-linked glycosylation
Unimod:7#N
Deamidated
Deamidation
modification from Unimod Chemical derivative
297.15
Br 1 C 12 H 13 N 2 O 2
296.01605
Br 1 C 15 H 18 N 3 O 3 S 1
400.29
399.02524
C
artifact
Unimod:243
PSI-MOD
IGBP
Light IDBEST tag for quantitation
MOD:00566
"IDBEST tag for quantitation, http://www.targetdiscovery.com/index.php?topic=prod.idbe"
label cysteine with IGBP reagent
modification from Unimod Chemical derivative
Unimod:243
IGBP
Light IDBEST tag for quantitation
OBSOLETE because Unimod entry 244 is redundant with Unimod 348. Remap to MOD:00775.
-23.04
C -2 H -1 N -1 O 1
-23.015984
H
artifact
Unimod:244
PSI-MOD
MOD:00567
histidine oxidation to asparagine
true
OBSOLETE because Unimod entry 244 is redundant with Unimod 348. Remap to MOD:00775.
ChEBI:29956
PubMed:15736973
PubMed:5681232
PubMed:6692818
PubMed:9789001
RESID:AA0003
Unimod:244
OBSOLETE because Unimod entry 245 is redundant with Unimod 349. Remap to MOD:00776
MOD:00776
-22.05
C -2 H -2 N -2 O 2
-22.03197
H
artifact
Unimod:245
PSI-MOD
MOD:00568
histidine oxidation to aspartic acid
true
OBSOLETE because Unimod entry 245 is redundant with Unimod 349. Remap to MOD:00776
PubMed:1097438
PubMed:339692
PubMed:4399050
PubMed:5764436
PubMed:6692818
PubMed:8089117
PubMed:9521123
PubMed:9582379
Unimod:245
Natural or modified residues that are isobaric at a resolution below 0.000001 Da.
PSI-MOD
MOD:00569
residues isobaric at a resolution below 0.000001 Da
Natural or modified residues that are isobaric at a resolution below 0.000001 Da.
PubMed:18688235
Natural or modified residues with a mass of 71.037114 Da.
PSI-MOD
MOD:00570
residues isobaric at 71.037114 Da
Natural or modified residues with a mass of 71.037114 Da.
PubMed:18688235
A modification that effectively oxygenates C5 of an L-proline residue to form a 2-pyrrolidone-5-carboxylic acid, pyroglutamic acid.
13.98
H -2 O 1
13.979265
C 5 H 6 N 1 O 2
112.11
112.039856
P
artifact
Unimod:359
PyrGlu(Pro)
pyroglutamicp
PSI-MOD
Pro->pyro-Glu
Pyroglutamic
MOD:00571
The review article PubMed:9252331 does not provide an original citation for this modification [JSG].
2-pyrrolidone-5-carboxylic acid (Pro)
A modification that effectively oxygenates C5 of an L-proline residue to form a 2-pyrrolidone-5-carboxylic acid, pyroglutamic acid.
OMSSA:111
PubMed:9252331
Unimod:359
PyrGlu(Pro)
pyroglutamicp
Pro->pyro-Glu
Pyroglutamic
modification from Unimod Chemical derivative
199.27
C 9 H 13 N 1 O 2 S 1
199.0667
C 15 H 25 N 5 O 3 S 1
355.46
355.16782
R
artifact
Unimod:343
PSI-MOD
Argbiotinhydrazide
oxidized Arginine biotinylated with biotin hydrazide
MOD:00572
oxidized arginine biotinylated with biotin hydrazide
modification from Unimod Chemical derivative
PubMed:15174056
PubMed:15828771
Unimod:343
Argbiotinhydrazide
oxidized Arginine biotinylated with biotin hydrazide
modification from Unimod Chemical derivative
241.31
C 10 H 15 N 3 O 2 S 1
241.0885
C 16 H 27 N 5 O 3 S 1
369.48
369.18347
K
artifact
Unimod:353
PSI-MOD
Lysbiotinhydrazide
oxidized Lysine biotinylated with biotin hydrazide
MOD:00573
"http://www.piercenet.com/Proteomics/browse.cfm?fldID=84EBE112-F871-4CA5-807F-47327153CFCB"
oxidized lysine biotinylated with biotin hydrazide
modification from Unimod Chemical derivative
PubMed:15174056
Unimod:353
Lysbiotinhydrazide
oxidized Lysine biotinylated with biotin hydrazide
modification from Unimod Chemical derivative
258.34
C 10 H 18 N 4 O 2 S 1
258.11505
C 15 H 25 N 5 O 3 S 1
355.46
355.16782
P
artifact
Unimod:357
PSI-MOD
oxidized proline biotinylated with biotin hydrazide
probiotinhydrazide
MOD:00574
"http://www.piercenet.com/Proteomics/browse.cfm?fldID=84EBE112-F871-4CA5-807F-47327153CFCB"
oxidized proline biotinylated with biotin hydrazide
modification from Unimod Chemical derivative
PubMed:15174056
Unimod:357
oxidized proline biotinylated with biotin hydrazide
probiotinhydrazide
modification from Unimod Chemical derivative
240.32
C 10 H 16 N 4 O 1 S 1
240.10448
C 14 H 23 N 5 O 3 S 1
341.43
341.15216
T
artifact
Unimod:361
PSI-MOD
Thrbiotinhydrazide
oxidized Threonine biotinylated with biotin hydrazide
MOD:00575
"http://www.piercenet.com/Proteomics/browse.cfm?fldID=84EBE112-F871-4CA5-807F-47327153CFCB"
oxidized threonine biotinylated with biotin hydrazide
modification from Unimod Chemical derivative
PubMed:15174056
Unimod:361
Thrbiotinhydrazide
oxidized Threonine biotinylated with biotin hydrazide
modification from Unimod Other
70.09
C 4 H 6 O 1
70.04186
X
artifact
Unimod:253
PSI-MOD
Crotonaldehyde
MOD:00576
crotonylated residue
modification from Unimod Other
PubMed:11283024
PubMed:25907603
Unimod:253
Crotonaldehyde
Crotonaldehyde
modification occurs as a Schiff base in the presence of pentalysine
26.04
C 2 H 2
26.01565
C 8 H 14 N 2 O 1
666.91
666.4905
K, K, K, K, K
artifact
Unimod:254
PSI-MOD
Acetaldehyde +26
Delta:H(2)C(2)
MOD:00577
acetaldehyde crosslinked penta-L-lysine
modification occurs as a Schiff base in the presence of pentalysine
PubMed:7744761
Unimod:254
Acetaldehyde +26
Delta:H(2)C(2)
OBSOLETE because this modification not supported by any literature that I can find [PMT]
28.05
C 2 H 4
28.0313
C
X
artifact
Unimod:255
PSI-MOD
Acetaldehyde +28
Delta:H(4)C(2)
MOD:00578
acetaldehyde +28
true
OBSOLETE because this modification not supported by any literature that I can find [PMT]
Unimod:255
Acetaldehyde +28
Delta:H(4)C(2)
OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other
40.06
C 3 H 4
40.0313
X
artifact
Unimod:256
PSI-MOD
Delta:H(4)C(3)
Propionaldehyde +40
MOD:00579
propionaldehyde +40
true
OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other
Unimod:256
Delta:H(4)C(3)
Propionaldehyde +40
OBSOLETE because entry removed from Unimod. Remap potentially to MOD:00579 propionaldehyde +40
MOD:00579
42.08
C 3 H 6
42.04695
X
artifact
Unimod:257
PSI-MOD
MOD:00580
propionaldehyde +42
true
OBSOLETE because entry removed from Unimod. Remap potentially to MOD:00579 propionaldehyde +40
Unimod:257
A protein modification that effectively substitutes one (18)O atom for one (16)O atom.
2.0
(16)O -1 (18)O 1
2.004246
X
artifact
C-term
Unimod:258
ctermpepo18
PSI-MOD
Label:18O(1)
O18 Labeling
MOD:00581
(18)O monosubstituted residue
A protein modification that effectively substitutes one (18)O atom for one (16)O atom.
OMSSA:87
PubMed:11467524
Unimod:258
ctermpepo18
Label:18O(1)
O18 Labeling
A protein modification that effectively converts an L-lysine residue to 6x(13)C,2x(15)N labeled L-lysine.
8.01
(12)C -6 (13)C 6 (14)N -2 (15)N 2
8.014199
(13)C 6 H 12 (15)N 2 O 1
136.11
136.10916
K
artifact
Unimod:259
lys-13C615N2
PSI-MOD
13C(6) 15N(2) Silac label
Label:13C(6)15N(2)
MOD:00582
6x(13)C,2x(15)N labeled L-lysine
A protein modification that effectively converts an L-lysine residue to 6x(13)C,2x(15)N labeled L-lysine.
OMSSA:181
PubMed:12716131
Unimod:259
lys-13C615N2
13C(6) 15N(2) Silac label
Label:13C(6)15N(2)
A protein modification that effectively replaces a hydrogen atom with a thiophosphono group (H2PO2S, 'thiophosphate').
96.04
H 1 O 2 P 1 S 1
95.94349
X
artifact
Unimod:260
PSI-MOD
Thiophospho
Thiophosphorylation
MOD:00583
thiophosphorylated residue
A protein modification that effectively replaces a hydrogen atom with a thiophosphono group (H2PO2S, 'thiophosphate').
PubMed:12110917
Unimod:260
Thiophospho
Thiophosphorylation
A protein modification produced by formation of an adduct with 4-sulfophenyl isothiocyanate.
215.24
C 7 H 5 N 1 O 3 S 2
214.97108
X
artifact
N-term
Unimod:261
PSI-MOD
4-sulfophenyl isothiocyanate
SPITC
MOD:00584
4-sulfophenyl isothiocyanate derivatized residue
A protein modification produced by formation of an adduct with 4-sulfophenyl isothiocyanate.
PubMed:14689565
PubMed:14745769
PubMed:16526082
Unimod:261
4-sulfophenyl isothiocyanate
SPITC
A protein modification that effectively substitutes three (2)H deuterium atoms for three (1)H protium atoms.
3.02
(1)H -3 (2)H 3
3.01883
X
artifact
Unimod:262
D(H)3Res
PSI-MOD
Label:2H(3)
Trideuteration
MOD:00585
deuterium trisubstituted residue
A protein modification that effectively substitutes three (2)H deuterium atoms for three (1)H protium atoms.
Unimod:262
D(H)3Res
Label:2H(3)
Trideuteration
modification from Unimod Chemical derivative
121.2
C 7 H 7 N 1 O -1 S 1
121.035
X
artifact
Unimod:264
PSI-MOD
PET
phosphorylation to pyridyl thiol
MOD:00586
pyridyl thiol modified residue
modification from Unimod Chemical derivative
Unimod:264
PET
phosphorylation to pyridyl thiol
A protein modification that effectively converts an L-arginine residue to 6x(13)C, 4x(15)N labeled L-arginine.
10.01
(12)C -6 (13)C 6 (14)N -4 (15)N 4
10.008269
(13)C 6 H 12 (15)N 4 O 1
166.11
166.10938
R
artifact
Unimod:267
arg-13c6-15n4
PSI-MOD
13C(6) 15N(4) Silac label
Label:13C(6)15N(4)
MOD:00587
6x(13)C,4x(15)N labeled L-arginine
A protein modification that effectively converts an L-arginine residue to 6x(13)C, 4x(15)N labeled L-arginine.
OMSSA:137
PubMed:12716131
Unimod:267
arg-13c6-15n4
13C(6) 15N(4) Silac label
Label:13C(6)15N(4)
A protein modification that effectively converts an L-valine residue to 5x(13)C,1x(15)N labeled L-valine.
6.01
(12)C -5 (13)C 5 (14)N -1 (15)N 1
6.013809
(13)C 5 H 9 (15)N 1 O 1
105.08
105.08222
V
artifact
Unimod:268
PSI-MOD
13C(5) 15N(1) Silac label
Label:13C(5)15N(1)
MOD:00588
5x(13)C,1x(15)N labeled L-valine
A protein modification that effectively converts an L-valine residue to 5x(13)C,1x(15)N labeled L-valine.
PubMed:12771378
Unimod:268#V
13C(5) 15N(1) Silac label
Label:13C(5)15N(1)
A protein modification that effectively converts an L-phenylalanine residue to (13)C,(15)N labeled L-phenylalanine.
10.03
(12)C -9 (13)C 9 (14)N -1 (15)N 1
10.027228
(13)C 9 H 9 (15)N 1 O 1
157.1
157.09564
F
artifact
Unimod:269
PSI-MOD
13C(9) 15N(1) Silac label
Label:13C(9)15N(1)
MOD:00589
9x(13)C,1x(15)N labeled L-phenylalanine
A protein modification that effectively converts an L-phenylalanine residue to (13)C,(15)N labeled L-phenylalanine.
PubMed:12771378
Unimod:269
13C(9) 15N(1) Silac label
Label:13C(9)15N(1)
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative
362.38
C 19 H 22 O 7
362.13657
X
artifact
Unimod:270
PSI-MOD
Cytopiloyne
nucleophilic addtion to cytopiloyne
MOD:00590
nucleophilic addtion to cytopiloyne
true
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative
PubMed:15549660
Unimod:270
Cytopiloyne
nucleophilic addtion to cytopiloyne
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative
380.39
C 19 H 24 O 8
380.14713
X
artifact
Unimod:271
PSI-MOD
Cytopiloyne+water
nucleophilic addition to cytopiloyne+H2O
MOD:00591
nucleophilic addition to cytopiloyne+H2O
true
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative
PubMed:15549660
Unimod:271
Cytopiloyne+water
nucleophilic addition to cytopiloyne+H2O
modification from Unimod Chemical derivative
136.12
C 3 H 4 O 4 S 1
135.98303
X
artifact
N-term
Unimod:272
PSI-MOD
CAF
sulfonation of N-terminus
MOD:00592
sulfonation of N-terminal
modification from Unimod Chemical derivative
PubMed:12705581
PubMed:15732931
PubMed:16046801
Unimod:272
CAF
sulfonation of N-terminus
OBSOLETE because removed from Unimod. modification from Unimod Chemical derivative
253.25
C 12 H 15 N 1 O 5
253.09502
C 18 H 27 N 3 O 6
381.43
381.18997
K
artifact
Unimod:273
PSI-MOD
Xlink:SSD
covalent modification of lysine by cross-linking reagent
MOD:00593
J. Prot. Chem. 2, 263-277, 1983
covalent modification of lysine by omega-maleimido alkanoyl N-hydroxysuccinimido esters
true
OBSOLETE because removed from Unimod. modification from Unimod Chemical derivative
Unimod:273
Xlink:SSD
covalent modification of lysine by cross-linking reagent
Natural or modified resiues with a mass of 113.047678 Da.
PSI-MOD
MOD:00594
residues isobaric at 113.047678 Da
Natural or modified resiues with a mass of 113.047678 Da.
PubMed:18688235
A protein modification that effectively replaces a hydrogen atom with an manose group through a glycosidic bond
162.14
C 6 H 10 O 5
162.05283
X
natural
ManRes
PSI-MOD
MOD:00595
monomannosylated residue
A protein modification that effectively replaces a hydrogen atom with an manose group through a glycosidic bond
PubMed:18688235
ManRes
A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS.
183.23
C 8 H 9 N 1 O 2 S 1
183.0354
X
artifact
Unimod:276
AEBSF
PSI-MOD
AEBS
Aminoethylbenzenesulfonylation
MOD:00596
From DeltaMass: Average Mass: 183 Average Mass Change:183 References:We have found that AEBSF modifies many proteins by covalent attachment, preferentially on Tyr, and to a lesser extent on Lys, His, and the amino-terminus. These modifications were identified by electrospray MS of the proteins (adds 183 Da per AEBS-group) and by peptide mapping and MS/MS. All the proteins we examined were modified after 24 hrs. at 4 C with 1 mM AEBSF in TRIS, pH 8.0. The reaction is 10-20x slower at pH 7; however AEBSF is quite stable in aqueous solution and the extent of to which the protein is modified continues to increase for several days. We have seen the addition of 10 or more AEBS-groups to proteins after prolonged storage. We found no equivalent modification from PMSF, probably because it degrades so quickly. We no longer use AEBSF, and urge caution to those who do. To address the problem, Boehringer Mannheim (now Roche Molecular Biochemicals) introduced Pefabloc PLUS which includes an additional component to compete for these side reactions. In our limited experience with Pefabloc PLUS, it reduces the +183 modifications, but does not always eliminate them. As a result, we prefer PMSF, despite its own set of drawbacks. We have never found PMSF-induced modification of proteins (except trypsin), probably due to its short half-life in aqeous solution.
4-(2-aminoethyl)benzenesulfonyl fluoride derivatized residue
A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS.
DeltaMass:235
PubMed:8597590
Unimod:276
AEBSF
AEBS
Aminoethylbenzenesulfonylation
OBSOLETE because Unimod entry 277 redundant with Unimod 39. Remap to MOD:00110.
MOD:00110
46.09
C 1 H 2 S 1
45.98772
C
artifact
Unimod:277
PSI-MOD
MOD:00597
methyl methanethiosulfonate
true
OBSOLETE because Unimod entry 277 redundant with Unimod 39. Remap to MOD:00110.
Unimod:277
A protein modification that effectively converts an L-cysteine residue to S-(2-hydroxyethyl)cysteine
44.05
C 2 H 4 O 1
44.026215
C 5 H 9 N 1 O 2 S 1
147.19
147.0354
C
artifact
Unimod:278
PSI-MOD
Ethanolation of Cys
Ethanolyl
MOD:00598
This modification of cysteine is produced by the reagent iodoethanol with triethylphosphine [JSG].
S-(2-hydroxyethyl)cysteine
A protein modification that effectively converts an L-cysteine residue to S-(2-hydroxyethyl)cysteine
PubMed:15351294
Unimod:278
Ethanolation of Cys
Ethanolyl
A protein modification that effectively replaces one hydrogen atom with one methyl group.
14.03
C 1 H 2
14.01565
X
Unimod:34
Me1Res
PSI-MOD
Methyl
Methylation
MOD:00599
monomethylated residue
A protein modification that effectively replaces one hydrogen atom with one methyl group.
PubMed:11875433
Unimod:34
Me1Res
Methyl
Methylation
A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-ethyl ester.
28.05
C 2 H 4
28.0313
C 7 H 11 N 1 O 3
157.17
157.0739
E
artifact
Unimod:280
Ethyl
PSI-MOD
Ethyl
Ethylation
MOD:00600
From DeltaMass: Average Mass: 28 with no citation. The Unimod citation refers to the formation of glutamate ethyl ester and not to either lysine or N-terminal alkylation. For dimethylated residues, see MOD:00429 and its children [JSG].
L-glutamic acid 5-ethyl ester
A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-ethyl ester.
DeltaMass:0
PubMed:9629898
Unimod:280#E
Ethyl
Ethyl
Ethylation
A protein modification that effectively produces an heterocyclic amino acid with a covalent bond between the side chain and either its alpha amino or 1-carboxyl group, possibly breaking the peptide chain.
CycRes
PSI-MOD
MOD:00601
cyclized residue
A protein modification that effectively produces an heterocyclic amino acid with a covalent bond between the side chain and either its alpha amino or 1-carboxyl group, possibly breaking the peptide chain.
PubMed:18688235
CycRes
A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with an methyl group.
NMeRes
PSI-MOD
MOD:00602
N-methylated residue
A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with an methyl group.
PubMed:18688235
NMeRes
OBSOLETE because Unimod entry 283 is redundant with Unimod 280. Remap to MOD:00600
MOD:00600
28.05
C 2 H 4
28.0313
X
artifact
N-term
Unimod:283
PSI-MOD
MOD:00603
N-ethylation
true
OBSOLETE because Unimod entry 283 is redundant with Unimod 280. Remap to MOD:00600
Unimod:283
A protein modification that effectively converts an L-lysine residue to 2x(2)H labeled monomethylated L-lysine.
16.03
C 1 (2)H 2
16.028204
C 7 (1)H 12 (2)H 2 N 2 O 1
144.12
144.12317
K
artifact
Unimod:284
PSI-MOD
Deuterium Methylation of Lysine
Methyl:2H(2)
MOD:00604
2x(2)H monomethylated L-lysine
A protein modification that effectively converts an L-lysine residue to 2x(2)H labeled monomethylated L-lysine.
PubMed:15525938
Unimod:284
Deuterium Methylation of Lysine
Methyl:2H(2)
modification from Unimod Chemical derivative, C-Terminal/Glutamate/Aspartate sulfonation
155.0
(12)C 6 H 5 N 1 O 2 S 1
155.0041
X
artifact
C-term
Unimod:285
PSI-MOD
Light Sulfanilic Acid (SA) C12
SulfanilicAcid
MOD:00605
Sulfanilic Acid (SA), light C12
modification from Unimod Chemical derivative, C-Terminal/Glutamate/Aspartate sulfonation
Unimod:285
Light Sulfanilic Acid (SA) C12
SulfanilicAcid
modification from Unimod Chemical derivative
161.02
(13)C 6 H 5 N 1 O 2 S 1
161.02423
X
artifact
C-term
Unimod:286
PSI-MOD
Heavy Sulfanilic Acid (SA) C13
SulfanilicAcid:13C(6)
MOD:00606
Sulfanilic Acid (SA), heavy C13
modification from Unimod Chemical derivative
PubMed:9254591
Unimod:286
Heavy Sulfanilic Acid (SA) C13
SulfanilicAcid:13C(6)
modification from Unimod Chemical derivative
30.99
H -1 O 2
30.982004
C 11 H 9 N 2 O 3
217.2
217.06131
W
artifact
C-term
Unimod:288
PSI-MOD
Trp->Oxolactone
Tryptophan oxidation to oxolactone
MOD:00607
Unimod name, formula, and terminal specification corrected. Formula corresponded to uncleaved intermediate [JSG].
dioxoindolealanine lactone
modification from Unimod Chemical derivative
PubMed:7949339
Unimod:288
Trp->Oxolactone
Tryptophan oxidation to oxolactone
modification from Unimod Chemical derivative
X
artifact
Unimod:289
PSI-MOD
Biotin polyethyleneoxide amine
Biotin-PEO-Amine
MOD:00608
biotin polyethyleneoxide amine
modification from Unimod Chemical derivative
Unimod:289
Biotin polyethyleneoxide amine
Biotin-PEO-Amine
modification from Unimod Chemical derivative
428.61
C 19 H 32 N 4 O 3 S 2
428.1916
C 22 H 37 N 5 O 4 S 3
531.75
531.20074
C
artifact
Unimod:290
PSI-MOD
Biotin-HPDP
Pierce EZ-Link Biotin-HPDP
MOD:00609
Pierce EZ-Link Biotin-HPDP modified L-cysteine
modification from Unimod Chemical derivative
Unimod:290
Biotin-HPDP
Pierce EZ-Link Biotin-HPDP
modification from Unimod Chemical derivative
200.59
Hg 1
201.97064
C 3 H 5 Hg 1 N 1 O 1 S 1
303.73
304.97983
C
artifact
Unimod:291
PSI-MOD
Delta:Hg(1)
Mercury Mercaptan
MOD:00610
cysteinyl mercury
modification from Unimod Chemical derivative
PubMed:10695144
Unimod:291
Delta:Hg(1)
Mercury Mercaptan
A protein modification that is produced by reaction of iodouridine monophosphate with a residue.
322.17
C 9 H 11 N 2 O 9 P 1
322.0202
X
artifact
Unimod:292
PSI-MOD
Cross-link of (Iodo)-uracil MP with W,F,Y
IodoU-AMP
MOD:00611
iodouridine monophosphate derivatized residue
A protein modification that is produced by reaction of iodouridine monophosphate with a residue.
PubMed:11112526
PubMed:11567090
PubMed:6540775
Unimod:292
Cross-link of (Iodo)-uracil MP with W,F,Y
IodoU-AMP
A protein modification that is produced by derivatization of a residue with 3,3-dithiobis[sulfosuccinimidyl propanoate], DTSSP, or with Pierce EZ-Link Sulfo-NHS-SS-Biotin reagent, sulfosuccinimidyl 3-[(2-[biotinamido]ethyl)disulfanyl]propanoate, followed by reduction with dithiothreitol and then reaction with iodoacetamide.
145.18
C 5 H 7 N 1 O 2 S 1
145.01974
X
artifact
Unimod:293
PSI-MOD
3-(carbamidomethylthio)propanoyl
CAMthiopropanoyl
MOD:00612
3-(carboxamidomethylthio)propanoylated residue
A protein modification that is produced by derivatization of a residue with 3,3-dithiobis[sulfosuccinimidyl propanoate], DTSSP, or with Pierce EZ-Link Sulfo-NHS-SS-Biotin reagent, sulfosuccinimidyl 3-[(2-[biotinamido]ethyl)disulfanyl]propanoate, followed by reduction with dithiothreitol and then reaction with iodoacetamide.
PubMed:15121203
Unimod:293
3-(carbamidomethylthio)propanoyl
CAMthiopropanoyl
modification from Unimod Chemical derivative
326.42
C 14 H 22 N 4 O 3 S 1
326.14127
C 17 H 27 N 5 O 4 S 2
429.55
429.15045
C
artifact
Unimod:294
PSI-MOD
IED-Biotin
biotinoyl-iodoacetyl-ethylenediamine
MOD:00613
biotinoyl-iodoacetyl-ethylenediamine
modification from Unimod Chemical derivative
PubMed:10906242
Unimod:294
IED-Biotin
biotinoyl-iodoacetyl-ethylenediamine
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a fucose (6-deoxy-D-galactose) group through a glycosidic bond.
146.14
C 6 H 10 O 4
146.0579
X
natural
GNO:G49112ZN
Unimod:295
Fuc
PSI-MOD
Fucose
dHex
MOD:00614
fucosylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a fucose (6-deoxy-D-galactose) group through a glycosidic bond.
PubMed:11344537
PubMed:15189151
Unimod:295
Fuc
Fucose
dHex
OBSOLETE because entry Unimod:261 site N-term R was abandoned. Remap to MOD:00584
MOD:00584
215.24
C 7 H 5 N 1 O 3 S 2
214.97108
R
artifact
N-term
Unimod:261
PSI-MOD
MOD:00615
4-sulfophenyl isothiocyante modification to N-term R
true
OBSOLETE because entry Unimod:261 site N-term R was abandoned. Remap to MOD:00584
PubMed:14689565
Unimod:261
Natural or modified residues that are isobaric at a resolution below 0.1 Da.
PSI-MOD
MOD:00616
residues isobaric at a resolution below 0.1 Da
Natural or modified residues that are isobaric at a resolution below 0.1 Da.
PubMed:18688235
A protein modification that effectively converts a residue containing common isotopes to a 3x(2)H labeled residue methyl ester.
17.03
C 1 (1)H -1 (2)H 3
17.03448
X
artifact
C-term
Unimod:298
ctermpeptrideuteromethyl
PSI-MOD
Methyl:2H(3)
deuterated methyl ester
MOD:00617
3x(2)H residue methyl ester
A protein modification that effectively converts a residue containing common isotopes to a 3x(2)H labeled residue methyl ester.
OMSSA:21
Unimod:298
ctermpeptrideuteromethyl
Methyl:2H(3)
deuterated methyl ester
modification from Unimod Chemical derivative
44.01
C 1 O 2
43.98983
C 12 H 10 N 2 O 3
230.22
230.06914
W
artifact
Unimod:299
PSI-MOD
Carboxy
Carboxylation
MOD:00618
There is no literature citation for this Unimod entry [JSG].
tryptophan carboxylation
modification from Unimod Chemical derivative
Unimod:299#W
Carboxy
Carboxylation
OBSOLETE because entry 300 is redundant with Unimod 6 remap to MOD:01328
MOD:01328
58.04
C 2 H 2 O 2
58.005478
W
artifact
Unimod:300
PSI-MOD
MOD:00619
hydroxylethanone
true
OBSOLETE because entry 300 is redundant with Unimod 6 remap to MOD:01328
Unimod:300
modification from Unimod Chemical derivative
190.2
C 10 H 10 N 2 O 2
190.07423
C 13 H 15 N 3 O 3 S 1
293.34
293.0834
C
artifact
Unimod:301
PSI-MOD
Bromobimane
Monobromobimane derivative
MOD:00620
1-(bromomethyl)-2,6,7-trimethylpyrazolo[1,2-a]pyrazole-3,5-dione, C 10 H 11 Br 1 N 2 O 2.
cysteine monobromobimane derivative
modification from Unimod Chemical derivative
PubMed:7856876
Unimod:301
Bromobimane
Monobromobimane derivative
modification from Unimod Chemical derivative
170.17
C 11 H 6 O 2
170.03677
X
artifact
Unimod:302
PSI-MOD
Menadione
Menadione quinone derivative
MOD:00621
menadione quinone derivative
modification from Unimod Chemical derivative
PubMed:15939799
Unimod:302
Menadione
Menadione quinone derivative
modification from Unimod Chemical derivative
76.11
C 2 H 4 O 1 S 1
75.99828
C 5 H 9 N 1 O 2 S 2
179.25
179.00748
C
artifact
Unimod:303
Beta mercaptoethanol adduct
PSI-MOD
Cysteine mercaptoethanol
DeStreak
MOD:00622
From DeltaMass: Average Mass: 76 Average Mass Change:76 PubMed:8019414.
cysteine mercaptoethanol
modification from Unimod Chemical derivative
DeltaMass:80
PubMed:12442261
Unimod:303
Beta mercaptoethanol adduct
Cysteine mercaptoethanol
DeStreak
modification from Unimod N-linked glycosylation
1443.33
C 56 H 90 N 4 O 39
1442.5182
C 60 H 96 N 6 O 41
1557.43
1556.5612
N
natural
GNO:G25987BV
Unimod:305
PSI-MOD
Fucosylated biantennary (-2 galactose)
dHex(1)Hex(3)HexNAc(4)
MOD:00623
fucosylated biantennary (-2 galactose) N4-glycosylated asparagine
modification from Unimod N-linked glycosylation
Unimod:305
Fucosylated biantennary (-2 galactose)
dHex(1)Hex(3)HexNAc(4)
Natural or modified residues with a mass of 113.0-113.1 Da.
PSI-MOD
MOD:00624
residues isobaric at 113.0-113.1 Da
Natural or modified residues with a mass of 113.0-113.1 Da.
PubMed:18688235
modification from Unimod Chemical derivative
111.1
C 5 H 5 N 1 O 2
111.03203
X
artifact
Unimod:314
PSI-MOD
Nmethylmaleimide
MOD:00625
N-methylmaleimide derivatized residue
modification from Unimod Chemical derivative
Unimod:314
Nmethylmaleimide
Nmethylmaleimide
modification from Unimod Chemical derivative
421.43
C 21 H 15 N 3 O 5 S 1
421.07324
X
artifact
Unimod:478
PSI-MOD
FTC
fluorescein-5-thiosemicarbazide
MOD:00626
fluorescein-5-thiosemicarbazide modified residue
modification from Unimod Chemical derivative
PubMed:2883911
Unimod:478
FTC
fluorescein-5-thiosemicarbazide
modification from Unimod Chemical derivative
78.11
C 6 H 6
78.04695
C 12 H 18 N 2 O 1
206.29
206.1419
K
artifact
Unimod:316
(2S)-2-amino-6-(2,5-dimethylpyrrolidin-1-yl)hexanoic acid
6-(2,5-dimethylpyrrolidin-1-yl)norleucine
PSI-MOD
2,5-dimethypyrrole
DimethylpyrroleAdduct
MOD:00627
There is no citation for this Unimod entry. Add PubMed:7981420, correct spelling [JSG].
2,5-dimethylpyrrole lysine from 2,5-hexanedione adduct
modification from Unimod Chemical derivative
Unimod:316
(2S)-2-amino-6-(2,5-dimethylpyrrolidin-1-yl)hexanoic acid
6-(2,5-dimethylpyrrolidin-1-yl)norleucine
2,5-dimethypyrrole
DimethylpyrroleAdduct
a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with two hexose sugar groups through glycosidic bonds
324.28
C 12 H 20 O 10
324.10565
X
natural
GNO:G90627TW
PSI-MOD
MOD:00628
Hex2
a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with two hexose sugar groups through glycosidic bonds
PubMed:18688235
modification from Unimod Chemical derivative
62.07
C 5 H 2
62.01565
C 11 H 14 N 2 O 1
190.25
190.11061
K
artifact
Unimod:318
PSI-MOD
Delta:H(2)C(5)
MDA adduct +62
MOD:00629
Usually major adduct formed from malondialdehyde (MDA) with the amino group of lysine residues [UniProt].
MDA adduct +62
modification from Unimod Chemical derivative
Unimod:318
Delta:H(2)C(5)
MDA adduct +62
modification from Unimod Chemical derivative
54.05
C 3 H 2 O 1
54.010567
X
artifact
Unimod:319
PSI-MOD
Delta:H(2)C(3)O(1)
MDA adduct +54
MOD:00630
This is not a legitimate ontological entry and will become obsolete when the children are reassigned [JSG]
C3-H2-O adduct (+54 amu) of malondialdehyde with lysine or methylglyoxal with arginine.
modification from Unimod Chemical derivative
PubMed:9328283
Unimod:319
Delta:H(2)C(3)O(1)
MDA adduct +54
modification from Unimod Chemical derivative
143.14
C 6 H 9 N 1 O 3
143.05824
X
artifact
Unimod:320
PSI-MOD
Nethylmaleimide+water
Nethylmaleimidehydrolysis
MOD:00631
N-ethylmaeimide adduct + H20 (a mixture of isobaric products) [JSG].
hydrolyzed N-ethylmaleimide adduct
modification from Unimod Chemical derivative
Unimod:320
Nethylmaleimide+water
Nethylmaleimidehydrolysis
OBSOLETE because this chemical derivative modification from Unimod 321 is deprecated.
-17.01
H -1 O -1
-17.00274
N
artifact
Unimod:321
PSI-MOD
MOD:00632
N-succinimide
true
OBSOLETE because this chemical derivative modification from Unimod 321 is deprecated.
Unimod:321
modification from Unimod Chemical derivative
713.57
C 31 H 30 I 1 N 4 O 6 S 1
713.0931
C 34 H 35 I 1 N 5 O 7 S 2
816.71
816.10223
C
artifact
Unimod:323
bis-((N-iodoacetyl)piperazinyl)sulfonerhodamine
PSI-MOD
Xlink:B10621
bis-N-I-sulfonerahodamine
MOD:00633
Invitrogen B-10621, a red fluorescent cross-linking reagent (only link to Cys is indicated) [Unimod].
bis-N-I-sulfonerahodamine
modification from Unimod Chemical derivative
Unimod:323
bis-((N-iodoacetyl)piperazinyl)sulfonerhodamine
Xlink:B10621
bis-N-I-sulfonerahodamine
modification from Unimod Chemical derivative
123.6
C 3 Cl 1 H 6 N 1 S 1
122.99095
X
artifact
Unimod:324
PSI-MOD
DTBP
dimethyl 3,3'-dithiobispropionimidate
MOD:00634
Pierce reagent, needs sites for N, Q, R, K, and N-term [JSG].
dimethyl 3,3'-dithiobispropionimidate
modification from Unimod Chemical derivative
PubMed:770170
Unimod:324
DTBP
dimethyl 3,3'-dithiobispropionimidate
modification from Unimod Chemical derivative
572.75
C 27 H 49 N 4 O 5 P 1 S 1
572.3161
C 30 H 54 N 5 O 7 P 1 S 1
659.82
659.34814
S
artifact
Unimod:325
PSI-MOD
10-ethoxyphosphinyl-N-(biotinamidopentyl)decanamide
FP-Biotin
MOD:00635
10-fluoroethoxyphosphinyl-N-(biotinamidopentyl)decanamide
modification from Unimod Chemical derivative
PubMed:10611275
Unimod:325
10-ethoxyphosphinyl-N-(biotinamidopentyl)decanamide
FP-Biotin
A protein modification that effectively converts an L-serine residue to S-ethylcysteine.
44.11
C 2 H 4 O -1 S 1
44.008457
C 5 H 9 N 1 O 1 S 1
131.19
131.04048
S
artifact
Unimod:327
PSI-MOD
Delta:H(4)C(2)O(-1)S(1)
S-Ethylcystine from Serine
MOD:00636
Modification from Unimod. Phosphoserine is converted to dehydroalanine then by Michael addition of ethanethiol to S-ethylcysteine. Needs parent and sibling for S-ethyl-cysteine.
S-ethylcysteine (Ser)
A protein modification that effectively converts an L-serine residue to S-ethylcysteine.
Unimod:327
Delta:H(4)C(2)O(-1)S(1)
S-Ethylcystine from Serine
A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with a (13)C,3x(2)H labeled methyl group to form a 1x(13)C,3x(2)H labeled monomethylated L-arginine.
18.04
(13)C 1 (1)H -1 (2)H 3
18.037834
(12)C 6 (13)C 1 (1)H 11 (2)H 3 N 4 O 1
174.14
174.13895
R
artifact
Unimod:329
PSI-MOD
Methyl:2H(3)13C(1)
monomethylated arginine
MOD:00637
1x(13)C,3x(2)H labeled monomethylated L-arginine
A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with a (13)C,3x(2)H labeled methyl group to form a 1x(13)C,3x(2)H labeled monomethylated L-arginine.
Unimod:329
Methyl:2H(3)13C(1)
monomethylated arginine
A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated L-arginine.
36.08
(13)C 2 (1)H -2 (2)H 6
36.07567
(12)C 6 (13)C 2 (1)H 10 (2)H 6 N 4 O 1
192.18
192.17679
R
artifact
Unimod:330
PSI-MOD
Dimethyl:2H(6)13C(2)
dimethylated arginine
MOD:00638
2x(13)C,6x(2)H labeled dimethylated L-arginine
A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated L-arginine.
PubMed:15782174
Unimod:330
Dimethyl:2H(6)13C(2)
dimethylated arginine
modification from Unimod Chemical derivative
525.66
C 19 H 34 N 4 O 5 P 1 S 3
525.1429
X
artifact
Unimod:332
PSI-MOD
Thiophos-S-S-biotin
thiophosphate labeled with biotin-HPDP
MOD:00639
thiophosphate labeled with biotin-HPDP
modification from Unimod Chemical derivative
Unimod:332
Thiophos-S-S-biotin
thiophosphate labeled with biotin-HPDP
modification from Unimod Chemical derivative
467.54
C 19 F 1 H 35 N 3 O 5 P 1 S 1
467.2019
C 22 F 1 H 40 N 4 O 7 P 1 S 1
554.62
554.23395
S
artifact
Unimod:333
PSI-MOD
6-N-biotinylaminohexyl isopropyl phosphate
Can-FP-biotin
MOD:00640
6-N-biotinylaminohexyl isopropyl phosphorofluoridate
modification from Unimod Chemical derivative
Unimod:333
6-N-biotinylaminohexyl isopropyl phosphate
Can-FP-biotin
OBSOLETE because Unimod entry 334 is merged with Unimod 293. Remap to MOD:00612
MOD:00612
146.18
C 5 H 8 N 1 O 2 S 1
146.02757
K
artifact
Unimod:334
PSI-MOD
MOD:00641
CAMthiopropanoyl of Lys
true
OBSOLETE because Unimod entry 334 is merged with Unimod 293. Remap to MOD:00612
Unimod:334
A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4.
158.24
C 9 H 18 O 2
158.13068
X
artifact
Unimod:335
PSI-MOD
HNE+Delta:H(2)
reduced 4-Hydroxynonenal
MOD:00642
4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG].
reduced 4-hydroxynonenal adduct
A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4.
PubMed:11910026
PubMed:15133838
Unimod:335
HNE+Delta:H(2)
reduced 4-Hydroxynonenal
modification from Unimod Artifact
13.04
C 1 H 3 N 1 O -1
13.031634
X
artifact
Unimod:337
PSI-MOD
Methylamine
Michael addition with methylamine
MOD:00643
methylamine Michael addition derivatized residue
modification from Unimod Artifact
PubMed:11968134
Unimod:337
Methylamine
Michael addition with methylamine
A protein modification that effectively replaces a residue hydroxyl group with an acetoxy group.
42.04
C 2 H 2 O 1
42.010567
X
natural
OAcRes
PSI-MOD
MOD:00644
mono O-acetylated residue
A protein modification that effectively replaces a residue hydroxyl group with an acetoxy group.
PubMed:18688235
OAcRes
A protein modification that effectively replaces a residue sulfanyl group with an acetylsulfanyl group.
42.04
C 2 H 2 O 1 S 0
42.010567
X
natural
SAcRes
PSI-MOD
MOD:00645
mono S-acetylated residue
A protein modification that effectively replaces a residue sulfanyl group with an acetylsulfanyl group.
PubMed:18688235
SAcRes
A protein modification that effectively converts an L-cysteine residue to either N-acetyl-L-cysteine or S-acetyl-L-cysteine.
42.04
C 2 H 2 N 0 O 1 S 0
42.010567
C 5 H 7 N 1 O 2 S 1
145.18
145.01974
C
natural
AcCys
PSI-MOD
MOD:00646
monoacetylated L-cysteine
A protein modification that effectively converts an L-cysteine residue to either N-acetyl-L-cysteine or S-acetyl-L-cysteine.
PubMed:18688235
AcCys
A protein modification that effectively converts an L-serine residue to either N-acetyl-L-serine, O-acetyl-L-serine, or N,O-diacetyl-L-serine.
42.04
C 2 H 2 N 0 O 1
42.010567
S
natural
AcSer
PSI-MOD
MOD:00647
monoacetylated L-serine
A protein modification that effectively converts an L-serine residue to either N-acetyl-L-serine, O-acetyl-L-serine, or N,O-diacetyl-L-serine.
PubMed:18688235
AcSer
A protein modification that effectively converts an L-serine residue to N,O-diacetyl-L-serine.
84.07
C 4 H 4 N 0 O 2
84.021126
C 7 H 10 N 1 O 4
172.16
172.06099
S
artifact
N-term
(S)-2-acetamido-3-acetyloxypropanoic acid
N,O-diacetyl-L-serine
N,O-diacetylserine
NOAc2Ser
PSI-MOD
MOD:00648
In one paper, the samples were prepared using glacial acetic acid, and were probably artifactual [JSG].
N,O-diacetylated L-serine
A protein modification that effectively converts an L-serine residue to N,O-diacetyl-L-serine.
PubMed:16731519
PubMed:489587
PubMed:7309355
RESID:AA0051#var
RESID:AA0364#var
(S)-2-acetamido-3-acetyloxypropanoic acid
N,O-diacetyl-L-serine
N,O-diacetylserine
NOAc2Ser
A protein modification that effectively replaces a hydrogen atom with an acyl group.
AcylRes
PSI-MOD
MOD:00649
acylated residue
A protein modification that effectively replaces a hydrogen atom with an acyl group.
PubMed:18688235
AcylRes
A protein modification that effectively replaces a residue amino group with a myristoylamino group.
210.36
C 14 H 26 O 1
210.19836
X
natural
NMyrRes
PSI-MOD
MOD:00650
N-myristoylated residue
A protein modification that effectively replaces a residue amino group with a myristoylamino group.
PubMed:18688235
NMyrRes
A protein modification that effectively replaces a residue amino group with a palmitoylamino group.
238.41
C 16 H 30 O 1
238.22966
X
natural
N-hexadecanoylated residue
NPamRes
PSI-MOD
MOD:00651
N-palmitoylated residue
A protein modification that effectively replaces a residue amino group with a palmitoylamino group.
PubMed:18688235
N-hexadecanoylated residue
NPamRes
A protein modification that effectively replaces a residue hydroxyl group with a palmitoyloxy group.
238.41
C 16 H 30 O 1
238.22966
X
natural
O-hexadecanoylated residue
OPamRes
PSI-MOD
MOD:00652
O-palmitoylated residue
A protein modification that effectively replaces a residue hydroxyl group with a palmitoyloxy group.
PubMed:18688235
O-hexadecanoylated residue
OPamRes
A protein modification that effectively replaces a residue sulfanyl group with an palmitoylsulfanyl group.
238.41
C 16 H 30 O 1 S 0
238.22966
X
natural
S-hexadecanoylated residue
SPamRes
PSI-MOD
MOD:00653
S-palmitoylated residue
A protein modification that effectively replaces a residue sulfanyl group with an palmitoylsulfanyl group.
PubMed:18688235
S-hexadecanoylated residue
SPamRes
a protein modification that effectively replaces a sulfanyl group with a methylsulfanyl group
SMeRes
PSI-MOD
MOD:00654
S-methylated residue
a protein modification that effectively replaces a sulfanyl group with a methylsulfanyl group
PubMed:18688235
SMeRes
A protein modification that effectively replaces a residue sulfanyl group with an myristoylsulfanyl group.
210.36
C 14 H 26 O 1 S 0
210.19836
X
natural
SMyrRes
PSI-MOD
MOD:00655
S-myristoylated residue
A protein modification that effectively replaces a residue sulfanyl group with an myristoylsulfanyl group.
PubMed:18688235
SMyrRes
A protein modification that effectively replaces a residue hydrocarbyl hydrogen with an methyl group.
CMeRes
PSI-MOD
MOD:00656
C-methylated residue
A protein modification that effectively replaces a residue hydrocarbyl hydrogen with an methyl group.
PubMed:18688235
CMeRes
A protein modification that effectively converts an L-glutamine residue to L-glutamate 5-methyl ester.
15.01
C 1 H 1 N -1 O 1
14.999666
C 6 H 9 N 1 O 3
143.14
143.05824
Q
natural
Unimod:528
uniprot.ptm:PTM-0127
(2S)-2-amino-5-methoxy-5-oxopentanoic acid
(5)-methyl L-hydrogen glutamate
2-aminopentanedioic acid 5-methyl ester
5-methyl L-2-aminoglutarate
5-methyl L-glutamate
L-glutamic acid 5-methyl ester
MOD_RES Glutamate methyl ester (Gln)
O5MeGlu(Gln)
deamidated 5-methyl esterified glutamine
glutamic acid 5-methyl ester
glutamic acid gamma-methyl ester
PSI-MOD
Deamidation followed by a methylation
Methyl+Deamidated
MOD:00657
This is known to be a natural modification of glutamine in prokaryotes.
L-glutamic acid 5-methyl ester (Gln)
A protein modification that effectively converts an L-glutamine residue to L-glutamate 5-methyl ester.
PubMed:16888
PubMed:6300110
RESID:AA0072#GLN
Unimod:528
(2S)-2-amino-5-methoxy-5-oxopentanoic acid
(5)-methyl L-hydrogen glutamate
2-aminopentanedioic acid 5-methyl ester
5-methyl L-2-aminoglutarate
5-methyl L-glutamate
L-glutamic acid 5-methyl ester
MOD_RES Glutamate methyl ester (Gln)
O5MeGlu(Gln)
deamidated 5-methyl esterified glutamine
glutamic acid 5-methyl ester
glutamic acid gamma-methyl ester
Deamidation followed by a methylation
Methyl+Deamidated
A protein modification that effectively converts an L-arginine residue to a methylated arginine, either 5-methylargine, N5-methylarginine, or an omega-N-methylated L-arginine.
R
uniprot.ptm:PTM-0238
MeArg
PSI-MOD
MOD:00658
methylated arginine
A protein modification that effectively converts an L-arginine residue to a methylated arginine, either 5-methylargine, N5-methylarginine, or an omega-N-methylated L-arginine.
PubMed:18688235
MeArg
A protein modification that effectively converts an L-glutamine residue to a methylated glutamine, either 2-methylated glutamine, N5-methylated glutamine, or methyl esterified deamidated glutamine.
Q
natural
MeGln
PSI-MOD
MOD:00659
methylated glutamine
A protein modification that effectively converts an L-glutamine residue to a methylated glutamine, either 2-methylated glutamine, N5-methylated glutamine, or methyl esterified deamidated glutamine.
PubMed:18688235
MeGln
A protein modification that effectively converts an L-cysteine residue to a methylated cysteine, either S-methylcysteine, or cysteine methyl ester.
C
natural
MeCys
PSI-MOD
MOD:00660
methylated cysteine
A protein modification that effectively converts an L-cysteine residue to a methylated cysteine, either S-methylcysteine, or cysteine methyl ester.
PubMed:18688235
MeCys
A protein modification that effectively converts an L-histidine residue to a methylated histidine, such as pros-methylhistidine, or tele-methylhistidine.
H
natural
MeHis
PSI-MOD
MOD:00661
methylated histidine
A protein modification that effectively converts an L-histidine residue to a methylated histidine, such as pros-methylhistidine, or tele-methylhistidine.
PubMed:18688235
MeHis
A protein modification that effectively converts an L-leucine residue to a methylated leucine, either N-methylleucine, or leucine methyl ester.
L
natural
MeLeu
PSI-MOD
MOD:00662
methylated leucine
A protein modification that effectively converts an L-leucine residue to a methylated leucine, either N-methylleucine, or leucine methyl ester.
PubMed:18688235
MeLeu
A protein modification that effectively converts an L-lysine residue to a methylated lysine.
K
natural
uniprot.ptm:PTM-0193
MeLys
PSI-MOD
MOD:00663
methylated lysine
A protein modification that effectively converts an L-lysine residue to a methylated lysine.
PubMed:18688235
MeLys
A protein modification that effectively replaces a residue L-enantiomer (stereoisomer) with a D-enantiomer or with a different diastereomeric isomer.
D-Res
PSI-MOD
MOD:00664
stereoisomerized residue
A protein modification that effectively replaces a residue L-enantiomer (stereoisomer) with a D-enantiomer or with a different diastereomeric isomer.
PubMed:18688235
D-Res
A protein modification that effectively converts an L-alanine residue to a methylated alanine, such as N-methylalanine, N,N-dimethylalanine, or N,N,N-trimethylalanine.
A
natural
MeAla
PSI-MOD
MOD:00665
methylated alanine
A protein modification that effectively converts an L-alanine residue to a methylated alanine, such as N-methylalanine, N,N-dimethylalanine, or N,N,N-trimethylalanine.
PubMed:18688235
MeAla
A protein modification that effectively replaces a hydrogen atom with an octanoyl group.
126.2
C 8 H 14 N 0 O 1
126.10446
X
natural
OctRes
PSI-MOD
MOD:00666
octanoylated residue
A protein modification that effectively replaces a hydrogen atom with an octanoyl group.
PubMed:18688235
OctRes
A protein modification that effectively replaces a hydrogen atom with a decanoyl group.
154.25
C 10 H 18 N 0 O 1
154.13576
X
natural
DecRes
PSI-MOD
MOD:00667
decanoylated residue
A protein modification that effectively replaces a hydrogen atom with a decanoyl group.
PubMed:18688235
DecRes
A protein modification that effectively replaces a residue hydroxyl group with a decanoyloxy group.
154.25
C 10 H 18 N 0 O 1
154.13576
X
natural
Unimod:449
ODecRes
PSI-MOD
Decanoyl
lipid
MOD:00668
O-decanoylated residue
A protein modification that effectively replaces a residue hydroxyl group with a decanoyloxy group.
Unimod:449
ODecRes
Decanoyl
lipid
A protein modification that effectively replaces a residue hydroxyl group with a octanoyloxy group.
126.2
C 8 H 14 N 0 O 1
126.10446
X
natural
Unimod:426
OOctRes
PSI-MOD
Octanoyl
octanoyl
MOD:00669
O-octanoylated residue
A protein modification that effectively replaces a residue hydroxyl group with a octanoyloxy group.
Unimod:426
OOctRes
Octanoyl
octanoyl
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group.
NAcylRes
PSI-MOD
MOD:00670
N-acylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group.
PubMed:18688235
NAcylRes
A protein modification that effectively replaces a residue hydroxyl group with a acyloxy group.
OAcylRes
PSI-MOD
MOD:00671
O-acylated residue
A protein modification that effectively replaces a residue hydroxyl group with a acyloxy group.
PubMed:18688235
OAcylRes
A protein modification that effectively replaces a residue sulfanyl group with an acylsulfanyl group.
SAcylRes
PSI-MOD
MOD:00672
S-acylated residue
A protein modification that effectively replaces a residue sulfanyl group with an acylsulfanyl group.
PubMed:18688235
SAcylRes
A protein modification that effectively converts an L-asparagine residue to a methylated asparagine, such as N4-methyl-L-asparagine, or N4,N4-dimethyl-L-asparagine.
N
natural
MeAsn
PSI-MOD
MOD:00673
methylated asparagine
A protein modification that effectively converts an L-asparagine residue to a methylated asparagine, such as N4-methyl-L-asparagine, or N4,N4-dimethyl-L-asparagine.
PubMed:18688235
MeAsn
A protein modification that effectively replaces a carboxyl group with a carboxamido group.
-0.98
C 0 H 1 N 1 O -1
-0.984016
X
PSI-MOD
MOD:00674
amidated residue
A protein modification that effectively replaces a carboxyl group with a carboxamido group.
PubMed:18688235
A protein modification that effectively either removes neutral hydrogen atoms (proton and electron), or adds oxygen atoms to a residue with or without the removal of hydrogen atoms.
X
OxRes
PSI-MOD
MOD:00675
oxidized residue
A protein modification that effectively either removes neutral hydrogen atoms (proton and electron), or adds oxygen atoms to a residue with or without the removal of hydrogen atoms.
PubMed:18688235
OxRes
A protein modification that effectively adds oxygen atoms to a residue with or without the removal of hydrogen atoms.
X
OxyRes
PSI-MOD
MOD:00676
oxygenated residue
A protein modification that effectively adds oxygen atoms to a residue with or without the removal of hydrogen atoms.
PubMed:18688235
OxyRes
A protein modification that effectively replaces a hydrogen atom with an hydroxyl group.
X
HyRes
Hydroxylation (of delta C of Lysine, beta C of Tryptophan, C3 or C4 of Proline, beta C of Aspartate)
PSI-MOD
MOD:00677
From DeltaMass: Average Mass: 16
hydroxylated residue
A protein modification that effectively replaces a hydrogen atom with an hydroxyl group.
DeltaMass:0
HyRes
Hydroxylation (of delta C of Lysine, beta C of Tryptophan, C3 or C4 of Proline, beta C of Aspartate)
A protein modification that effectively converts an L-proline residue to an hydroxylated L-proline.
P
HyPro
PSI-MOD
MOD:00678
hydroxylated proline
A protein modification that effectively converts an L-proline residue to an hydroxylated L-proline.
PubMed:18688235
HyPro
A protein modification that effectively adds oxygen atoms to a carbon atom of a residue and removes hydrogen atoms.
COxyRes
PSI-MOD
MOD:00679
carbon oxygenated residue
A protein modification that effectively adds oxygen atoms to a carbon atom of a residue and removes hydrogen atoms.
PubMed:18688235
COxyRes
A protein modification that effectively adds oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms.
SOxyRes
PSI-MOD
MOD:00680
sulfur oxygenated residue
A protein modification that effectively adds oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms.
PubMed:18688235
SOxyRes
A protein modification that effectively converts an L-lysine residue to a hydroxylated L-lysine.
K
HyLys
PSI-MOD
MOD:00681
hydroxylated lysine
A protein modification that effectively converts an L-lysine residue to a hydroxylated L-lysine.
PubMed:18688235
HyLys
A protein modification that effectively converts an L-arginine residue to a hydroxylated L-arginine.
R
uniprot.ptm:PTM-0498
HyArg
PSI-MOD
MOD:00682
hydroxylated arginine
A protein modification that effectively converts an L-arginine residue to a hydroxylated L-arginine.
PubMed:18688235
HyArg
A protein modification that effectively removes neutral hydrogen atoms (proton and electron) from a residue.
X
dHRes
PSI-MOD
MOD:00683
dehydrogenated residue
A protein modification that effectively removes neutral hydrogen atoms (proton and electron) from a residue.
PubMed:18688235
dHRes
A protein modification that effectively converts an L-asparagine residue to L-aspartic acid.
0.98
C 0 H -1 N -1 O 1
0.984016
C 4 H 5 N 1 O 3
115.09
115.02694
N
natural
Unimod:7
uniprot.ptm:PTM-0116
(2S)-2-aminobutanedioic acid
2-azanylbutanedioic acid
L-aspartic acid
MOD_RES Deamidated asparagine
aminosuccinic acid
dNAsn
PSI-MOD
MOD:00684
incidental to RESID:AA0059
deamidated L-asparagine
A protein modification that effectively converts an L-asparagine residue to L-aspartic acid.
PubMed:1097438
PubMed:339692
PubMed:4399050
PubMed:5764436
PubMed:6692818
PubMed:8089117
PubMed:9521123
PubMed:9582379
RESID:AA0004#ASN
Unimod:7#N
(2S)-2-aminobutanedioic acid
2-azanylbutanedioic acid
L-aspartic acid
MOD_RES Deamidated asparagine
aminosuccinic acid
dNAsn
A protein modification that effectively converts an L-glutamine residue to L-glutamic acid.
0.98
C 0 H -1 N -1 O 1
0.984016
C 5 H 7 N 1 O 3
129.12
129.04259
Q
natural
Unimod:7
uniprot.ptm:PTM-0117
(2S)-2-aminopentanedioic acid
1-aminopropane-1,3-dicarboxylic acid
2-aminoglutaric acid
2-azanylpentanedioic acid
L-glutamic acid
MOD_RES Deamidated glutamine
alpha-aminoglutaric acid
dNGln
glutaminic acid
PSI-MOD
MOD:00685
deamidated L-glutamine
A protein modification that effectively converts an L-glutamine residue to L-glutamic acid.
PubMed:1881881
PubMed:4565668
PubMed:4922541
PubMed:6692818
PubMed:9192900
PubMed:957425
RESID:AA0006#GLN
Unimod:7#Q
(2S)-2-aminopentanedioic acid
1-aminopropane-1,3-dicarboxylic acid
2-aminoglutaric acid
2-azanylpentanedioic acid
L-glutamic acid
MOD_RES Deamidated glutamine
alpha-aminoglutaric acid
dNGln
glutaminic acid
A protein modification that effectively converts an L-cysteine residue to L-selenocysteine (not known as a natural, post-translational modification process).
46.91
C 0 H 0 N 0 O 0 S -1 Se 1
47.94445
C 3 H 5 N 1 O 1 Se 1
150.05
150.95363
C
artifact
Unimod:162
(2R)-2-amino-3-selanylpropanoic acid
2-azanyl-3-selanylpropanoic acid
3-selenylalanine
L-selenocysteine
NON_STD Selenocysteine
SeCys
Sec(Cys)
selenium cysteine
PSI-MOD
MOD:00686
This entry is for the artifactual formation of L-selenocysteine from cysteine. For encoded L-selenocysteine, use MOD:00031 [JSG].
L-selenocysteine (Cys)
A protein modification that effectively converts an L-cysteine residue to L-selenocysteine (not known as a natural, post-translational modification process).
PubMed:10523135
PubMed:2037562
PubMed:2963330
PubMed:6217842
PubMed:6714945
RESID:AA0022#CYS
Unimod:162#C
(2R)-2-amino-3-selanylpropanoic acid
2-azanyl-3-selanylpropanoic acid
3-selenylalanine
L-selenocysteine
NON_STD Selenocysteine
SeCys
Sec(Cys)
selenium cysteine
A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and either an alkyl C as in lanthionine, or an aryl C as 2'-(S-cysteinyl)-L-histidine.
PSI-MOD
MOD:00687
thioether crosslinked residues
A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and either an alkyl C as in lanthionine, or an aryl C as 2'-(S-cysteinyl)-L-histidine.
PubMed:18688235
A protein modification that crosslinks two residues with an amide bond where either the donor amino or carboxyl is not an alpha group.
PSI-MOD
MOD:00688
isopeptide crosslinked residues
A protein modification that crosslinks two residues with an amide bond where either the donor amino or carboxyl is not an alpha group.
PubMed:18688235
A protein modification that crosslinks two cysteine residues by formation of a disulfide bond.
PSI-MOD
MOD:00689
disulfide crosslinked residues
A protein modification that crosslinks two cysteine residues by formation of a disulfide bond.
PubMed:18688235
A protein modification that crosslinks two residues by formation of an oxazole or thiazole ring.
PSI-MOD
MOD:00690
oxazole/thiazole ring crosslinked residues
A protein modification that crosslinks two residues by formation of an oxazole or thiazole ring.
PubMed:18688235
A protein modification that crosslinks two residues by formation of an 5-imidazolinone ring.
PSI-MOD
MOD:00691
5-imidazolinone ring crosslinked residues
A protein modification that crosslinks two residues by formation of an 5-imidazolinone ring.
PubMed:18688235
A protein crosslink modification that is not chemically categorized.
PSI-MOD
MOD:00692
uncategorized crosslinked residues
A protein crosslink modification that is not chemically categorized.
PubMed:18688235
A protein modification that effectively replaces a hydrogen atom with an carbohydrate-like group through a glycosidic bond.
natural
GlycoRes
PSI-MOD
MOD:00693
glycosylated residue
A protein modification that effectively replaces a hydrogen atom with an carbohydrate-like group through a glycosidic bond.
PubMed:18688235
GlycoRes
A protein modification that effectively substitutes a halogen atom for a hydrogen atom.
HalRes
halogenated residue
PSI-MOD
MOD:00694
halogen containing residue
A protein modification that effectively substitutes a halogen atom for a hydrogen atom.
PubMed:18688235
HalRes
halogenated residue
A protein modification that effectively substitutes a sulfonyl group for the hydrogen atom of a hydroxyl or sulfanyl group.
80.06
O 3 S 1
79.95682
X
natural
Unimod:40
SulfRes
Sulphonation (SO3H) (of PMC group)
PSI-MOD
O-Sulfonation
Sulfo
MOD:00695
From DeltaMass: Average Mass: 80.
sulfated residue
A protein modification that effectively substitutes a sulfonyl group for the hydrogen atom of a hydroxyl or sulfanyl group.
DeltaMass:0
PubMed:14752058
Unimod:40
SulfRes
Sulphonation (SO3H) (of PMC group)
O-Sulfonation
Sulfo
A protein modification that effectively replaces a hydrogen atom with a phosphono group (H2PO3 or 'phosphate').
79.98
H 1 O 3 P 1
79.96633
X
Unimod:21
PhosRes
Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine)
PSI-MOD
Phospho
Phosphorylation
MOD:00696
From DeltaMass: Average Mass: 80.
phosphorylated residue
A protein modification that effectively replaces a hydrogen atom with a phosphono group (H2PO3 or 'phosphate').
DeltaMass:0
Unimod:21
PhosRes
Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine)
Phospho
Phosphorylation
A protein modification that effectively results from forming an adduct with a compound containing a flavin group.
X
natural
FlavRes
PSI-MOD
FAD
Flavin adenine dinucleotide
MOD:00697
flavin modified residue
FlavRes
FAD
Flavin adenine dinucleotide
A protein modification that effectively substitutes a metal atom or a metal cluster for hydrogen atoms, or coordinates a metal ion.
MetalRes
PSI-MOD
MOD:00698
metal or metal cluster containing modified residue
A protein modification that effectively substitutes a metal atom or a metal cluster for hydrogen atoms, or coordinates a metal ion.
PubMed:18688235
MetalRes
A protein modification that effectively results from forming an adduct with a compound containing a porphyrin group.
PorphRes
PSI-MOD
MOD:00699
porphyrin modified residue
A protein modification that effectively results from forming an adduct with a compound containing a porphyrin group.
PubMed:18688235
PorphRes
A protein modification that effectively results from forming an adduct with a compound containing a tetrapyrrole group.
TetrapyrRes
PSI-MOD
MOD:00700
tetrapyrrole modified residue
A protein modification that effectively results from forming an adduct with a compound containing a tetrapyrrole group.
PubMed:18688235
TetrapyrRes
A protein modification that effectively results from forming an adduct with a compound containing a nucleotide or a polynucleotide through formation of either a phosphodiester bond, a phosphoramide ester bond, or a glycosidic bond.
NucRes
PSI-MOD
MOD:00701
nucleotide or nucleic acid modified residue
A protein modification that effectively results from forming an adduct with a compound containing a nucleotide or a polynucleotide through formation of either a phosphodiester bond, a phosphoramide ester bond, or a glycosidic bond.
PubMed:18688235
NucRes
A protein modification that effectively substitutes atoms of particular common isotopes with atoms or groups containing isotopes that are not the most common.
IsoTagRes
SILAC
PSI-MOD
MOD:00702
In SILAC (stable isotope labelling of amino acids in cell culture), the label may be introduced either through labeling of an incorporated residue or labeling of the substrates in a metabolic modification. For isotope labeling introduced through a modification reagent see MOD:01426.
isotope labeled residue
A protein modification that effectively substitutes atoms of particular common isotopes with atoms or groups containing isotopes that are not the most common.
PubMed:18688235
IsoTagRes
SILAC
A protein modification that effectively replaces a hydrogen atom with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20) group.
IpRes
PSI-MOD
MOD:00703
isoprenylated residue
A protein modification that effectively replaces a hydrogen atom with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20) group.
PubMed:18688235
IpRes
A protein modification that effectively forms a double bond by removing a molecule of water from a residue.
-18.02
C 0 H -2 N 0 O -1
-18.010565
X
natural
Unimod:23
PSI-MOD
Dehydrated
Dehydration
MOD:00704
dehydrated residue
A protein modification that effectively forms a double bond by removing a molecule of water from a residue.
DeltaMass:0
Unimod:23
Dehydrated
Dehydration
A protein modification that effectively converts an L-valine residue to D-valine.
0.0
C 0 H 0 N 0 O 0
0.0
C 5 H 9 N 1 O 1
99.13
99.06841
V
natural
uniprot.ptm:PTM-0124
(R)-2-amino-3-methylbutanoic acid
D-Val
D-valine
MOD_RES D-valine
alpha-amino-beta-methylbutyric acid
alpha-aminoisovaleric acid
PSI-MOD
MOD:00705
D-valine
A protein modification that effectively converts an L-valine residue to D-valine.
ChEBI:30016
PubMed:15853325
RESID:AA0200
(R)-2-amino-3-methylbutanoic acid
D-Val
D-valine
MOD_RES D-valine
alpha-amino-beta-methylbutyric acid
alpha-aminoisovaleric acid
A protein modification that effectively converts L-tyrosine to 2,3-didehydrotyrosine.
-2.02
C 0 H -2 N 0 O 0
-2.01565
C 9 H 7 N 1 O 2
161.16
161.04768
Y
natural
Unimod:401
uniprot.ptm:PTM-0008
MOD_RES 2,3-didehydrotyrosine
dHTyr
PSI-MOD
MOD:00706
dehydrogenated tyrosine
A protein modification that effectively converts L-tyrosine to 2,3-didehydrotyrosine.
Unimod:401#Y
MOD_RES 2,3-didehydrotyrosine
dHTyr
a protein modification that effectively converts an L-tyrosine residue to a multihydroxylated L-phenylalanine
Y
natural
HyTyr
PSI-MOD
MOD:00707
hydroxylated tyrosine
a protein modification that effectively converts an L-tyrosine residue to a multihydroxylated L-phenylalanine
PubMed:18688235
HyTyr
A protein modification that effectively adds oxygen atoms to a sulfur atom of L-cysteine residue without removing hydrogen atoms.
C
artifact
SOxyCys
PSI-MOD
MOD:00708
sulfur oxygenated L-cysteine
A protein modification that effectively adds oxygen atoms to a sulfur atom of L-cysteine residue without removing hydrogen atoms.
PubMed:18688235
SOxyCys
A protein modification that effectively adds oxygen atoms to a sulfur atom of L-methionine residue without removing hydrogen atoms.
M
artifact
SOxyMet
PSI-MOD
MOD:00709
sulfur oxygenated L-methionine
A protein modification that effectively adds oxygen atoms to a sulfur atom of L-methionine residue without removing hydrogen atoms.
PubMed:18688235
SOxyMet
A protein modification that effectively adds a proton and replaces two hydrogen atoms with two methyl groups.
Me2+Res
PSI-MOD
MOD:00710
For N-terminal proline residues, dimethylation can effectively only be accomplished with a protonated imino group. This process accounts for both protonation and dimethylation. The alternative Me2Res process accounts only for dimethylation and not protonation.
protonated-dimethylated residue
A protein modification that effectively adds a proton and replaces two hydrogen atoms with two methyl groups.
PubMed:18688235
Me2+Res
A protein modification that effectively replaces three hydrogen atoms with three methyl groups, after a proton has been added to form an aminium group.
43.09
C 3 H 7 N 0 O 0 S 0
43.054226
1+
X
natural
Me3+Res
PSI-MOD
MOD:00711
For amino acids residues, amine trimethylation can effectively only be accomplished with a protonated primary amino group. This process accounts for both protonation and trimethylation. The alternative Me3Res process accounts only for trimethylation and not protonation.
trimethylated protonated-residue
A protein modification that effectively replaces three hydrogen atoms with three methyl groups, after a proton has been added to form an aminium group.
PubMed:18688235
Me3+Res
A protein modification that effectively converts an L-proline residue to a methylated proline, such as N,N-dimethylproline.
P
natural
MePro
PSI-MOD
MOD:00712
methylated proline
A protein modification that effectively converts an L-proline residue to a methylated proline, such as N,N-dimethylproline.
PubMed:18688235
MePro
A protein modification that effectively converts an L-glutamic acid residue to a methylated glutamic acid, such as L-glutamate 5-methyl ester.
X
natural
MeGlu
PSI-MOD
MOD:00713
methylated glutamic acid
A protein modification that effectively converts an L-glutamic acid residue to a methylated glutamic acid, such as L-glutamate 5-methyl ester.
PubMed:18688235
MeGlu
A protein modification that effectively converts a glycine residue to a methylated glycine, such as N-methylglycine.
G
natural
MeGly
PSI-MOD
MOD:00714
methylated glycine
A protein modification that effectively converts a glycine residue to a methylated glycine, such as N-methylglycine.
PubMed:18688235
MeGly
A protein modification that effectively converts an L-isoleucine residue to a methylated isoleucine residue, such as N-methyl-L-isoleucine.
I
natural
MeIle
PSI-MOD
MOD:00715
methylated isoleucine
A protein modification that effectively converts an L-isoleucine residue to a methylated isoleucine residue, such as N-methyl-L-isoleucine.
PubMed:18688235
MeIle
A protein modification that effectively converts an L-methionine residue to a methylated methionine, such as N-methyl-L-methionine.
M
natural
N-term
MeMet
PSI-MOD
MOD:00716
methylated methionine
A protein modification that effectively converts an L-methionine residue to a methylated methionine, such as N-methyl-L-methionine.
PubMed:18688235
MeMet
A protein modification that effectively converts an L-phenylalanine residue to a methylated phenylalanine, such as N-methyl-L-phenylalanine.
F
natural
MePhe
PSI-MOD
MOD:00717
methylated phenylalanine
A protein modification that effectively converts an L-phenylalanine residue to a methylated phenylalanine, such as N-methyl-L-phenylalanine.
PubMed:18688235
MePhe
A protein modification that effectively converts an L-tyrosine residue to a methylated tyrosine, such as N-methyl-L-tyrosine.
Y
natural
N-term
MeTyr
PSI-MOD
MOD:00718
methylated tyrosine
A protein modification that effectively converts an L-tyrosine residue to a methylated tyrosine, such as N-methyl-L-tyrosine.
PubMed:18688235
MeTyr
A protein modification that oxygenates an L-methionine residue to one of the diastereomeric L-methionine sulfoxide residues.
16.0
C 0 H 0 N 0 O 1 S 0
15.994915
C 5 H 9 N 1 O 2 S 1
147.19
147.0354
M
artifact
Unimod:35
uniprot.ptm:PTM-0469
(2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid
L-methionine (R)-S-oxide
L-methionine (R)-sulfoxide
L-methionine S-oxide
L-methionine sulfoxide
MOD_RES Methionine sulfoxide
MetO
Methionyl Sulfoxide
oxym
PSI-MOD
Oxidation
MOD:00719
From DeltaMass: Average Mass: 147 Formula:C5H9O1N2S Monoisotopic Mass Change:147.035 Average Mass Change:147.195 (formula incorrect, N and O reversed) References:PE Sciex.
L-methionine sulfoxide
A protein modification that oxygenates an L-methionine residue to one of the diastereomeric L-methionine sulfoxide residues.
DeltaMass:177
OMSSA:1
PubMed:21406390
PubMed:22116028
RESID:AA0581
Unimod:35#M
(2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid
L-methionine (R)-S-oxide
L-methionine (R)-sulfoxide
L-methionine S-oxide
L-methionine sulfoxide
MOD_RES Methionine sulfoxide
MetO
Methionyl Sulfoxide
oxym
Oxidation
A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide R-diastereomer.
16.0
C 0 H 0 N 0 O 1 S 0
15.994915
C 5 H 9 N 1 O 2 S 1
147.19
147.0354
M
natural
uniprot.ptm:PTM-0480
(2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid
L-methionine (R)-S-oxide
L-methionine (R)-sulfoxide
MOD_RES Methionine (R)-sulfoxide
R-MetO
PSI-MOD
MOD:00720
L-methionine (R)-sulfoxide
A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide R-diastereomer.
ChEBI:45764
PubMed:21406390
PubMed:22116028
PubMed:23911929
RESID:AA0581
(2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid
L-methionine (R)-S-oxide
L-methionine (R)-sulfoxide
MOD_RES Methionine (R)-sulfoxide
R-MetO
A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide S-diastereomer.
16.0
C 0 H 0 N 0 O 1 S 0
15.994915
C 5 H 9 N 1 O 2 S 1
147.19
147.0354
M
artifact
uniprot.ptm:PTM-0481
MOD_RES Methionine (S)-sulfoxide
S-MetO
PSI-MOD
MOD:00721
L-methionine (S)-sulfoxide
A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide S-diastereomer.
PubMed:18688235
MOD_RES Methionine (S)-sulfoxide
S-MetO
A protein modification that effectively replaces one hydrogen atom of an L-glutamine residue with one methyl group.
14.03
C 1 H 2 N 0 O 0
14.01565
C 6 H 10 N 2 O 2
142.16
142.07423
Q
natural
Unimod:34
Me1Gln
methylq
PSI-MOD
MOD:00722
monomethylated L-glutamine
A protein modification that effectively replaces one hydrogen atom of an L-glutamine residue with one methyl group.
OMSSA:14
Unimod:34#Q
Me1Gln
methylq
A protein modification that effectively converts an L-lysine residue to either N2-acetyl-L-lysine, or N6-acetyl-L-lysine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 8 H 15 N 2 O 2
171.22
171.11336
K
natural
NAcLys
PSI-MOD
MOD:00723
N-acetylated L-lysine
A protein modification that effectively converts an L-lysine residue to either N2-acetyl-L-lysine, or N6-acetyl-L-lysine.
PubMed:18688235
NAcLys
A protein modification that effectively replaces one hydrogen atom on a nitrogen of an L-histidine residue with one methyl group.
14.03
C 1 H 2 N 0 O 0
14.01565
C 7 H 9 N 3 O 1
151.17
151.07455
H
natural
Unimod:34
NMeHis
methylh
PSI-MOD
Methyl
MOD:00724
N-methylated L-histidine
A protein modification that effectively replaces one hydrogen atom on a nitrogen of an L-histidine residue with one methyl group.
OMSSA:74
Unimod:34#H
NMeHis
methylh
Methyl
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group linked through a glycosidic bond.
PSI-MOD
MOD:00725
complex glycosylation
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a carbohydrate-like group linked through a glycosidic bond.
PubMed:18688235
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a glucose group through a glycosidic bond.
MOD:00433
X
natural
Glc
PSI-MOD
MOD:00726
glucosylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a glucose group through a glycosidic bond.
PubMed:18688235
Glc
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a mannose group through a glycosidic bond,
X
natural
Man
PSI-MOD
MOD:00727
mannosylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a mannose group through a glycosidic bond,
PubMed:18688235
Man
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a galactose group through a glycosidic bond.
X
natural
Gal
PSI-MOD
MOD:00728
galactosylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a galactose group through a glycosidic bond.
PubMed:18688235
Gal
a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a pentose sugar group through a glycosidic bond
132.12
C 5 H 8 O 4
132.04225
X
natural
Pent
Pentoses (Ara, Rib, Xyl)
Pentosyl
PSI-MOD
MOD:00729
for Pentoses DeltaMass gives mass 132, for Pentosyl DeltaMass gives formula C 6 H 10 N4 with mass 146
pentosylated residue
a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a pentose sugar group through a glycosidic bond
DeltaMass:172
Pent
Pentoses (Ara, Rib, Xyl)
Pentosyl
a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a arabinose sugar group through a glycosidic bond
132.12
C 5 H 8 O 4
132.04225
X
natural
Ara
PSI-MOD
MOD:00730
arabinosylated residue
a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a arabinose sugar group through a glycosidic bond
PubMed:18688235
Ara
a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a ribose sugar group through a glycosidic bond
132.12
C 5 H 8 O 4
132.04225
X
natural
Rib
PSI-MOD
MOD:00731
ribosylated residue
a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a ribose sugar group through a glycosidic bond
PubMed:18688235
Rib
a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a xylose sugar group through a glycosidic bond
132.12
C 5 H 8 O 4
132.04225
X
natural
Xyl
PSI-MOD
MOD:00732
xylosylated residue
a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a xylose sugar group through a glycosidic bond
PubMed:18688235
Xyl
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylglucosamine group through a glycosidic bond.
203.19
C 8 H 13 N 1 O 5
203.07938
X
GlcNAc
PSI-MOD
MOD:00733
N-acetylaminoglucosylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylglucosamine group through a glycosidic bond.
PubMed:18688235
GlcNAc
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylgalactosamine group through a glycosidic bond.
203.19
C 8 H 13 N 1 O 5
203.07938
X
GalNAc
N-acetylhexosamines (GalNAc, GlcNAc)
PSI-MOD
MOD:00734
From DeltaMass: Average Mass: 203 Formula:C8H13O5N1 Monoisotopic Mass Change:203.079 Average Mass Change:203.196 References:PE Sciex
N-acetylaminogalactosylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylgalactosamine group through a glycosidic bond.
DeltaMass:247
GalNAc
N-acetylhexosamines (GalNAc, GlcNAc)
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexosuronic acid group through a glycosidic bond.
176.12
C 6 H 8 O 6
176.03209
X
natural
HexA
PSI-MOD
MOD:00735
hexosuronylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexosuronic acid group through a glycosidic bond.
PubMed:18688235
HexA
a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a deoxyhexose group through a glycosidic bond
146.14
C 6 H 10 O 4
146.0579
X
natural
GNO:G02438LG
Deoxyhexoses (Fuc, Rha)
dHex
PSI-MOD
MOD:00736
From DeltaMass: Average Mass: 146
deoxyhexosylated residue
a protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a deoxyhexose group through a glycosidic bond
DeltaMass:0
Deoxyhexoses (Fuc, Rha)
dHex
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylneuraminic acid (sialic acid) group through a glycosidic bond.
291.26
C 11 H 17 N 1 O 8
291.09543
X
natural
GNO:G76685HR
N-acetylneuraminic acid (Sialic acid, NeuAc, NANA, SA)
NeuNAc
PSI-MOD
MOD:00737
From DeltaMass: Average Mass: 291
N-acetylneuraminylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with an N-acetylneuraminic acid (sialic acid) group through a glycosidic bond.
DeltaMass:0
N-acetylneuraminic acid (Sialic acid, NeuAc, NANA, SA)
NeuNAc
A protein modification that effectively substitutes an iron atom or a cluster containing iron for hydrogen atoms, or that coordinates an iron ion.
FeRes
PSI-MOD
MOD:00738
iron containing modified residue
A protein modification that effectively substitutes an iron atom or a cluster containing iron for hydrogen atoms, or that coordinates an iron ion.
PubMed:18688235
FeRes
A protein modification that effectively substitutes a cluster of iron and sulfur atoms for hydrogen atoms.
FeSRes
PSI-MOD
MOD:00739
iron-sulfur cluster containing modification
A protein modification that effectively substitutes a cluster of iron and sulfur atoms for hydrogen atoms.
PubMed:18688235
FeSRes
A protein modification that effectively substitutes a manganese atom or a cluster containing manganese for hydrogen atoms, or that coordinates a manganese ion.
MnRes
PSI-MOD
MOD:00740
manganese containing modified residue
A protein modification that effectively substitutes a manganese atom or a cluster containing manganese for hydrogen atoms, or that coordinates a manganese ion.
PubMed:18688235
MnRes
A protein modification that effectively substitutes a nickel atom or a cluster containing nickel for hydrogen atoms, or that coordinates a nickel ion.
NiRes
PSI-MOD
MOD:00741
nickel containing modified residue
A protein modification that effectively substitutes a nickel atom or a cluster containing nickel for hydrogen atoms, or that coordinates a nickel ion.
PubMed:18688235
NiRes
A protein modification that effectively substitutes a copper atom or a cluster containing copper for hydrogen atoms, or that coordinates a copper ion.
CuRes
PSI-MOD
MOD:00742
copper containing modified residue
A protein modification that effectively substitutes a copper atom or a cluster containing copper for hydrogen atoms, or that coordinates a copper ion.
PubMed:18688235
CuRes
A protein modification that effectively substitutes a molybdenum atom or a cluster containing molybdenum for hydrogen atoms, or that coordinates a molybdenum ion.
MoRes
PSI-MOD
MOD:00743
molybdenum containing modified residue
A protein modification that effectively substitutes a molybdenum atom or a cluster containing molybdenum for hydrogen atoms, or that coordinates a molybdenum ion.
PubMed:18688235
MoRes
A protein modification containing a molybdenum atom in a pterin ring system.
MoPterRes
PSI-MOD
MOD:00744
molybdenum pterin containing modification
A protein modification containing a molybdenum atom in a pterin ring system.
PubMed:18688235
MoPterRes
A protein modification that effectively substitutes a selenium atom or a cluster containing selenium for hydrogen atoms.
SeRes
PSI-MOD
MOD:00745
selenium containing residue
A protein modification that effectively substitutes a selenium atom or a cluster containing selenium for hydrogen atoms.
PubMed:18688235
SeRes
A protein modification that effectively substitutes a tungsten atom or a cluster containing tungsten for hydrogen atoms, or that coordinates a tungsten ion.
WRes
PSI-MOD
MOD:00746
tungsten containing modified residue
A protein modification that effectively substitutes a tungsten atom or a cluster containing tungsten for hydrogen atoms, or that coordinates a tungsten ion.
PubMed:18688235
WRes
A protein modification that effectively substitutes a sodium atom for a hydrogen atom.
NaRes
PSI-MOD
MOD:00747
sodium containing modified residue
A protein modification that effectively substitutes a sodium atom for a hydrogen atom.
PubMed:18688235
NaRes
A protein modification that effectively results from forming an adduct with a compound containing a pterin group.
PterRes
PSI-MOD
MOD:00748
pterin modified residue
A protein modification that effectively results from forming an adduct with a compound containing a pterin group.
PubMed:18688235
PterRes
A protein modification that effectively substitutes a sulfur atom for an oxygen atom.
S(O)Res
PSI-MOD
MOD:00749
sulfur substitution for oxygen
A protein modification that effectively substitutes a sulfur atom for an oxygen atom.
PubMed:18688235
S(O)Res
A protein modification that effectively crosslinks an amino acid residue and the 3'- or 5'-end of DNA through a phosphodiester bond.
DNARes
PSI-MOD
MOD:00750
deoxyribonucleic acid linked residue
A protein modification that effectively crosslinks an amino acid residue and the 3'- or 5'-end of DNA through a phosphodiester bond.
PubMed:18688235
DNARes
a protein modification
RNARes
PSI-MOD
MOD:00751
ribonucleic acid linked residue
a protein modification
PubMed:18688235
RNARes
A protein modification that effectively results from forming an adduct with one ADP-ribose through formation of a glycosidic bond.
541.3
C 15 H 21 N 5 O 13 P 2
541.0611
X
natural
ADP-rybosylation (from NAD)
ADPRib1Res
PSI-MOD
MOD:00752
From DeltaMass: Average Mass: 541.
monoadenosine diphosphoribosyl (ADP-ribosyl) modified residue
A protein modification that effectively results from forming an adduct with one ADP-ribose through formation of a glycosidic bond.
DeltaMass:0
ADP-rybosylation (from NAD)
ADPRib1Res
A protein modification that effectively substitutes a chlorine atom for a hydrogen atom.
X
ClRes
PSI-MOD
MOD:00753
chlorinated residue
A protein modification that effectively substitutes a chlorine atom for a hydrogen atom.
PubMed:18688235
ClRes
A protein modification that effectively substitutes a bromine atom for a hydrogen atom.
X
BrRes
PSI-MOD
MOD:00754
brominated residue
A protein modification that effectively substitutes a bromine atom for a hydrogen atom.
PubMed:18688235
BrRes
A protein modification that effectively substitutes an iodine atom of a residue for a hydrogen atom.
X
IRes
PSI-MOD
MOD:00755
iodinated residue
A protein modification that effectively substitutes an iodine atom of a residue for a hydrogen atom.
PubMed:18688235
IRes
A protein modification that effectively converts an L-valine residue to 4-hydroxy-D-valine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 5 H 9 N 1 O 2
115.13
115.06333
V
natural
uniprot.ptm:PTM-0111
(2R,3Xi)-2-amino-4-hydroxy-3-methylbutanoic acid
4-hydroxy-D-valine
D-4HyVal
D-gamma-hydroxyvaline
MOD_RES D-4-hydroxyvaline
PSI-MOD
MOD:00756
4-hydroxy-D-valine
A protein modification that effectively converts an L-valine residue to 4-hydroxy-D-valine.
PubMed:15853325
RESID:AA0388
(2R,3Xi)-2-amino-4-hydroxy-3-methylbutanoic acid
4-hydroxy-D-valine
D-4HyVal
D-gamma-hydroxyvaline
MOD_RES D-4-hydroxyvaline
A protein modification that effectively converts an L-proline residue to O4-galactosyl-L-hydroxyproline.
178.14
C 6 H 10 N 0 O 6
178.04774
C 11 H 17 N 1 O 7
275.26
275.1005
P
natural
uniprot.ptm:PTM-0558
(2S,4R)-4-(beta-D-galactopyranosyloxy)pyrrolidine-2-carboxylic acid
4-(beta-D-galactopyranosyloxy)proline
4-(galactosyloxy)proline
CARBOHYD O-linked (Gal) hydroxyproline
O4-galactosyl-L-hydroxyproline
O4-glycosyl-hydroxyproline
beta-galactopyranosyl-4-hydroxyproline
PSI-MOD
MOD:00757
secondary to RESID:AA0030
O4-galactosyl-L-hydroxyproline
A protein modification that effectively converts an L-proline residue to O4-galactosyl-L-hydroxyproline.
RESID:AA0389
(2S,4R)-4-(beta-D-galactopyranosyloxy)pyrrolidine-2-carboxylic acid
4-(beta-D-galactopyranosyloxy)proline
4-(galactosyloxy)proline
CARBOHYD O-linked (Gal) hydroxyproline
O4-galactosyl-L-hydroxyproline
O4-glycosyl-hydroxyproline
beta-galactopyranosyl-4-hydroxyproline
A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)glucosyl-L-hydroxyproline.
219.19
C 8 H 13 N 1 O 6
219.07428
C 13 H 20 N 2 O 7
316.31
316.12704
P
natural
uniprot.ptm:PTM-0578
(2S,4R)-4-[2-acetamido-2-deoxy-alpha-D-glucopyranosyloxy]pyrrolidine-2-carboxylic acid
4-(N-acetylglucosaminyloxy)proline
4-[(2-N-acetylamino)-alpha-D-glucopyranosyl]oxyproline
CARBOHYD O-linked (GlcNAc) hydroxyproline
O4-(N-acetylamino)glucosyl-L-hydroxyproline
O4-glycosyl-hydroxyproline
O4GlcNAcHyPro
alpha-2-(N-acetylamino)glucopyranosyl-4-hydroxyproline
PSI-MOD
HexNAc
MOD:00758
secondary to RESID:AA0030
O4-(N-acetylamino)glucosyl-L-hydroxyproline
A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)glucosyl-L-hydroxyproline.
PubMed:15238247
PubMed:9660787
RESID:AA0390
(2S,4R)-4-[2-acetamido-2-deoxy-alpha-D-glucopyranosyloxy]pyrrolidine-2-carboxylic acid
4-(N-acetylglucosaminyloxy)proline
4-[(2-N-acetylamino)-alpha-D-glucopyranosyl]oxyproline
CARBOHYD O-linked (GlcNAc) hydroxyproline
O4-(N-acetylamino)glucosyl-L-hydroxyproline
O4-glycosyl-hydroxyproline
O4GlcNAcHyPro
alpha-2-(N-acetylamino)glucopyranosyl-4-hydroxyproline
HexNAc
modification from Unimod N-linked glycosylation
1607.48
C 62 H 102 N 4 O 44
1606.5867
C 66 H 108 N 6 O 46
1721.59
1720.6296
N
natural
GNO:G59937CP
Unimod:307
PSI-MOD
Fucosylated biantennary (-1 galactose)
dHex(1)Hex(4)HexNAc(4)
MOD:00759
fucosylated biantennary (-1 galactose) N4-glycosylated asparagine
modification from Unimod N-linked glycosylation
Unimod:307
Fucosylated biantennary (-1 galactose)
dHex(1)Hex(4)HexNAc(4)
modification from Unimod N-linked glycosylation - missing ref
1623.48
C 62 H 102 N 4 O 45
1622.5817
C 66 H 108 N 6 O 47
1737.59
1736.6245
N
natural
GNO:G10486CT
Unimod:311
PSI-MOD
Biantennary
Hex(5)HexNAc(4)
MOD:00760
biantennary N4-glycosylated asparagine
modification from Unimod N-linked glycosylation - missing ref
Unimod:311
Biantennary
Hex(5)HexNAc(4)
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with one hexose sugar group through a glycosidic bond.
162.14
C 6 H 10 O 5
162.05283
X
natural
GNO:G81399MY
Hex1
PSI-MOD
MOD:00761
monohexosylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with one hexose sugar group through a glycosidic bond.
PubMed:18688235
Hex1
modification from Unimod N-linked glycosylation - missing ref
1299.2
C 50 H 82 N 4 O 35
1298.476
C 54 H 88 N 6 O 37
1413.3
1412.5189
N
natural
GNO:G35029YA
Unimod:309
PSI-MOD
Biantennary (-2 galactose)
Hex(3)HexNAc(4)
MOD:00762
biantennary (-2 galactose) N4-glycosylated asparagine
modification from Unimod N-linked glycosylation - missing ref
Unimod:309
Biantennary (-2 galactose)
Hex(3)HexNAc(4)
modification from Unimod N-linked glycosylation - missing ref
1461.34
C 56 H 92 N 4 O 40
1460.5288
C 60 H 98 N 6 O 42
1575.44
1574.5717
N
natural
GNO:G72787SB
Unimod:310
PSI-MOD
Biantennary (-1 galactose)
Hex(4)HexNAc(4)
MOD:00763
biantennary (-1 galactose) N4-glycosylated asparagine
modification from Unimod N-linked glycosylation - missing ref
Unimod:310
Biantennary (-1 galactose)
Hex(4)HexNAc(4)
A protein modification that effectively results from forming an adduct with a carbohydrate-like group either through enzymatic formation of a glycosidic bond, or through non-enzymatic glycation formation of a Schiff-base or an Amadori ketosamine residue adduct.
PSI-MOD
MOD:00764
glycoconjugated residue
A protein modification that effectively results from forming an adduct with a carbohydrate-like group either through enzymatic formation of a glycosidic bond, or through non-enzymatic glycation formation of a Schiff-base or an Amadori ketosamine residue adduct.
PubMed:18688235
PubMed:3743566
A protein modification that effectively converts an L-cysteine residue to S-(L-cysteinyl)-L-cysteine, forming a disulfide bond with free cysteine.
119.14
C 3 H 5 N 1 O 2 S 1
119.0041
C 6 H 10 N 2 O 3 S 2
222.28
222.01329
C
natural
Unimod:312
uniprot.ptm:PTM-0415
(2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid)
3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid)
3,3'-dithiobis(2-aminopropanoic acid)
3,3'-dithiobisalanine
3,3'-dithiodialanine
Cysteinylation
L-cystine
MOD_RES S-cysteinyl cysteine
S-cystenyl cystenyl
SCysCys
beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide
beta,beta'-dithiodialanine
bis(alpha-aminopropionic acid)-beta-disulfide
bis(beta-amino-beta-carboxyethyl)disulfide
dicysteine
PSI-MOD
2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid
MOD:00765
This entry is for formation of a disulfide bond between a peptide cysteine and a free cysteine. For the cystine cross-link, see MOD:00234. From DeltaMass: (name misspelled and formula incorrect, N and O reversed) Formula: C6H10O2N3S2 Monoisotopic Mass Change: 222.013 Average Mass Change: 222.283
cysteinylation (disulfide with free L-cysteine)
A protein modification that effectively converts an L-cysteine residue to S-(L-cysteinyl)-L-cysteine, forming a disulfide bond with free cysteine.
DeltaMass:260
PubMed:1988019
PubMed:2001356
PubMed:2076469
PubMed:3083866
PubMed:366603
PubMed:7918467
PubMed:8344916
RESID:AA0025#CYS1
Unimod:312
(2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid)
3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid)
3,3'-dithiobis(2-aminopropanoic acid)
3,3'-dithiobisalanine
3,3'-dithiodialanine
Cysteinylation
L-cystine
MOD_RES S-cysteinyl cysteine
S-cystenyl cystenyl
SCysCys
beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide
beta,beta'-dithiodialanine
bis(alpha-aminopropionic acid)-beta-disulfide
bis(beta-amino-beta-carboxyethyl)disulfide
dicysteine
2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid
modification from Unimod Post-translational - C-terminal loss of lysine OBSOLETE because the idenical to MOD:01642. Remap to MOD:01642
MOD:01642
-128.18
C -6 H -12 N -2 O -1
-128.09496
X
C-term
Unimod:313
PSI-MOD
Loss of C-terminal K from Heavy Chain of MAb
Lys-loss
MOD:00766
C terminal -K from HC of MAb
true
modification from Unimod Post-translational - C-terminal loss of lysine OBSOLETE because the idenical to MOD:01642. Remap to MOD:01642
PubMed:16078144
Unimod:313
Loss of C-terminal K from Heavy Chain of MAb
Lys-loss
A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and a protein amino group to form a Schiff-base or an Amadori ketosamine residue adduct.
artifact
PSI-MOD
MOD:00767
glycated residue
A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and a protein amino group to form a Schiff-base or an Amadori ketosamine residue adduct.
PubMed:18688235
Oxidation of methionine to methionine sulfone with neutral loss of CH3SO2H.
-80.1
C -1 H -4 N 0 O -2 S -1
-79.9932
C 4 H 5 N 1 O 1 S 0
83.09
83.03712
M
artifact
PSI-MOD
MOD:00768
Originally created from Unimod:508 that was later deleted.
methionine oxidation with neutral loss of 80 Da
Oxidation of methionine to methionine sulfone with neutral loss of CH3SO2H.
PubMed:18688235
PubMed:9004526
Natural or modified residues with a mass of 71.0-71.1 Da.
PSI-MOD
MOD:00769
residues isobaric at 71.0-71.1 Da
Natural or modified residues with a mass of 71.0-71.1 Da.
PubMed:18688235
Natural or modified residues that are isobaric at a resolution below 0.01 Da.
PSI-MOD
MOD:00770
residues isobaric at a resolution below 0.01 Da
Natural or modified residues that are isobaric at a resolution below 0.01 Da.
PubMed:18688235
Natural or modified residues with a mass of 166.98-167.00 Da.
PSI-MOD
MOD:00771
residues isobaric at 166.98-167.00 Da
Natural or modified residues with a mass of 166.98-167.00 Da.
PubMed:18688235
A protein modification that effectively substitutes a vanadium atom or a cluster containing vanadium for hydrogen atoms, or that coordinates a vanadium ion.
VRes
PSI-MOD
MOD:00772
vanadium containing modified residue
A protein modification that effectively substitutes a vanadium atom or a cluster containing vanadium for hydrogen atoms, or that coordinates a vanadium ion.
PubMed:18688235
VRes
Natural or modified residues with a mass of 181.00-181.02 Da.
PSI-MOD
MOD:00773
residues isobaric at 181.00-181.02 Da
Natural or modified residues with a mass of 181.00-181.02 Da.
PubMed:18688235
Natural or modified residues with a mass of 243.02-243.03 Da.
PSI-MOD
MOD:00774
residues isobaric at 243.02-243.03 Da
Natural or modified residues with a mass of 243.02-243.03 Da.
PubMed:18688235
An artifactual protein modification that converts an L-histidine residue to L-asparagine by oxidative degradation.
-23.04
C -2 H -1 N -1 O 1
-23.015984
C 4 H 6 N 2 O 2
114.1
114.04293
H
artifact
Unimod:348
his2asnh
PSI-MOD
His->Asn
histidine oxidation to aspargine
MOD:00775
L-asparagine (His)
An artifactual protein modification that converts an L-histidine residue to L-asparagine by oxidative degradation.
OMSSA:54
PubMed:9252331
Unimod:348
his2asnh
His->Asn
histidine oxidation to aspargine
An artifactual protein modification that converts an L-histidine residue to L-aspartic acid by oxidative degradation.
-22.05
C -2 H -2 N -2 O 2
-22.03197
C 4 H 5 N 1 O 3
115.09
115.02694
H
artifact
Unimod:349
his2asph
PSI-MOD
His->Asp
histidine oxidation to aspartic acid
MOD:00776
From OMSSA: desc="oxidation of H to D" monomass= -23.015984 (this is the same mass difference as OMSSA:54, his2asnh) [JSG].
L-aspartic acid (His)
An artifactual protein modification that converts an L-histidine residue to L-aspartic acid by oxidative degradation.
OMSSA:55
PubMed:9252331
Unimod:349
his2asph
His->Asp
histidine oxidation to aspartic acid
Natural or modified residues with a mass of 182.96-182.98 Da.
PSI-MOD
MOD:00777
residues isobaric at 182.96-182.98 Da
Natural or modified residues with a mass of 182.96-182.98 Da.
PubMed:18688235
Natural or modified residues with a mass of 182.9-183.0 Da.
PSI-MOD
MOD:00778
residues isobaric at 182.9-183.0 Da
Natural or modified residues with a mass of 182.9-183.0 Da.
PubMed:18688235
OBSOLETE because redundant with MOD:00130. Remap to MOD:00130.
MOD:00130
-1.03
H -3 N -1 O 1
-1.031634
K
natural
Unimod:352
Oxidation of lysine (to aminoadipic semialdehyde)
PSI-MOD
MOD:00779
From DeltaMass: Average Mass: -1 Average Mass Change:-1 References:Amici A, Levine, RL, Tsai, L, and Stadtman, ER: Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. Journal of Biological Chemistry 264: 3341-3346 1989.Requena JR, Chao CC, Levine RL, and Stadtman ER: Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proceedings of the National Academy of Sciences USA 98: 69-74 2001.
lysine oxidation to aminoadipic semialdehyde
true
OBSOLETE because redundant with MOD:00130. Remap to MOD:00130.
DeltaMass:352
PubMed:11332453
PubMed:358196
PubMed:5337886
PubMed:5529814
Unimod:352
Oxidation of lysine (to aminoadipic semialdehyde)
A protein modification that effectively converts an L-asparagine residue to N-acetyl-L-asparagine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 6 H 8 N 2 O 3
156.14
156.0535
N
artifact
N-term
AcAsn
PSI-MOD
MOD:00780
This modification has not been observed to occur naturally.
N-acetyl-L-asparagine
A protein modification that effectively converts an L-asparagine residue to N-acetyl-L-asparagine.
PubMed:18688235
AcAsn
A protein modification that effectively converts an L-histidine residue to N2-acetyl-L-histidine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 8 H 9 N 3 O 2
179.18
179.06947
H
artifact
N-term
AcHis
PSI-MOD
MOD:00781
This modification has not been observed to occur naturally.
N2-acetyl-L-histidine
A protein modification that effectively converts an L-histidine residue to N2-acetyl-L-histidine.
PubMed:18688235
AcHis
A protein modification that effectively converts an L-leucine residue to N-acetyl-L-leucine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 8 H 14 N 1 O 2
156.2
156.10245
L
artifact
N-term
AcLeu
PSI-MOD
MOD:00782
This modification has not been observed to occur naturally.
N-acetyl-L-leucine
A protein modification that effectively converts an L-leucine residue to N-acetyl-L-leucine.
PubMed:18688235
AcLeu
A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two methyl groups.
28.05
C 2 H 4 N 0 O 0
28.0313
C 8 H 16 N 4 O 1
184.24
184.13242
R
natural
Unimod:36
uniprot.ptm:PTM-0341
NNMe2Arg
dimethylr
PSI-MOD
Dimethyl
MOD:00783
dimethylated L-arginine
A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two methyl groups.
OMSSA:37
Unimod:36#R
NNMe2Arg
dimethylr
Dimethyl
A protein modification that effectively converts an L-phenylalanine residue to N-acetyl-L-phenylalanine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 11 H 11 N 1 O 2
189.21
189.07898
F
artifact
N-term
AcPhe
PSI-MOD
MOD:00784
This modification has not been observed to occur naturally.
N-acetyl-L-phenylalanine
A protein modification that effectively converts an L-phenylalanine residue to N-acetyl-L-phenylalanine.
PubMed:18688235
AcPhe
A protein modification that effectively converts an L-tryptophan residue to N2-acetyl-L-tryptophan.
42.04
C 2 H 2 N 0 O 1
42.010567
C 13 H 12 N 2 O 2
228.25
228.08987
W
artifact
N-term
AcTrp
PSI-MOD
MOD:00785
This modification has not been observed to occur naturally.
N2-acetyl-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to N2-acetyl-L-tryptophan.
PubMed:18688235
AcTrp
A protein modification that effectively substitutes one or more (2)H deuterium atoms for (1)H protium atoms.
D(H)Res
PSI-MOD
MOD:00786
deuterium substituted residue
A protein modification that effectively substitutes one or more (2)H deuterium atoms for (1)H protium atoms.
PubMed:18688235
D(H)Res
modification from Unimod - label for the active site serine of the serine esterase/protease family also shown to label tyrosine in serum albumin
164.14
C 6 H 13 O 3 P 1
164.06023
C 9 H 18 N 1 O 5 P 1
251.22
251.09225
S
artifact
Unimod:362
PSI-MOD
Diisopropylphosphate
O-Diisopropylphosphorylation
MOD:00787
diisopropylphosphoserine
modification from Unimod - label for the active site serine of the serine esterase/protease family also shown to label tyrosine in serum albumin
Unimod:362
Diisopropylphosphate
O-Diisopropylphosphorylation
modification from Unimod
122.06
C 3 H 7 O 3 P 1
122.01328
C 12 H 16 N 1 O 5 P 1
285.24
285.0766
Y
artifact
Unimod:363
PSI-MOD
Isopropylphospho
O-Isopropylphosphorylation
MOD:00788
isopropylphosphotyrosine
modification from Unimod
Unimod:363
Isopropylphospho
O-Isopropylphosphorylation
modification from Unimod - isotopic label ICPL method - The paper describes an H/D labeling strategy whereas the commercial product follows a C/13C labeling strategy. The digest is typically applied AFTER ICPL_light/heavy labeling, only Protein N-term labeling and Lys-specific labeling is applied.
111.04
(13)C 6 H 3 N 1 O 1
111.041595
X
artifact
Unimod:364
PSI-MOD
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form
ICPL:13C(6)
MOD:00789
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form
modification from Unimod - isotopic label ICPL method - The paper describes an H/D labeling strategy whereas the commercial product follows a C/13C labeling strategy. The digest is typically applied AFTER ICPL_light/heavy labeling, only Protein N-term labeling and Lys-specific labeling is applied.
PubMed:15602776
URL:http://www.serva.de/products/sheets/39230-E.pdf
Unimod:364
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form
ICPL:13C(6)
modification from Unimod - isotopic label ICPL method - The paper describes an H/D labeling strategy whereas the commercial product follows a C/13C labeling strategy. The digest is typically applied AFTER ICPL_light/heavy labeling, only Protein N-term labeling and Lys-specific labeling is applied.
105.02
(12)C 6 H 3 N 1 O 1
105.02146
X
artifact
Unimod:365
PSI-MOD
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form
ICPL
MOD:00790
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form
modification from Unimod - isotopic label ICPL method - The paper describes an H/D labeling strategy whereas the commercial product follows a C/13C labeling strategy. The digest is typically applied AFTER ICPL_light/heavy labeling, only Protein N-term labeling and Lys-specific labeling is applied.
PubMed:15602776
URL:http://www.serva.de/products/sheets/39230-E.pdf
Unimod:365
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form
ICPL
A protein modification that effectively converts an L-glutamine residue to L-glutamic acid with one (18)O.
2.99
H -1 N -1 (18)O 1
2.988262
C 5 H 7 N 1 (16)O 2 (18)O 1
131.05
131.04684
Q
artifact
Unimod:366
PSI-MOD
Deamidated:18O(1)
Deamidation in presence of O18
MOD:00791
1x(18)O labeled deamidated L-glutamine
A protein modification that effectively converts an L-glutamine residue to L-glutamic acid with one (18)O.
PubMed:8382902
Unimod:366#Q
Deamidated:18O(1)
Deamidation in presence of O18
A protein modification that effectively substitutes one (2)H deuterium atom for one (1)H protium atom.
D(H)1Res
PSI-MOD
MOD:00792
deuterium monosubstituted residue
A protein modification that effectively substitutes one (2)H deuterium atom for one (1)H protium atom.
PubMed:18688235
D(H)1Res
A protein modification that effectively converts an L-cysteine residue to dehydroalanine.
-34.08
C 0 H -2 N 0 O 0 S -1
-33.98772
C 3 H 3 N 1 O 1
69.06
69.02146
C
natural
Unimod:368
uniprot.ptm:PTM-0468
2,3-didehydroalanine
2-aminoacrylic acid
2-aminopropenoic acid
4-methylidene-imidazole-5-one (MIO) active site
Dehydroalanine (from Cysteine)
Dha
MOD_RES 2,3-didehydroalanine (Cys)
anhydroserine
dHAla(Cys)
dehydroalanine
PSI-MOD
Cys->Dha
Dehydroalanine (from Cysteine)
MOD:00793
From DeltaMass: In an attempt to clarfiy the difference between the modification of cysteine to lanthionine and cysteine to dehydroalanine, the following contributions from the ABRF email forum are presented:Structurally speaking lanthionine is like cystine but lacks one S atom. I imagine one can think of it as a condensation of cysteine and dehydroalanine but I do not know how it is made biologically. Dehydroalanine could be derived from either serine or cysteine. If I recall Biochem 101 correctly lanthionine was first found in wool.-Lowell Ericsson (ERICSSONLH@U.WASHINGTON.EDU)As far as I know, the structure of lanthionine is two Ala's joined by a single sulphur with the loss of two hydrogens from the methyl group of the Ala.Stephen Bayne (sbay@novo.dk)Regarding the structure of lanthionine and dehydroalanine: dehydroalanine is formed by the loss of one sulfur atom and two hydrogen atoms from ONE cysteine residue. lanthionine is formed from TWO cysteines, is a thioether, and contains one sulfur atom less than the amino acid cystine. Dan McCormick (MCCORMICK@rcf.mayo.edu) [DeltaMass]. Most bacterially produced lanthionine crosslinks are made by dehydration of L-serine to dehydroalanine, and then reaction with L-cysteine so as to produce chiral inversion at the alpha-carbon of the original L-serine; the lanthionine is a meso-diastereomer with L-configuration of the original cysteine alpha-carbon and D-configuration of the original L-serine alpha-carbon. In cypemycin dehydroalanine has been shown to be produced by loss of hydrogen sulfide from cysteine. Beta-elimination of hydrogen sulfide does occur during treatment with performic acid [JSG].
dehydroalanine (Cys)
A protein modification that effectively converts an L-cysteine residue to dehydroalanine.
ChEBI:17123
DeltaMass:8
PubMed:10220322
PubMed:11212008
PubMed:1547888
PubMed:15799070
PubMed:1815586
PubMed:20805503
PubMed:2914619
PubMed:7947813
PubMed:8239649
RESID:AA0181#CYS
Unimod:368
2,3-didehydroalanine
2-aminoacrylic acid
2-aminopropenoic acid
4-methylidene-imidazole-5-one (MIO) active site
Dehydroalanine (from Cysteine)
Dha
MOD_RES 2,3-didehydroalanine (Cys)
anhydroserine
dHAla(Cys)
dehydroalanine
Cys->Dha
Dehydroalanine (from Cysteine)
OBSOLETE because redundant and identical to MOD:00477. Remap to MOD:00477.
MOD:00477
-28.01
C -1 O -1
-27.994915
C 4 H 7 N 1 O 0
69.11
69.057846
P
artifact
Unimod:369
PSI-MOD
Pro->Pyrrolidone
Pyrrolidone from Proline
MOD:00794
This Unimod entry appears to have come from the same description in PubMed:9252331 as Unimod:360. This entry was not annotated as being approved. Neither difference formula corresponds to the result described in the original citation PubMed:2161657.
pyrrolidone from proline
true
OBSOLETE because redundant and identical to MOD:00477. Remap to MOD:00477.
PubMed:9252331
Unimod:369
Pro->Pyrrolidone
Pyrrolidone from Proline
modification from Unimod
86.09
C 4 H 6 O 2
86.03678
C 7 H 11 N 1 O 3 S 1
189.23
189.04596
C
artifact
Unimod:371
PSI-MOD
HMVK
Michael addition of hydroxymethylvinyl ketone to cysteine
MOD:00795
Michael addition of hydroxymethylvinyl ketone to cysteine
modification from Unimod
PubMed:11743741
Unimod:371
HMVK
Michael addition of hydroxymethylvinyl ketone to cysteine
A protein modification that effectively converts an L-arginine residue to L-ornithine.
-42.04
C -1 H -2 N -2
-42.021797
C 5 H 10 N 2 O 1
114.15
114.079315
R
artifact
Unimod:372
Ornithine (from Arginine)
Ornithyl
arg2orn
PSI-MOD
Arg->Orn
Ornithine from Arginine
MOD:00796
L-ornithine (Arg)
A protein modification that effectively converts an L-arginine residue to L-ornithine.
DeltaMass:129
OMSSA:163
PubMed:15489230
Unimod:372
Ornithine (from Arginine)
Ornithyl
arg2orn
Arg->Orn
Ornithine from Arginine
a protein modification that effectively converts an L-cysteine residue to the PEP adduct, 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal
168.04
C 3 H 5 N 0 O 6 P 1 S 0
167.98238
C 6 H 10 N 1 O 7 P 1 S 1
271.18
270.99155
C
natural
uniprot.ptm:PTM-0424
(2R)-2-amino-3-[1-carboxy-1-(phosphonooxy)ethyl]sulfanylpropanoic acid
2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal
2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-2-(phosphonooxy)propanoic acid
2-([(2R)-2-azanyl-2-carboxyethyl]sulfanyl)-2-(phosphonooxy)propanoic acid
MOD_RES 2-(S-cysteinyl)pyruvic acid O-phosphothioketal
S-[1-carboxy-1-(phosphonooxy)ethyl]cysteine
SPEPCys
cysteinyl pyruvate O-phosphothioketal
phosphoenolpyruvate cysteine adduct
phospholactoyl cysteine adduct
PSI-MOD
MOD:00797
2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal
a protein modification that effectively converts an L-cysteine residue to the PEP adduct, 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal
ChEBI:149496
PubMed:4696757
PubMed:7999765
PubMed:8664284
RESID:AA0391
(2R)-2-amino-3-[1-carboxy-1-(phosphonooxy)ethyl]sulfanylpropanoic acid
2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal
2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-2-(phosphonooxy)propanoic acid
2-([(2R)-2-azanyl-2-carboxyethyl]sulfanyl)-2-(phosphonooxy)propanoic acid
MOD_RES 2-(S-cysteinyl)pyruvic acid O-phosphothioketal
S-[1-carboxy-1-(phosphonooxy)ethyl]cysteine
SPEPCys
cysteinyl pyruvate O-phosphothioketal
phosphoenolpyruvate cysteine adduct
phospholactoyl cysteine adduct
A protein modification that can be regarded as effectively either one half of a cystine cross-link, or a cysteine residue with one hydrogen atom or proton removed.
-1.01
C 0 H -1 N 0 O 0 S 0
-1.007825
C 3 H 4 N 1 O 1 S 1
102.13
102.00136
C
Unimod:374
PSI-MOD
Dehydro
Half of a disulfide bridge
MOD:00798
half cystine
A protein modification that can be regarded as effectively either one half of a cystine cross-link, or a cysteine residue with one hydrogen atom or proton removed.
PubMed:1988019
PubMed:2001356
PubMed:2076469
PubMed:3083866
PubMed:366603
PubMed:7918467
PubMed:8344916
Unimod:374
Dehydro
Half of a disulfide bridge
A protein modification that effectively converts an L-cysteine residue to S-galactosyl-L-cysteine.
162.14
C 6 H 10 N 0 O 5 S 0
162.05283
C 9 H 15 N 1 O 6 S 1
265.28
265.062
C
artifact
uniprot.ptm:PTM-0624
(2R)-2-amino-3-(D-galactopyranosylsulfanyl)propanoic acid
CARBOHYD S-linked (Gal) cysteine
S-(beta-D-galactopyranosyl)cysteine
S-galactosyl-L-cysteine
S-glycosyl-cysteine
SGalCys
PSI-MOD
MOD:00799
The reported peptide has not been isolated or characterized in subsequent work, and the peptide sequence has not been found in the human proteome. This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
S-galactosyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-galactosyl-L-cysteine.
PubMed:11945907
RESID:AA0392
(2R)-2-amino-3-(D-galactopyranosylsulfanyl)propanoic acid
CARBOHYD S-linked (Gal) cysteine
S-(beta-D-galactopyranosyl)cysteine
S-galactosyl-L-cysteine
S-glycosyl-cysteine
SGalCys
A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and a one-vanadium seven-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide.
932.51
C 7 Fe 7 H 6 N 0 O 7 S 9 V 1
932.24854
C 16 Fe 7 H 18 N 4 O 9 S 10 V 1
1172.8
1172.3167
C, H
hypothetical
CysHis-[V7Fe9S]
L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide carbide
nitrogenase iron-vanadium cofactor
PSI-MOD
MOD:00800
Cross-link 2; incidental to RESID:AA0300.
L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide
A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and a one-vanadium seven-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide.
PubMed:2345152
RESID:AA0393
CysHis-[V7Fe9S]
L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide carbide
nitrogenase iron-vanadium cofactor
A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and an eight-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl octairon nonasulfide.
937.42
C 7 Fe 8 H 6 N 0 O 7 S 9
937.2406
2-
C 16 Fe 8 H 18 N 4 O 9 S 10
1177.7
1177.3087
C, H
hypothetical
CysHis-[8Fe9S]
L-cysteinyl-L-histidino-homocitryl octairon nonasulfide carbide
nitrogenase iron-iron cofactor
PSI-MOD
MOD:00801
Cross-link 2; incidental to RESID:AA0300.
L-cysteinyl-L-histidino-homocitryl octairon nonasulfide
A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and an eight-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl octairon nonasulfide.
PubMed:8392330
RESID:AA0394
CysHis-[8Fe9S]
L-cysteinyl-L-histidino-homocitryl octairon nonasulfide carbide
nitrogenase iron-iron cofactor
a protein modification that effectively converts an L-histidine residue to L-histidino vanadium tetraoxide
116.95
C 0 H 2 N 0 O 4 V 1
116.93927
C 6 H 9 N 3 O 5 V 1
254.1
253.99818
H
natural
(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (dihydroxy)dioxovanadium
1'-vanadato-L-histidine
L-histidino vanadium tetraoxide
N(tau)-vanadatohistidine
NtauH2VO4His
bromoperoxidase vanadium cofactor
chloroperoxidase vanadium cofactor
dihydrogen (4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (tetraoxido)vanadate
haloperoxidase vanadium cofactor
histidine-1-vanadate
histidine-N(epsilon)-vanadate
histidine-N1'-vanadate
tele-vanadatohistidine
PSI-MOD
MOD:00802
L-histidino vanadium tetraoxide
a protein modification that effectively converts an L-histidine residue to L-histidino vanadium tetraoxide
PubMed:10543953
PubMed:16494433
PubMed:8552646
RESID:AA0395
(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (dihydroxy)dioxovanadium
1'-vanadato-L-histidine
L-histidino vanadium tetraoxide
N(tau)-vanadatohistidine
NtauH2VO4His
bromoperoxidase vanadium cofactor
chloroperoxidase vanadium cofactor
dihydrogen (4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (tetraoxido)vanadate
haloperoxidase vanadium cofactor
histidine-1-vanadate
histidine-N(epsilon)-vanadate
histidine-N1'-vanadate
tele-vanadatohistidine
A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 3-(S-L-cysteinyl)-L-tyrosine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 12 H 12 N 2 O 3 S 1
264.3
264.05685
C, Y
natural
uniprot.ptm:PTM-0020
(2S,3R)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-(4-hydroxyphenyl)propanoic acid
2-amino-3-(2-amino-2-carboxyethylthio)-3-(4-hydroxyphenyl)propanoic acid
3-(L-cystein-S-yl)-L-tyrosine
CROSSLNK 3-(S-cysteinyl)-tyrosine (Cys-Tyr)
S-(tyros-3'-yl)cysteine
XLNKSCys3Tyr
PSI-MOD
MOD:00803
Cross-link 2.
3-(S-L-cysteinyl)-L-tyrosine
A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 3-(S-L-cysteinyl)-L-tyrosine.
PubMed:15342250
RESID:AA0396
(2S,3R)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-(4-hydroxyphenyl)propanoic acid
2-amino-3-(2-amino-2-carboxyethylthio)-3-(4-hydroxyphenyl)propanoic acid
3-(L-cystein-S-yl)-L-tyrosine
CROSSLNK 3-(S-cysteinyl)-tyrosine (Cys-Tyr)
S-(tyros-3'-yl)cysteine
XLNKSCys3Tyr
A protein modification that effectively converts an L-serine residue to O3-beta-glucosylated L-serine.
162.14
C 6 H 10 N 0 O 5
162.05283
C 9 H 15 N 1 O 7
249.22
249.08485
S
natural
uniprot.ptm:PTM-0573
(2S)-2-amino-3-(beta-D-glucopyranosyloxy)propanoic acid
CARBOHYD O-linked (Glc) serine
CARBOHYD O-linked (Hex)
O-glucosyl-L-serine
O-glycosylserine
O3-glucosylserine
OGlcSer
PSI-MOD
MOD:00804
O-glucosyl-L-serine
A protein modification that effectively converts an L-serine residue to O3-beta-glucosylated L-serine.
PubMed:10734111
PubMed:2105311
PubMed:2511201
RESID:AA0397
(2S)-2-amino-3-(beta-D-glucopyranosyloxy)propanoic acid
CARBOHYD O-linked (Glc) serine
CARBOHYD O-linked (Hex)
O-glucosyl-L-serine
O-glycosylserine
O3-glucosylserine
OGlcSer
A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminoglucosyl)-L-serine.
203.19
C 8 H 13 N 1 O 5
203.07938
C 11 H 18 N 2 O 7
290.27
290.1114
S
natural
uniprot.ptm:PTM-0580
(2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)propanoic acid
CARBOHYD O-linked (GlcNAc) serine
CARBOHYD O-linked (HexNAc)
O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-L-serine
O-(N-acetylamino)glucosyl-L-serine
O-(N-acetylglucosaminyl)serine
O-glycosylserine
O-seryl-beta-N-acetylglucosaminide
O3-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-serine
O3-(N-acetylglucosaminyl)serine
OGlcNAcSer
PSI-MOD
HexNAc
MOD:00805
O-(N-acetylamino)glucosyl-L-serine
A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminoglucosyl)-L-serine.
PubMed:3086323
PubMed:8404891
RESID:AA0398
(2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)propanoic acid
CARBOHYD O-linked (GlcNAc) serine
CARBOHYD O-linked (HexNAc)
O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-L-serine
O-(N-acetylamino)glucosyl-L-serine
O-(N-acetylglucosaminyl)serine
O-glycosylserine
O-seryl-beta-N-acetylglucosaminide
O3-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-serine
O3-(N-acetylglucosaminyl)serine
OGlcNAcSer
HexNAc
A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminoglucosyl)-L-threonine.
203.19
C 8 H 13 N 1 O 5
203.07938
C 12 H 20 N 2 O 7
304.3
304.12704
T
natural
uniprot.ptm:PTM-0582
(2S,3R)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)butanoic acid
CARBOHYD O-linked (GlcNAc) threonine
CARBOHYD O-linked (HexNAc)
O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-L-threonine
O-(N-acetylamino)glucosyl-L-threonine
O-(N-acetylglucosaminyl)-L-threonine
O-glycosylthreonine
O-threonyl-beta-N-acetylglucosaminide
O3-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-threonine
O3-(N-acetylglucosaminyl)threonine
OGlcNAcThr
PSI-MOD
HexNAc
MOD:00806
O-(N-acetylamino)glucosyl-L-threonine
A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminoglucosyl)-L-threonine.
PubMed:3086323
PubMed:8404891
RESID:AA0399
(2S,3R)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)butanoic acid
CARBOHYD O-linked (GlcNAc) threonine
CARBOHYD O-linked (HexNAc)
O-(2-acetylamino-2-deoxy-beta-D-glucopyranosyl)-L-threonine
O-(N-acetylamino)glucosyl-L-threonine
O-(N-acetylglucosaminyl)-L-threonine
O-glycosylthreonine
O-threonyl-beta-N-acetylglucosaminide
O3-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-threonine
O3-(N-acetylglucosaminyl)threonine
OGlcNAcThr
HexNAc
A protein modification that effectively converts an L-serine residue to pyruvic acid.
-17.03
C 0 H -3 N -1 O 0
-17.026548
C 3 H 3 O 2
71.06
71.013306
S
natural
N-term
Unimod:385
uniprot.ptm:PTM-0266
2-oxopropanoic acid
MOD_RES Pyruvic acid (Ser)
Pyruvate
Pyruvoyl- (Serine)
pyruvic acid
PSI-MOD
MOD:00807
DeltaMass gives mass 70 and difference mass -16 with no formula
pyruvic acid (Ser)
A protein modification that effectively converts an L-serine residue to pyruvic acid.
DeltaMass:23
PubMed:10085076
PubMed:3042771
PubMed:8464063
RESID:AA0127#SER
Unimod:385#S
2-oxopropanoic acid
MOD_RES Pyruvic acid (Ser)
Pyruvate
Pyruvoyl- (Serine)
pyruvic acid
A protein modification that effectively converts an L-serine residue to O3-galactosylserine.
162.14
C 6 H 10 N 0 O 5
162.05283
C 9 H 15 N 1 O 7
249.22
249.08485
S
natural
uniprot.ptm:PTM-0560
(2S)-2-amino-3-(alpha-D-galactopyranosyloxy)propanoic acid
CARBOHYD O-linked (Gal) serine
CARBOHYD O-linked (Hex)
O-galactosyl-L-serine
O-glycosylserine
O3-galactosylserine
OGalSer
PSI-MOD
MOD:00808
O-galactosyl-L-serine
A protein modification that effectively converts an L-serine residue to O3-galactosylserine.
PubMed:666730
RESID:AA0400
(2S)-2-amino-3-(alpha-D-galactopyranosyloxy)propanoic acid
CARBOHYD O-linked (Gal) serine
CARBOHYD O-linked (Hex)
O-galactosyl-L-serine
O-glycosylserine
O3-galactosylserine
OGalSer
A protein modification that effectively converts an L-threonine residue to O3-galactosylthreonine.
162.14
C 6 H 10 N 0 O 5
162.05283
C 10 H 17 N 1 O 7
263.25
263.1005
T
natural
uniprot.ptm:PTM-0562
(2S,3R)-2-amino-3-(alpha-D-galactopyranosyloxy)butanoic acid
CARBOHYD O-linked (Gal) threonine
CARBOHYD O-linked (Hex)
O-galactosyl-L-threonine
O-glycosylthreonine
O3-galactosylthreonine
OGalThr
PSI-MOD
MOD:00809
O-galactosyl-L-threonine
A protein modification that effectively converts an L-threonine residue to O3-galactosylthreonine.
PubMed:2673008
RESID:AA0401
(2S,3R)-2-amino-3-(alpha-D-galactopyranosyloxy)butanoic acid
CARBOHYD O-linked (Gal) threonine
CARBOHYD O-linked (Hex)
O-galactosyl-L-threonine
O-glycosylthreonine
O3-galactosylthreonine
OGalThr
A protein modification that effectively converts an L-serine residue to O3-mannosylserine.
162.14
C 6 H 10 N 0 O 5
162.05283
C 9 H 15 N 1 O 7
249.22
249.08485
S
natural
uniprot.ptm:PTM-0588
(2S)-2-amino-3-(alpha-D-mannopyranosyloxy)propanoic acid
CARBOHYD O-linked (Hex)
CARBOHYD O-linked (Man) serine
O-glycosylserine
O-mannopyranosylserine
O-mannosyl-L-serine
O3-mannosylserine
OManSer
PSI-MOD
MOD:00810
O-mannosyl-L-serine
A protein modification that effectively converts an L-serine residue to O3-mannosylserine.
PubMed:391559
RESID:AA0402
(2S)-2-amino-3-(alpha-D-mannopyranosyloxy)propanoic acid
CARBOHYD O-linked (Hex)
CARBOHYD O-linked (Man) serine
O-glycosylserine
O-mannopyranosylserine
O-mannosyl-L-serine
O3-mannosylserine
OManSer
a protein modification that effectively forms a O3-mannosylthreonine
162.14
C 6 H 10 N 0 O 5
162.05283
C 10 H 17 N 1 O 7
263.25
263.1005
T
natural
uniprot.ptm:PTM-0591
(2S,3R)-2-amino-3-(alpha-D-mannopyranosyloxy)butanoic acid
CARBOHYD O-linked (Hex)
CARBOHYD O-linked (Man) threonine
O-glycosylthreonine
O-mannosyl-L-threonine
O3-mannosylthreonine
OManThr
PSI-MOD
MOD:00811
O-mannosyl-L-threonine
a protein modification that effectively forms a O3-mannosylthreonine
PubMed:391559
RESID:AA0403
(2S,3R)-2-amino-3-(alpha-D-mannopyranosyloxy)butanoic acid
CARBOHYD O-linked (Hex)
CARBOHYD O-linked (Man) threonine
O-glycosylthreonine
O-mannosyl-L-threonine
O3-mannosylthreonine
OManThr
A protein modification that effectively converts an L-serine residue to an O-fucosylserine.
146.14
C 6 H 10 N 0 O 4
146.0579
C 9 H 15 N 1 O 6
233.22
233.08994
S
natural
Unimod:295
uniprot.ptm:PTM-0550
(2S)-2-amino-3-(6-deoxy-alpha-D-galactopyranosyloxy)propanoic acid
CARBOHYD O-linked (Fuc)
CARBOHYD O-linked (Fuc) serine
CARBOHYD O-linked (dHex)
O-fucosyl-L-serine
O-glycosylserine
O3-fucosylserine
OFucSer
PSI-MOD
Fucose
dHex
MOD:00812
O-fucosyl-L-serine
A protein modification that effectively converts an L-serine residue to an O-fucosylserine.
PubMed:10734111
PubMed:11067851
PubMed:11344537
PubMed:12096136
PubMed:1517205
PubMed:15189151
PubMed:1904059
PubMed:3311742
PubMed:3578767
RESID:AA0404
Unimod:295#S
(2S)-2-amino-3-(6-deoxy-alpha-D-galactopyranosyloxy)propanoic acid
CARBOHYD O-linked (Fuc)
CARBOHYD O-linked (Fuc) serine
CARBOHYD O-linked (dHex)
O-fucosyl-L-serine
O-glycosylserine
O3-fucosylserine
OFucSer
Fucose
dHex
A protein modification that effectively converts an threonine residue to an O-fucosylthreonine.
146.14
C 6 H 10 N 0 O 4
146.0579
C 10 H 17 N 1 O 6
247.25
247.10559
T
natural
Unimod:295
uniprot.ptm:PTM-0552
(2S,3R)-2-amino-3-(6-deoxy-alpha-D-galactopyranosyloxy)butanoic acid
CARBOHYD O-linked (Fuc) threonine
CARBOHYD O-linked (dHex)
O-fucosyl-L-threonine
O-glycosylthreonine
O3-fucosylthreonine
OFucThr
PSI-MOD
Fucose
dHex
MOD:00813
O-fucosyl-L-threonine
A protein modification that effectively converts an threonine residue to an O-fucosylthreonine.
PubMed:11344537
PubMed:11857757
PubMed:15189151
PubMed:1740125
PubMed:1900431
RESID:AA0405
Unimod:295#T
(2S,3R)-2-amino-3-(6-deoxy-alpha-D-galactopyranosyloxy)butanoic acid
CARBOHYD O-linked (Fuc) threonine
CARBOHYD O-linked (dHex)
O-fucosyl-L-threonine
O-glycosylthreonine
O3-fucosylthreonine
OFucThr
Fucose
dHex
A protein modification that effectively converts an L-serine residue to O3-xylosylserine.
132.12
C 5 H 8 N 0 O 4
132.04225
C 8 H 13 N 1 O 6
219.19
219.07428
S
artifact
uniprot.ptm:PTM-0598
(2S)-2-amino-3-(alpha-D-xylopyranosyloxy)propanoic acid
CARBOHYD O-linked (Xyl) serine
O-(beta-D-xylopyranosyl)-L-serine
O-glycosylserine
O-xylosyl-L-serine
O3-xylosylserine
OXylSer
PSI-MOD
MOD:00814
One glycosylated serine with weak electron density was modeled as O3-alpha-xylosylserine, while O3-alpha-mannosyl serine and threonine were modeled at ten other positions. The authors do not discuss this exception or provide chemical evidence for it. Since an O3-xylosyl serine modification has not been reported in any other fungal proteins, the modification is probably also an O3-alpha-mannosyl serine, see MOD:00810 [JSG].
O-xylosyl-L-serine
A protein modification that effectively converts an L-serine residue to O3-xylosylserine.
PubMed:8747463
RESID:AA0406
(2S)-2-amino-3-(alpha-D-xylopyranosyloxy)propanoic acid
CARBOHYD O-linked (Xyl) serine
O-(beta-D-xylopyranosyl)-L-serine
O-glycosylserine
O-xylosyl-L-serine
O3-xylosylserine
OXylSer
OBSOLETE because redundant with MOD:00151. Remap to MOD:00151.
MOD:00151
520.27
C 10 H 11 Mo 1 N 5 O 8 P 1 S 2
521.8841
C
natural
PSI-MOD
MOD:00815
molybdopterin
true
OBSOLETE because redundant with MOD:00151. Remap to MOD:00151.
PubMed:14527393
PubMed:7878465
PubMed:9428520
A protein modification that effectively converts an L-cysteine residue to S-stearoyl-L-cysteine.
266.47
C 18 H 34 N 0 O 1 S 0
266.26096
C 21 H 39 N 1 O 2 S 1
369.61
369.27014
C
natural
uniprot.ptm:PTM-0283
(R)-2-amino-3-(octadecanoylsulfanyl)propanoic acid
2-amino-3-(octadecanoylthio)propanoic acid
LIPID S-stearoyl cysteine
S-stearoyl-L-cysteine
SSteCys
Stearoylation
cysteine octadecanoate thioester
cysteine stearate thioester
PSI-MOD
MOD:00816
From DeltaMass: Average Mass: 266
S-stearoyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-stearoyl-L-cysteine.
DeltaMass:0
PubMed:2371783
PubMed:3143715
PubMed:8761467
RESID:AA0407
(R)-2-amino-3-(octadecanoylsulfanyl)propanoic acid
2-amino-3-(octadecanoylthio)propanoic acid
LIPID S-stearoyl cysteine
S-stearoyl-L-cysteine
SSteCys
Stearoylation
cysteine octadecanoate thioester
cysteine stearate thioester
A protein modification that effectively converts an L-tryptophan residue to 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan.
136.24
C 10 H 16 N 0 O 0
136.1252
C 21 H 26 N 2 O 1
322.45
322.2045
W
natural
uniprot.ptm:PTM-0026
(2S,3R)-3-geranyl-2,3-dihydro-2,N(alpha)-cyclo-L-tryptophan
(2S,3aR,8aS)-3a-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid
3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan
3'Ger2'N2cycTrp
LIPID 3'-geranyl-2',N2-cyclotryptophan
PSI-MOD
MOD:00817
3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan.
ChEBI:35304
PubMed:16407988
PubMed:8168130
RESID:AA0408
(2S,3R)-3-geranyl-2,3-dihydro-2,N(alpha)-cyclo-L-tryptophan
(2S,3aR,8aS)-3a-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid
3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan
3'Ger2'N2cycTrp
LIPID 3'-geranyl-2',N2-cyclotryptophan
A protein modification that effectively converts a residue to a glycosylphosphatidylinositolethanolamidated.
123.05
C 2 H 6 N 1 O 3 P 1
123.00853
X
natural
C-term
Unimod:394
uniprot.ptm:PTM-0139
GPIRes
LIPID GPI-anchor amidated carboxyl end
PSI-MOD
GPIanchor
glycosylphosphatidylinositol
MOD:00818
glycosylphosphatidylinositolated residue
A protein modification that effectively converts a residue to a glycosylphosphatidylinositolethanolamidated.
PubMed:12643538
Unimod:394#C-term
GPIRes
LIPID GPI-anchor amidated carboxyl end
GPIanchor
glycosylphosphatidylinositol
A protein modification that effectively converts an L-glutamic acid residue to L-2-aminobutanoic acid.
-44.01
C -1 H 0 N 0 O -2
-43.98983
C 4 H 7 N 1 O 1
85.11
85.052765
E
natural
(S)-2-aminobutanoic acid
Abu
L-2-amino-n-butyric acid
L-2-aminobutanoic acid
L-2-aminobutyric acid
L-alpha-amino-n-butyric acid
L-alpha-aminobutyric acid
L-butyrine
alpha-amino-n-butyric acid
alpha-aminobutyric acid
butyrine
dCbxGlu
PSI-MOD
MOD:00819
L-2-aminobutanoic acid (Glu)
A protein modification that effectively converts an L-glutamic acid residue to L-2-aminobutanoic acid.
ChEBI:35619
DeltaMass:0
PubMed:11740505
RESID:AA0409
(S)-2-aminobutanoic acid
Abu
Abu
L-2-amino-n-butyric acid
L-2-aminobutanoic acid
L-2-aminobutyric acid
L-alpha-amino-n-butyric acid
L-alpha-aminobutyric acid
L-butyrine
alpha-amino-n-butyric acid
alpha-aminobutyric acid
butyrine
dCbxGlu
A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue to form 2-imino-alanine 5-imidazolinone glycine.
-64.04
C -1 H -4 N 0 O -3
-64.016045
C 5 H 4 N 2 O 1
108.1
108.032364
D, G
natural
(2-ethanimidoyl-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2,N-didehydroalanyl-5-imidazolinone glycine
2-(1-iminoethyl)-1-carboxymethyl-1-imidazolin-5-one
2-imino-alanine 5-imidazolinone glycine
2-imino-alanyl-5-imidazolinone glycine
[2-(1-iminoethyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
alanyl-5-imidazolinone glycine
para-hydroxybenzylidene-imidazolidinone chromophore
red fluorescent protein zRFP574 chromophore
PSI-MOD
MOD:00820
Cross-link 2; carboxamidine.
2-imino-alanine 5-imidazolinone glycine
A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue to form 2-imino-alanine 5-imidazolinone glycine.
PubMed:16627946
RESID:AA0410
(2-ethanimidoyl-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid
2,N-didehydroalanyl-5-imidazolinone glycine
2-(1-iminoethyl)-1-carboxymethyl-1-imidazolin-5-one
2-imino-alanine 5-imidazolinone glycine
2-imino-alanyl-5-imidazolinone glycine
[2-(1-iminoethyl)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid
alanyl-5-imidazolinone glycine
para-hydroxybenzylidene-imidazolidinone chromophore
red fluorescent protein zRFP574 chromophore
A protein modification that effectively crosslinks an L-alanine residue and an L-cysteine residue by a thioester bond to form S-(L-alanyl)-L-cysteine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 6 H 9 N 2 O 2 S 1
173.21
173.03847
A, C
hypothetical
C-term
(2R)-2-amino-3-([(2S)-2-aminopropanoyl]sulfanyl)propanoic acid
CROSSLNK Alanyl cysteine thioester (Cys-Ala)
S-(2-aminopropanoyl)cysteine
S-(L-alanyl)-L-cysteine
XLNK1AlaSCys
alanine cysteine thioester
PSI-MOD
MOD:00821
Cross-link 2.
S-(L-alanyl)-L-cysteine
A protein modification that effectively crosslinks an L-alanine residue and an L-cysteine residue by a thioester bond to form S-(L-alanyl)-L-cysteine.
PubMed:11807079
RESID:AA0411
(2R)-2-amino-3-([(2S)-2-aminopropanoyl]sulfanyl)propanoic acid
CROSSLNK Alanyl cysteine thioester (Cys-Ala)
S-(2-aminopropanoyl)cysteine
S-(L-alanyl)-L-cysteine
XLNK1AlaSCys
alanine cysteine thioester
A protein modification that effectively crosslinks an L-leucine residue and an L-cysteine residue by a thioester bond to form S-(L-leucyl)-L-cysteine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 9 H 15 N 2 O 2 S 1
215.29
215.08542
C, L
natural
C-term
(2R)-2-amino-3-([(2S)-2-amino-4-methylpentanoyl]sulfanyl)propanoic acid
CROSSLNK Leucyl cysteine thioester (Cys-Leu)
S-(2-amino-4-methylpentanoyl)cysteine
S-(L-leucyl)-L-cysteine
XLNK1LeuSCys
leucine cysteine thioester
PSI-MOD
MOD:00822
Cross-link 2.
S-(L-leucyl)-L-cysteine
A protein modification that effectively crosslinks an L-leucine residue and an L-cysteine residue by a thioester bond to form S-(L-leucyl)-L-cysteine.
PubMed:12591958
RESID:AA0412
(2R)-2-amino-3-([(2S)-2-amino-4-methylpentanoyl]sulfanyl)propanoic acid
CROSSLNK Leucyl cysteine thioester (Cys-Leu)
S-(2-amino-4-methylpentanoyl)cysteine
S-(L-leucyl)-L-cysteine
XLNK1LeuSCys
leucine cysteine thioester
A protein modification that effectively crosslinks an L-methionine residue and an L-cysteine residue by a thioester bond to form S-(L-methionyl)-L-cysteine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 8 H 13 N 2 O 2 S 2
233.32
233.04184
C, M
natural
C-term
(2R)-2-amino-3-([(2S)-2-amino-4-(methylsulfanyl)butanoyl]sulfanyl)propanoic acid
CROSSLNK Methionyl cysteine thioester (Cys-Met)
S-(2-amino-4-methylthiobutanoyl)cysteine
S-(L-methionyl)-L-cysteine
XLNK1MetSCys
methionine cysteine thioester
PSI-MOD
MOD:00823
Cross-link 2.
S-(L-methionyl)-L-cysteine
A protein modification that effectively crosslinks an L-methionine residue and an L-cysteine residue by a thioester bond to form S-(L-methionyl)-L-cysteine.
PubMed:12146974
RESID:AA0413
(2R)-2-amino-3-([(2S)-2-amino-4-(methylsulfanyl)butanoyl]sulfanyl)propanoic acid
CROSSLNK Methionyl cysteine thioester (Cys-Met)
S-(2-amino-4-methylthiobutanoyl)cysteine
S-(L-methionyl)-L-cysteine
XLNK1MetSCys
methionine cysteine thioester
A protein modification that effectively converts an L-tyrosine residue to dehydroalanine.
-94.11
C -6 H -6 N 0 O -1
-94.04186
C 3 H 3 N 1 O 1
69.06
69.02146
Y
natural
Unimod:400
uniprot.ptm:PTM-0647
2,3-didehydroalanine
2-aminoacrylic acid
2-aminopropenoic acid
4-methylidene-imidazole-5-one (MIO) active site
Dha
anhydroserine
dHAla(Tyr)
dehydroalanine
PSI-MOD
MOD:00824
incidental to RESID:AA0178
dehydroalanine (Tyr)
A protein modification that effectively converts an L-tyrosine residue to dehydroalanine.
PubMed:10220322
PubMed:1547888
PubMed:1815586
PubMed:2914619
PubMed:6838602
PubMed:7947813
PubMed:8239649
RESID:AA0181#TYR
Unimod:400
2,3-didehydroalanine
2-aminoacrylic acid
2-aminopropenoic acid
4-methylidene-imidazole-5-one (MIO) active site
Dha
anhydroserine
dHAla(Tyr)
dehydroalanine
A protein modification that effectively crosslinks an L-phenylalanine residue and an L-cysteine residue by a thioester bond to form S-(L-phenylalaninyl)-L-cysteine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 12 H 13 N 2 O 2 S 1
249.31
249.06978
C, F
natural
C-term
(2R)-2-amino-3-([(2S)-2-amino-3-phenylpropanoyl]sulfanyl)propanoic acid
CROSSLNK Phenylalanyl cysteine thioester (Cys-Phe)
S-(2-amino-3-phenylpropanoyl)cysteine
S-(L-phenylalanyl)-L-cysteine
XLNK1PheSCys
phenylalanine cysteine thioester
PSI-MOD
MOD:00825
Cross-link 2.
S-(L-phenylalanyl)-L-cysteine
A protein modification that effectively crosslinks an L-phenylalanine residue and an L-cysteine residue by a thioester bond to form S-(L-phenylalaninyl)-L-cysteine.
PubMed:12591958
RESID:AA0414
(2R)-2-amino-3-([(2S)-2-amino-3-phenylpropanoyl]sulfanyl)propanoic acid
CROSSLNK Phenylalanyl cysteine thioester (Cys-Phe)
S-(2-amino-3-phenylpropanoyl)cysteine
S-(L-phenylalanyl)-L-cysteine
XLNK1PheSCys
phenylalanine cysteine thioester
A protein modification that effectively crosslinks an L-threonine residue and an L-cysteine residue by a thioester bond to form S-(L-threonyl)-L-cysteine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 7 H 11 N 2 O 3 S 1
203.24
203.04904
C, T
natural
C-term
(2R)-2-amino-3-([(2S,3R)-2-amino-3-hydroxybutanoyl]sulfanyl)propanoic acid
CROSSLNK Threonyl cysteine thioester (Cys-Thr)
S-(2-amino-3-hydroxybutanoyl)cysteine
S-(L-threonyl)-L-cysteine
XLNK1ThrSCys
threonine cysteine thioester
PSI-MOD
MOD:00826
Cross-link 2.
S-(L-threonyl)-L-cysteine
A protein modification that effectively crosslinks an L-threonine residue and an L-cysteine residue by a thioester bond to form S-(L-threonyl)-L-cysteine.
PubMed:15268951
RESID:AA0415
(2R)-2-amino-3-([(2S,3R)-2-amino-3-hydroxybutanoyl]sulfanyl)propanoic acid
CROSSLNK Threonyl cysteine thioester (Cys-Thr)
S-(2-amino-3-hydroxybutanoyl)cysteine
S-(L-threonyl)-L-cysteine
XLNK1ThrSCys
threonine cysteine thioester
A protein modification that effectively crosslinks an L-tyrosine residue and an L-cysteine residue by a thioester bond to form S-(L-tyrosyl)-L-cysteine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 12 H 13 N 2 O 3 S 1
265.31
265.0647
C, Y
natural
C-term
(2R)-2-amino-3-([(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]sulfanyl)propanoic acid
CROSSLNK Tyrosyl cysteine thioester (Cys-Tyr)
S-(L-tyrosyl)-L-cysteine
S-[2-amino-3-(4-hydoxyphenyl)propanoyl]cysteine
XLNK1TyrSCys
tyrosine cysteine thioester
PSI-MOD
MOD:00827
Cross-link 2.
S-(L-tyrosyl)-L-cysteine
A protein modification that effectively crosslinks an L-tyrosine residue and an L-cysteine residue by a thioester bond to form S-(L-tyrosyl)-L-cysteine.
PubMed:11807079
RESID:AA0416
(2R)-2-amino-3-([(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]sulfanyl)propanoic acid
CROSSLNK Tyrosyl cysteine thioester (Cys-Tyr)
S-(L-tyrosyl)-L-cysteine
S-[2-amino-3-(4-hydoxyphenyl)propanoyl]cysteine
XLNK1TyrSCys
tyrosine cysteine thioester
A protein modification that effectively crosslinks an L-tryptophan residue and an L-cysteine residue by a thioester bond to form S-(L-tryptophanyl)-L-cysteine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 14 H 14 N 3 O 2 S 1
288.35
288.08066
C, W
natural
C-term
(2R)-2-amino-3-([(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]sulfanyl)propanoic acid
CROSSLNK Tryptophanyl cysteine thioester (Cys-Trp)
S-(L-tryptophanyl)-L-cysteine
S-[2-amino-3-(1H-indol-3-yl)propanoyl]cysteine
XLNK1TrpSCys
tryptophan cysteine thioester
PSI-MOD
MOD:00828
Cross-link 2.
S-(L-tryptophanyl)-L-cysteine
A protein modification that effectively crosslinks an L-tryptophan residue and an L-cysteine residue by a thioester bond to form S-(L-tryptophanyl)-L-cysteine.
PubMed:16030216
RESID:AA0417
(2R)-2-amino-3-([(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]sulfanyl)propanoic acid
CROSSLNK Tryptophanyl cysteine thioester (Cys-Trp)
S-(L-tryptophanyl)-L-cysteine
S-[2-amino-3-(1H-indol-3-yl)propanoyl]cysteine
XLNK1TrpSCys
tryptophan cysteine thioester
A protein modification that effectively crosslinks an L-phenylalanine residue and an L-serine residue by an ester bond to form S-(L-phenylalaninyl)-L-serine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 12 H 13 N 2 O 3
233.25
233.09262
F, S
natural
C-term
(2S)-2-amino-3-([(2S)-2-amino-3-phenylpropanoyl]oxy)propanoic acid
CROSSLNK Phenylalanyl serine ester (Ser-Phe)
O-(2-amino-3-phenylpropanoyl)serine
O-(L-phenylalanyl)-L-serine
XLNK1PheOSer
phenylalanine serine ester
PSI-MOD
MOD:00829
Cross-link 2.
O-(L-phenylalanyl)-L-serine
A protein modification that effectively crosslinks an L-phenylalanine residue and an L-serine residue by an ester bond to form S-(L-phenylalaninyl)-L-serine.
PubMed:12591958
RESID:AA0418
(2S)-2-amino-3-([(2S)-2-amino-3-phenylpropanoyl]oxy)propanoic acid
CROSSLNK Phenylalanyl serine ester (Ser-Phe)
O-(2-amino-3-phenylpropanoyl)serine
O-(L-phenylalanyl)-L-serine
XLNK1PheOSer
phenylalanine serine ester
A protein modification that effectively converts an L-proline residue to an N-methyl-L-proline.
14.03
C 1 H 2 N 0 O 0
14.01565
C 6 H 10 N 1 O 1
112.15
112.07624
P
natural
N-term
uniprot.ptm:PTM-0219
(S)-1-methylpyrrolidine-2-carboxylic acid
1-methylpyrrolidine-2-carboxylic acid
MOD_RES N-methylproline
N-methyl-L-proline
N-methylated L-proline
NMePro
hygric acid
PSI-MOD
MOD:00830
Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG].
N-methyl-L-proline
A protein modification that effectively converts an L-proline residue to an N-methyl-L-proline.
PubMed:3127388
RESID:AA0419
(S)-1-methylpyrrolidine-2-carboxylic acid
1-methylpyrrolidine-2-carboxylic acid
MOD_RES N-methylproline
N-methyl-L-proline
N-methylated L-proline
NMePro
hygric acid
A protein modification that effectively converts an L-asparagine residue to N4-(N-acetylaminoglucosyl)-L-asparagine.
203.19
C 8 H 13 N 1 O 5
203.07938
C 12 H 19 N 3 O 7
317.3
317.1223
N
natural
uniprot.ptm:PTM-0527
CARBOHYD N-linked (GlcNAc) asparagine
N4GlcNAcAsn
PSI-MOD
HexNAc
MOD:00831
N4-(N-acetylamino)glucosyl-L-asparagine
A protein modification that effectively converts an L-asparagine residue to N4-(N-acetylaminoglucosyl)-L-asparagine.
PubMed:111247
PubMed:1694179
PubMed:5490222
RESID:AA0151#var
CARBOHYD N-linked (GlcNAc) asparagine
N4GlcNAcAsn
HexNAc
A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminogalactosyl)-L-asparagine.
203.19
C 8 H 13 N 1 O 5
203.07938
C 12 H 19 N 3 O 7
317.3
317.1223
N
natural
uniprot.ptm:PTM-0512
(2S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)amino-4-oxobutanoic acid
CARBOHYD N-linked (GalNAc) asparagine
N4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)-L-asparagine
N4-(2-acetylamino-2-deoxy-beta-D-galactopyranosyl)-L-asparagine
N4-(N-acetylamino)galactosyl-L-asparagine
N4-(N-acetylgalactosaminyl)asparagine
N4-asparagine-beta-N-acetylgalactosaminide
N4-glycosyl-L-asparagine
N4-glycosylasparagine
N4GalNAcAsn
PSI-MOD
HexNAc
MOD:00832
N4-(N-acetylamino)galactosyl-L-asparagine
A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminogalactosyl)-L-asparagine.
PubMed:8262914
RESID:AA0420
(2S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)amino-4-oxobutanoic acid
CARBOHYD N-linked (GalNAc) asparagine
N4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)-L-asparagine
N4-(2-acetylamino-2-deoxy-beta-D-galactopyranosyl)-L-asparagine
N4-(N-acetylamino)galactosyl-L-asparagine
N4-(N-acetylgalactosaminyl)asparagine
N4-asparagine-beta-N-acetylgalactosaminide
N4-glycosyl-L-asparagine
N4-glycosylasparagine
N4GalNAcAsn
HexNAc
A protein modification that effectively converts an L-asparagine residue to N4-glucosyl-asparagine.
162.14
C 6 H 10 N 0 O 5
162.05283
C 10 H 16 N 2 O 7
276.25
276.09576
N
natural
uniprot.ptm:PTM-0517
(2S)-2-amino-4-(D-glucopyranosyl)amino-4-oxobutanoic acid
CARBOHYD N-linked (Glc)
CARBOHYD N-linked (Glc) asparagine
N4-(D-glucopyranosyl)-L-asparagine
N4-asparagine-glucoside
N4-glucosyl-L-asparagine
N4-glucosylasparagine
N4-glycosyl-L-asparagine
N4-glycosylasparagine
N4GlcAsn
PSI-MOD
MOD:00833
N4-glucosyl-L-asparagine
A protein modification that effectively converts an L-asparagine residue to N4-glucosyl-asparagine.
PubMed:1569073
PubMed:3410849
RESID:AA0421
(2S)-2-amino-4-(D-glucopyranosyl)amino-4-oxobutanoic acid
CARBOHYD N-linked (Glc)
CARBOHYD N-linked (Glc) asparagine
N4-(D-glucopyranosyl)-L-asparagine
N4-asparagine-glucoside
N4-glucosyl-L-asparagine
N4-glucosylasparagine
N4-glycosyl-L-asparagine
N4-glycosylasparagine
N4GlcAsn
A protein modification that effectively converts an L-serine residue to O3-(N-acetamino)fucosylserine.
187.19
C 8 H 13 N 1 O 4
187.08446
C 11 H 18 N 2 O 6
274.27
274.1165
S
natural
uniprot.ptm:PTM-0553
(2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-fucopyranosyloxy)propanoic acid
CARBOHYD O-linked (FucNAc) serine
O-(2-acetylamino-2-deoxy-beta-D-fucopyranosyl)-L-serine
O-(N-acetylamino)fucosyl-L-serine
O-(N-acetylfucosaminyl)serine
O-seryl-beta-N-acetylfucosaminide
O3-(2-acetamido-2-deoxy-beta-D-fucopyranosyl)-L-serine
O3-(N-acetylfucosaminyl)serine
OFucNAcSer
PSI-MOD
MOD:00834
O-(N-acetylamino)fucosyl-L-serine
A protein modification that effectively converts an L-serine residue to O3-(N-acetamino)fucosylserine.
PubMed:11342554
PubMed:12010970
RESID:AA0422
(2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-fucopyranosyloxy)propanoic acid
CARBOHYD O-linked (FucNAc) serine
O-(2-acetylamino-2-deoxy-beta-D-fucopyranosyl)-L-serine
O-(N-acetylamino)fucosyl-L-serine
O-(N-acetylfucosaminyl)serine
O-seryl-beta-N-acetylfucosaminide
O3-(2-acetamido-2-deoxy-beta-D-fucopyranosyl)-L-serine
O3-(N-acetylfucosaminyl)serine
OFucNAcSer
A protein modification that effectively converts an L-serine residue to L-oxoalanine.
-2.02
C 0 H -2 N 0 O 0
-2.01565
C 3 H 3 N 1 O 2
85.06
85.01638
S
natural
Unimod:401
(S)-2-amino-3-oxopropanoic acid
2-amino-3-oxopropionic acid
L-3-oxoalanine
L-amino-malonic acid semialdehyde
L-aminomalonaldehydic acid
MOD_RES 3-oxoalanine (Ser)
formylglycine (from serine)
PSI-MOD
C(alpha)-formylglycine
Didehydro
L-serinesemialdehyde
dehydrogenated serine residue
formylglycine
oxoalanine
MOD:00835
L-3-oxoalanine (Ser)
A protein modification that effectively converts an L-serine residue to L-oxoalanine.
DeltaMass:349
PubMed:14563551
PubMed:7628016
PubMed:8681943
PubMed:9276974
PubMed:9478923
RESID:AA0185#SER
Unimod:401#S
(S)-2-amino-3-oxopropanoic acid
2-amino-3-oxopropionic acid
L-3-oxoalanine
L-amino-malonic acid semialdehyde
L-aminomalonaldehydic acid
MOD_RES 3-oxoalanine (Ser)
formylglycine (from serine)
C(alpha)-formylglycine
Didehydro
L-serinesemialdehyde
dehydrogenated serine residue
formylglycine
oxoalanine
A protein modification that effectively substitutes two (2)H deuterium atoms for two (1)H protium atoms.
D(H)2Res
PSI-MOD
MOD:00836
deuterium disubstituted residue
A protein modification that effectively substitutes two (2)H deuterium atoms for two (1)H protium atoms.
PubMed:18688235
D(H)2Res
A protein modification that effectively substitutes four (2)H deuterium atoms for four (1)H protium atoms.
D(H)4Res
PSI-MOD
MOD:00837
deuterium tetrasubstituted residue
A protein modification that effectively substitutes four (2)H deuterium atoms for four (1)H protium atoms.
PubMed:18688235
D(H)4Res
A protein modification that effectively substitutes three (1)H protium atoms with three (2)H deuterium atoms to produce 3x(2)H labeled L-leucine.
3.02
(1)H -3 (2)H 3
3.01883
C 6 (1)H 8 (2)H 3 N 1 O 1
116.1
116.1029
L
artifact
Unimod:262
D(H)3Leu
PSI-MOD
Label:2H(3)
Trideuteration
MOD:00838
3x(2)H labeled L-leucine
A protein modification that effectively substitutes three (1)H protium atoms with three (2)H deuterium atoms to produce 3x(2)H labeled L-leucine.
Unimod:262#L
D(H)3Leu
Label:2H(3)
Trideuteration
A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing deuteriumm, (2)H.
PSI-MOD
MOD:00839
(2)H deuterium labeled residue
A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing deuteriumm, (2)H.
PubMed:18688235
A protein modification produced by formation of an adduct with an isocyanate compound.
PSI-MOD
MOD:00840
isocyanate reagent derivatized residue
A protein modification produced by formation of an adduct with an isocyanate compound.
PubMed:18688235
A protein modification produced by formation of an adduct with an isothiocyanate compound.
PSI-MOD
MOD:00841
isothiocyanate reagent derivatized residue
A protein modification produced by formation of an adduct with an isothiocyanate compound.
PubMed:18688235
A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (13)C.
PSI-MOD
MOD:00842
(13)C labeled residue
A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (13)C.
PubMed:18688235
A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (15)N.
PSI-MOD
MOD:00843
(15)N labeled residue
A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (15)N.
PubMed:18688235
A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (18)O.
PSI-MOD
MOD:00844
(18)O labeled residue
A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (18)O.
PubMed:18688235
A protein modification that effectively substitutes one or more (18)O atoms for (16)O atoms.
PSI-MOD
MOD:00845
(18)O substituted residue
A protein modification that effectively substitutes one or more (18)O atoms for (16)O atoms.
PubMed:18688235
stub
PSI-MOD
MOD:00846
levuglandinyl (prostaglandin H2) adduct
stub
PubMed:18688235
A protein modification that effectively substitutes two (18)O atom for two (16)O atoms.
PSI-MOD
MOD:00847
(18)O disubstituted residue
A protein modification that effectively substitutes two (18)O atom for two (16)O atoms.
PubMed:18688235
A protein modification that is produced by formation of an adduct with a particular compound used as a reagent.
PSI-MOD
MOD:00848
reagent derivatized residue
A protein modification that is produced by formation of an adduct with a particular compound used as a reagent.
PubMed:18688235
A protein modification that effectively substitutes a potassium atom for a hydrogen atom.
KRes
PSI-MOD
MOD:00849
potassium containing modified residue
A protein modification that effectively substitutes a potassium atom for a hydrogen atom.
PubMed:18688235
KRes
A protein modification that inserts or replaces a residue with an unnatural residue that is not considered to be derived from a natural residue by some chemical process.
PSI-MOD
MOD:00850
unnatural residue
A protein modification that inserts or replaces a residue with an unnatural residue that is not considered to be derived from a natural residue by some chemical process.
PubMed:18688235
A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with (18)O.
X
artifact
PSI-MOD
MOD:00851
(18)O labeled deamidated residue
A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with (18)O.
PubMed:18688235
A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with one (18)O.
2.99
H -1 N -1 (18)O 1
2.988262
X
artifact
Unimod:366
PSI-MOD
MOD:00852
1x(18)O labeled deamidated residue
A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with one (18)O.
PubMed:8382902
Unimod:366
A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with two (18)O.
4.99
H -1 N -1 (16)O -1 (18)O 2
4.992508
X
artifact
PSI-MOD
MOD:00853
2x(18)O labeled deamidated residue
A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with two (18)O.
PubMed:18688235
A protein modification that effectively converts an L-lysine to L-lysinium (protonated L-lysine).
1.01
C 0 H 1 N 0 O 0
1.007276
1+
C 6 H 13 N 2 O 1
129.18
129.10223
K
natural
PSI-MOD
MOD:00854
Some sources compute the difference formula for charged, quatenary modified lysine based on protonated lysine rather than neutral lysine residue. In such cases, a comparable difference formula can be calculated based on this derivative.
protonated L-lysine (L-lysinium) residue
A protein modification that effectively converts an L-lysine to L-lysinium (protonated L-lysine).
PubMed:18688235
A protein modification that effectively converts an L-lysinium (N6-protonated L-lysine) residue to an N6,N6,N6-trimethyl-L-lysine.
42.08
C 3 H 6 N 0 O 0
42.046402
1+
C 9 H 19 N 2 O 1
171.26
171.14919
MOD:00854
natural
Unimod:37
N6Me3Lys
trimethylk
PSI-MOD
MOD:00855
For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative N6Me3+Lys process (MOD:00083) accounts for both protonation and trimethylation.
N6,N6,N6-trimethyl-L-lysine (from L-lysinium residue)
A protein modification that effectively converts an L-lysinium (N6-protonated L-lysine) residue to an N6,N6,N6-trimethyl-L-lysine.
DeltaMass:0
OMSSA:15
PubMed:12590383
PubMed:3145979
PubMed:4304194
PubMed:6778808
PubMed:7093227
PubMed:8453381
Unimod:37#K
N6Me3Lys
trimethylk
A protein modification that effectively converts an L-alanine residue to an L-alaninium (protonated L-alanine).
1.01
C 0 H 1 N 0 O 0
1.007276
1+
C 3 H 7 N 1 O 1
73.09
73.052216
A
natural
N-term
PSI-MOD
MOD:00856
protonated L-alanine (L-alaninium) residue
A protein modification that effectively converts an L-alanine residue to an L-alaninium (protonated L-alanine).
PubMed:18688235
A protein modification that effectively converts an L-alaninium (protonated L-alanine) residue to an N,N,N-trimethyl-L-alanine.
42.08
C 3 H 6 N 0 O 0
42.046402
1+
C 6 H 13 N 1 O 1
115.18
115.09917
MOD:00856
natural
N-term
Unimod:37
N2Me3Ala
PSI-MOD
MOD:00857
For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative N2Me3+Ala process (MOD:00071) accounts for both protonation and trimethylation.
N,N,N-trimethyl-L-alanine (from L-alaninium)
A protein modification that effectively converts an L-alaninium (protonated L-alanine) residue to an N,N,N-trimethyl-L-alanine.
PubMed:12590383
PubMed:332162
PubMed:3979397
PubMed:6778808
PubMed:7715456
Unimod:37#A
N2Me3Ala
A protein modification that effectively converts an L-serine residue to D-alanine.
-16.0
C 0 H 0 N 0 O -1
-15.994915
C 3 H 5 N 1 O 1
71.08
71.03712
S
natural
uniprot.ptm:PTM-0113
(R)-2-aminopropanoic acid
D-Ala(Ser)
D-alanine
MOD_RES D-alanine (Ser)
PSI-MOD
MOD:00858
D-alanine (Ser)
A protein modification that effectively converts an L-serine residue to D-alanine.
PubMed:7961627
RESID:AA0191#SER
(R)-2-aminopropanoic acid
D-Ala(Ser)
D-alanine
MOD_RES D-alanine (Ser)
A protein modification that can be derived from different natural residues by different chemical processes.
X
natural
PSI-MOD
MOD:00859
modified residue that can arise from different natural residues
A protein modification that can be derived from different natural residues by different chemical processes.
PubMed:18688235
A protein modification that produces an amino acid residue containing an exogenous sulfur atom.
PSI-MOD
MOD:00860
sulfur containing modified residue
A protein modification that produces an amino acid residue containing an exogenous sulfur atom.
PubMed:18688235
A protein modification that produces an amino acid residue containing a phosphorus atom.
PSI-MOD
MOD:00861
phosphorus containing modified residue
A protein modification that produces an amino acid residue containing a phosphorus atom.
PubMed:18688235
A protein modification that effectively converts a source amino acid residue to D-alanine.
C 3 H 5 N 1 O 1
71.08
71.03712
X
natural
(R)-2-aminopropanoic acid
D-alanine
MOD_RES D-alanine (Ala)
MOD_RES D-alanine (Ser)
PSI-MOD
MOD:00862
D-alanine
A protein modification that effectively converts a source amino acid residue to D-alanine.
ChEBI:29949
PubMed:7287302
PubMed:7961627
RESID:AA0191
(R)-2-aminopropanoic acid
D-alanine
MOD_RES D-alanine (Ala)
MOD_RES D-alanine (Ser)
A protein modification that effectively converts an L-threonine residue to D-allo-threonine.
0.0
C 0 H 0 N 0 O 0
0.0
C 4 H 7 N 1 O 2
101.1
101.047676
T
natural
uniprot.ptm:PTM-0310
(2R,3R)-2-amino-3-hydroxybutanoic acid
D-Thr
D-threonine
MOD_RES D-threonine
PSI-MOD
MOD:00863
D-allo-threonine
A protein modification that effectively converts an L-threonine residue to D-allo-threonine.
ChEBI:32826
PubMed:18025465
PubMed:6893271
RESID:AA0199
(2R,3R)-2-amino-3-hydroxybutanoic acid
D-Thr
D-threonine
MOD_RES D-threonine
A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-histidino diiron disulfide.
171.78
C 0 Fe 2 H -4 N 0 O 0 S 2
171.78381
2-
C 15 Fe 2 H 18 N 6 O 4 S 5
618.34
617.8703
C, C, C, H
natural
CDGSH domain iron-sulfur cluster
METAL Iron-sulfur (2Fe-2S)
METAL Iron-sulfur (2Fe-2S); via pros nitrogen
di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-N3'-histidinoiron)
tris-L-cysteinyl L-histidino diiron disulfide
PSI-MOD
MOD:00864
Cross-link 4.
tris-L-cysteinyl L-histidino diiron disulfide
A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-histidino diiron disulfide.
PubMed:17766439
PubMed:17766440
RESID:AA0438
CDGSH domain iron-sulfur cluster
METAL Iron-sulfur (2Fe-2S)
METAL Iron-sulfur (2Fe-2S); via pros nitrogen
di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-N3'-histidinoiron)
tris-L-cysteinyl L-histidino diiron disulfide
A protein modification that effectively converts an L-aspartic acid residue to N-aspartyl-glycosylsphingolipidinositolethanolamine.
123.05
C 2 H 6 N 1 O 3 P 1
123.00853
C 6 H 12 N 2 O 7 P 1
255.14
255.03821
D
hypothetical
C-term
uniprot.ptm:PTM-0322
GSIAsp
LIPID GPI-like-anchor amidated aspartate
N-aspartyl-glycosylsphingolipidinositolethanolamine
PSI-MOD
MOD:00865
N-aspartyl-glycosylsphingolipidinositolethanolamine
A protein modification that effectively converts an L-aspartic acid residue to N-aspartyl-glycosylsphingolipidinositolethanolamine.
RESID:AA0439
GSIAsp
LIPID GPI-like-anchor amidated aspartate
N-aspartyl-glycosylsphingolipidinositolethanolamine
A protein modification that effectively converts an L-proline residue to one of several dihydroxylated proline residues, such as (2S,3R,4R)-3,4-dihydroxyproline or (2S,3R,4S)-3,4-dihydroxyproline.
32.0
C 0 H 0 N 0 O 2
31.989828
C 5 H 7 N 1 O 3
129.12
129.04259
P
natural
uniprot.ptm:PTM-0024
Hy2Pro
PSI-MOD
MOD:00866
dihydroxylated proline
A protein modification that effectively converts an L-proline residue to one of several dihydroxylated proline residues, such as (2S,3R,4R)-3,4-dihydroxyproline or (2S,3R,4S)-3,4-dihydroxyproline.
PubMed:18688235
Hy2Pro
A protein modification that effectively cross-links an L-cysteine residue and an L-cysteine converted to an L-selenocysteine residue to form L-cysteinyl-L-selenocystine.
44.9
C 0 H -2 N 0 O 0 S -1 Se 1
45.9288
C 6 H 8 N 2 O 2 S 1 Se 1
251.17
251.94717
C, C
natural
(R,R)-2-amino-3-[3-(2-aminopropanoic acid)sulfanyl]selanylpropanoic acid
CROSSLNK Cysteinyl-selenocysteine (Cys-Sec)
CROSSLNK Cysteinyl-selenocysteine (Sec-Cys)
L-cysteinyl-L-selenocysteine
PSI-MOD
MOD:00867
Cross-link 2.
L-cysteinyl-L-selenocysteine (Cys-Cys)
A protein modification that effectively cross-links an L-cysteine residue and an L-cysteine converted to an L-selenocysteine residue to form L-cysteinyl-L-selenocystine.
PubMed:10801974
PubMed:12911312
PubMed:17177418
RESID:AA0358#CYS
(R,R)-2-amino-3-[3-(2-aminopropanoic acid)sulfanyl]selanylpropanoic acid
CROSSLNK Cysteinyl-selenocysteine (Cys-Sec)
CROSSLNK Cysteinyl-selenocysteine (Sec-Cys)
L-cysteinyl-L-selenocysteine
A protein modification that inserts or replaces a residue with a natural, non-standard encoded residue, such as N-formyl-L-methionine, L-selenocysteine, or L-pyrrolysine.
X
natural
PSI-MOD
MOD:00868
These are produced exclusively by modification of amino acids acylated to special tRNA before incorporation by ribosomes into proteins. For this reason, they have also been referred to as pre-translational modifications.
natural, non-standard encoded residue
A protein modification that inserts or replaces a residue with a natural, non-standard encoded residue, such as N-formyl-L-methionine, L-selenocysteine, or L-pyrrolysine.
PubMed:18688235
A protein modification that effectively converts an L-aspartic acid residue to L-alanine.
-44.01
C -1 H 0 N 0 O -2
-43.98983
C 3 H 5 N 1 O 1
71.08
71.03712
D
natural
uniprot.ptm:PTM-0314
(2S)-2-aminopropanoic acid
2-aminopropionic acid
2-azanylpropanoic acid
Asp(Ala)
L-alanine
MOD_RES Beta-decarboxylated aspartate
alpha-alanine
alpha-aminopropionic acid
PSI-MOD
MOD:00869
This has been reported to occur by a natural process of beta-decarboxylation.
L-alanine residue (Asp)
A protein modification that effectively converts an L-aspartic acid residue to L-alanine.
PubMed:17138938
RESID:AA0001#ASP
(2S)-2-aminopropanoic acid
2-aminopropionic acid
2-azanylpropanoic acid
Asp(Ala)
L-alanine
MOD_RES Beta-decarboxylated aspartate
alpha-alanine
alpha-aminopropionic acid
A protein modification produced by formation of an adduct with phenyl isocyanate.
119.12
C 7 H 5 N 1 O 1
119.03712
X
artifact
N-term
Unimod:411
PSI-MOD
Phenylisocyanate
phenyl isocyanate
MOD:00870
From Unimod with no citation.
phenyl isocyanate derivatized residue
A protein modification produced by formation of an adduct with phenyl isocyanate.
Unimod:411
Phenylisocyanate
phenyl isocyanate
A protein modification produced by formation of an adduct with (2)H5-phenyl isocyanate.
124.07
C 7 (2)H 5 N 1 O 1
124.0685
X
artifact
N-term
Unimod:412
PSI-MOD
Phenylisocyanate:2H(5)
d5-phenyl isocyanate
MOD:00871
From Unimod with no citation.
(2)H5-phenyl isocyanate derivatized residue
A protein modification produced by formation of an adduct with (2)H5-phenyl isocyanate.
Unimod:412
Phenylisocyanate:2H(5)
d5-phenyl isocyanate
OBSOLETE because redundant and identical to MOD:01970. Remap to MOD:01970.
MOD:01970
129.12
C 5 H 7 N 1 O 3
129.04259
C 10 H 14 N 2 O 6
258.23
258.08517
E
natural
Unimod:450
N alpha -(gamma-Glutamyl)-Glu
PSI-MOD
Glu
monoglutamyl
MOD:00872
L-isoglutamyl monoglutamic acid
true
OBSOLETE because redundant and identical to MOD:01970. Remap to MOD:01970.
PubMed:10747868
PubMed:15525938
PubMed:1680872
RESID:AA0202#var
Unimod:450
N alpha -(gamma-Glutamyl)-Glu
Glu
monoglutamyl
A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamic acid, forming an isopeptide bond with a diglutamic acid.
258.23
C 10 H 14 N 2 O 6
258.08517
C 15 H 21 N 3 O 9
387.35
387.12778
E
natural
Unimod:451
PSI-MOD
GluGlu
diglutamyl
MOD:00873
L-isoglutamyl diglutamic acid
A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamic acid, forming an isopeptide bond with a diglutamic acid.
DeltaMass:0
PubMed:10747868
PubMed:1680872
RESID:AA0202#var
Unimod:451
GluGlu
diglutamyl
A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamyl-glutamic acid, forming an isopeptide bond with a triglutamic acid.
387.35
C 15 H 21 N 3 O 9
387.12778
C 20 H 28 N 4 O 12
516.46
516.17035
E
natural
Unimod:452
N alpha -(gamma-Glutamyl)-Glu3
PSI-MOD
GluGluGlu
triglutamyl
MOD:00874
From DeltaMass: Average Mass: 388.
L-isoglutamyl triglutamic acid
A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamyl-glutamic acid, forming an isopeptide bond with a triglutamic acid.
DeltaMass:0
PubMed:10747868
PubMed:1680872
RESID:AA0202#var
Unimod:452
N alpha -(gamma-Glutamyl)-Glu3
GluGluGlu
triglutamyl
A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamyl-glutamyl-glutamic acid, forming an isopeptide bond with a tetraglutamic acid.
516.46
C 20 H 28 N 4 O 12
516.17035
C 25 H 35 N 5 O 15
645.57
645.21295
E
natural
Unimod:453
PSI-MOD
GluGluGluGlu
tetraglutamyl
MOD:00875
L-isoglutamyl tetraglutamic acid
A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl glutamyl-glutamyl-glutamyl-glutamic acid, forming an isopeptide bond with a tetraglutamic acid.
PubMed:10747868
PubMed:1680872
RESID:AA0202#var
Unimod:453
GluGluGluGlu
tetraglutamyl
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexosamine sugar group through a glycosidic bond.
161.16
C 6 H 11 N 1 O 4
161.0688
X
natural
Unimod:454
Hexosamines (GalN, GlcN)
PSI-MOD
HexN
Hexosamine
MOD:00876
hexosaminylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a hexosamine sugar group through a glycosidic bond.
Unimod:454
Hexosamines (GalN, GlcN)
HexN
Hexosamine
dimethyl pimelimidate modification from Unimod
154.21
C 8 H 14 N 2 O 1
154.11061
X
artifact
Unimod:455
PSI-MOD
One end of crosslink attached, one end free
Xlink:DMP-s
MOD:00877
imidoester crosslink dimethyl pimelimidate singly attached
dimethyl pimelimidate modification from Unimod
URL:http://www.piercenet.com/files/0668ss5.pdf
Unimod:455
One end of crosslink attached, one end free
Xlink:DMP-s
dimethyl pimelimidate modification from Unimod - Mechanism of the reaction of imidoesters with amines
122.17
C 7 H 10 N 2
122.0844
X
artifact
Unimod:456
PSI-MOD
Both ends of crosslink attached to same peptide
Xlink:DMP
MOD:00878
imidoester crosslink dimethyl pimelimidate doubly attached
dimethyl pimelimidate modification from Unimod - Mechanism of the reaction of imidoesters with amines
PubMed:7171546
URL:http://dx.doi.org/10.1021/ja00877a017
Unimod:456
Both ends of crosslink attached to same peptide
Xlink:DMP
modification from Unimod
175.19
C 13 H 5 N 1
175.0422
X
artifact
Unimod:457
PSI-MOD
NDA
naphthalene-2,3-dicarboxaldehyde
MOD:00879
naphthalene-2,3-dicarboxaldehyde
modification from Unimod
PubMed:2081203
Unimod:457
NDA
naphthalene-2,3-dicarboxaldehyde
A protein modification produced by formation of an adduct with 6x(13)C labeled 4-sulfophenyl isothiocyanate.
220.99
(12)C 1 (13)C 6 H 5 N 1 O 3 S 2
220.99121
X
artifact
Unimod:464
PSI-MOD
4-sulfophenyl isothiocyanate (Heavy C13)
SPITC:13C(6)
MOD:00880
6x(13)C labeled 4-sulfophenyl isothiocyanate derivatized residue
A protein modification produced by formation of an adduct with 6x(13)C labeled 4-sulfophenyl isothiocyanate.
PubMed:15536630
PubMed:16526082
Unimod:464
4-sulfophenyl isothiocyanate (Heavy C13)
SPITC:13C(6)
OBSOLETE because Unimod entry 465 megerd with 199. Remap to MOD:00552 DiMethyl-CH2D.
MOD:00552
32.06
C 2 (2)H 4
32.056408
X
artifact
Unimod:465
PSI-MOD
MOD:00881
N-reductive amination-D
true
OBSOLETE because Unimod entry 465 megerd with 199. Remap to MOD:00552 DiMethyl-CH2D.
PubMed:9252331
Unimod:465
A protein modification that effectively converts an L-serine residue to S-(2-aminoethyl)cysteine.
59.13
C 2 H 5 N 1 O -1 S 1
59.019356
C 5 H 10 N 2 O 1 S 1
146.21
146.05139
S
artifact
Unimod:472
Aminoethyl Cysteinyl (AECys)
PSI-MOD
AEC-MAEC
aminoethylcysteine
MOD:00882
From DeltaMass: Average Mass: 146 Abbreviation:-AECys_ Formula:C5H10O2N1S1 Monoisotopic Mass Change:146.051 Average Mass Change:146.214 References:PE Sciex.
S-(2-aminoethyl)cysteine (Ser)
A protein modification that effectively converts an L-serine residue to S-(2-aminoethyl)cysteine.
DeltaMass:171
PubMed:12923550
Unimod:472#S
Aminoethyl Cysteinyl (AECys)
AEC-MAEC
aminoethylcysteine
A protein modification that effectively replaces a 1-carboxyl group (usually referred to as the alpha-carboxyl) with a carboxamido group.
-0.98
C 0 H 1 N 1 O -1
-0.984016
X
natural
C-term
Unimod:2
Amide formation (C terminus)
ResN
alpha-amidated residue
ctermamide
PSI-MOD
Amidated
Amidation
MOD:00883
The normal biological process involves formation of an amide of an amino acid residue in a peptide sequence where it is followed by a glycine and two basic residues, either arginine or lysine, although in some taxa only one basic residue is required. The peptide is cleaved after the basic residues, glycine is oxidized to hydroxyglycine, which decomposes to release a carboxamide C-terminal [JSG].
C1-amidated residue
A protein modification that effectively replaces a 1-carboxyl group (usually referred to as the alpha-carboxyl) with a carboxamido group.
DeltaMass:0
OMSSA:25
Unimod:2
Amide formation (C terminus)
ResN
alpha-amidated residue
ctermamide
Amidated
Amidation
A protein modification that effectively converts an L-cysteine residue to S-2-aminoethylcysteine.
43.07
C 2 H 5 N 1 O 0 S 0
43.0422
C 5 H 10 N 2 O 1 S 1
146.21
146.05139
C
artifact
4-thialysine
L-cysteine aziridine adduct
S-(2-aminoethyl)-L-cysteine
PSI-MOD
MOD:00884
This modified residue is a chemical isolog of L-lysine for trypsin hydolysis produced from L-cysteine by aziridine.
S-aminoethylcysteine (Cys)
A protein modification that effectively converts an L-cysteine residue to S-2-aminoethylcysteine.
PubMed:1175632
PubMed:18688235
4-thialysine
L-cysteine aziridine adduct
S-(2-aminoethyl)-L-cysteine
A protein modification that crosslinks two residues by formation of an ester bond.
PSI-MOD
MOD:00885
ester crosslinked residues
A protein modification that crosslinks two residues by formation of an ester bond.
PubMed:18688235
A protein modification that effectively converts an L-tryptophan residue to 6'-chloro-L-tryptophan.
34.44
C 0 Cl 1 H -1 N 0 O 0
33.96103
C 11 Cl 1 H 9 N 2 O 1
220.66
220.04034
W
natural
Unimod:936
uniprot.ptm:PTM-0052
(2S)-2-amino-3-(6-chloro-1H-indol-3-yl)propanoic acid
6'-ClTrp
6'-chloro-L-tryptophan
MOD_RES 6'-chlorotryptophan
PSI-MOD
MOD:00886
The Unimod:340 cross-reference to RESID:AA0180 is incorrect. RESID:AA0180 should be cross-referenced by Unimod:936 [JSG].
6'-chloro-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to 6'-chloro-L-tryptophan.
PubMed:9033387
RESID:AA0180
Unimod:936#W
(2S)-2-amino-3-(6-chloro-1H-indol-3-yl)propanoic acid
6'-ClTrp
6'-chloro-L-tryptophan
MOD_RES 6'-chlorotryptophan
A protein modification that effectively converts an L-aspartic acid residue to a methylated aspartic acid, such as aspartic acid 4-methyl ester.
PSI-MOD
MOD:00887
methylated aspartic acid
A protein modification that effectively converts an L-aspartic acid residue to a methylated aspartic acid, such as aspartic acid 4-methyl ester.
PubMed:18688235
A protein modification that effectively converts an L-proline to an L-prolinium (protonated L-proline).
1.01
C 0 H 1 N 0 O 0
1.007276
1+
C 5 H 9 N 1 O 1
99.13
99.06786
P
natural
N-term
PSI-MOD
MOD:00888
protonated L-proline (L-prolinium) residue
A protein modification that effectively converts an L-proline to an L-prolinium (protonated L-proline).
PubMed:18688235
A protein modification that effectively converts an L-prolinium (charged L-proline) residue to N,N-dimethyl-L-proline.
28.05
C 2 H 4 N 0 O 0
28.030752
1+
C 7 H 13 N 1 O 1
127.19
127.09917
MOD:00888
natural
N-term
Unimod:36
PSI-MOD
MOD:00889
N,N-dimethyl-L-proline (from L-prolinium)
A protein modification that effectively converts an L-prolinium (charged L-proline) residue to N,N-dimethyl-L-proline.
Unimod:36#P
A protein modification that effectively converts an L-histidine residue to a phosphorylated L-histidine, such as pros-phosphohistidine, or tele-phosphohistidine.
79.98
C 0 H 1 N 0 O 3 P 1
79.96633
C 6 H 8 N 3 O 4 P 1
217.12
217.02524
H
natural
Unimod:21
uniprot.ptm:PTM-0252
NPhosHis
mod192
phosphohistidine
PSI-MOD
Phospho
MOD:00890
phosphorylated L-histidine
A protein modification that effectively converts an L-histidine residue to a phosphorylated L-histidine, such as pros-phosphohistidine, or tele-phosphohistidine.
OMSSA:192
Unimod:21#H
NPhosHis
mod192
phosphohistidine
Phospho
A protein modification that effectively converts a source amino acid residue to D-serine.
C 3 H 5 N 1 O 2
87.08
87.03203
X
natural
(R)-2-amino-3-hydroxypropanoic acid
D-Ser
D-serine
PSI-MOD
MOD:00891
D-serine
A protein modification that effectively converts a source amino acid residue to D-serine.
ChEBI:29998
PubMed:6893271
PubMed:7973665
RESID:AA0195
(R)-2-amino-3-hydroxypropanoic acid
D-Ser
D-serine
A protein modification that effectively converts an L-cysteine residue to D-serine.
-16.06
C 0 H 0 N 0 O 1 S -1
-15.977156
C 3 H 5 N 1 O 2
87.08
87.03203
C
natural
uniprot.ptm:PTM-0309
(R)-2-amino-3-hydroxypropanoic acid
D-serine
MOD_RES D-serine (Cys)
PSI-MOD
MOD:00892
D-serine (Cys)
A protein modification that effectively converts an L-cysteine residue to D-serine.
PubMed:18025465
PubMed:6893271
RESID:AA0195#CYS
(R)-2-amino-3-hydroxypropanoic acid
D-serine
MOD_RES D-serine (Cys)
Natural or modified residues with a mass of 128.0-128.1 Da.
PSI-MOD
MOD:00893
residues isobaric at 128.0-128.1
Natural or modified residues with a mass of 128.0-128.1 Da.
PubMed:18688235
Natural or modified resiues with a mass of 128.058578 Da.
PSI-MOD
MOD:00894
residues isobaric at 128.058578 Da
Natural or modified resiues with a mass of 128.058578 Da.
PubMed:18688235
A protein modification that effectively results from forming an adduct with a compound containing a flavin adenine dinucleotide (FAD) group.
783.54
C 27 H 31 N 9 O 15 P 2
783.1415
X
natural
FADRes
PSI-MOD
MOD:00895
FAD modified residue
A protein modification that effectively results from forming an adduct with a compound containing a flavin adenine dinucleotide (FAD) group.
PubMed:18688235
FADRes
A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group.
X
natural
FMNRes
PSI-MOD
MOD:00896
FMN modified residue
A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group.
PubMed:18688235
FMNRes
A protein modification that effectively converts an L-cysteine residue to N-acetyl-S-archeol-L-cysteine.
677.2
C 45 H 88 N 0 O 3 S 0
676.67334
C 48 H 93 N 1 O 4 S 1
780.34
779.68256
C
natural
N-term
PSI-MOD
MOD:00897
N-acetyl-S-archeol-cysteine
A protein modification that effectively converts an L-cysteine residue to N-acetyl-S-archeol-L-cysteine.
RESID:AA0043#var
RESID:AA0223#var
A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine.
576.95
C 37 H 68 N 0 O 4 S 0
576.5118
C 40 H 73 N 1 O 5 S 1
680.09
679.52094
C
natural
Unimod:377
PSI-MOD
Diacylglycerol
diacylglycerol
MOD:00898
Incidental to RESID:AA0060.
S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine
A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine.
PubMed:10896212
PubMed:4575979
PubMed:9056182
RESID:AA0107#var
Unimod:377
Diacylglycerol
diacylglycerol
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-diacylglycerol-L-cysteine.
C
natural
N-term
PSI-MOD
MOD:00899
N-palmitoyl-S-diacylglycerol-L-cysteine
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-diacylglycerol-L-cysteine.
RESID:AA0069#var
RESID:AA0107#var
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine.
815.36
C 53 H 98 N 0 O 5 S 0
814.74146
C 56 H 103 N 1 O 6 S 1
918.5
917.7506
C
natural
N-term
(R)-2-hexadecanoylamino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]sulfanylpropanoic acid
2-hexadecanoylamino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]thiopropanoic acid
PSI-MOD
MOD:00900
N-palmitoyl-S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine
A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine.
PubMed:18688235
(R)-2-hexadecanoylamino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]sulfanylpropanoic acid
2-hexadecanoylamino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]thiopropanoic acid
A protein modification that modifies an L-alanine.
A
ModAla
PSI-MOD
MOD:00901
modified L-alanine residue
A protein modification that modifies an L-alanine.
PubMed:18688235
ModAla
A protein modification that modifies an L-arginine residue.
R
ModArg
PSI-MOD
MOD:00902
modified L-arginine residue
A protein modification that modifies an L-arginine residue.
PubMed:18688235
ModArg
A protein modification that modifies an L-asparagine residue.
N
ModAsn
PSI-MOD
MOD:00903
modified L-asparagine residue
A protein modification that modifies an L-asparagine residue.
PubMed:18688235
ModAsn
A protein modification that modifies an L-aspartic acid residue.
D
ModAsp
PSI-MOD
MOD:00904
modified L-aspartic acid residue
A protein modification that modifies an L-aspartic acid residue.
PubMed:18688235
ModAsp
A protein modification that modifies an L-cysteine residue.
C
ModCys
PSI-MOD
MOD:00905
modified L-cysteine residue
A protein modification that modifies an L-cysteine residue.
PubMed:18688235
ModCys
A protein modification that modifies an L-glutamic acid residue.
E
ModGlu
PSI-MOD
MOD:00906
modified L-glutamic acid residue
A protein modification that modifies an L-glutamic acid residue.
PubMed:18688235
ModGlu
A protein modification that modifies an L-glutamine residue.
Q
ModGln
PSI-MOD
MOD:00907
modified L-glutamine residue
A protein modification that modifies an L-glutamine residue.
PubMed:18688235
ModGln
A protein modification that modifies a glycine residue.
G
ModGly
PSI-MOD
MOD:00908
modified glycine residue
A protein modification that modifies a glycine residue.
PubMed:18688235
ModGly
A protein modification that modifies an L-histidine residue.
H
ModHis
PSI-MOD
MOD:00909
modified L-histidine residue
A protein modification that modifies an L-histidine residue.
PubMed:18688235
ModHis
A protein modification that modifies an L-isoleucine residue.
I
ModIle
PSI-MOD
MOD:00910
modified L-isoleucine residue
A protein modification that modifies an L-isoleucine residue.
PubMed:18688235
ModIle
A protein modification that modifies an L-leucine residue.
L
ModLeu
PSI-MOD
MOD:00911
modified L-leucine residue
A protein modification that modifies an L-leucine residue.
PubMed:18688235
ModLeu
A protein modification that modifies an L-lysine residue.
K
ModLys
PSI-MOD
MOD:00912
modified L-lysine residue
A protein modification that modifies an L-lysine residue.
PubMed:18688235
ModLys
A protein modification that modifies an L-methionine residue.
M
ModMet
PSI-MOD
MOD:00913
modified L-methionine residue
A protein modification that modifies an L-methionine residue.
PubMed:18688235
ModMet
A protein modification that modifies an L-phenylalanine residue.
F
ModPhe
PSI-MOD
MOD:00914
modified L-phenylalanine residue
A protein modification that modifies an L-phenylalanine residue.
PubMed:18688235
ModPhe
A protein modification that modifies an L-proline residue.
P
ModPro
PSI-MOD
MOD:00915
modified L-proline residue
A protein modification that modifies an L-proline residue.
PubMed:18688235
ModPro
A protein modification that modifies an L-serine residue.
S
ModSer
PSI-MOD
MOD:00916
modified L-serine residue
A protein modification that modifies an L-serine residue.
PubMed:18688235
ModSer
A protein modification that modifies an L-threonine residue.
T
ModThr
PSI-MOD
MOD:00917
modified L-threonine residue
A protein modification that modifies an L-threonine residue.
PubMed:18688235
ModThr
A protein modification that modifies an L-tryptophan residue.
W
ModTrp
PSI-MOD
MOD:00918
modified L-tryptophan residue
A protein modification that modifies an L-tryptophan residue.
PubMed:18688235
ModTrp
A protein modification that modifies an L-tyrosine residue.
Y
ModTyr
PSI-MOD
MOD:00919
modified L-tyrosine residue
A protein modification that modifies an L-tyrosine residue.
PubMed:18688235
ModTyr
A protein modification that modifies an L-valine residue.
V
ModVal
PSI-MOD
MOD:00920
modified L-valine residue
A protein modification that modifies an L-valine residue.
PubMed:18688235
ModVal
New uncategorized Unimod. OBSOLETE because organizational use is no longer required.
PSI-MOD
MOD:00921
new uncategorized Unimod entries
true
New uncategorized Unimod. OBSOLETE because organizational use is no longer required.
PubMed:18688235
modification from Unimod Chemical derivative
672.84
C 37 H 44 N 4 O 6 S 1
672.29816
C 40 H 49 N 5 O 7 S 2
775.98
775.3073
C
artifact
Unimod:494
PSI-MOD
Cy3 CyDye DIGE Fluor saturation dye
CyDye-Cy3
MOD:00922
Cy3 CyDye DIGE Fluor saturation dye
modification from Unimod Chemical derivative
Unimod:494
Cy3 CyDye DIGE Fluor saturation dye
CyDye-Cy3
modification from Unimod Chemical derivative
684.85
C 38 H 44 N 4 O 6 S 1
684.29816
C 41 H 49 N 5 O 7 S 2
787.99
787.3073
C
artifact
Unimod:495
PSI-MOD
Cy5 CyDye DIGE Fluor saturation dye
CyDye-Cy5
MOD:00923
Cy5 CyDye DIGE Fluor saturation dye
modification from Unimod Chemical derivative
Unimod:495
Cy5 CyDye DIGE Fluor saturation dye
CyDye-Cy5
A protein modification that effectively crosslinks an L-lysine residue and an L-threonine residue by an isopeptide bond to form N6-(L-threonyl)-L-lysine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 10 H 18 N 3 O 3
228.27
228.13481
K, T
natural
C-term
uniprot.ptm:PTM-0326
(2S)-2-amino-6-([(2S,3R)-2-amino-3-hydroxybutanoyl]amino)hexanoic acid
N6-(L-threonyl)-L-lysine
N6-threonyl-lysine
PSI-MOD
MOD:00924
Cross-link 2.
N6-(L-threonyl)-L-lysine
A protein modification that effectively crosslinks an L-lysine residue and an L-threonine residue by an isopeptide bond to form N6-(L-threonyl)-L-lysine.
PubMed:18063774
RESID:AA0440
(2S)-2-amino-6-([(2S,3R)-2-amino-3-hydroxybutanoyl]amino)hexanoic acid
N6-(L-threonyl)-L-lysine
N6-threonyl-lysine
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a heptose sugar group through a glycosidic bond.
192.17
C 7 H 12 O 6
192.06339
X
natural
Unimod:490
PSI-MOD
Hep
Heptose
MOD:00925
From Unimod with no citation [JSG].
heptosylated residue
A protein modification that effectively replaces a hydrogen atom of an amino acid residue or of a modifying group with a heptose sugar group through a glycosidic bond.
Unimod:490
Hep
Heptose
Modification from Unimod Non-standard residue. OBSOLETE because not an amino acid modification. From Unimod not an approved entry.
340.42
C 21 H 24 O 4
340.16745
X
artifact
Unimod:493
PSI-MOD
BADGE
Bisphenol A diglycidyl ether derivative
MOD:00926
Bisphenol A diglycidyl ether derivative
true
Modification from Unimod Non-standard residue. OBSOLETE because not an amino acid modification. From Unimod not an approved entry.
PubMed:11225353
Unimod:493
BADGE
Bisphenol A diglycidyl ether derivative
A protein modification that effectively replaces two hydrogen atoms of a residue containing common isotopes with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated residue.
34.06
(13)C 2 (2)H 4
34.063118
X
artifact
Unimod:510
PSI-MOD
DiMethyl-C13HD2
Dimethyl:2H(4)13C(2)
MOD:00927
2x(13)C,4x(2)H labeled dimethylated residue
A protein modification that effectively replaces two hydrogen atoms of a residue containing common isotopes with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated residue.
PubMed:16335955
PubMed:3802193
Unimod:510
DiMethyl-C13HD2
Dimethyl:2H(4)13C(2)
modification from Unimod Chemical derivative
227.39
C 14 H 29 N 1 O 1
227.22491
X
artifact
Unimod:513
PSI-MOD
C8-QAT
[3-(2,5)-Dioxopyrrolidin-1-yloxycarbonyl)-propyl]dimethyloctylammonium
MOD:00928
Should have children for K and X-N-term [JSG].
[3-(2,5)-dioxopyrrolidin-1-yloxycarbonyl)-propyl]dimethyloctylammonium
modification from Unimod Chemical derivative
PubMed:16771548
Unimod:513
C8-QAT
[3-(2,5)-Dioxopyrrolidin-1-yloxycarbonyl)-propyl]dimethyloctylammonium
A modification produced in a non-enzymatic reaction between a lactose carbonyl group and an L-lysine to form a Schiff-base or an Amadori ketosamine lysine adduct.
342.3
C 12 H 22 O 11
342.1162
C 18 H 34 N 2 O 12
470.47
470.21118
K
natural
Unimod:512
uniprot.ptm:PTM-0511
CARBOHYD N-linked (Lac) (glycation) lysine
PSI-MOD
Hex(2)
Lactosylation
MOD:00929
The term lactosylation used with this meaning is a misnomer [JSG].
lactose glycated lysine
A modification produced in a non-enzymatic reaction between a lactose carbonyl group and an L-lysine to form a Schiff-base or an Amadori ketosamine lysine adduct.
PubMed:9606156
Unimod:512
CARBOHYD N-linked (Lac) (glycation) lysine
Hex(2)
Lactosylation
tyrosine adduct with substrate analog inhibitor 1,2-dideoxy-2'-methyl-alpha-D-glucopyranoso-[2,1-d]-Delta2'-thiazoline.
232.27
C 9 H 14 N 1 O 4 S 1
232.06436
C 18 H 23 N 2 O 6 S 1
395.45
395.1277
Y
artifact
Unimod:514
PSI-MOD
MOD:00930
propyl-NAG tyrosine adduct
tyrosine adduct with substrate analog inhibitor 1,2-dideoxy-2'-methyl-alpha-D-glucopyranoso-[2,1-d]-Delta2'-thiazoline.
PubMed:15795231
Unimod:514
modification from Unimod Other - BHTOH is formed upon metabolism of BHT with P450 enzymes. The BHTOH is further metabolized to its quinone methide (electrophile) which reacts with -SH and -NH2 groups
234.34
C 15 H 22 O 2
234.16199
X
artifact
Unimod:498
PSI-MOD
BHTOH
Michael addition of t-butyl hydroxylated BHT (BHTOH) to C, H or K
MOD:00931
Michael addition of t-butyl hydroxylated BHT (BHTOH) to C, H or K
modification from Unimod Other - BHTOH is formed upon metabolism of BHT with P450 enzymes. The BHTOH is further metabolized to its quinone methide (electrophile) which reacts with -SH and -NH2 groups
PubMed:11085420
Unimod:498
BHTOH
Michael addition of t-butyl hydroxylated BHT (BHTOH) to C, H or K
modification from Unimod Isotopic label
298.02
Br 1 (12)C 10 (13)C 2 H 13 N 2 O 2
298.02274
Br 1 (12)C 13 (13)C 2 H 18 N 3 O 3 S 1
401.03
401.03192
C
artifact
Unimod:499
PSI-MOD
Heavy IDBEST tag for quantitation
IGBP:13C(2)
MOD:00932
IDBEST tag for quantitation
modification from Unimod Isotopic label
PubMed:11821862
Unimod:499
Heavy IDBEST tag for quantitation
IGBP:13C(2)
modification from Unimod Chemical derivative - 5-hydro-5-methylimidazol-4-one, arginine methylglyoxal arginine adduct (+54 amu)
54.05
C 3 H 2 O 1
54.010567
C 9 H 14 N 4 O 2
210.24
210.11168
R
artifact
Unimod:319
PSI-MOD
Delta:H(2)C(3)O(1)
MDA adduct +54
MOD:00933
Ref. Uchida K, Sakai K, Itakura K, Osawa T, Toyokuni S. 1977. Protein modification by lipid peroxidation products: formation of malondialdehyde-derived N(epsilon)-(2-propenol)lysine in proteins. Arch Biochem Biophys. 346(1):45-52.
methylglyoxal arginine adduct (+54 amu)
modification from Unimod Chemical derivative - 5-hydro-5-methylimidazol-4-one, arginine methylglyoxal arginine adduct (+54 amu)
Unimod:319#R
Delta:H(2)C(3)O(1)
MDA adduct +54
modification from Unimod Post-translational
306.4
C 19 H 26 N -2 O 5
306.17188
C 25 H 38 N 2 O 6
462.59
462.27298
R
natural
Unimod:506
PSI-MOD
LG-Hlactam-R
Levuglandinyl - arginine hydroxylactam adduct
MOD:00934
Levuglandinyl - arginine hydroxylactam adduct
modification from Unimod Post-translational
Unimod:506
LG-Hlactam-R
Levuglandinyl - arginine hydroxylactam adduct
Oxidation of methionine to methionine sulfoxide with neutral loss of CH3SOH.
-64.1
C -1 H -4 N 0 O -1 S -1
-63.998287
C 4 H 5 N 1 O 1 S 0
83.09
83.03712
M
artifact
PSI-MOD
MOD:00935
Originally created from Unimod:507 that was later deleted.
methionine oxidation with neutral loss of 64 Da
Oxidation of methionine to methionine sulfoxide with neutral loss of CH3SOH.
PubMed:18688235
PubMed:9004526
modification from Unimod Post-translational
348.44
C 20 H 28 O 5
348.19366
X
artifact
Unimod:504
PSI-MOD
LG-Hlactam-K
Levuglandinyl - lysine hydroxylactam adduct
MOD:00936
Levuglandinyl - hydroxylactam adduct, K and N-term
modification from Unimod Post-translational
Unimod:504
LG-Hlactam-K
Levuglandinyl - lysine hydroxylactam adduct
modification from Unimod Post-translational
290.4
C 19 H 26 N -2 O 4
290.17697
C 25 H 38 N 2 O 5
446.59
446.27808
R
artifact
Unimod:505
PSI-MOD
LG-lactam-R
Levuglandinyl - arginine lactam adduct
MOD:00937
Levuglandinyl - arginine lactam adduct
modification from Unimod Post-translational
Unimod:505
LG-lactam-R
Levuglandinyl - arginine lactam adduct
modification from Unimod Post-translational
332.44
C 20 H 28 O 4
332.19876
X
artifact
Unimod:503
PSI-MOD
LG-lactam-K
Levuglandinyl - lysine lactam adduct
MOD:00938
Levuglandinyl - lactam adduct, K and N-term
modification from Unimod Post-translational
PubMed:12590383
Unimod:503
LG-lactam-K
Levuglandinyl - lysine lactam adduct
modification from Unimod Chemical derivative
129.12
C 5 H 7 N 1 O 3
129.04259
C 8 H 12 N 2 O 4 S 1
232.25
232.05177
C
artifact
Unimod:500
PSI-MOD
Nmethylmaleimide+water
Nmethylmaleimidehydrolysis
MOD:00939
hydrolyzed N-methylmaleimide cysteine adduct
modification from Unimod Chemical derivative
Unimod:500
Nmethylmaleimide+water
Nmethylmaleimidehydrolysis
A protein modification produced by formation of an adduct with 3-methyl-2-pyridyl isocyanate.
134.14
C 7 H 6 N 2 O 1
134.04802
X
artifact
N-term
Unimod:501
PSI-MOD
3-methyl-2-pyridyl isocyanate
PyMIC
MOD:00940
3-methyl-2-pyridyl isocyanate derivatized residue
A protein modification produced by formation of an adduct with 3-methyl-2-pyridyl isocyanate.
PubMed:11078590
Unimod:501
3-methyl-2-pyridyl isocyanate
PyMIC
modification from Unimod Chemical derivative
118.16
C 8 H 8 N 1
118.065674
C 11 H 13 N 2 S 1
205.3
205.07994
C
artifact
Unimod:488
PSI-MOD
DHP
Dehydropyrrolizidine alkaloid (dehydroretronecine) on cysteines
MOD:00941
dehydropyrrolizidine alkaloid (dehydroretronecine) derivatized cysteine
modification from Unimod Chemical derivative
PubMed:12175151
Unimod:488
DHP
Dehydropyrrolizidine alkaloid (dehydroretronecine) on cysteines
A protein modification that effectively substitutes four (1)H protium atoms with four (2)H deuterium atoms to produce (4,4,5,5-(2)H4)-L-lysine.
4.03
(1)H -4 (2)H 4
4.025107
C 6 (1)H 8 (2)H 4 N 2 O 1
132.12
132.12007
K
artifact
Unimod:481
4,4,5,5-tetradeuterolysine
lys-2H4
PSI-MOD
4,4,5,5-D4 Lysine
Label:2H(4)
MOD:00942
For SILAC experiments.
(4,4,5,5-(2)H4)-L-lysine
A protein modification that effectively substitutes four (1)H protium atoms with four (2)H deuterium atoms to produce (4,4,5,5-(2)H4)-L-lysine.
OMSSA:180
Unimod:481
4,4,5,5-tetradeuterolysine
lys-2H4
4,4,5,5-D4 Lysine
Label:2H(4)
modification from Unimod Isotopic label
128.19
C 7 H 14 N 1 O 1
128.10754
X
artifact
Unimod:476
PSI-MOD
4-trimethyllammoniumbutyryl-
TMAB
MOD:00943
4-trimethylammoniumbutanoyl derivatized residue
modification from Unimod Isotopic label
PubMed:12643539
Unimod:476
4-trimethyllammoniumbutyryl-
TMAB
modification from Unimod Isotopic label
137.16
C 7 (1)H 5 (2)H 9 N 1 O 1
137.16403
X
artifact
Unimod:477
PSI-MOD
TMAB:2H(9)
d9-4-trimethyllammoniumbutyryl-
MOD:00944
d9-4-trimethylammoniumbutanoyl derivatized residue
modification from Unimod Isotopic label
Unimod:477
TMAB:2H(9)
d9-4-trimethyllammoniumbutyryl-
OBSOLETE because redundant and identical to MOD:00626. Remap to MOD:00626.
MOD:00626
421.43
C 21 H 15 N 3 O 5 S 1
421.07324
S
artifact
PSI-MOD
MOD:00945
fluorescein-5-thiosemicarbazide adduct
true
OBSOLETE because redundant and identical to MOD:00626. Remap to MOD:00626.
PubMed:18688235
A protein modification that crosslinks two residues with a covalent bond and the loss of ammonia.
PSI-MOD
MOD:00946
crosslinked residues with loss of ammonia
A protein modification that crosslinks two residues with a covalent bond and the loss of ammonia.
PubMed:18688235
Entries from DeltaMass see http://www.abrf.org/index.cfm/dm.home?AvgMass=all.
PSI-MOD
MOD:00947
DeltaMass
Entries from DeltaMass see http://www.abrf.org/index.cfm/dm.home?AvgMass=all.
PubMed:18688235
OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
X
PSI-MOD
MOD:00948
From DeltaMass: Average Mass: -79
5'-dephospho
true
OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
DeltaMass:0
OBSOLETE because redundant and identical to MOD:01933. Remap to MOD:01933.
MOD:01933
K
PSI-MOD
MOD:00949
From DeltaMass: Average Mass: -58
desmosine
true
OBSOLETE because redundant and identical to MOD:01933. Remap to MOD:01933.
DeltaMass:0
OBSOLETE because this modification has not been seen/reported on since this original publication in 1994 and carboxymethylation of proteins is common enough for this mass shift to have been seen in the intervening 25+ years. modification from DeltaMass
M
PSI-MOD
MOD:00950
From DeltaMass: Average Mass: -48 Average Mass Change:-48 References:Anal. Biochem. Vol 216 No.1 p141
decomposed carboxymethylated methionine
true
OBSOLETE because this modification has not been seen/reported on since this original publication in 1994 and carboxymethylation of proteins is common enough for this mass shift to have been seen in the intervening 25+ years. modification from DeltaMass
DeltaMass:3
Covalent modification of a peptide or protein L-glutamic acid residue to gamma-carboxyglutamic acid with secondary loss of a neutral carbon dioxide molecular fragment.
-44.01
C -1 H 0 N 0 O -2
-43.98983
C 5 H 7 N 1 O 3
129.12
129.04259
E
artifact
d4CbxGlu
PSI-MOD
MOD:00951
From DeltaMass: Average Mass: -44 Formula:CO2 Average Mass Change:-44 References:Nakamura T, Yu Z, Fainzilber M, Burlingame AL. Protein Sci (1996) 5, 524-530 Mass spectrometric-based revision of the structure of a cysteine-rich peptide toxin with gamma-carboxyglutamic acid, TxVIIA, from the sea snail, Conus textile. Notes: The elimination of CO2 will regenerate glutamate as if there was no modification. However, peaks appearing with an interval of 44 is quite characteristic. It would be noteworthy to remind that loss of 44 from a gamma-carboxyglutamate-containing peptide may be observed not only as a result of spontaneous decarboxylation but also as an artifact under some ionization conditions such as negative ion mode MALDI.
L-gamma-carboxyglutamic acid with neutral loss of carbon dioxide
Covalent modification of a peptide or protein L-glutamic acid residue to gamma-carboxyglutamic acid with secondary loss of a neutral carbon dioxide molecular fragment.
DeltaMass:58
d4CbxGlu
A protein modification that crosslinks an aspartic acid and the following glycine residue with the formation of (2-aminosuccinimidyl)acetic acid and the loss of a water molecule.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 6 H 6 N 2 O 3
154.13
154.03784
D, G
hypothetical
uniprot.ptm:PTM-0312
(2-aminosuccinimidyl)acetic acid
(3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid
CROSSLNK (2-aminosuccinimidyl)acetic acid (Asp-Gly)
N-(2-aminosuccinyl)glycine
[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]acetic acid
anhydroaspartyl glycine
aspartimide glycine
PSI-MOD
MOD:00952
Cross-link 2; this cross-link is formed by the condensation of an aspartic acid residue with the alpha-amido of the following residue.
(2-aminosuccinimidyl)acetic acid (Asp)
A protein modification that crosslinks an aspartic acid and the following glycine residue with the formation of (2-aminosuccinimidyl)acetic acid and the loss of a water molecule.
PubMed:10801322
RESID:AA0441#ASP
(2-aminosuccinimidyl)acetic acid
(3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid
CROSSLNK (2-aminosuccinimidyl)acetic acid (Asp-Gly)
N-(2-aminosuccinyl)glycine
[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]acetic acid
anhydroaspartyl glycine
aspartimide glycine
A protein modification that effectively crosslinks an L-glutamic acid residue and an L-serine residue by an ester bond and releasing water to form O-(L-isoglutamyl)-L-serine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 8 H 10 N 2 O 4
198.18
198.06406
E, S
artifact
(2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid
CROSSLNK isoglutamyl serine ester (Ser-Glu)
O(beta)-(gamma-glutamyl)serine
O-(L-isoglutamyl)-L-serine
O-gamma-Glutamyl- (Crosslink to Serine)
O3-(isoglutamyl)-serine
PSI-MOD
MOD:00953
Cross-link 2; From DeltaMass: with no citation.
O-(L-isoglutamyl)-L-serine (Glu-Ser)
A protein modification that effectively crosslinks an L-glutamic acid residue and an L-serine residue by an ester bond and releasing water to form O-(L-isoglutamyl)-L-serine.
DeltaMass:0
PubMed:19035375
RESID:AA0597#ESX
(2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid
CROSSLNK isoglutamyl serine ester (Ser-Glu)
O(beta)-(gamma-glutamyl)serine
O-(L-isoglutamyl)-L-serine
O-gamma-Glutamyl- (Crosslink to Serine)
O3-(isoglutamyl)-serine
A protein modification that crosslinks two residues with a covalent bond and the loss of water.
PSI-MOD
MOD:00954
crosslinked residues with loss of water
A protein modification that crosslinks two residues with a covalent bond and the loss of water.
PubMed:18688235
A protein modification that effectively crosslinks an L-serine residue and an L-histidine residue to release water and form tele- or pros-(2-amino-2-carboxyethyl)histidine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 9 H 10 N 4 O 2
206.2
206.08038
H, S
artifact
beta-alaninohistidine
PSI-MOD
MOD:00955
Cross-link 2; From DeltaMass with no citation or formula: Average Mass: -18. The DeltaMass description "Serine crosslinked to theta or pi carbon of Histidine" is incorrect. The histidine ring nitrogens (not carbons) are designated tele or N-tau (not theta), and pros or N-pi [JSG].
alaninohistidine (serine crosslinked to tele or pros nitrogen of histidine)
A protein modification that effectively crosslinks an L-serine residue and an L-histidine residue to release water and form tele- or pros-(2-amino-2-carboxyethyl)histidine.
DeltaMass:0
beta-alaninohistidine
modification from DeltaMass
-18.03
C 1 H 2 N 0 O 0 S -1
-17.95642
C 6 H 11 N 1 O 1
113.16
113.08406
M
PSI-MOD
MOD:00956
From DeltaMass: Average Mass: -18 Average Mass Change:-18 Notes: It has the same mass as leucine or isoleucine and can be charged on the methionyl t-RNA. This often happens in minimal media-prepared fermentations that are not supplemented with enough free methionine. It gives a mass change of -18 and can often be confused with dehydration.
misincorporation of norleucine for methionine
modification from DeltaMass
DeltaMass:10
Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral carbon dioxide molecular fragment.
-44.01
C -1 H 0 N 0 O -2
-43.98983
X
artifact
dCO2ModRes
PSI-MOD
MOD:00957
modified residue with neutral loss of carbon dioxide
Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid residue with a secondary loss of a neutral carbon dioxide molecular fragment.
PubMed:18688235
dCO2ModRes
modification from DeltaMass
H, R
PSI-MOD
MOD:00958
Cross-link 2; From DeltaMass: Average Mass: -5
crosslink between Arg and His sidechains
modification from DeltaMass
DeltaMass:0
modification from DeltaMass
Y, Y, Y, Y
PSI-MOD
MOD:00959
Cross-link 4; From DeltaMass: Average Mass: -4
3,3',5,5'-TerTyr (Crosslink)
modification from DeltaMass
DeltaMass:0
A protein modification that effectively replaces a carboxylic acid group with a hydrogen atom.
-44.01
C -1 H 0 N 0 O -2
-43.98983
X
artifact
PSI-MOD
MOD:00960
decarboxylated residue
A protein modification that effectively replaces a carboxylic acid group with a hydrogen atom.
PubMed:18688235
A protein modification that effectively reduces the disulfide bond of cystine to form two cysteine residues.
2.02
C 0 H 2 N 0 O 0 S 0
2.01565
C 6 H 10 N 2 O 2 S 2
206.28
206.01837
MOD:00034
PSI-MOD
MOD:00961
Cross-link 2; this modification destroys the cross-link. From DeltaMass: Treatment of cystine (cys-cys) by reducing agents such as dithiothreitol (DTT) or triscarboxyethylphosphine (TCEP) results in cleavage of the disulphide bond and reduction of the sulphur atom of each molecule to create cysteine.
reduction of disulfide crosslink in cystine to two cysteines
A protein modification that effectively reduces the disulfide bond of cystine to form two cysteine residues.
DeltaMass:333
A protein modification that by reducing the indole ring system of tryptophan to indoline effectively converts an L-tryptophan residue to 2',3'-dihydrotryptophan.
2.02
C 0 H 2 N 0 O 0 S 0
2.01565
C 11 H 12 N 2 O 1
188.23
188.09496
W
artifact
PSI-MOD
MOD:00962
From DeltaMass: References:1. Pearson,D.A., Blanchette,M., Baker,M.L. and Guindon,C.A. (1989) Trialkylsilanes as scavengers for the trifluoroacetic acid deblocking ofprotecting groups in peptide synthesis. Tetrahedron Lett., 30(21), 2739-2742 Notes: Reduction of indole double bond of Trp which occurs when triethylsilane (TES) is used as a scavenger and Trp is incorporated without protection of indole nitrogen [1]. This side reaction is likely to be accompanied by oxidation of indoline ring with formation of intensively colored peptide by-products. Triisopropylsilane (TIPS) does not give this side reaction. See structure at http://www.abrf.org/images/misc/dmass2.gif. [However, the pictured indoline structure is incorrect - JSG].
2',3'-dihydrotryptophan
A protein modification that by reducing the indole ring system of tryptophan to indoline effectively converts an L-tryptophan residue to 2',3'-dihydrotryptophan.
DeltaMass:343
URL:http://dx.doi.org/10.1016/S0040-4039(00)99113-5
Modification from DeltaMass. OBSOLETE because redundant and identical to MOD:00462. Remap to MOD:00462.
MOD:00462
W
artifact
PSI-MOD
MOD:00963
From DeltaMass: Average Mass: 4 Monoisotopic Mass Change:3.995 Average Mass Change:3.989 References:Ruoppolo M, Amoresano A, Pucci P, Pascarella S, Polticelli F, Trovato M,Menegatti E, Ascenzi P.Characterization of five new low-molecular-mass trypsin inhibitors fromwhite mustard (Sinapis alba L.) seed.Eur J Biochem. 2000 267:6486-92. Notes: See structure at http://www.abrf.org/images/misc/dmass32.jpg.
Oxidation of Trp to kynurenine
true
Modification from DeltaMass. OBSOLETE because redundant and identical to MOD:00462. Remap to MOD:00462.
DeltaMass:357
modification from DeltaMass
12.01
C 1 H 0 N 0 O 0
12.0
C 7 H 12 N 2 O 1
140.19
140.09496
K
artifact
N6-(methylidene)-lysine
PSI-MOD
MOD:00964
From DeltaMass: Average Mass: 12 Average Mass Change: 12 References: Mathews, W. Rodney; Runge, Thomas A.; Haroldsen, Peter E.; Gaskell, Simon J. (1989) Characterization of impurities in a synthetic renin substrate peptide by fast-atom bombardment mass spectrometry and hybrid tandem mass spectrometry. Rapid Commun. Mass Spectrom. 3(9), 314-19 Notes: Fast-atom bombardment mass spectrometry of a synthetic renin substrate decapeptide (Pro-His-Pro-Phe-His-Leu-Val-Ile-His-D-Lys) indicated the presence of several side products, including a component 12 Da higher in mass. Low-energy collisionally activated ***decompn*** analyses were performed using a hybrid tandem instrument and demonstrated that the heavier side product had two components, in which the structural modification was either at the N- or the C-terminus. Addnl. analyses of the N-acetyl deriv. indicated that for each component the structural modification blocked a site of N-acetylation. It is suggested that the formation of these side products is attributable to the generation of formaldehyde, during removal of the histidine protecting group (benzyloxymethyl), which reacts with the N-terminus of the peptide to give an imidazolidinone structure or with the D- ***lysine***.epsilon.-amine group to yield an ***imine*** . While the precise genesis of the side-products remains speculative, it is clear that the combined strategy of derivatization and tandem mass spectrometry has allowed structural conclusions concerning individual components of an isobaric mixt.
lysine epsilon amino to imine + 12 amu
modification from DeltaMass
DeltaMass:34
N6-(methylidene)-lysine
A protein modification that effectively converts an N-terminal L-cysteine residue by a formadehyde adduct to 4-thiazolidinecarboxylic acid.
12.01
C 1 H 0 N 0 O 0 S 0
12.0
C 4 H 6 N 1 O 1 S 1
116.16
116.01701
C
artifact
N-term
thioproline
PSI-MOD
MOD:00965
From DeltaMass: References: Mitchell, M.A., Runge, T.A., Mathews, W.R., Ichhpurani, A.K., Harn, N.K., Dobrowolski, P.J. and Eckenrrrode, F.M. Problems associated with use of the benzylozymethyl protecting group for histidines. Formaldehyde adducts formed during cleavage by hydrogen fluoride. Int. J. Pept. Protein Res. 1990, 36(4), 350-355. Gesquiere, J.-C., Diesis, E. and Tartar, A. Conversion of N-terminal cysteine to thiazolidine carboxylic acid during hydrogen fluoride deprotection of peptides containing pi-N-Bom protected histidine. J. Chem. Soc. Chem. Commun. 1990, (20), 1402-1403. Kumagaye, K.Y., Inui, T., Nakajima, K., Kimura,T. and Sakakibara, S. Suppression of a side reaction associated with Nim-benzyloxymethyl group during synthesis of peptides containing cysteinyl residue at the N-terminus. Pept. Res. 1991, 4(2), 84-87. Colombo, R., Colombo, F. and Jones, J.H. Acid-labile histidine side-chain protection. The N(pi)-t-butoxymethyl group. J. Chem. Soc. Chem. Commun. 1984, (5), 292-293. Notes: Conversion of N-term Cys to thiazolidine during HF deprotection of His(Bom)-containing peptides [1-3]. See structure at http://www.abrf.org/images/misc/dmass12b.gif; modification in red. This modification cannot be excluded during final deprotection/cleavage in Fmoc-chemistry in cases when His(Bum) was employed [4]. For formation of free imino acid see PubMed:1527501.
4-thiazolidinecarboxylic acid
A protein modification that effectively converts an N-terminal L-cysteine residue by a formadehyde adduct to 4-thiazolidinecarboxylic acid.
DeltaMass:342
thioproline
A protein modification that effectively converts an N-terminal L-tryptophan residue by a formadehyde adduct to 1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acid.
12.01
C 1 H 0 N 0 O 0 S 0
12.0
C 12 H 10 N 2 O 1
198.22
198.07932
W
artifact
PSI-MOD
MOD:00966
From DeltaMass: Average Mass: 12 Average Mass Change: 12 References: Lippke, K. P., W. G. Schunack, W. Wenning, W. E. Mueller. 1983..beta.-Carbolines as benzodiazepine receptor ligands. 1. Synthesis andbenzodiazepine receptor interaction of esters of.beta.-carboline-3-carboxylic acid. J. Med. Chem.26: 499-503 Cain, M., R. W. Weber, F. Guzman, J. M. Cook, S. A. Barker, K. C.Rice, J. N. Crawley, S. M. Paul, P. Skolnick. 1982. .beta.-Carbolines:synthesis and neurochemical and pharmacological actions on brainbenzodiazepine receptors.J. Med. Chem. 25: 1081-91 Notes: +12 Da modification corresponds to formaldehyde adduct of Trp having beta-carboline structure (methylene bridge links carbon-2 of indole ring and alfa-N. See structure at http://www.abrf.org/images/misc/dmass12a.gif; modification in red.
1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acid
A protein modification that effectively converts an N-terminal L-tryptophan residue by a formadehyde adduct to 1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acid.
DeltaMass:339
A protein modification that effectively cross-links two L-lysine residues to form syndesine, hydroxylysinohydroxynorleucine.
16.96
C 0 H -3 N -2 O 3
16.95512
C 12 H 21 N 2 O 5
273.31
273.14505
K, K
hydroxylysinohydroxynorleucine
PSI-MOD
MOD:00967
Cross-link 2; From DeltaMass: Average Mass: 13 Average Mass Change: 13 (incorrect) [JSG].
syndesine
A protein modification that effectively cross-links two L-lysine residues to form syndesine, hydroxylysinohydroxynorleucine.
DeltaMass:35
PubMed:75151974
hydroxylysinohydroxynorleucine
OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass
C
artifact
PSI-MOD
MOD:00968
From DeltaMass: Average Mass: 13 Formula:C2H2O2 vs C3H5ON Monoisotopic Mass Change:13.03 Average Mass Change:13.05 Notes:Residual acrylamide in SDS gels can partly label cysteine residues in proteins (propionamido-Cys, PAM-Cys, DeltaMass +71Da; see entry). Subsequent alkylation of protein bands with iodoacetic acid e.g. in preparation for proteomic analysis, will convert remaining free cysteines into carboxymethyl-Cys (CM-Cys, DeltaMass +58Da; see entry). Peptide mass fingerprinting may therefore potentially reveal the same cysteine-containing peptide in two forms, differing in mass by 13Da. The relative ratios of the peaks will depend on the initial degree of labelling with acrylamide. Use of high quality, deionised acrylamide in the SDS gel will minimise modification of cysteine through this route. Where it remains a problem, deliberate alkylation using acrylamide instead of iodoacetamide will ensure chemical homogeneity of the final product.
CM-Cys vs PAM-Cys
true
OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass
DeltaMass:347
OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass
C
artifact
PSI-MOD
MOD:00969
From DeltaMass: Average Mass: 14 Formula:CH2 Monoisotopic Mass Change:14.016 Average Mass Change:14.027 Notes: Residual acrylamide in SDS gels can partly label cysteine residues in proteins (propionamido-Cys, PAM-Cys, DeltaMass +71Da; see entry). Subsequent alkylation of protein bands with iodoacetamide e.g. in preparation for proteomic analysis, will convert remaining free cysteines into carboxamidomethyl-Cys (CAM-Cys, DeltaMass +57Da; see entry). Peptide mass fingerprinting may therefore potentially reveal the same cysteine-containing peptide in two forms, differing in mass by 14Da. The relative ratios of the peaks will depend on the initial degree of labelling with acrylamide. Use of high quality, deionised acrylamide in the SDS gel will minimise modification of cysteine through this route. Where it remains a problem, deliberate alkylation using acrylamide instead of iodoacetamide will ensure chemical homogeneity of the final product.
CAM-Cys vs PAM-Cys
true
OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass
DeltaMass:346
modification from DeltaMass
K
natural
PSI-MOD
MOD:00970
From DeltaMass: Average Mass: 15 Average Mass Change:15 Notes:In going from Lys to hydroxy-allysine, two separate reactions are involved:1. the oxidative deamination converting Lys to allysine (-CH2NH2 being converted to -CHO) with a net mass change of -1;2.conversion of allysine to delta-hydroxy-allysine (-CH2-CHO being converted to -CH(OH)-CHO) with a mass change of +16. The net change from Lys to hydroxyallysine thus is +15.
delta-hydroxy-allysine (Lys)
modification from DeltaMass
DeltaMass:37
A protein modification that effectively converts an L-histidine residue to 2-oxohistidine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 6 H 7 N 3 O 2
153.14
153.05383
H
natural
PSI-MOD
MOD:00971
From DeltaMass: Average Mass: 16 Average Mass Change:16 References:Lewisch, S. A. and Levine, R. L. (1995) Anal. Biochem. 231, 440-446. Determination of 2-oxo-histidine by amino acid analysis Notes:Rod LevineNIHBldg 3, Room 106 MSC 0320Bethesda, MD 20892-0320email: rlevine@nih.govvoice: 1 (301) 496-2310fax: 1 (301) 496-0599
2-Oxohistidine
A protein modification that effectively converts an L-histidine residue to 2-oxohistidine.
DeltaMass:38
PubMed:8405458
A protein modification that effectively converts an L-phenylalanine residue to a monobrominated L-phenylalanine, such as L-2'-bromophenylalanine.
78.9
Br 1 C 0 H -1 N 0 O 0
77.910515
Br 1 C 9 H 8 N 1 O 1
226.07
224.97893
F
natural
Unimod:340
Br1Phe
PSI-MOD
Bromo
bromination
MOD:00972
From DeltaMass: Average Mass: 78 Average Mass Change:78 References:Yoshino,K et.al. Biochemistry Vol. 30 pg 6203-9 (1991) Identifidation of a novel amino acid, o-bromo-L-phenylananine, in egg-associated peptides that activate spermatozoa
monobrominated L-phenylalanine
A protein modification that effectively converts an L-phenylalanine residue to a monobrominated L-phenylalanine, such as L-2'-bromophenylalanine.
Unimod:340#F
Br1Phe
Bromo
bromination
modification from DeltaMass
P
artifact
PSI-MOD
MOD:00973
From DeltaMass: Average Mass: 32 Monoisotopic Mass Change:31.99 Average Mass Change:32 References:Amici A, Levine, RL, Tsai, L, and Stadtman, ER: Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. Journal of Biological Chemistry 264: 3341-3346 1989.Rod Levine (unpublished)
Oxidation of proline (to glutamic acid)
modification from DeltaMass
DeltaMass:355
modification from DeltaMass
33.96
(35)Cl 1 H -1
33.96103
C 9 (35)Cl 1 H 8 N 1 O 2
197.02
197.02435
Y
artifact
PSI-MOD
MOD:00974
From DeltaMass: Average Mass: 34
(35)Cl labeled 3'-chlorotyrosine
modification from DeltaMass
DeltaMass:0
modification from DeltaMass
35.96
(37)Cl 1 H -1
35.958076
C 9 (37)Cl 1 H 8 N 1 O 2
199.02
199.02141
Y
artifact
PSI-MOD
MOD:00975
From DeltaMass: Average Mass: 36
(37)Cl labeled 3'-chlorotyrosine
modification from DeltaMass
DeltaMass:0
modification from DeltaMass - OBSOLETE because redundant and identical to MOD:01072. Remap to MOD:01072.
MOD:01072
38.09
H -1 K 1
37.955883
X
PSI-MOD
MOD:00976
From DeltaMass: Average Mass: 38
potassium salt
true
modification from DeltaMass - OBSOLETE because redundant and identical to MOD:01072. Remap to MOD:01072.
DeltaMass:0
modification from DeltaMass
43.96
H -2 Na 2
43.963886
X
PSI-MOD
MOD:00977
From DeltaMass: Average Mass: 44
disodium salt
modification from DeltaMass
DeltaMass:0
modification from DeltaMass
C
artifact
PSI-MOD
MOD:00978
From DeltaMass: Average Mass: 51 Average Mass Change: 51 References:Lukszo, Patterson, Albericio, and Kates, Letters in Peptide Science 3, 157-166(1996) Notes:The side reaction can be very significant, and the level to which it occurs depends on how the C-terminal Cys is anchored and what the side-chain protecting group is. The mechanism involves piperidine-mediated beta-elimination of sulfur (with the protecting group on), followed by addition of piperidine across the C-terminaldehydroalanine. Since this last-mentioned step creates a chiral center, a mixture of diastereomers is formed which in special cases can be separatedby HPLC. Another problem with C-terminal Cys is racemization; some references in the review article by Andreu, Albericio, Sole, Munson, Ferrer, and Barany in Pennington-Dunn Peptide Synthesis and Purification Protocols, vol 35, 1994, pp. 91-169.
piperidine adduct to C-terminal Cys
modification from DeltaMass
DeltaMass:345
modification from DeltaMass
X
artifact
PSI-MOD
MOD:00979
From DeltaMass: Average Mass: 56
t-butyl ester (OtBu) and t-butyl (tBu)
modification from DeltaMass
DeltaMass:0
modification from DeltaMass - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060.
MOD:01060
C
artifact
PSI-MOD
MOD:00980
From DeltaMass: Average Mass: 57 Abbreviation:CamCys Formula:C2H3NO Monoisotopic Mass Change:57.021 Average Mass Change:57.051 Notes:Cysteine reacts with iodoacetamide to produce carboxamidomethyl cysteine. Alternative names are often used, such as amidocarboxymethylcysteine and carbamoylmethylcysteine
Carboxamidomethyl (on Cysteine)
true
modification from DeltaMass - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060.
DeltaMass:337
modification from DeltaMass
60.07
H -2 K 1 Na 1
59.937824
X
PSI-MOD
MOD:00981
From DeltaMass: Average Mass: 60
sodium and potassium salt
modification from DeltaMass
DeltaMass:0
A protein modification that effectively converts an L-serine residue to L-selenocysteine (not known as a natural post-translational modification process).
62.97
C 0 H 0 N 0 O -1 Se 1
63.921608
C 3 H 5 N 1 O 1 Se 1
150.05
150.95363
S
artifact
Sec(Ser)
Selenocysteine (from Serine)
PSI-MOD
MOD:00982
[From DeltaMass: Average Mass: 64.] Although selenocysteine-charged tRNA(Sec) is biosynthesized from serine-charged tRNA(Sec), in peptide work selenocysteine is usually considered as either a natural residue or as a modified cysteine residue. This entry is for the artifactual formation of L-selenocysteine from serine. For encoded L-selenocysteine, use MOD:00031 [JSG].
L-selenocysteine (Ser)
A protein modification that effectively converts an L-serine residue to L-selenocysteine (not known as a natural post-translational modification process).
DeltaMass:0
Sec(Ser)
Selenocysteine (from Serine)
modification from DeltaMass
D
artifact
PSI-MOD
MOD:00983
From DeltaMass: Average Mass: 67 Average Mass Change:67 References:http://www.abrf.org/archives/hmail/0008/0007.html Notes:1.) Get rid of the DBU. It can cause piperidine amides at Asp residues. The tbu ester side chain comes off during synthesis and the residue is trans-amidated with piperidine (+67Da by MS). If you haven't yet seen this, you will. Even "normal" 20% pip/DMF (NMP) will cause this, but less frequently. Literature exists for this; I don't remember the exact reference. David H. Singleton Scientist Pfizer Central Research PO Box 8118-101 Eastern Point Road Groton, CT 06340 (860)441-4404.
Asp transamidation with piperidine
modification from DeltaMass
DeltaMass:67
modification from DeltaMass
67.92
(35)Cl 2 H -2
67.92206
C 9 (35)Cl 2 H 7 N 1 O 2
230.99
230.98538
Y
artifact
PSI-MOD
MOD:00984
From DeltaMass: Average Mass: 68
(35)Cl labeled 3',5'-dichlorotyrosine
modification from DeltaMass
DeltaMass:0
A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a halogen atom.
Y
HalTyr
PSI-MOD
MOD:00985
halogenated tyrosine
A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a halogen atom.
PubMed:18688235
HalTyr
modification from DeltaMass
69.92
(35)Cl 1 (37)Cl 1 H -2
69.919106
C 9 (35)Cl 1 (37)Cl 1 H 7 N 1 O 2
232.98
232.98244
Y
artifact
PSI-MOD
MOD:00986
From DeltaMass: Average Mass: 70.
(35)Cl and (37)Cl labeled 3',5'-dichlorotyrosine
modification from DeltaMass
DeltaMass:0
A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a chlorine atom.
Y
ClTyr
PSI-MOD
MOD:00987
chlorinated tyrosine
A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a chlorine atom.
PubMed:18688235
ClTyr
A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a bromine atom.
Y
BrTyr
PSI-MOD
MOD:00988
brominated tyrosine
A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a bromine atom.
PubMed:18688235
BrTyr
OBSOLETE because redundant, the difference component of MOD:01079. Remap to MOD:01079.
MOD:01079
C
artifact
PSI-MOD
MOD:00989
From DeltaMass with no citation or formula.
acetamidomethyl (Acm)
true
OBSOLETE because redundant, the difference component of MOD:01079. Remap to MOD:01079.
DeltaMass:0
modification from DeltaMass
71.92
(37)Cl 2 H -2
71.91615
C 9 (37)Cl 2 H 7 N 1 O 2
234.98
234.97948
Y
artifact
PSI-MOD
MOD:00990
From DeltaMass: Average Mass: 72
(37)Cl labeled 3',5'-dichlorotyrosine
modification from DeltaMass
DeltaMass:0
modification from DeltaMass
74.08
C 3 H 6 O 2
74.03678
C 6 H 11 N 1 O 3 S 1
177.22
177.04596
C
artifact
PSI-MOD
MOD:00991
From DeltaMass: Average Mass: 74 with no citation.
S-(sn-1-glyceryl)-L-cysteine
modification from DeltaMass
DeltaMass:0
modification from DeltaMass
74.08
C 3 H 6 O 2
74.03678
C 8 H 13 N 1 O 5
203.19
203.07938
E
artifact
PSI-MOD
MOD:00992
From DeltaMass: Average Mass: 74 Average Mass Change: 74 References: Anal. Biochem. 1993 Vol 208 No. 2 382-386, PubMed:8452236. [DeltaMass] This article only suggests this as a possible modification and does no characterization. Isolation and stuctural evidence for artifactual modification are found in PubMed:18767873 [JSG].
glutamate 5-glycerol ester
modification from DeltaMass
DeltaMass:78
PubMed:18767873
modification from DeltaMass
76.1
C 6 H 4
76.0313
X
artifact
OPh
PSI-MOD
MOD:00993
From DeltaMass: Average Mass: 76, on acidic amino acids
phenyl ester
modification from DeltaMass
DeltaMass:0
OPh
modification from DeltaMass
77.91
(79)Br 1 H -1
77.910515
(79)Br 1 C 9 H 8 N 1 O 2
240.97
240.97385
Y
artifact
PSI-MOD
MOD:00994
From DeltaMass: Average Mass: 78
(79)Br labeled 3'-bromotyrosine
modification from DeltaMass
DeltaMass:0
A protein modification that effectively converts an L-phenylalanine residue to (81)Br-L-2'-bromophenylalanine.
79.91
(81)Br 1 H -1
79.90846
(81)Br 1 C 9 H 8 N 1 O 1
226.98
226.97688
F
artifact
PSI-MOD
MOD:00995
From DeltaMass: Average Mass: 80
(81)Br labeled 2'-bromophenylalanine
A protein modification that effectively converts an L-phenylalanine residue to (81)Br-L-2'-bromophenylalanine.
DeltaMass:0
modification from DeltaMass
79.91
(81)Br 1 H -1
79.90846
(81)Br 1 C 9 H 8 N 1 O 2
242.97
242.97179
Y
artifact
PSI-MOD
MOD:00996
From DeltaMass: Average Mass: 80
(81)Br labeled 3'-bromotyrosine
modification from DeltaMass
DeltaMass:0
modification from DeltaMass
82.15
C 6 H 10
82.07825
X
artifact
OcHex
PSI-MOD
MOD:00997
From DeltaMass: Average Mass: 82
cyclohexyl ester
modification from DeltaMass
DeltaMass:0
OcHex
A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with an iodine atom.
Y
ITyr
PSI-MOD
MOD:00998
iodinated tyrosine
A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with an iodine atom.
PubMed:18688235
ITyr
OBSOLETE because redundant and identical to MOD:00404. Remap to MOD:00404.
MOD:00404
M
artifact
PSI-MOD
MOD:00999
From DeltaMass: Average Mass: 83 Formula:C4H5O1N1 Monoisotopic Mass Change:83.037 Average Mass Change:83.09
homoseryl lactone
true
OBSOLETE because redundant and identical to MOD:00404. Remap to MOD:00404.
DeltaMass:90
A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one bromine atom.
Y
Br1Tyr
PSI-MOD
MOD:01000
monobrominated tyrosine
A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one bromine atom.
PubMed:18688235
Br1Tyr
A protein modification that inserts or replaces a residue with a 2-aminoisobutyric acid.
C 4 H 7 N 1 O 1
85.11
85.052765
X
artifact
2-amino-2-methylpropanoic acid
2-amino-2-methylpropionic acid
2-methylalanine
Aib
alpha,alpha-dimethylglycine
alpha-aminoisobutyric acid
alpha-methylalanine
PSI-MOD
MOD:01001
Modification from DeltaMass: Average Mass: 85.
2-aminoisobutyric acid residue (Aib)
A protein modification that inserts or replaces a residue with a 2-aminoisobutyric acid.
DeltaMass:0
2-amino-2-methylpropanoic acid
2-amino-2-methylpropionic acid
2-methylalanine
Aib
alpha,alpha-dimethylglycine
alpha-aminoisobutyric acid
alpha-methylalanine
modification from DeltaMass
85.11
C 4 H 7 N 1 O 1
85.052765
X
artifact
PSI-MOD
MOD:01002
From DeltaMass: Average Mass: 85 Formula: C 4 H 7 O 1 N 1 Monoisotopic Mass Change: 85.053 Average Mass Change: 85.106
gamma-aminobutyryl
modification from DeltaMass
DeltaMass:92
modification from DeltaMass
X
artifact
PSI-MOD
MOD:01003
From DeltaMass: Average Mass: 86
t-butyloxymethyl (Bum)
modification from DeltaMass
DeltaMass:0
modification from DeltaMass
86.09
C 3 H 6 N 2 O 1
86.04801
X
artifact
PSI-MOD
MOD:01004
From DeltaMass: Average Mass: 86 Formula: C 3 H 6 O 2 N 1 Monoisotopic Mass Change: 86.048 Average Mass Change: 86.094
diaminopropionyl
modification from DeltaMass
DeltaMass:95
modification from DeltaMass
X
artifact
StBu
PSI-MOD
MOD:01005
From DeltaMass: Average Mass: 88
t-butylsulfenyl
modification from DeltaMass
DeltaMass:0
StBu
A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two bromine atoms.
Y
Unimod:534
Br2Tyr
PSI-MOD
Dibromo
MOD:01006
dibrominated tyrosine
A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two bromine atoms.
Unimod:534
Br2Tyr
Dibromo
Dibromo
A protein modification that effectively substitutes an anisyl (methoxyphenyl) group for a hydroxyl group, typically at the 4 or para position.
90.13
C 7 H 6
90.04695
X
artifact
PSI-MOD
MOD:01007
From DeltaMass with no citation or formula: Average Mass: 90.
anisyl modified residue
A protein modification that effectively substitutes an anisyl (methoxyphenyl) group for a hydroxyl group, typically at the 4 or para position.
DeltaMass:0
A protein modification that effectively substitutes a benzyl (phenylmethyl) group for a hydrogen atom.
90.13
C 7 H 6
90.04695
X
artifact
PSI-MOD
MOD:01008
From DeltaMass with no citation or formula: Average Mass: 90
benzyl (Bzl) and benzyl ester (OBzl) modified residue
A protein modification that effectively substitutes a benzyl (phenylmethyl) group for a hydrogen atom.
DeltaMass:0
modification from DeltaMass
-2.02
C 0 H -2 N 0 O 0
-2.01565
C 5 H 5 N 1 O 1
95.1
95.03712
P
PSI-MOD
MOD:01009
From DeltaMass with no citation.
dehydrogenated proline
modification from DeltaMass
DeltaMass:0
A protein modification that effectively substitutes a trifluoroacetyl group for a hydrogen atom.
96.01
C 2 F 3 H -1 O 1
95.9823
X
artifact
TFA
PSI-MOD
MOD:01010
trifluoroacetylated residue
A protein modification that effectively substitutes a trifluoroacetyl group for a hydrogen atom.
DeltaMass:0
TFA
modification from DeltaMass
X
artifact
PSI-MOD
MOD:01011
From DeltaMass: Average Mass: 97
N-hydroxysuccinimide (ONSu, OSu)
modification from DeltaMass
DeltaMass:0
A protein modification that effectively oxidizes the disulfide bond of a cystine crosslink to form two cysteic acid residues.
98.01
C 0 H 2 N 0 O 6 S 0
97.98514
C 6 H 10 N 2 O 8 S 2
302.27
301.98785
MOD:00034
artifact
PSI-MOD
MOD:01012
Cross-link 2. This modification destroys a cross-link. From DeltaMass: Average Mass: 98 Abbreviation: Cya Average Mass Change: 98 Notes: Treatment of cystine by strongly oxidising reagents such as performic acid results in the breakage of the disulphide bond and complete oxidation of the sulphur atoms on each molecule. Such treatment is often carried out prior to amino acid analysis as the resulting cysteic acid is then resistant to acid degradation during the hydrolysis procedure.
oxidation of disulfide crosslink in cystine to two cysteic acids
A protein modification that effectively oxidizes the disulfide bond of a cystine crosslink to form two cysteic acid residues.
DeltaMass:335
modification from DeltaMass
X
PSI-MOD
MOD:01013
From DeltaMass: Average Mass: 98
tetramethylguanidinium termination by-product on amine
modification from DeltaMass
DeltaMass:0
modification from DeltaMass
X
PSI-MOD
MOD:01014
From DeltaMass: Average Mass: 98 Formula:H3PO4 or H2SO4 Monoisotopic Mass Change:97.97 Average Mass Change:98 Notes:Proteins may pick up non-covalent salt adducts during purification. Phosphate and sulphate salts are commonly used and may be observed as +98 amu adducts (or multiples thereof) forming ion pairs with basic residues. Monoisotopic masses H2SO4 97.967, H3PO4 97.977
phosphate/sulphate adduct of proteins
modification from DeltaMass
DeltaMass:358
A protein modification that inserts or replaces a residue with an isovaline.
C 5 H 9 N 1 O 1
99.13
99.06841
X
artifact
2-amino-2-methylbutanoic acid
Isovalyl (-I-,-Iva-)
Iva
PSI-MOD
MOD:01015
isovaline residue (Iva)
A protein modification that inserts or replaces a residue with an isovaline.
DeltaMass:110
2-amino-2-methylbutanoic acid
Isovalyl (-I-,-Iva-)
Iva
modification from DeltaMass
X
artifact
tBoc
PSI-MOD
MOD:01016
From DeltaMass: Average Mass: 100
t-butyloxycarbonyl
modification from DeltaMass
DeltaMass:0
tBoc
OBSOLETE because redundant and identical to MOD:00403. Remap to MOD:00403.
MOD:00403
M
artifact
PSI-MOD
MOD:01017
From DeltaMass: Average Mass: 101 Abbreviation:-Hse- Formula:C4H7O2N Monoisotopic Mass Change:101.048 Average Mass Change:101.105
homoseryl (-Hse-)
true
OBSOLETE because redundant and identical to MOD:00403. Remap to MOD:00403.
DeltaMass:113
modification from DeltaMass
X
artifact
Meb
PSI-MOD
MOD:01018
From DeltaMass: Average Mass: 104
4-methylbenzyl
modification from DeltaMass
DeltaMass:0
Meb
modification from DeltaMass
X
artifact
HMP
PSI-MOD
MOD:01019
From DeltaMass: Average Mass: 106
hydroxymethylphenyl linker
modification from DeltaMass
DeltaMass:0
HMP
modification from DeltaMass
X
artifact
PSI-MOD
MOD:01020
From DeltaMass: Average Mass: 106
thioanisyl
modification from DeltaMass
DeltaMass:0
modification from DeltaMass
X
artifact
PSI-MOD
MOD:01021
From DeltaMass: Average Mass: 106
thiocresyl
modification from DeltaMass
DeltaMass:0
A protein modification that effectively converts an L-lysine residue to 2-piperidinecarboxylic acid.
-17.03
C 0 H -3 N -1 O 0
-17.026548
C 6 H 9 N 1 O 1
111.14
111.06841
K
artifact
Pip
PSI-MOD
MOD:01022
2-piperidinecarboxylic acid
A protein modification that effectively converts an L-lysine residue to 2-piperidinecarboxylic acid.
DeltaMass:0
Pip
A protein modification that effectively converts an L-tyrosine residue to 3',5'-dibromo-L-tyrosine.
157.79
Br 2 C 0 H -2 N 0 O 0
155.82103
Br 2 C 9 H 7 N 1 O 2
320.97
318.88434
Y
3',5'-Br2Tyr
PSI-MOD
MOD:01023
3',5'-dibromo-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to 3',5'-dibromo-L-tyrosine.
DeltaMass:156
3',5'-Br2Tyr
A protein modification that effectively converts an L-proline residue to one of several monohydroxylated proline residues, including 3-hydroxy-L-proline and 4-hydroxy-L-proline.
16.0
C 0 H 0 N 0 O 1
15.994915
C 5 H 7 N 1 O 2
113.12
113.047676
P
natural
Unimod:35
uniprot.ptm:PTM-0149
Hy1Pro
Hydroxyproline
Hyp
hydroxylationp
PSI-MOD
Oxidation
MOD:01024
From DeltaMass: Average Mass: 131. This is the mass of the free amino acid [JSG].
monohydroxylated proline
A protein modification that effectively converts an L-proline residue to one of several monohydroxylated proline residues, including 3-hydroxy-L-proline and 4-hydroxy-L-proline.
DeltaMass:0
OMSSA:62
Unimod:35#P
Hy1Pro
Hydroxyproline
Hyp
hydroxylationp
Oxidation
A protein modification that effectively converts an L-tyrosine residue to 3'-bromo-L-tyrosine.
78.9
Br 1 H -1
77.910515
Br 1 C 9 H 8 N 1 O 2
242.07
240.97385
Y
3'-BrTyr
PSI-MOD
MOD:01025
3'-bromo-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to 3'-bromo-L-tyrosine.
PubMed:18688235
3'-BrTyr
A protein modification that inserts or replaces a residue with a norleucine.
C 6 H 11 N 1 O 1
113.16
113.08406
X
artifact
Nle
PSI-MOD
MOD:01026
norleucine residue (Nle)
A protein modification that inserts or replaces a residue with a norleucine.
DeltaMass:126
Nle
modification from DeltaMass
X
artifact
Aoc
PSI-MOD
MOD:01027
From DeltaMass: Average Mass: 114
t-amyloxycarbonyl
modification from DeltaMass
DeltaMass:0
Aoc
A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one chlorine atom.
34.44
C 0 Cl 1 H -1 N 0 O 0
33.96103
C 9 Cl 1 H 8 N 1 O 2
197.62
197.02435
Y
artifact
Cl1Tyr
PSI-MOD
MOD:01028
monochlorinated L-tyrosine
A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one chlorine atom.
PubMed:18688235
Cl1Tyr
A protein modification that effectively replaces a hydrogen atom with a succinyl group linked through a carbonyl carbon.
100.07
C 4 H 4 O 3
100.016045
X
Unimod:64
PSI-MOD
Succinic anhydride labeling reagent light form (N-term & K)
MOD:01029
From DeltaMass with no citation or formula, Average Mass: 117 [JSG].
succinylated residue
A protein modification that effectively replaces a hydrogen atom with a succinyl group linked through a carbonyl carbon.
DeltaMass:0
Unimod:64
Succinic anhydride labeling reagent light form (N-term & K)
modification from DeltaMass
X
artifact
HOBt
PSI-MOD
MOD:01030
From DeltaMass: Average Mass: 117
hydroxybenzotriazole ester
modification from DeltaMass
DeltaMass:0
HOBt
modification from DeltaMass
X
artifact
diMeBzl
PSI-MOD
MOD:01031
From DeltaMass: Average Mass: 118
dimethylbenzyl
modification from DeltaMass
DeltaMass:0
diMeBzl
A protein modification that effectively substitutes a benzyloxymethyl group for a hydrogen atom.
120.15
C 8 H 8 O 1
120.05752
X
artifact
Bom
PSI-MOD
MOD:01032
benzyloxymethyl modified residue
A protein modification that effectively substitutes a benzyloxymethyl group for a hydrogen atom.
DeltaMass:0
Bom
A protein modification that effectively substitutes a p-methoxybenzyl group for a hydrogen atom.
120.15
C 8 H 8 O 1
120.05752
X
artifact
Mbzl
Mob
PSI-MOD
MOD:01033
p-methoxybenzyl modified residue
A protein modification that effectively substitutes a p-methoxybenzyl group for a hydrogen atom.
DeltaMass:0
Mbzl
Mob
A protein modification that effectively substitutes a 4-nitrophenyl group for a hydrogen atom.
121.1
C 6 H 3 N 1 O 2
121.01638
X
artifact
ONp
p-nitrophenyl
PSI-MOD
MOD:01034
4-nitrophenyl modified residue
A protein modification that effectively substitutes a 4-nitrophenyl group for a hydrogen atom.
DeltaMass:0
ONp
p-nitrophenyl
modification from DeltaMass
X
artifact
ClBzl
PSI-MOD
MOD:01035
From DeltaMass: Average Mass: 125
chlorobenzyl
modification from DeltaMass
DeltaMass:0
ClBzl
OBSOLETE because redundant and identical to MOD:01181. Remap to MOD:01181.
MOD:01181
C 5 H 7 N 1 O 3
129.12
129.04259
D
PSI-MOD
MOD:01036
From DeltaMass:148 (name misspelled "aspartamyl", and formula incorrect, N and O reversed) Average Mass: 129 Formula: C5H7O1N3 Monoisotopic Mass Change: 129.042 Average Mass Change: 129.116
O-methyl aspartyl
true
OBSOLETE because redundant and identical to MOD:01181. Remap to MOD:01181.
PubMed:18688235
A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two chlorine atoms.
68.88
C 0 Cl 2 H -2 N 0 O 0
67.92206
C 9 Cl 2 H 7 N 1 O 2
232.06
230.98538
Y
artifact
Cl2Tyr
PSI-MOD
MOD:01037
dichlorinated tyrosine
A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two chlorine atoms.
PubMed:18688235
Cl2Tyr
OBSOLETE because this represents a free amino acid and the corresponding residue is MOD:01026.
PSI-MOD
MOD:01038
From DeltaMass: Average Mass: 131.
norleucine (Nle)
true
OBSOLETE because this represents a free amino acid and the corresponding residue is MOD:01026.
DeltaMass:0
OBSOLETE because redundant and identical to MOD:00036. Remap to MOD:00036.
MOD:00036
C 4 H 5 N 1 O 4
131.09
131.02185
D
PSI-MOD
MOD:01039
From DeltaMass:152 (name misspelled "aspartamyl", and formula incorrect, N and O reversed) Average Mass: 131 Formula:C4H5O1N4 Monoisotopic Mass Change:131.022 Average Mass Change:131.088
hydroxy aspartyl
true
OBSOLETE because redundant and identical to MOD:00036. Remap to MOD:00036.
PubMed:18688235
A protein modification that inserts or replaces a residue with a penicillamine.
C 5 H 9 N 1 O 1 S 1
131.19
131.04048
X
artifact
2-amino-3-mercapto-3-methylbutanoic acid
2-amino-3-methyl-3-sulfanylbutanoic acid
3,3-dimethylcysteine
3-mercapto-L-valine
Pen
beta,beta-dimethylcysteine
PSI-MOD
MOD:01040
From DeltaMass: Name misspelled 'bb-dimethyl cystenyl'. No citation provided.
penicillamine residue
A protein modification that inserts or replaces a residue with a penicillamine.
DeltaMass:154
2-amino-3-mercapto-3-methylbutanoic acid
2-amino-3-methyl-3-sulfanylbutanoic acid
3,3-dimethylcysteine
3-mercapto-L-valine
Pen
Pen
beta,beta-dimethylcysteine
A protein modification that effectively substitutes a benzyloxycarbonyl group for a hydrogen atom.
134.13
C 8 H 6 O 2
134.03677
artifact
Z
PSI-MOD
MOD:01041
benzyloxycarbonyl modified residue
A protein modification that effectively substitutes a benzyloxycarbonyl group for a hydrogen atom.
DeltaMass:0
Z
A protein modification that effectively substitutes a adamantyl group for a hydrogen atom.
134.22
C 10 H 14
134.10954
artifact
Ada
PSI-MOD
MOD:01042
adamantyl modified residue
A protein modification that effectively substitutes a adamantyl group for a hydrogen atom.
DeltaMass:0
Ada
A protein modification that effectively substitutes a p-nitrobenzyl group for the hydrogen atom of a carboxyl group.
135.12
C 7 H 5 N 1 O 2
135.03203
artifact
ONb
PSI-MOD
MOD:01043
p-nitrobenzyl ester modified residue
A protein modification that effectively substitutes a p-nitrobenzyl group for the hydrogen atom of a carboxyl group.
DeltaMass:0
ONb
OBSOLETE because redundant and identical to MOD:00080. Remap to MOD:00080.
MOD:00080
Q
PSI-MOD
MOD:01044
From DeltaMass with no citation. Formula:C6H10O2N2 (name misspelled, formula for N5-methylglutaminyl, rather than N2-methylglutamyl)
N-methyl glutamyl
true
OBSOLETE because redundant and identical to MOD:00080. Remap to MOD:00080.
DeltaMass:166
A protein modification that effectively converts an L-tyrosine residue to 3',5'-dichloro-L-tyrosine.
68.88
C 0 Cl 2 H -2 N 0 O 0
67.92206
C 9 Cl 2 H 7 N 1 O 2
232.06
230.98538
Y
artifact
3',5'-Cl2Tyr
PSI-MOD
MOD:01045
3',5'-dichloro-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to 3',5'-dichloro-L-tyrosine.
PubMed:18688235
3',5'-Cl2Tyr
A protein modification that effectively converts an L-tyrosine residue to 3'-chloro-L-tyrosine.
34.44
C 0 Cl 1 H -1 N 0 O 0
33.96103
C 9 Cl 1 H 8 N 1 O 2
197.62
197.02435
Y
artifact
3'-ClTyr
PSI-MOD
MOD:01046
3'-chloro-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to 3'-chloro-L-tyrosine.
PubMed:18688235
3'-ClTyr
A protein modification that effectively converts an L-lysine residue to a monohydroxylated lysine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 6 H 12 N 2 O 2
144.17
144.08987
K
natural
Unimod:35
Hy1Lys
Hydroxy Lysyl (-Hyl-)
hydroxylationk
PSI-MOD
Oxidation
MOD:01047
From DeltaMass: Average Mass: 144 Abbreviation:-Hyl- Formula:C6H12N2O2 Monoisotopic Mass Change:144.09 Average Mass Change:144.174.
monohydroxylated lysine
A protein modification that effectively converts an L-lysine residue to a monohydroxylated lysine.
DeltaMass:168
OMSSA:60
Unimod:35#K
Hy1Lys
Hydroxy Lysyl (-Hyl-)
hydroxylationk
Oxidation
A protein modification that effectively converts a source amino acid residue to 2-pyrrolidone-5-carboxylic acid.
C 5 H 6 N 1 O 2
112.11
112.039856
X
N-term
PyrGlu
PSI-MOD
MOD:01048
From DeltaMass: Average Mass: -18 Average Mass Change: -18.01 References:The conversion of glutamic acid to pyroglutamic was reported for the beta-amiloid protein. Miller et al. Arch. Biochem. Biophy. (1993) 301, 41-52.
2-pyrrolidone-5-carboxylic acid
A protein modification that effectively converts a source amino acid residue to 2-pyrrolidone-5-carboxylic acid.
PubMed:18688235
PyrGlu
A protein modification that effectively substitutes a hydrogen atom of an L-histidine residue with a halogen atom.
H
HalHis
PSI-MOD
MOD:01049
halogenated histidine
A protein modification that effectively substitutes a hydrogen atom of an L-histidine residue with a halogen atom.
PubMed:18688235
HalHis
modification from DeltaMass
A
artifact
PSI-MOD
MOD:01050
From DeltaMass: Average Mass: 148 Formula:C8H8O2N1 Monoisotopic Mass Change:148.064 Average Mass Change:148.165
pyridyl alanyl
modification from DeltaMass
DeltaMass:180
modification from DeltaMass
artifact
NBz
PSI-MOD
MOD:01051
From DeltaMass: Average Mass: 149
2-nitrobenzoyl
modification from DeltaMass
DeltaMass:0
NBz
modification from DeltaMass
W
artifact
PSI-MOD
MOD:01052
From DeltaMass: Average Mass: 150
dimethoxybenzyl Trp
modification from DeltaMass
DeltaMass:0
modification from DeltaMass
artifact
Nps
PSI-MOD
MOD:01053
From DeltaMass: Average Mass: 153
2-nitrophenylsulphenyl
modification from DeltaMass
DeltaMass:0
Nps
modification from DeltaMass
artifact
4-toluenesulphonyl
Tos
Tosyl
PSI-MOD
MOD:01054
From DeltaMass: Average Mass: 154
4-toluenesulfonyl
modification from DeltaMass
DeltaMass:0
4-toluenesulphonyl
Tos
Tosyl
modification from DeltaMass
artifact
Npys
PSI-MOD
MOD:01055
From DeltaMass: Average Mass: 154
3-nitro-2-pyridinesulfenyl
modification from DeltaMass
DeltaMass:0
Npys
modification from DeltaMass
155.82
(79)Br 2 C 0 H -2 N 0 O 0
155.82103
(79)Br 2 C 9 H 7 N 1 O 2
318.88
318.88434
Y
artifact
PSI-MOD
MOD:01056
From DeltaMass: Average Mass: 156
(79)Br labeled 3',5'-dibromotyrosine
modification from DeltaMass
DeltaMass:0
modification from DeltaMass
157.82
(79)Br 1 (81)Br 1 C 0 H -2 N 0 O 0
157.81898
(79)Br 1 (81)Br 1 C 9 H 7 N 1 O 2
320.88
320.8823
Y
artifact
PSI-MOD
MOD:01057
From DeltaMass: Average Mass: 158
(79)Br and (81)Br labeled 3',5'-dibromotyrosine
modification from DeltaMass
DeltaMass:0
modification from DeltaMass
artifact
Dcb
PSI-MOD
MOD:01058
From DeltaMass: Average Mass: 159
dichlorobenzyl
modification from DeltaMass
DeltaMass:0
Dcb
modification from DeltaMass
159.82
(81)Br 2 C 0 H -2 N 0 O 0
159.81693
(81)Br 2 C 9 H 7 N 1 O 2
322.88
322.88025
Y
artifact
PSI-MOD
MOD:01059
From DeltaMass: Average Mass: 160
(81)Br labeled 3',5'-dibromotyrosine
modification from DeltaMass
DeltaMass:0
A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine.
57.05
C 2 H 3 N 1 O 1 S 0
57.021465
C 5 H 8 N 2 O 2 S 1
160.19
160.03065
C
artifact
Unimod:4
CamC
CamCys
Carboxamidomethyl (on Cysteine)
Carboxyamidomethyl Cystenyl
S-carbamoylmethyl-L-cysteine
amidocarboxymethylcysteine
carbamidomethylc
carbamoylmethylcysteine
PSI-MOD
Carbamidomethyl
Iodoacetamide derivative
MOD:01060
From DeltaMass: (name misspelled "Carboxyamidomethyl Cystenyl") [JSG].
S-carboxamidomethyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine.
DeltaMass:196
DeltaMass:337
OMSSA:3
PubMed:10504701
PubMed:11510821
PubMed:12422359
PubMed:18306178
Unimod:4#C
CamC
CamCys
Carboxamidomethyl (on Cysteine)
Carboxyamidomethyl Cystenyl
S-carbamoylmethyl-L-cysteine
amidocarboxymethylcysteine
carbamidomethylc
carbamoylmethylcysteine
Carbamidomethyl
Iodoacetamide derivative
A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine.
58.04
C 2 H 2 N 0 O 2 S 0
58.005478
C 5 H 7 N 1 O 3 S 1
161.18
161.01466
C
artifact
Unimod:6
Carboxymethyl Cystenyl
Carboxymethyl cysteine
CmC
carboxymethylc
PSI-MOD
Carboxymethyl
Iodoacetic acid derivative
MOD:01061
From DeltaMass with no citation, name misspelled "Carboxymethyl Cystenyl", and formula incorrect, N and O reversed: Average Mass: 161 Abbreviation: -Cmc- Formula: C5H7O1N3S1 Monoisotopic Mass Change: 161.015 Average Mass Change: 161.179 [JSG].
S-carboxymethyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine.
DeltaMass:0
DeltaMass:197
OMSSA:2
Unimod:6#C
Carboxymethyl Cystenyl
Carboxymethyl cysteine
CmC
carboxymethylc
Carboxymethyl
Iodoacetic acid derivative
OBSOLETE because duplicate and redundant with MOD:01061. Remap to MOD:01061
MOD:01061
C 5 H 7 N 3 O 1 S 1
157.19
157.03099
C
artifact
Carboxymethyl Cystenyl
PSI-MOD
MOD:01062
From DeltaMass:197 (Name misspelled "cystenyl", and formula incorrect, N and O reversed) Abbreviation:-Cmc- Formula:C5H7O1N3S1 Monoisotopic Mass Change:161.015 Average Mass Change:161.179
carboxymethyl cysteinyl
true
OBSOLETE because duplicate and redundant with MOD:01061. Remap to MOD:01061
DeltaMass:197
Carboxymethyl Cystenyl
A protein modification that effectively converts an L-phenylalanine residue to a monomethylated phenylalanine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 10 H 11 N 1 O 1
161.2
161.08406
F
NMePhe
PSI-MOD
MOD:01063
From DeltaMass: Average Mass: 161 Formula: C10H11O1N1 Monoisotopic Mass Change: 161.084 Average Mass Change: 161.205. No citation provided. It is not obvious whether the DeltaMass entry is supposed to represent N-methylphenylalanine, alpha-methylphenylalanine, 2'-, 3'-, or 4'-methylphenylalanine [JSG].
monomethylated phenylalanine
A protein modification that effectively converts an L-phenylalanine residue to a monomethylated phenylalanine.
DeltaMass:198
NMePhe
modification from DeltaMass
PSI-MOD
MOD:01064
From DeltaMass: Average Mass: 162
inositol
modification from DeltaMass
DeltaMass:0
A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and a protein N-terminal amino group to form a Schiff-base or an Amadori ketosamine (or aminoketose) residue adduct.
162.14
C 6 H 10 O 5
162.05283
N-term
Unimod:41
PSI-MOD
MOD:01065
From DeltaMass: Average Mass: 162
hexose glycated N-terminal
A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and a protein N-terminal amino group to form a Schiff-base or an Amadori ketosamine (or aminoketose) residue adduct.
DeltaMass:0
Unimod:41#N-term
A protein modification that effectively substitutes a hydrogen atom of an L-phenylalanine residue with a halogen atom.
F
HalPhe
PSI-MOD
MOD:01066
halogenated phenylalanine
A protein modification that effectively substitutes a hydrogen atom of an L-phenylalanine residue with a halogen atom.
PubMed:18688235
HalPhe
modification from DeltaMass
artifact
PSI-MOD
MOD:01067
From DeltaMass: Average Mass: 162 Average Mass Change:162 Notes: (from the ABRF discussion list archive) There may be ... things in the reagent K that would allow cleavage of the peptide to occur at the wrong place...in this case it removes the dimethoxybenzyl group first inactivating that site for cleavage, and it goes after tne next amide bond closer to the resin. Try the TFA/TIS/water/EDT cocktail...TFA = 92%, TIS =3%, and water is at 5%. .. had this issue on longer peptides.. and by increasing the amount of water a little bit... able to elminate this problem.
linker attached to peptide in Fmoc peptide synthesis
modification from DeltaMass
DeltaMass:341
A protein modification that effectively substitutes a hydrogen atom of an L-tryptophan residue with a halogen atom.
W
HalTrp
PSI-MOD
MOD:01068
halogenated tryptophan
A protein modification that effectively substitutes a hydrogen atom of an L-tryptophan residue with a halogen atom.
PubMed:18688235
HalTrp
A protein modification that effectively substitutes a 2,4-dinitrophenyl group for a hydrogen atom.
166.09
C 6 H 2 N 2 O 4
166.00145
artifact
Dnp
PSI-MOD
MOD:01069
2,4-dinitrophenyl modified residue
A protein modification that effectively substitutes a 2,4-dinitrophenyl group for a hydrogen atom.
DeltaMass:0
Dnp
A protein modification that effectively substitutes a pentafluorophenyl group for a hydrogen atom.
166.05
C 6 F 5 H -1
165.98419
artifact
Pfp
PSI-MOD
MOD:01070
From DeltaMass: name mispelled "pentaflourophenyl"
pentafluorophenyl modified residue
A protein modification that effectively substitutes a pentafluorophenyl group for a hydrogen atom.
DeltaMass:0
Pfp
A protein modification that effectively substitutes a diphenylmethyl group for a hydrogen atom.
166.22
C 13 H 10
166.07825
X
artifact
Dpm
PSI-MOD
MOD:01071
diphenylmethyl modified residue
A protein modification that effectively substitutes a diphenylmethyl group for a hydrogen atom.
DeltaMass:0
Dpm
A protein modification that effectively substitutes one potassium atom for one hydrogen atom.
38.09
H -1 K 1
37.955883
X
K1Res
PSI-MOD
MOD:01072
monopotassium salt
A protein modification that effectively substitutes one potassium atom for one hydrogen atom.
DeltaMass:0
K1Res
A protein modification that effectively substitutes a 2-chlorobenzyloxycarbonyl group for a hydrogen atom.
169.58
C 8 Cl 1 H 6 O 2
169.00563
X
artifact
Clz
PSI-MOD
MOD:01073
2-chlorobenzyloxycarbonyl modified residue
A protein modification that effectively substitutes a 2-chlorobenzyloxycarbonyl group for a hydrogen atom.
DeltaMass:0
Clz
A protein modification that effectively substitutes a napthylacetyl group for a hydrogen atom.
169.2
C 12 H 9 O 1
169.06534
X
artifact
PSI-MOD
MOD:01074
napthylacetyl modified residue
A protein modification that effectively substitutes a napthylacetyl group for a hydrogen atom.
DeltaMass:0
A protein modification that effectively substitutes a mercury atom or a cluster containing mercury for hydrogen atoms, or that coordinates a mercury ion.
HgRes
PSI-MOD
MOD:01075
mercury containing modified residue
A protein modification that effectively substitutes a mercury atom or a cluster containing mercury for hydrogen atoms, or that coordinates a mercury ion.
PubMed:18688235
HgRes
modification from DeltaMass - OBSOLETE because redundant and identical to MOD:00414. Remap to MOD:00414.
MOD:00414
C 7 H 14 N 4 O 1
170.22
170.11676
R
PSI-MOD
MOD:01076
From DeltaMass: Average Mass: 170 Formula:C7H14O4N1 Monoisotopic Mass Change:170.117 Average Mass Change:170.215
N-methyl arginyl
true
modification from DeltaMass - OBSOLETE because redundant and identical to MOD:00414. Remap to MOD:00414.
DeltaMass:215
modification from DeltaMass
artifact
PSI-MOD
MOD:01077
From DeltaMass: Average Mass: 172 Average Mass Change:172 References:[1]. Sieber,P.(1987) Modification of tryptophan residues during acidolysis of4-methoxy-2,3,6-trimethylbenzenesulfonyl groups. Effects of scavengers. Tetrahedron Lett., 28(15),1637-1640. Notes: TFA-cyclic dithioketal by-product is formed when Trp-containing peptide is subjected to prolonged TFA/EDT treatment [1]. See structure at http://www.abrf.org/images/misc/dmass172.gif. Additional discussion of this adduct, and how to avoid it, can befound in Methods in Enzymology 289, 67 (1997)
ethanedithiol/TFA cyclic adduct
modification from DeltaMass
DeltaMass:216
A protein modification that effectively converts an L-threonine residue to S-(2-aminoethyl)-3-methylcysteine.
59.13
C 2 H 5 N 1 O -1 S 1
59.019356
C 6 H 12 N 2 O 1 S 1
160.24
160.06703
T
artifact
Unimod:472
2-amino-3-(2-aminoethyl)sulfanyl-3-methylbutanoic acid
S-aminoethyl-3-methylcysteine
PSI-MOD
AEC-MAEC
beta-methylaminoethylcysteine
MOD:01078
From DeltaMass: Average Mass: 146 Abbreviation:-AECys_ Formula:C5H10O2N1S1 Monoisotopic Mass Change:146.051 Average Mass Change:146.214 References:PE Sciex.
S-(2-aminoethyl)-3-methylcysteine (Thr)
A protein modification that effectively converts an L-threonine residue to S-(2-aminoethyl)-3-methylcysteine.
PubMed:12923550
Unimod:472#T
2-amino-3-(2-aminoethyl)sulfanyl-3-methylbutanoic acid
S-aminoethyl-3-methylcysteine
AEC-MAEC
beta-methylaminoethylcysteine
A protein modification that effectively converts an L-cysteine residue to S-[(acetylamino)methyl]-L-cysteine.
71.08
C 3 H 5 N 1 O 1 S 0
71.03712
C 6 H 10 N 2 O 2 S 1
174.22
174.0463
C
artifact
Acetamidomethyl Cystenyl
Acm-Cys
N-(hydroxymethyl)acetamide derivatized L-cysteine
S-(acetamido)methyl-L-cysteine
PSI-MOD
MOD:01079
From DeltaMass: (name misspelled "Acetamidomethyl Cystenyl") Average Mass: 174 Formula: C 6 H 10 O 2 N 2 S 1 Monoisotopic Mass Change: 174.046 Average Mass Change: 174.221. [These are aggregate masses, not delta masses.] See Organic Syntheses, Coll. Vol. 6, p.5 (1988); Vol. 59, p.190 (1979); http://www.orgsyn.org/orgsyn/orgsyn/prepContent.asp?prep=cv6p0005 [JSG].
S-(acetylamino)methyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-[(acetylamino)methyl]-L-cysteine.
DeltaMass:218
PubMed:8572278
Acetamidomethyl Cystenyl
Acm-Cys
N-(hydroxymethyl)acetamide derivatized L-cysteine
S-(acetamido)methyl-L-cysteine
OBSOLETE because this is identical to MOD:00417. modification from DeltaMass
MOD:00417
C 6 H 10 N 2 O 2 S 1
174.22
174.0463
C
artifact
Acrylamidyl Cystenyl
PSI-MOD
MOD:01080
From DeltaMass: (name misspelled "Acrylamidyl Cystenyl") Average Mass: 174 Formula: C6H10O2N2S1 Monoisotopic Mass Change: 174.046 Average Mass Change: 174.221
acrylamidyl cysteinyl
true
OBSOLETE because this is identical to MOD:00417. modification from DeltaMass
DeltaMass:219
Acrylamidyl Cystenyl
modification from DeltaMass
178.14
C 6 H 10 O 6
178.04774
PSI-MOD
MOD:01081
From DeltaMass: Average Mass: 177. CAUTION - mass does not match formula.
delta-glycosyloxy- (of lysine) or beta-glycosyloxy- (of phenylalanine or tyrosine)
modification from DeltaMass
DeltaMass:0
OBSOLETE because redundant with MOD:00757, remap. modification from DeltaMass
MOD:00757
178.14
C 6 H 10 O 6
178.04774
C 11 H 17 N 1 O 6
259.26
259.1056
P
PSI-MOD
MOD:01082
From DeltaMass: Average Mass: 177. Caution: Formula does not match mass. The natural glycosylating sugar of hydroxyproline is galactose.
4-glycosyloxy- (hexosyl, C6) (of proline)
true
OBSOLETE because redundant with MOD:00757, remap. modification from DeltaMass
DeltaMass:0
A protein modification that effectively converts an L-serine residue to O-benzyl-L-serine.
90.13
C 7 H 6
90.04695
C 10 H 11 N 1 O 2
177.2
177.07898
S
artifact
PSI-MOD
MOD:01083
O-benzyl-L-serine
A protein modification that effectively converts an L-serine residue to O-benzyl-L-serine.
DeltaMass:0
A protein modification that by reaction of iodoacetic acid effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a carboxymethyl group.
58.04
C 2 H 2 O 2
58.005478
X
artifact
N-term
Unimod:6
Carboxymethyl (on Cysteine)
PSI-MOD
Carboxymethyl
Iodoacetic acid derivative
MOD:01084
iodoacetic acid derivatized amino-terminal residue
A protein modification that by reaction of iodoacetic acid effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a carboxymethyl group.
Unimod:6#N-term
Carboxymethyl (on Cysteine)
Carboxymethyl
Iodoacetic acid derivative
A protein modification that effectively replaces the N-terminal hydrogen atom of a N-terminal histidine residue with a gluconoyl group linked through a glycosidic bond. modification from DeltaMass
179.15
C 6 H 11 O 6
179.05556
C 12 H 18 N 3 O 7
316.29
316.11447
H
natural
N-term
PSI-MOD
MOD:01085
Occurs on His-tagged proteins expresssed in E. coli. From DeltaMass: Average Mass: 178 Formula: C6H10O6 Monoisotopic Mass Change: 178.05 Average Mass Change: 178.14 References: Geoghegan, K. F., H. B. Dixon, et al. (1999). Spontaneous alpha-N-6-phosphogluconoylation of a His tag in Escherichia coli: the cause of extra mass of 258 or 178 Da in fusion proteins. Anal Biochem 267(1): 169-84. Mass listed here is 179 because it's N-terminal.
alpha-N-gluconoylated L-histidine
A protein modification that effectively replaces the N-terminal hydrogen atom of a N-terminal histidine residue with a gluconoyl group linked through a glycosidic bond. modification from DeltaMass
DeltaMass:226
PubMed:9918669
modification from DeltaMass
artifact
4Nz
PSI-MOD
MOD:01086
From DeltaMass: Average Mass: 179
p-nitrobenzyloxycarbonyl
modification from DeltaMass
DeltaMass:0
4Nz
A protein modification that effectively substitutes a 2,4,5-trichlorophenyl group for a hydrogen atom.
179.42
C 6 Cl 3 H 1
177.91438
artifact
PSI-MOD
MOD:01087
2,4,5-trichlorophenyl modified residue
A protein modification that effectively substitutes a 2,4,5-trichlorophenyl group for a hydrogen atom.
DeltaMass:0
A protein modification that effectively substitutes a 2,4,6-trimethyloxybenzyl group for a hydrogen atom.
180.2
C 10 H 12 O 3
180.07864
X
artifact
Tmob
PSI-MOD
MOD:01088
2,4,6-trimethyloxybenzyl modified residue
A protein modification that effectively substitutes a 2,4,6-trimethyloxybenzyl group for a hydrogen atom.
DeltaMass:0
Tmob
modification from DeltaMass
artifact
Xan
PSI-MOD
MOD:01089
From DeltaMass: Average Mass: 180
xanthyl
modification from DeltaMass
DeltaMass:0
Xan
A protein modification that by reaction of iodoacetamide effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a carboxamidomethyl group.
57.05
C 2 H 3 N 1 O 1
57.021465
X
artifact
N-term
Unimod:4
(carbamoylmethyl)amino
PSI-MOD
Carbamidomethyl
Iodoacetamide derivative
MOD:01090
iodoacetamide derivatized amino-terminal residue
A protein modification that by reaction of iodoacetamide effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a carboxamidomethyl group.
PubMed:11327326
PubMed:11510821
PubMed:12422359
Unimod:4#N-term
(carbamoylmethyl)amino
Carbamidomethyl
Iodoacetamide derivative
A protein modification that effectively substitutes one hydrogen atom of an L-phenylalanine residue with one chlorine atom.
34.44
C 0 Cl 1 H -1 N 0 O 0
33.96103
C 9 Cl 1 H 8 N 1 O 1
181.62
181.02945
F
artifact
Cl1Phe
PSI-MOD
MOD:01091
From DeltaMass: Average Mass: 182 Formula:C9H8O1N1Cl1 Monoisotopic Mass Change:181.029 Average Mass Change:181.623
monochlorinated L-phenylalanine
A protein modification that effectively substitutes one hydrogen atom of an L-phenylalanine residue with one chlorine atom.
DeltaMass:233
Cl1Phe
modification from DeltaMass
artifact
Mts
PSI-MOD
MOD:01092
From DeltaMass: Average Mass: 182
mesitylene-2-sulfonyl
modification from DeltaMass
DeltaMass:0
Mts
modification from DeltaMass
C 9 H 16 N 2 O 2
184.24
184.12119
K
artifact
PSI-MOD
MOD:01093
From DeltaMass: Average Mass: 184 Formula: C9H16O2N2 Monoisotopic Mass Change: 184.12 Average Mass Change: 184.24 with no citation.
isopropyl lysyl
modification from DeltaMass
DeltaMass:236
A protein modification that effectively converts an L-lysine residue to N6-carboxymethyl-L-lysine.
58.04
C 2 H 2 O 2
58.005478
C 8 H 14 N 2 O 3
186.21
186.10045
K
artifact
Unimod:6
Carboxymethyl Lysyl
PSI-MOD
Carboxymethyl
Iodoacetic acid derivative
MOD:01094
From DeltaMass:237 (with no citation, formula incorrect, N and O reversed) Average Mass: 186 Formula: C8H14O2N3 Monoisotopic Mass Change: 186.1 Average Mass Change: 186.211 [JSG].
N6-carboxymethyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-carboxymethyl-L-lysine.
DeltaMass:237
Unimod:6#K
Carboxymethyl Lysyl
Carboxymethyl
Iodoacetic acid derivative
Modification from DeltaMass. OBSOLETE because not an amino acid modification.
C 10 H 8 N 1 O 3
190.18
190.05042
X
artifact
PSI-MOD
MOD:01095
From DeltaMass with no citation, formula incorrect, N and O reversed: Formula: C10H8O1N3 Monoisotopic Mass Change: 190.05 Average Mass Change: 190.18.
Matrix alpha cyano MH+
true
Modification from DeltaMass. OBSOLETE because not an amino acid modification.
DeltaMass:240
A protein modification that effectively converts an L-threonine residue to O-benzyl-L-threonine.
90.13
C 7 H 6
90.04695
C 11 H 13 N 1 O 2
191.23
191.09464
T
artifact
PSI-MOD
MOD:01096
O-benzyl-L-threonine
A protein modification that effectively converts an L-threonine residue to O-benzyl-L-threonine.
DeltaMass:0
A protein modification that effectively converts an L-cysteine residue to S-benzyl-L-cysteine.
90.13
C 7 H 6
90.04695
C 10 H 11 N 1 O 1 S 1
193.26
193.05614
C
artifact
PSI-MOD
MOD:01097
From DeltaMass: misspelled "Benzyl Cystenyl".
S-benzyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-benzyl-L-cysteine.
DeltaMass:242
A protein modification that inserts or replaces a residue with a naphthylalanine.
C 13 H 11 N 1 O 1
197.24
197.08406
X
artifact
PSI-MOD
MOD:01098
From DeltaMass: Average Mass: 197 Formula: C13H11O1N1 Monoisotopic Mass Change: 197.084 Average Mass Change: 197.238. No citation provided. It is not obvious which isomer of naphthylalanine this DeltaMass entry is supposed to represent [JSG].
naphthylalanine residue
A protein modification that inserts or replaces a residue with a naphthylalanine.
DeltaMass:243
A protein modification that effectively converts an L-aspartic acid residue to succinyl beta-aspartyl anhydride.
82.06
C 4 H 2 N 0 O 2
82.00548
C 8 H 8 N 1 O 5
198.15
198.04025
D
artifact
N-term
succinyl aspartamyl
PSI-MOD
MOD:01099
From DeltaMass with no citation (name misspelled "aspartamyl", and formula incorrect, N and O reversed) Average Mass: 198 Formula: C8H8O1N5 Monoisotopic Mass Change: 198.04 Average Mass Change: 198.156 [JSG].
succinyl beta-aspartyl anhydride
A protein modification that effectively converts an L-aspartic acid residue to succinyl beta-aspartyl anhydride.
DeltaMass:244
succinyl aspartamyl
modification from DeltaMass
artifact
PSI-MOD
MOD:01100
From DeltaMass: Average Mass: 201 with no citation.
HMP (hydroxymethylphenyl)/TFA adduct
modification from DeltaMass
DeltaMass:0
OBSOLETE because erroneous and apparently redundant to MOD:00111. Remap to MOD:00111.
MOD:00111
PSI-MOD
MOD:01101
Modification from DeltaMass: Average Mass: 206. This entry with no other information available appears to be the same as the entry at 204 for "Farnesylation" but with an incorrect mass.
S-Farnesyl-
true
OBSOLETE because erroneous and apparently redundant to MOD:00111. Remap to MOD:00111.
DeltaMass:0
OBSOLETE because redundant and identical to MOD:00504. Remap to MOD:00504.
MOD:00504
natural
PSI-MOD
MOD:01102
From DeltaMass: Average Mass: 206 Formula: C14 H22 O1 Monoisotopic Mass Change: 206.167 Average Mass Change: 206.324 References: Neubert TA, Johnson RS, Hurley JB, Walsh KA (1992). The rod transducin alpha subunit amino terminus is heterogeneously fatty acylated. J Biol Chem. 267(26), 18274-7. Notes: Modification of protein N-terminus with (cis,cis-delta 5, delta 8)-tetradecadienoyl group (myristoylation with 2 double bonds)
myristoylation-4H (two double bonds)
true
OBSOLETE because redundant and identical to MOD:00504. Remap to MOD:00504.
DeltaMass:348
OBSOLETE because redundant and identical to MOD:00503. Remap to MOD:00503.
MOD:00503
natural
PSI-MOD
MOD:01103
From DeltaMass with no citation or formula: Average Mass: 208.
myristoleylation (one double bond)
true
OBSOLETE because redundant and identical to MOD:00503. Remap to MOD:00503.
DeltaMass:0
modification from DeltaMass
artifact
Mtr
PSI-MOD
MOD:01104
From DeltaMass: Average Mass: 212 with no citation.
4-methoxy-2,3,6-trimethylbenzenesulfonyl
modification from DeltaMass
DeltaMass:0
Mtr
modification from DeltaMass
artifact
BrZ
PSI-MOD
MOD:01105
From DeltaMass: Average Mass: 213 with no citation.
2-bromobenzyloxycarbonyl
modification from DeltaMass
DeltaMass:0
BrZ
A protein modification that effectively converts an L-tryptophan residue to N-formyl-L-tryptophan.
28.01
C 1 H 0 N 0 O 1
27.994915
C 12 H 10 N 2 O 2
214.22
214.07423
W
artifact
formyl tryptophanyl
PSI-MOD
MOD:01106
From DeltaMass with no citation or formula: Average Mass: 214. It is not clear what this is supposed to represent. The mass corresponds to an N-formyl tryptophan (either N2 or N1'), but neither of these modifications has been reported as commonly encountered. It may have been confused with N'-formyl-L-kynurenine, see MOD:00464 [JSG]
N-formyl-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to N-formyl-L-tryptophan.
DeltaMass:0
formyl tryptophanyl
A protein modification that effectively converts an L-glutamic acid residue to O5-benzyl-L-glutamate.
90.13
C 7 H 6
90.04695
C 12 H 13 N 1 O 3
219.24
219.08954
E
artifact
PSI-MOD
MOD:01107
From DeltaMass with no citation: (formula incorrect, N and O reversed; mass incorrect, aggregate not delta) Average Mass: 219 Formula: C12H13O1N3 Monoisotopic Mass Change: 219.241 Average Mass Change: 219.09 [JSG].
O5-benzyl-L-glutamate
A protein modification that effectively converts an L-glutamic acid residue to O5-benzyl-L-glutamate.
DeltaMass:258
A protein modification that effectively converts an L-glutamic acid residue to 2-amino-5-(4-methoxyphenyl)-5-oxopentanoic acid, glutamtic acid anisole adduct.
90.13
C 7 H 6
90.04695
C 12 H 13 N 1 O 3
219.24
219.08954
E
artifact
anisole adducted glutamyl
PSI-MOD
MOD:01108
From DeltaMass with no citation: (formula incorrect, N and O reversed; mass incorrect, aggregate not delta) Average Mass: 219 Formula: C12H13O1N3 Monoisotopic Mass Change: 219.241 Average Mass Change: 219.09 [JSG].
2-amino-5-(4-methoxyphenyl)-5-oxopentanoic acid (Glu)
A protein modification that effectively converts an L-glutamic acid residue to 2-amino-5-(4-methoxyphenyl)-5-oxopentanoic acid, glutamtic acid anisole adduct.
DeltaMass:259
anisole adducted glutamyl
modification from DeltaMass
artifact
PSI-MOD
MOD:01109
From DeltaMass: Average Mass: 222 with no citation.
9-fluorenylmethyloxycarbonyl (Fmoc)
modification from DeltaMass
DeltaMass:0
A protein modification that effectively replaces a hydrogen atom of an L-cysteine residue with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20).
C
IpCys
PSI-MOD
MOD:01110
isoprenylated cysteine
A protein modification that effectively replaces a hydrogen atom of an L-cysteine residue with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20).
PubMed:18688235
IpCys
A protein modification that effectively substitutes a dimethoxybenzhydryl group for a hydrogen atom.
226.27
C 15 H 14 O 2
226.09938
artifact
4,4'-dimethoxybenzhydryl
Mbh
bis(4-methoxyphenyl)methyl
PSI-MOD
MOD:01111
From DeltaMass: Average Mass: 226 with no citation. A reagent, typically 4,4'-dimethoxybenzhydryl chloride, used as a protecting group for the carboxamido group of asparagine and glutamine during chemical peptide synthesis [JSG].
dimethoxybenzhydryl modified residue
A protein modification that effectively substitutes a dimethoxybenzhydryl group for a hydrogen atom.
DeltaMass:0
4,4'-dimethoxybenzhydryl
Mbh
bis(4-methoxyphenyl)methyl
modification from DeltaMass
105.1
C 6 H 3 N 1 O 1
105.02146
C 12 H 15 N 3 O 2
233.27
233.11642
K
artifact
nicotinyl lysyl
PSI-MOD
MOD:01112
From DeltaMass: (name misspelled "nicotinyl"; formula incorrect, N and O reversed; mass incorrect, aggregate not delta) Average Mass: 233 Formula: C12H15O3N2 Monoisotopic Mass Change: 233.116 Average Mass Change: 233.271
nicotinoyl lysine
modification from DeltaMass
DeltaMass:266
nicotinyl lysyl
modification from DeltaMass
artifact
Bpoc
PSI-MOD
MOD:01113
From DeltaMass: Average Mass: 238 with no citation.
2-(p-biphenyl)isopropyl-oxycarbonyl
modification from DeltaMass
DeltaMass:0
Bpoc
modification from DeltaMass
242.32
C 19 H 14
242.10954
artifact
Trityl
Trt
PSI-MOD
MOD:01114
From DeltaMass: Average Mass: 242 Average Mass Change: 242.3 Notes: blocking group used in peptide synthesis for C,H,Q,N
triphenylmethyl
modification from DeltaMass
DeltaMass:270
Trityl
Trt
A protein modification that effectively replaces a hydrogen atom of an L-tryptophan residue with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20).
W
IpTrp
PSI-MOD
MOD:01115
isoprenylated tryptophan
A protein modification that effectively replaces a hydrogen atom of an L-tryptophan residue with a group derived from an isoprene polymer, such as a geranyl (C10), farnesyl (C15) or geranylgeranyl (C20).
PubMed:18688235
IpTrp
A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine methyl ester.
218.38
C 16 H 26 N 0 O 0 S 0
218.20345
C 19 H 32 N 1 O 2 S 1
338.53
338.21536
C
natural
C-term
SFarnOMeCys
PSI-MOD
MOD:01116
S-farnesyl-L-cysteine methyl ester
A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine methyl ester.
PubMed:15609361
RESID:AA0102#var
RESID:AA0105#var
SFarnOMeCys
modification from DeltaMass
artifact
Pbf
PSI-MOD
MOD:01117
From DeltaMass: Average Mass: 252 with no citation.
pentamethyldihydrobenzofuransulfonyl
modification from DeltaMass
DeltaMass:0
Pbf
A protein modification that effectively replaces the N-terminal hydrogen atom of a N-terminal histidine residue with a 6-phosphogluconoyl group linked through a glycosidic bond. modification from DeltaMass
259.12
C 6 H 12 O 9 P 1
259.02188
C 12 H 19 N 3 O 10 P 1
396.27
396.0808
H
natural
N-term
PSI-MOD
MOD:01118
Occurs on His-tagged proteins expresssed in E. coli.From DeltaMass: Average Mass: 258 Formula: C6H10O6HPO3 Monoisotopic Mass Change: 258.01 Average Mass Change: 258.12 References: Geoghegan, K. F., H. B. Dixon, et al. (1999). Spontaneous alpha-N-6-phosphogluconoylation of a His tag in Escherichia coli: the cause of extra mass of 258 or 178 Da in fusion proteins. Anal Biochem 267(1): 169-84. Mass is one Da higher because this is an N-terminal modification
alpha-N-6-phosphogluconoylated L-histidine
A protein modification that effectively replaces the N-terminal hydrogen atom of a N-terminal histidine residue with a 6-phosphogluconoyl group linked through a glycosidic bond. modification from DeltaMass
DeltaMass:275
PubMed:9918669
A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine methyl ester.
286.5
C 21 H 34 N 0 O 0 S 0
286.26605
C 24 H 40 N 1 O 2 S 1
406.65
406.27798
C
natural
C-term
SGergerOMeCys
PSI-MOD
MOD:01119
S-geranylgeranyl-L-cysteine methyl ester
A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine methyl ester.
PubMed:1483450
PubMed:15609361
RESID:AA0104#var
RESID:AA0105#var
SGergerOMeCys
A protein modification that is produced by formation of an adduct with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride.
266.36
C 14 H 18 O 3 S 1
266.09766
X
artifact
2,2,5,7,8-pentamethyl-3,4-dihydro-2H-chromene-6-sulfonyl
2,2,5,7,8-pentamethyl-6-chromansulfonyl
2,2,5,7,8-pentamethyl-chromane-6-sulfonyl
2,2,5,7,8-pentamethylchroman-6-sulfonyl
2,2,5,7,8-pentamethylchroman-6-sulphonyl
3,4-dihydro-2,2,5,7,8-pentamethyl-2H-1-benzopyran-6-sulfonyl
Pmc
PmcRes
PSI-MOD
MOD:01120
From DeltaMass: Average Mass: 266 Notes: blocking group for Arg in peptide synthesis. CAS:112160-39-1 [JSG].
2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride derivatized residue
A protein modification that is produced by formation of an adduct with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride.
DeltaMass:0
2,2,5,7,8-pentamethyl-3,4-dihydro-2H-chromene-6-sulfonyl
2,2,5,7,8-pentamethyl-6-chromansulfonyl
2,2,5,7,8-pentamethyl-chromane-6-sulfonyl
2,2,5,7,8-pentamethylchroman-6-sulfonyl
2,2,5,7,8-pentamethylchroman-6-sulphonyl
3,4-dihydro-2,2,5,7,8-pentamethyl-2H-1-benzopyran-6-sulfonyl
Pmc
PmcRes
modification from DeltaMass
artifact
Mmt
PSI-MOD
MOD:01121
From DeltaMass: Average Mass: 272 Average Mass Change: 272
monomethoxytrityl
modification from DeltaMass
DeltaMass:280
Mmt
OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
PSI-MOD
MOD:01122
From DeltaMass: Average Mass: 289 with no citation.
5'phos dCytidinyl
true
OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
DeltaMass:0
OBSOLETE because redundant and identical to MOD:01123. Remap to MOD:01123.
MOD:01123
Y
PSI-MOD
MOD:01123
From DeltaMass: Average Mass: 289
monoiodated tyrosine
true
OBSOLETE because redundant and identical to MOD:01123. Remap to MOD:01123.
DeltaMass:0
modification from DeltaMass
162.14
C 6 H 10 N 0 O 5
162.05283
C 12 H 22 N 2 O 6
290.32
290.1478
K
PSI-MOD
MOD:01124
From DeltaMass: (formula incorrect, N and O reversed; mass incorrect, aggregate not delta) Average Mass: 290 Formula: C12H22O2N6 Monoisotopic Mass Change: 290.148 Average Mass Change: 290.317
aldohexosyl lysyl
modification from DeltaMass
DeltaMass:285
OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
PSI-MOD
MOD:01125
From DeltaMass: Average Mass: 304 with no citation.
5'phos dThymidinyl
true
OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
DeltaMass:0
OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
PSI-MOD
MOD:01126
From DeltaMass: Average Mass: 305 with no citation.
5'phos Cytidinyl
true
OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
DeltaMass:0
OBSOLETE because redundant and identical to MOD:01166. Remap to MOD:01166.
MOD:01166
PSI-MOD
MOD:01127
From DeltaMass: Average Mass: 306 Formula: C9H11O2N8P1 Monoisotopic Mass Change: 306.025 Average Mass Change: 306.17
5'phos Uridinyl
true
OBSOLETE because redundant and identical to MOD:01166. Remap to MOD:01166.
DeltaMass:292
modification from DeltaMass
NeuGc
PSI-MOD
MOD:01128
From DeltaMass: Average Mass: 307 with no citation.
N-glycolneuraminic acid
modification from DeltaMass
DeltaMass:0
NeuGc
OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
PSI-MOD
MOD:01129
From DeltaMass: Average Mass: 313 Formula: C10H12O5N5P1 Monoisotopic Mass Change: 313.058 Average Mass Change: 313.211
5'phos dAdenosyl
true
OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
DeltaMass:295
modification from DeltaMass
artifact
PSI-MOD
MOD:01130
From DeltaMass: Average Mass: 327 Formula: C17H17O3N4 Monoisotopic Mass Change: 327.122 Average Mass Change: 327.342
SucPhencarb Lysyl
modification from DeltaMass
DeltaMass:297
OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
PSI-MOD
MOD:01131
From DeltaMass: Average Mass: 329
5'phos dGuanosyl
true
OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
DeltaMass:0
OBSOLETE because redundant and identical to MOD:01165. Remap to MOD:01165.
MOD:01165
PSI-MOD
MOD:01132
From DeltaMass: Average Mass: 329
5'phos Adenosinyl
true
OBSOLETE because redundant and identical to MOD:01165. Remap to MOD:01165.
DeltaMass:0
A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine methyl ester.
234.38
C 16 H 26 N 0 O 1 S 0
234.19836
C 19 H 32 N 1 O 3 S 1
354.53
354.2103
C
natural
C-term
S12HyFarnOMeCys
PSI-MOD
MOD:01133
S-12-hydroxyfarnesyl-L-cysteine methyl ester
A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine methyl ester.
PubMed:17790543
RESID:AA0103#var
RESID:AA0105#var
S12HyFarnOMeCys
modification from DeltaMass
artifact
PSI-MOD
MOD:01134
From DeltaMass: Average Mass: 359 Formula: C21H11O6 Monoisotopic Mass Change: 359.055 Average Mass Change: 359.315 Notes: Using the DHB matrix at low pH the carboxyl group and one of the oxygens on the flurorescein molecule are protinated so the delta mass is 2Da higher than most text book illustrations would indicate. See Bioconjugate Techniques by Greg Hermanson, Academic Press, page 305, figure 204. Text books of course just show the coupling reaction at neutral or basic pH.
fluorescein labelling of peptide N-terminal using NHS ester
modification from DeltaMass
DeltaMass:306
modification from DeltaMass
PSI-MOD
MOD:01135
From DeltaMass: Average Mass: 365 with no citation.
Hex-HexNAc
modification from DeltaMass
DeltaMass:0
OBSOLETE because this is a small molecule contaminant and not a modification to a polypeptide. modification from DeltaMass
artifact
PSI-MOD
MOD:01136
From DeltaMass: Average Mass: 391 Average Mass Change: 391 Notes: A common plasticizer, and, unfortunaltely, a common contaminate. A sodium adduct is often associated with this peak at 413.
dioctyl phthalate
true
OBSOLETE because this is a small molecule contaminant and not a modification to a polypeptide. modification from DeltaMass
DeltaMass:309
A protein modification that is produced by reaction of a lysine residue with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride, to form N6-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-lysine.
266.36
C 14 H 18 O 3 S 1
266.09766
C 20 H 30 N 2 O 4 S 1
394.53
394.19263
K
artifact
PMC lysyl
PmcLys
PSI-MOD
MOD:01137
From DeltaMass: Average Mass: Formula: C20H30O2N4S1 Monoisotopic Mass Change: 394.192 Average Mass Change: 394.534
N6-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-lysine
A protein modification that is produced by reaction of a lysine residue with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride, to form N6-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-lysine.
DeltaMass:310
PMC lysyl
PmcLys
OBSOLETE because no evidence has been seen for this protein modification. modification from DeltaMass
C
artifact
PSI-MOD
MOD:01138
[probably aminoethyldansyl, JSG] From DeltaMass: (name misspelled "Aedans Cystenyl", and formula incorrect, N and O reversed) Average Mass: 409 Abbreviation: Aedans-Cys Formula: C17H19O3N5S2 Monoisotopic Mass Change: 409.077 Average Mass Change: 409.482
Aedans Cystenyl
true
OBSOLETE because no evidence has been seen for this protein modification. modification from DeltaMass
DeltaMass:311
OBSOLETE because this is a MS contaminant, not a known modification to a polypeptide. modification from DeltaMass
artifact
PSI-MOD
MOD:01139
From DeltaMass: Mass: Average Mass Change: 413 Notes: A common plasticizer, and, unfortunaltely, a common contaminate. A sodium adduct is often associated with this peak at 413.
dioctyl phthalate sodium adduct
true
OBSOLETE because this is a MS contaminant, not a known modification to a polypeptide. modification from DeltaMass
DeltaMass:312
A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two iodine atoms.
251.79
C 0 H -2 I 2 N 0 O 0
251.79329
C 9 H 7 I 2 N 1 O 2
414.97
414.85663
Y
natural
Unimod:130
3,5-Diiodination (of Tyrosine)
I2Tyr
diiodinationy
PSI-MOD
Diiodo
di-Iodination
MOD:01140
diiodinated tyrosine
A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two iodine atoms.
DeltaMass:0
OMSSA:35
PubMed:15627961
Unimod:130#Y
3,5-Diiodination (of Tyrosine)
I2Tyr
diiodinationy
Diiodo
di-Iodination
A protein modification that is produced by reaction with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride, to form omega-N-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-arginine.
266.36
C 14 H 18 O 3 S 1
266.09766
C 20 H 30 N 4 O 4 S 1
422.54
422.19876
R
artifact
PMC arginyl
PmcArg
PSI-MOD
MOD:01141
From DeltaMass: Average Mass: Formula: C20H30O4N4S1 Monoisotopic Mass Change: 422.199 Average Mass Change: 422.547
omega-N-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-arginine
A protein modification that is produced by reaction with 2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride, Pmc chloride, to form omega-N-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-arginine.
DeltaMass:314
PMC arginyl
PmcArg
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound 15,16-dihydrobiliverdin.
584.67
C 33 H 36 N 4 O 6 S 0
584.2635
C 36 H 41 N 5 O 7 S 1
687.81
687.27264
C
natural
(16R)-18-ethenyl-8,12-bis(2-carboxyethyl)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,7,13,17-tetramethyl-15,16-dihydrobilin-1,19(21H,24H)-dione
15,16-Dhbv
15,16-dihydrobiliverdin IXalpha
15,16-dihydrobiliverdin cysteine adduct
18-ethenyl-8,12-bis(2-carboxyethyl)-3-(2-(cysteinyl-S)-ethyl)-2,7,13,17-tetramethylbiladiene-ab-1,19(16H,21H)-dione
3'-cysteinyl-15,16-dihydrobiliverdin
3alpha-cysteinyl-15,16-dihydrobiliverdin
BINDING 15,16-dihydrobiliverdin (covalent; via 1 link)
DBV
S-15,16-dihydrobiliverdin-L-cysteine
PSI-MOD
MOD:01142
S-15,16-dihydrobiliverdin-L-cysteine
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound 15,16-dihydrobiliverdin.
PubMed:10430868
PubMed:15504407
PubMed:1559975
PubMed:3208761
RESID:AA0428
(16R)-18-ethenyl-8,12-bis(2-carboxyethyl)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,7,13,17-tetramethyl-15,16-dihydrobilin-1,19(21H,24H)-dione
15,16-Dhbv
15,16-dihydrobiliverdin IXalpha
15,16-dihydrobiliverdin cysteine adduct
18-ethenyl-8,12-bis(2-carboxyethyl)-3-(2-(cysteinyl-S)-ethyl)-2,7,13,17-tetramethylbiladiene-ab-1,19(16H,21H)-dione
3'-cysteinyl-15,16-dihydrobiliverdin
3alpha-cysteinyl-15,16-dihydrobiliverdin
BINDING 15,16-dihydrobiliverdin (covalent; via 1 link)
DBV
S-15,16-dihydrobiliverdin-L-cysteine
A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound 15,16-dihydrobiliverdin.
584.67
C 33 H 36 N 4 O 6 S 0
584.2635
C 39 H 46 N 6 O 8 S 2
790.95
790.28186
C, C
natural
(16R)-8,12-bis(2-carboxyethyl)-3-[2-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-18-[(1Xi)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,7,13,17-tetramethyl-15,16-dihydrobilin-1,19(21H,24H)-dione
15,16-Dhbv
15,16-dihydrobiliverdin IXalpha
15,16-dihydrobiliverdin cysteine adduct
15,16-dihydrobiliverdin-bis-L-cysteine
3'',18'-biscysteinyl-15,16-dihydrobiliverdin
3beta,18alpha-biscysteinyl-15,16-dihydrobiliverdin
8,12-bis(2-carboxyethyl)-3-(2-(cysteinyl-S)-ethyl)-18-(1-(cysteinyl-S)-ethyl)-2,7,13,17-tetramethylbiladiene-ab-1,19(16H,21H)-dione
BINDING 15,16-dihydrobiliverdin (covalent; via 2 links)
DBV
PSI-MOD
MOD:01143
Cross-link 2.
15,16-dihydrobiliverdin-bis-L-cysteine
A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound 15,16-dihydrobiliverdin.
PubMed:1559975
PubMed:2222853
PubMed:3208761
PubMed:8420941
RESID:AA0429
(16R)-8,12-bis(2-carboxyethyl)-3-[2-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-18-[(1Xi)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,7,13,17-tetramethyl-15,16-dihydrobilin-1,19(21H,24H)-dione
15,16-Dhbv
15,16-dihydrobiliverdin IXalpha
15,16-dihydrobiliverdin cysteine adduct
15,16-dihydrobiliverdin-bis-L-cysteine
3'',18'-biscysteinyl-15,16-dihydrobiliverdin
3beta,18alpha-biscysteinyl-15,16-dihydrobiliverdin
8,12-bis(2-carboxyethyl)-3-(2-(cysteinyl-S)-ethyl)-18-(1-(cysteinyl-S)-ethyl)-2,7,13,17-tetramethylbiladiene-ab-1,19(16H,21H)-dione
BINDING 15,16-dihydrobiliverdin (covalent; via 2 links)
DBV
A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine.
550.91
C 35 H 66 N 0 O 4 S 0
550.4961
C 38 H 71 N 1 O 5 S 1
654.05
653.5053
C
natural
S-(sn-1-Dipalmitoyl-glyceryl)- (on Cysteine)
PSI-MOD
MOD:01144
From DeltaMass: Average Mass: 524
S-(sn-1-2,3-dipalmitoylglycerol)-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine.
DeltaMass:0
PubMed:10896212
PubMed:4575979
PubMed:9056182
RESID:AA0107#var
S-(sn-1-Dipalmitoyl-glyceryl)- (on Cysteine)
A protein modification that effectively converts an L-histidine residue to N-tau-(ADP-ribosyl)diphthamide.
684.51
C 22 H 36 N 7 O 14 P 2
684.179
1+
C 28 H 43 N 10 O 15 P 2
821.65
821.2379
H
natural
uniprot.ptm:PTM-0672
MOD_RES ADP-ribosyldiphthamide
PSI-MOD
MOD:01145
From DeltaMass: (name misspelled "N theta -(ADP-ribosyl) diphthamide (of Histidine)") Average Mass: 648
N-tau-(ADP-ribosyl)diphthamide
A protein modification that effectively converts an L-histidine residue to N-tau-(ADP-ribosyl)diphthamide.
ChEBI:82697
DeltaMass:0
MOD_RES ADP-ribosyldiphthamide
A protein modification that effectively converts an L-cysteine residue to S-(6-FAD)-L-cystine.
783.54
C 27 H 31 N 9 O 15 P 2 S 0
783.1415
C 30 H 36 N 10 O 16 P 2 S 1
886.68
886.1507
C
hypothetical
S6FADCys
PSI-MOD
FAD
MOD:01146
From DeltaMass: Average Mass: 784 with no citation. This modification has not been reported [JSG].
S-(6-FAD)-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-(6-FAD)-L-cystine.
DeltaMass:0
S6FADCys
FAD
modification from DeltaMass
1038.95
C 40 H 66 N 2 O 29
1038.3751
C 44 H 72 N 4 O 31
1153.06
1152.4181
N
natural
GNO:G20956ZV
Unimod:1761
PSI-MOD
MOD:01147
From DeltaMass: Average Mass: 1,039
dHex1Hex3HexNAc2 N4-glycosylated asparagine
modification from DeltaMass
DeltaMass:0
Unimod:1761
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a ubiquitin.
K
natural
PSI-MOD
MOD:01148
ubiquitinylated lysine
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a ubiquitin.
PubMed:11125103
PubMed:18688235
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a sumo (Small Ubiquitin-related MOdifier) protein.
K
natural
PSI-MOD
MOD:01149
sumoylated lysine
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a sumo (Small Ubiquitin-related MOdifier) protein.
PubMed:12612601
PubMed:18688235
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a nedd8 protein.
K
natural
PSI-MOD
MOD:01150
neddylated lysine
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a nedd8 protein.
PubMed:11125103
PubMed:12612601
PubMed:18688235
Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid phosphorylated residue with a secondary loss of a neutral trihydrogen phosphate molecular fragment.
-97.99
C 0 H -3 N 0 O -4 P -1
-97.9769
X
artifact
PSI-MOD
MOD:01151
phosphorylated residue with neutral loss of phosphate
Covalent modification of, or a change resulting in an alteration of the measured molecular mass of, a peptide or protein amino acid phosphorylated residue with a secondary loss of a neutral trihydrogen phosphate molecular fragment.
PubMed:18688235
A protein modification that effectively replaces a hydrogen atom with a carboxylic acid group.
44.01
C 1 H 0 N 0 O 2
43.98983
X
Unimod:299
PSI-MOD
Carboxy
Carboxylation
MOD:01152
carboxylated residue
A protein modification that effectively replaces a hydrogen atom with a carboxylic acid group.
Unimod:299
Carboxy
Carboxylation
A protein modification that effectively replaces a hydrogen atom with an methylsulfanyl group (thiomethyl group).
46.09
C 1 H 2 N 0 O 0 S 1
45.98772
X
Unimod:39
PSI-MOD
Beta-methylthiolation
Methylthio
MOD:01153
methylthiolated residue
A protein modification that effectively replaces a hydrogen atom with an methylsulfanyl group (thiomethyl group).
Unimod:39
Beta-methylthiolation
Methylthio
A protein modification that effectively converts a source amino acid to pyruvic acid.
C 3 H 3 O 2
71.06
71.013306
X
N-term
2-oxopropanoic acid
MOD_RES Pyruvic acid (Cys)
MOD_RES Pyruvic acid (Ser)
pyruvic acid
PSI-MOD
MOD:01154
pyruvic acid
A protein modification that effectively converts a source amino acid to pyruvic acid.
PubMed:10085076
PubMed:3042771
PubMed:8464063
RESID:AA0127
2-oxopropanoic acid
MOD_RES Pyruvic acid (Cys)
MOD_RES Pyruvic acid (Ser)
pyruvic acid
A protein modification that effectively results from forming an adduct with a compound containing a lipid-like group either through acylation, alkylation, or amidation.
PSI-MOD
MOD:01155
lipoconjugated residue
A protein modification that effectively results from forming an adduct with a compound containing a lipid-like group either through acylation, alkylation, or amidation.
PubMed:18688235
Modified amino acid residue derived from a natural amino acid by a real or hypothetical chemical process.
PSI-MOD
MOD:01156
protein modification categorized by chemical process
Modified amino acid residue derived from a natural amino acid by a real or hypothetical chemical process.
PubMed:18688235
A protein modification considered either as modified amino acid residues derived from natural amino acids, as a replacement by another natural amino acid, or as a replacement by an unnatural amino acid.
PSI-MOD
MOD:01157
protein modification categorized by amino acid modified
A protein modification considered either as modified amino acid residues derived from natural amino acids, as a replacement by another natural amino acid, or as a replacement by an unnatural amino acid.
PubMed:18688235
A protein modification that modifies an L-selenocysteine residue.
U
PSI-MOD
MOD:01158
modified L-selenocysteine residue
A protein modification that modifies an L-selenocysteine residue.
PubMed:18688235
A protein modification that effectively attaches a residue to murein peptidoglycan by either a pentaglycine linker peptide or a peptide-like L-alanyl-D-glutamyl-2,6-diaminopimelic acid linkage.
X
natural
PSI-MOD
MOD:01159
peptidoglycanated residue
A protein modification that effectively attaches a residue to murein peptidoglycan by either a pentaglycine linker peptide or a peptide-like L-alanyl-D-glutamyl-2,6-diaminopimelic acid linkage.
PubMed:18688235
A protein modification that effectively results in the loss of an ammonia, usually by a process of vicinal dehydration, rearrangement, and rehydration with release of ammonia, resulting in a loss of nitrogen with no gain of oxygen.
-17.03
C 0 H -3 N -1 O 0
-17.026548
X
Unimod:385
PSI-MOD
Ammonia-loss
Loss of ammonia
MOD:01160
deaminated residue
A protein modification that effectively results in the loss of an ammonia, usually by a process of vicinal dehydration, rearrangement, and rehydration with release of ammonia, resulting in a loss of nitrogen with no gain of oxygen.
Unimod:385
Ammonia-loss
Loss of ammonia
A protein modification that effectively removes oxygen atoms from a residue without the removal of hydrogen atoms.
-16.0
C 0 H 0 N 0 O -1
-15.994915
X
Unimod:447
dOxyRes
PSI-MOD
Deoxy
reduction
MOD:01161
deoxygenated residue
A protein modification that effectively removes oxygen atoms from a residue without the removal of hydrogen atoms.
PubMed:14235557
Unimod:447
dOxyRes
Deoxy
reduction
modification from Unimod N-linked glycosylation
1769.62
C 68 H 112 N 4 O 49
1768.6395
C 72 H 118 N 6 O 51
1883.73
1882.6825
N
natural
GNO:G83555HU
Unimod:308
PSI-MOD
Fucosylated biantennary
dHex(1)Hex(5)HexNAc(4)
MOD:01162
fucosylated biantennary
modification from Unimod N-linked glycosylation
Unimod:308
Fucosylated biantennary
dHex(1)Hex(5)HexNAc(4)
A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoguanosine through either a phosphodiester or a phosphoramide bond.
345.21
C 10 H 12 N 5 O 7 P 1
345.04742
X
Unimod:413
5'phos Guanosyl
PSI-MOD
Phosphoguanosine
phospho-guanosine
MOD:01163
From DeltaMass: (formula incorrect, N and O reversed) Average Mass: 345 Formula: C10H12O5N7P1 Monoisotopic Mass Change: 345.047 Average Mass Change: 345.209.
guanylated residue
A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoguanosine through either a phosphodiester or a phosphoramide bond.
DeltaMass:304
Unimod:413
5'phos Guanosyl
Phosphoguanosine
phospho-guanosine
A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through a phosphodiester bond.
438.33
C 17 H 19 N 4 O 8 P 1
438.09406
X
Unimod:442
PSI-MOD
FMN
O3-(riboflavin phosphoryl)
MOD:01164
riboflavin-phosphorylated residue
A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through a phosphodiester bond.
Unimod:442
FMN
O3-(riboflavin phosphoryl)
A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoadenosine through either a phosphodiester or a phosphoramide bond.
329.21
C 10 H 12 N 5 O 6 P 1
329.05252
X
Unimod:405
5'phos Adenosinyl
PSI-MOD
AMP binding site
Phosphoadenosine
MOD:01165
From DeltaMass: (name misspelled "5'phos adenosinyl") Average Mass: 329
adenylated residue
A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoadenosine through either a phosphodiester or a phosphoramide bond.
DeltaMass:0
Unimod:405
5'phos Adenosinyl
AMP binding site
Phosphoadenosine
A protein modification that effectively crosslinks an amino acid residue and 5'-phosphouridine through either a phosphodiester or a phosphoramide bond.
306.17
C 9 H 11 N 2 O 8 P 1
306.0253
X
Unimod:417
5'phos Uridinyl
PSI-MOD
PhosphoUridine
uridine phosphodiester
MOD:01166
From DeltaMass: (name misspelled "5'phos Uridinyl" and formula incorrect, N and O reversed) Average Mass: 306 Formula: C9H11O2N8P1 Monoisotopic Mass Change: 306.025 Average Mass Change: 306.17
uridylated residue
A protein modification that effectively crosslinks an amino acid residue and 5'-phosphouridine through either a phosphodiester or a phosphoramide bond.
DeltaMass:292
Unimod:417
5'phos Uridinyl
PhosphoUridine
uridine phosphodiester
modification from Unimod
1572.02
C 40 H 47 Mo 1 N 20 O 26 P 4 S 4
1572.9857
X
Unimod:424
PSI-MOD
MolybdopterinGD
molybdenum bis(molybdopterin guanine dinucleotide)
MOD:01167
molybdopterin guanine dinucleotide
modification from Unimod
Unimod:424
MolybdopterinGD
molybdenum bis(molybdopterin guanine dinucleotide)
A protein modification that effectively converts a source amino acid residue to dehydroalanine.
C 3 H 3 N 1 O 1
69.06
69.02146
X
natural
2,3-didehydroalanine
2-aminoacrylic acid
2-aminopropenoic acid
4-methylidene-imidazole-5-one (MIO) active site
Dha
MOD_RES 2,3-didehydroalanine (Cys)
MOD_RES 2,3-didehydroalanine (Ser)
anhydroserine
dHAla
dehydroalanine
PSI-MOD
MOD:01168
dehydroalanine
A protein modification that effectively converts a source amino acid residue to dehydroalanine.
PubMed:10220322
PubMed:1547888
PubMed:1815586
PubMed:2914619
PubMed:6838602
PubMed:7947813
PubMed:8239649
RESID:AA0181
2,3-didehydroalanine
2-aminoacrylic acid
2-aminopropenoic acid
4-methylidene-imidazole-5-one (MIO) active site
Dha
MOD_RES 2,3-didehydroalanine (Cys)
MOD_RES 2,3-didehydroalanine (Ser)
anhydroserine
dHAla
dehydroalanine
A protein modification that effectively converts a source amino acid residue to L-oxoalanine.
C 3 H 3 N 1 O 2
85.06
85.01638
X
natural
(S)-2-amino-3-oxopropanoic acid
2-amino-3-oxopropionic acid
L-3-oxoalanine
L-amino-malonic acid semialdehyde
L-aminomalonaldehydic acid
MOD_RES 3-oxoalanine (Cys)
MOD_RES 3-oxoalanine (Ser)
PSI-MOD
C(alpha)-formylglycine
L-serinesemialdehyde
MOD:01169
L-3-oxoalanine
A protein modification that effectively converts a source amino acid residue to L-oxoalanine.
DeltaMass:349
PubMed:14563551
PubMed:7628016
PubMed:8681943
PubMed:9478923
RESID:AA0185
(S)-2-amino-3-oxopropanoic acid
2-amino-3-oxopropionic acid
L-3-oxoalanine
L-amino-malonic acid semialdehyde
L-aminomalonaldehydic acid
MOD_RES 3-oxoalanine (Cys)
MOD_RES 3-oxoalanine (Ser)
C(alpha)-formylglycine
L-serinesemialdehyde
A protein modification that effectively forms a 2-ketoimine of pyruvicacid with a residue amino group.
70.05
C 3 H 2 N 0 O 2
70.00548
X
N-term
Unimod:422
PSI-MOD
N-pyruvic acid 2-iminyl
PyruvicAcidIminyl
MOD:01170
pyruvic acid iminylated residue
A protein modification that effectively forms a 2-ketoimine of pyruvicacid with a residue amino group.
Unimod:422
N-pyruvic acid 2-iminyl
PyruvicAcidIminyl
A protein modification that effectively converts an L-threonine residue to O-acetyl-L-threonine.
42.04
C 2 H 2 N 0 O 1
42.010567
C 6 H 9 N 1 O 3
143.14
143.05824
T
natural
Unimod:1
uniprot.ptm:PTM-0233
(2S,3R)-3-(acetyloxy)-2-aminobutanoic acid
ACT_SITE O-acetylthreonine intermediate
MOD_RES O-acetylthreonine
O-acetyl-L-threonine
O-acetylthreonine
OAcThr
threonine acetate ester
PSI-MOD
Acetylation
MOD:01171
O-acetyl-L-threonine
A protein modification that effectively converts an L-threonine residue to O-acetyl-L-threonine.
PubMed:16728640
RESID:AA0423
Unimod:1#T
(2S,3R)-3-(acetyloxy)-2-aminobutanoic acid
ACT_SITE O-acetylthreonine intermediate
MOD_RES O-acetylthreonine
O-acetyl-L-threonine
O-acetylthreonine
OAcThr
threonine acetate ester
Acetylation
A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylsphingolipidinositolethanolamine.
123.05
C 2 H 6 N 1 O 3 P 1
123.00853
C 5 H 12 N 2 O 5 P 1
211.13
211.04839
A
hypothetical
C-term
uniprot.ptm:PTM-0144
GSIAla
LIPID GPI-like-anchor amidated alanine
N-alanyl-glycosylsphingolipidinositolethanolamine
PSI-MOD
MOD:01172
N-alanyl-glycosylsphingolipidinositolethanolamine
A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylsphingolipidinositolethanolamine.
PubMed:12626404
RESID:AA0424
GSIAla
LIPID GPI-like-anchor amidated alanine
N-alanyl-glycosylsphingolipidinositolethanolamine
A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylsphingolipidinositolethanolamine.
123.05
C 2 H 6 N 1 O 3 P 1
123.00853
C 6 H 13 N 3 O 6 P 1
254.16
254.0542
N
hypothetical
C-term
uniprot.ptm:PTM-0145
GSIAsn
LIPID GPI-like-anchor amidated asparagine
N-asparaginyl-glycosylsphingolipidinositolethanolamine
PSI-MOD
MOD:01173
N-asparaginyl-glycosylsphingolipidinositolethanolamine
A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylsphingolipidinositolethanolamine.
PubMed:12626404
RESID:AA0425
GSIAsn
LIPID GPI-like-anchor amidated asparagine
N-asparaginyl-glycosylsphingolipidinositolethanolamine
A protein modification that effectively converts an L-cysteine residue to S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine.
316.44
C 20 H 28 N 0 O 3 S 0
316.20386
C 23 H 33 N 1 O 4 S 1
419.58
419.21304
C
natural
uniprot.ptm:PTM-0447
(2R)-2-amino-3-([(5Z,9Xi,12E,14Z)-1-hydroxy-1,11-oxoprosta-5,12,14-trien-9-yl]sulfanyl)propanoic acid
(5Z,9Xi,12E,14Z)-9-([(2R)-2-amino-3-carboxyethyl]sulfanyl)-11-oxoprosta-5,12,14-trien-1-oic acid
LIPID S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine
PG-J2Cys
S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine
PSI-MOD
MOD:01174
S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine.
ChEBI:27485
PubMed:11466314
PubMed:12684535
RESID:AA0426
(2R)-2-amino-3-([(5Z,9Xi,12E,14Z)-1-hydroxy-1,11-oxoprosta-5,12,14-trien-9-yl]sulfanyl)propanoic acid
(5Z,9Xi,12E,14Z)-9-([(2R)-2-amino-3-carboxyethyl]sulfanyl)-11-oxoprosta-5,12,14-trien-1-oic acid
LIPID S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine
PG-J2Cys
S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycourobilin.
586.69
C 33 H 38 N 4 O 6 S 0
586.2791
C 36 H 43 N 5 O 7 S 1
689.83
689.2883
C
natural
(2S,3R,16R)-18-ethenyl-3-[(1R)-1-([(R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-4,5,15,16-tetrahydrobiline-1,19(21H,22H,24H)-dione
18-ethenyl-3-[1-(2-amino-2-carboxyethylsulfanyl)ethyl]-2,3,15,16-dihydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid
BINDING Phycourobilin chromophore (covalent; via 1 link)
PUB
PUBCys
S-phycourobilin-L-cysteine
phycourobilin cysteine adduct
PSI-MOD
MOD:01175
S-phycourobilin-L-cysteine
A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycourobilin.
PubMed:1903388
PubMed:3208761
PubMed:3838747
RESID:AA0427
(2S,3R,16R)-18-ethenyl-3-[(1R)-1-([(R)-2-amino-2-carboxyethyl]sulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-4,5,15,16-tetrahydrobiline-1,19(21H,22H,24H)-dione
18-ethenyl-3-[1-(2-amino-2-carboxyethylsulfanyl)ethyl]-2,3,15,16-dihydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid
BINDING Phycourobilin chromophore (covalent; via 1 link)
PUB
PUBCys
S-phycourobilin-L-cysteine
phycourobilin cysteine adduct
A protein modification that effectively cross-links an L-lysine residue and an L-lysine residue converted to allysine with a carbon-nitrogen bond to form L-dehydrolysinonorleucine.
-19.05
C 0 H -5 N -1 O 0
-19.042198
C 12 H 19 N 3 O 2
237.3
237.14772
K, K
natural
(2S)-2-amino-6-([(5S)-5-amino-5-carboxypentylidene]amino)hexanoic acid
6-(N6-L-didehydrolysino)-L-norleucine
CROSSLNK Dehydrolysinonorleucine (Lys-Lys)
L-dehydrolysinonorleucine
N6-[(5S)-5-amino-5-carboxypentylidene]-L-lysine
XLNK6NleN6Lys
dehydrolysinorleucine [misspelling]
dehydrolysylnorleucine
didehydrolysinonorleucine
PSI-MOD
MOD:01176
Cross-link 2.
L-dehydrolysinonorleucine
A protein modification that effectively cross-links an L-lysine residue and an L-lysine residue converted to allysine with a carbon-nitrogen bond to form L-dehydrolysinonorleucine.
PubMed:16929109
RESID:AA0430
(2S)-2-amino-6-([(5S)-5-amino-5-carboxypentylidene]amino)hexanoic acid
6-(N6-L-didehydrolysino)-L-norleucine
CROSSLNK Dehydrolysinonorleucine (Lys-Lys)
L-dehydrolysinonorleucine
N6-[(5S)-5-amino-5-carboxypentylidene]-L-lysine
XLNK6NleN6Lys
dehydrolysinorleucine [misspelling]
dehydrolysylnorleucine
didehydrolysinonorleucine
A protein modification that effectively converts an L-histidine residue to 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine.
90.08
C 3 H 6 N 0 O 3
90.03169
C 9 H 13 N 3 O 4
227.22
227.0906
H
natural
uniprot.ptm:PTM-0416
(S)-2-amino-3-[1-(1,2,3-trihydroxypropan-2-yl)-1H-imidazol-4-yl]propanoic acid
1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine
1-[1,2-dihydroxy-1-(hydroxymethyl)ethyl]-L-histidine
MOD_RES Tele-(1,2,3-trihydroxypropan-2-yl)histidine
N(epsilon)-histidine dihydroxyacetone adduct
N(tau)-(1,2,3-trihydroxypropan-2-yl)histidine
NtauDHAHis
tele-(1,2,3-trihydroxypropan-2-yl)histidine
PSI-MOD
MOD:01177
1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine
A protein modification that effectively converts an L-histidine residue to 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine.
PubMed:16760471
RESID:AA0431
(S)-2-amino-3-[1-(1,2,3-trihydroxypropan-2-yl)-1H-imidazol-4-yl]propanoic acid
1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine
1-[1,2-dihydroxy-1-(hydroxymethyl)ethyl]-L-histidine
MOD_RES Tele-(1,2,3-trihydroxypropan-2-yl)histidine
N(epsilon)-histidine dihydroxyacetone adduct
N(tau)-(1,2,3-trihydroxypropan-2-yl)histidine
NtauDHAHis
tele-(1,2,3-trihydroxypropan-2-yl)histidine
A protein modification that effectively converts an L-aspartic acid residue to S-(aspart-4-yloxy) thiocarbonate.
76.07
C 1 H 0 N 0 O 2 S 1
75.9619
C 5 H 5 N 1 O 5 S 1
191.16
190.98885
D
hypothetical
(2S)-2-amino-4-(carboxysulfanyl)oxy-4-oxobutanoic acid
4-aspartyloxysulfanylcarbonate
AspOSCO2H
O-carboxysulfanyl-4-oxo-L-homoserine
S-(aspart-4-yloxy) thiocarbonate
PSI-MOD
MOD:01178
This modification was originally observed in an Entamoeba histolytica enzyme expressed in Escherichia coli. It was not chemically confirmed or characterized. It did not appear in a later model at higher resolution by the same group. This is a deprecated entry in RESID. It probably does not occur naturally [JSG].
S-(aspart-4-yloxy) thiocarbonate
A protein modification that effectively converts an L-aspartic acid residue to S-(aspart-4-yloxy) thiocarbonate.
PubMed:16627948
RESID:AA0432
(2S)-2-amino-4-(carboxysulfanyl)oxy-4-oxobutanoic acid
4-aspartyloxysulfanylcarbonate
AspOSCO2H
O-carboxysulfanyl-4-oxo-L-homoserine
S-(aspart-4-yloxy) thiocarbonate
A protein modification that effectively converts an L-alanine residue to N,N-dimethyl-L-alanine.
28.05
C 2 H 4 N 0 O 0
28.0313
C 5 H 10 N 1 O 1
100.14
100.07624
A
natural
N-term
uniprot.ptm:PTM-0178
(S)-1-carboxy-N,N-dimethylaminoethane
(S)-2-(dimethylamino)propanoic acid
MOD_RES N,N-dimethylalanine
N,N-dimethyl-L-alanine
N,N-dimethylalanine
NMe2Ala
PSI-MOD
MOD:01179
N,N-dimethyl-L-alanine
A protein modification that effectively converts an L-alanine residue to N,N-dimethyl-L-alanine.
PubMed:17691833
PubMed:387091
RESID:AA0433
(S)-1-carboxy-N,N-dimethylaminoethane
(S)-2-(dimethylamino)propanoic acid
MOD_RES N,N-dimethylalanine
N,N-dimethyl-L-alanine
N,N-dimethylalanine
NMe2Ala
A protein modification that effectively converts a glycine residue to 2-hydroxyglycine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 2 H 3 N 1 O 2
73.05
73.01638
G
artifact
2-hydroxyglycine
2HyGly
alpha-hydroxyglycine
amino(hydroxy)acetic acid
aminohydroxyacetic acid
PSI-MOD
MOD:01180
CAUTION - peptides of 2-hydroxyglycine are known to be unstable, decaying to break the peptide backbone or to form peptidyl amides [see J. Am. Chem. Soc. 111, 1933-1934, 1989, and J. Org. Chem. 57, 3916-3921, 1992]. If computer analysis of tandem mass-spectrometric results predicts this modification, then it is most probable that there are multiple isobaric peptides differing in the location of multiple hydroxylation modifications [JSG].
2-hydroxyglycine observational artifact
A protein modification that effectively converts a glycine residue to 2-hydroxyglycine.
ChEBI:38048
PubMed:16178056
PubMed:17431180
PubMed:17823333
RESID:AA0434
2-hydroxyglycine
2HyGly
alpha-hydroxyglycine
amino(hydroxy)acetic acid
aminohydroxyacetic acid
A protein modification that effectively converts an L-aspartic acid residue to L-aspartate 4-methyl ester.
14.03
C 1 H 2 N 0 O 0
14.01565
C 5 H 7 N 1 O 3
129.12
129.04259
D
artifact
Unimod:34
(2S)-2-amino-4-methoxy-4-oxobutanoic acid
2-aminobutanedioic acid 4-methyl ester
4-methyl L-2-aminosuccinic acid
4-methyl L-aspartate
4-methyl L-hydrogen aspartate
L-aspartic acid 4-methyl ester
O4MeAsp
aspartic acid 4-methyl ester
aspartic acid beta-methyl ester
meesterd
PSI-MOD
Methyl
MOD:01181
CAUTION - observations of this modifation are attributable to artifacts produced in preparation. It is extremely unlikely that eukaryotes produce this modification, because an enzyme acting to form the methyl ester of L-aspartyl peptides would interfere with the D-aspartyl peptide repair mechanism [JSG].
L-aspartic acid 4-methyl ester
A protein modification that effectively converts an L-aspartic acid residue to L-aspartate 4-methyl ester.
OMSSA:69
PubMed:1556110
PubMed:16888766
PubMed:9629898
RESID:AA0435
Unimod:34#D
(2S)-2-amino-4-methoxy-4-oxobutanoic acid
2-aminobutanedioic acid 4-methyl ester
4-methyl L-2-aminosuccinic acid
4-methyl L-aspartate
4-methyl L-hydrogen aspartate
L-aspartic acid 4-methyl ester
O4MeAsp
aspartic acid 4-methyl ester
aspartic acid beta-methyl ester
meesterd
Methyl
A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD.
781.52
C 27 H 29 N 9 O 15 P 2 S 0
781.12585
C 36 H 41 N 13 O 17 P 2 S 1
1021.81
1021.1939
C, H
natural
uniprot.ptm:PTM-0681
6-((R)-2-amino-2-carboxyethyl)sulfanyl-8alpha-[4-((S)-2-amino-2-carboxyethyl)imidazol-3-yl]-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine
6-(S-L-cysteinyl)-8alpha-(N3'-L-histidino)-FAD
6-(S-cysteinyl)-8alpha-(N(delta1)-histidyl)-FAD
6-(S-cysteinyl)-8alpha-(N(pi)-histidyl)-FAD
6-(S-cysteinyl)-8alpha-(N3'-histidyl)-FAD
6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD
BINDING FAD (covalent; via 2 links)
BINDING FAD (covalent; via 2 links, pros nitrogen)
CROSSLNK 6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys)
SCys6-NprosHis8a-FAD
PSI-MOD
MOD:01182
Cross-link 2.
6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD
A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD.
PubMed:
RESID:AA0436
6-((R)-2-amino-2-carboxyethyl)sulfanyl-8alpha-[4-((S)-2-amino-2-carboxyethyl)imidazol-3-yl]-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine
6-(S-L-cysteinyl)-8alpha-(N3'-L-histidino)-FAD
6-(S-cysteinyl)-8alpha-(N(delta1)-histidyl)-FAD
6-(S-cysteinyl)-8alpha-(N(pi)-histidyl)-FAD
6-(S-cysteinyl)-8alpha-(N3'-histidyl)-FAD
6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD
BINDING FAD (covalent; via 2 links)
BINDING FAD (covalent; via 2 links, pros nitrogen)
CROSSLNK 6-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys)
SCys6-NprosHis8a-FAD
A protein modification that effectively cross-links two L-selenocysteine residues to form L-selenocystine,
-2.02
C 0 H -2 N 0 O 0 Se 0
-2.01565
C 6 H 8 N 2 O 2 Se 2
298.08
299.89163
U, U
hypothetical
(R,R)-3,3'-diselane-1,2-diylbis(2-aminopropanoic acid)
3,3'-diselenobis(2-aminopropanoic acid)
3,3'-diselenobisalanine
3,3'-diselenodialanine
CROSSLNK Selenocystine (Sec-Sec)
L-selenocystine
Sec2
beta,beta'-diamino-beta,beta'-dicarboxydiethyldiselenide
beta,beta'-diselenodialanine
bis(alpha-aminopropionic acid)-beta-diselenide
bis(beta-amino-beta-carboxyethyl)diselenide
diselenocysteine
selenium cystine
PSI-MOD
MOD:01183
Cross-link 2; for formation of the same modification by substitution of 2 selenium for 2 sulfur atoms in L-cystine, see MOD:01184.
L-selenocystine (oxidized selenocysteine) (Sec-Sec)
A protein modification that effectively cross-links two L-selenocysteine residues to form L-selenocystine,
ChEBI:28553
PubMed:17715293
PubMed:6076213
RESID:AA0437
(R,R)-3,3'-diselane-1,2-diylbis(2-aminopropanoic acid)
3,3'-diselenobis(2-aminopropanoic acid)
3,3'-diselenobisalanine
3,3'-diselenodialanine
CROSSLNK Selenocystine (Sec-Sec)
L-selenocystine
Sec2
beta,beta'-diamino-beta,beta'-dicarboxydiethyldiselenide
beta,beta'-diselenodialanine
bis(alpha-aminopropionic acid)-beta-diselenide
bis(beta-amino-beta-carboxyethyl)diselenide
diselenocysteine
selenium cystine
A protein modification that effectively substitutes two selenium atoms for two sulfur atoms in L-cystine to form L-selenocystine.
91.81
C 0 H -2 N 0 O 0 S -2 Se 2
93.87325
C 6 H 8 N 2 O 2 Se 2
298.08
299.89163
C, C
hypothetical
(R,R)-3,3'-diselane-1,2-diylbis(2-aminopropanoic acid)
3,3'-diselenobis(2-aminopropanoic acid)
3,3'-diselenobisalanine
3,3'-diselenodialanine
CROSSLNK Selenocystine (Sec-Sec)
L-selenocystine
Se2(S2)Cys2
beta,beta'-diamino-beta,beta'-dicarboxydiethyldiselenide
beta,beta'-diselenodialanine
bis(alpha-aminopropionic acid)-beta-diselenide
bis(beta-amino-beta-carboxyethyl)diselenide
diselenocysteine
selenium cystine
PSI-MOD
MOD:01184
Cross-link 2; for formation of the same modification by oxidation of two L-selenocysteine residues, see MOD:01183.
L-selenocystine (selenium disubstituted L-cystine)
A protein modification that effectively substitutes two selenium atoms for two sulfur atoms in L-cystine to form L-selenocystine.
PubMed:17715293
RESID:AA0437#CYS2
(R,R)-3,3'-diselane-1,2-diylbis(2-aminopropanoic acid)
3,3'-diselenobis(2-aminopropanoic acid)
3,3'-diselenobisalanine
3,3'-diselenodialanine
CROSSLNK Selenocystine (Sec-Sec)
L-selenocystine
Se2(S2)Cys2
beta,beta'-diamino-beta,beta'-dicarboxydiethyldiselenide
beta,beta'-diselenodialanine
bis(alpha-aminopropionic acid)-beta-diselenide
bis(beta-amino-beta-carboxyethyl)diselenide
diselenocysteine
selenium cystine
A protein modification that effectively converts an L-aspartic acid residue to L-asparagine.
-0.98
C 0 H 1 N 1 O -1
-0.984016
C 4 H 6 N 2 O 2
114.1
114.04293
D
natural
(2S)-2-amino-4-butanediamic acid
2,4-bis(azanyl)-4-oxobutanoic acid
2,4-diamino-4-oxobutanoic acid
2-amino-3-carbamoylpropanoic acid
2-amino-4-butanediamic acid
2-aminosuccinamic acid
2-aminosuccinic acid 4-amide
4NAsp
L-asparagine
MOD_RES Amidated aspartic acid
alpha-amino-beta-carbamylpropionic acid
alpha-aminosuccinamic acid
aspartic acid 4-amide
aspartic acid beta-amide
beta-asparagine
PSI-MOD
MOD:01185
4-amidated L-aspartic acid
A protein modification that effectively converts an L-aspartic acid residue to L-asparagine.
PubMed:17962566
RESID:AA0003#ASP
(2S)-2-amino-4-butanediamic acid
2,4-bis(azanyl)-4-oxobutanoic acid
2,4-diamino-4-oxobutanoic acid
2-amino-3-carbamoylpropanoic acid
2-amino-4-butanediamic acid
2-aminosuccinamic acid
2-aminosuccinic acid 4-amide
4NAsp
L-asparagine
MOD_RES Amidated aspartic acid
alpha-amino-beta-carbamylpropionic acid
alpha-aminosuccinamic acid
aspartic acid 4-amide
aspartic acid beta-amide
beta-asparagine
A protein modification that effectively converts an L-threonine residue to either N-acetyl-L-threonne, or O-acetyl-Lthreonine.
42.04
C 2 H 2 N 0 O 1
42.010567
T
natural
AcThr
PSI-MOD
MOD:01186
monoacetylated L-threonine
A protein modification that effectively converts an L-threonine residue to either N-acetyl-L-threonne, or O-acetyl-Lthreonine.
PubMed:18688235
AcThr
A protein modification that inserts or replaces a residue with an L-pyrrolysine residue, a natural pretranslational modification.
0.0
C 0 H 0 N 0 O 0
0.0
C 12 H 19 N 3 O 2
237.3
237.14772
O
natural
Unimod:435
(2S)-2-amino-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]aminohexanoic acid
2-azanyl-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]azanylhexanoic acid
L-pyrrolysine
N6-(4-methyl-1,2-didehydropyrrolidine-5-carboxyl)-L-lysine
N6-(4-methyl-delta-1-pyrroline-5-carboxyl)-L-lysine
N6-([(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl)-L-lysine
NON_STD Pyrrolysine
Pyl
monomethylamine methyltransferase cofactor lysine adduct
PSI-MOD
MOD:01187
L-pyrrolysine residue
A protein modification that inserts or replaces a residue with an L-pyrrolysine residue, a natural pretranslational modification.
ChEBI:21860
PubMed:11435424
PubMed:12029131
PubMed:12029132
PubMed:15314242
PubMed:16096277
RESID:AA0321
Unimod:435
(2S)-2-amino-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]aminohexanoic acid
2-azanyl-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]azanylhexanoic acid
L-pyrrolysine
N6-(4-methyl-1,2-didehydropyrrolidine-5-carboxyl)-L-lysine
N6-(4-methyl-delta-1-pyrroline-5-carboxyl)-L-lysine
N6-([(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl)-L-lysine
NON_STD Pyrrolysine
Pyl
monomethylamine methyltransferase cofactor lysine adduct
modification from Unimod Isotopic label -
90.08
C 4 (1)H 2 (2)H 5 N 1 O 1
90.084145
C 13 (1)H 11 (2)H 5 N 2 O 3
253.15
253.14748
Y
artifact
Unimod:212
PSI-MOD
N-ethyl iodoacetamide-d5
NEIAA:2H(5)
MOD:01188
N-ethyl iodoacetamide-d5 - site Y
modification from Unimod Isotopic label -
PubMed:11710128
PubMed:12766232
PubMed:3155470
PubMed:957432
Unimod:212#Y
N-ethyl iodoacetamide-d5
NEIAA:2H(5)
modification from Unimod Isotopic label -
90.08
C 4 (1)H 2 (2)H 5 N 1 O 1
90.084145
C 7 (1)H 7 (2)H 5 N 2 O 2 S 1
193.09
193.09334
C
artifact
Unimod:212
PSI-MOD
N-ethyl iodoacetamide-d5
NEIAA:2H(5)
MOD:01189
N-ethyl iodoacetamide-d5 - site C
modification from Unimod Isotopic label -
PubMed:12766232
Unimod:212#C
N-ethyl iodoacetamide-d5
NEIAA:2H(5)
Modification from Unimod Chemical derivative. OBSOLETE because duplicate and redundant with MOD:01006. Remap to MOD:01006.
MOD:01006
157.79
Br 2 H -2
155.82103
Y
Unimod:534
PSI-MOD
Dibromo
MOD:01190
dibromo
true
Modification from Unimod Chemical derivative. OBSOLETE because duplicate and redundant with MOD:01006. Remap to MOD:01006.
Unimod:534
Dibromo
Dibromo
modification from Unimod Isotopic label -
85.11
C 4 H 7 N 1 O 1
85.052765
C 7 H 12 N 2 O 2 S 1
188.25
188.06195
C
artifact
Unimod:211
PSI-MOD
N-ethyl iodoacetamide-d0
NEIAA
MOD:01191
N-ethyl iodoacetamide-d0 - site C
modification from Unimod Isotopic label -
PubMed:12766232
Unimod:211#C
N-ethyl iodoacetamide-d0
NEIAA
modification from Unimod Isotopic label -
85.11
C 4 H 7 N 1 O 1
85.052765
C 13 H 16 N 2 O 3
248.28
248.11609
Y
artifact
Unimod:211
PSI-MOD
N-ethyl iodoacetamide-d0
NEIAA
MOD:01192
N-ethyl iodoacetamide-d0 - site Y
modification from Unimod Isotopic label -
PubMed:11760118
PubMed:12766232
Unimod:211#Y
N-ethyl iodoacetamide-d0
NEIAA
modification from Unimod Chemical derivative -
121.2
C 7 H 7 N 1 O -1 S 1
121.035
C 11 H 14 N 2 O 1 S 1
222.31
222.08269
T
artifact
Unimod:264
PSI-MOD
PET
phosphorylation to pyridyl thiol
MOD:01193
pyridyl thiol modified L-threonine
modification from Unimod Chemical derivative -
PubMed:1093385
Unimod:264#T
PET
phosphorylation to pyridyl thiol
modification from Unimod Chemical derivative -
121.2
C 7 H 7 N 1 O -1 S 1
121.035
C 10 H 12 N 2 O 1 S 1
208.28
208.06703
S
artifact
Unimod:264
PSI-MOD
PET
phosphorylation to pyridyl thiol
MOD:01194
pyridyl thiol modified L-serine
modification from Unimod Chemical derivative -
PubMed:15279557
Unimod:264#S
PET
phosphorylation to pyridyl thiol
modification from Unimod Isotopic label -
104.11
C 7 H 4 O 1
104.026215
C 13 H 16 N 2 O 2
232.28
232.12119
K
artifact
Unimod:136
PSI-MOD
Benzoyl
labeling reagent light form (N-term & K)
MOD:01195
benzoyl labeling reagent light form - site K
modification from Unimod Isotopic label -
PubMed:11813307
PubMed:12777388
PubMed:15456300
Unimod:136#K
Benzoyl
labeling reagent light form (N-term & K)
OBSOLETE because redundant, replaced with MOD:01654. Remap to MOD:01654.
MOD:01654
233.29
C 12 H 11 N 1 O 2 S 1
233.05106
C 18 H 23 N 3 O 3 S 1
361.46
361.14603
K
artifact
Unimod:139
PSI-MOD
5-dimethylaminonaphthalene-1-sulfonyl
Dansyl
MOD:01196
5-dimethylaminonaphthalene-1-sulfonyl - site K
true
OBSOLETE because redundant, replaced with MOD:01654. Remap to MOD:01654.
Unimod:139
5-dimethylaminonaphthalene-1-sulfonyl
Dansyl
A protein modification that effectively converts an L-glutamine residue to N-heptosyl-L-glutamine.
192.17
C 7 H 12 O 6
192.06339
C 12 H 20 N 2 O 8
320.3
320.12198
Q
artifact
Unimod:490
PSI-MOD
Hep
Heptose
MOD:01197
From Unimod with no citation [JSG].
N-heptosyl-L-glutamine
A protein modification that effectively converts an L-glutamine residue to N-heptosyl-L-glutamine.
Unimod:490#Q
Hep
Heptose
A protein modification that effectively converts an L-serine residue to O-heptosyl-L-serine.
192.17
C 7 H 12 O 6
192.06339
C 10 H 17 N 1 O 8
279.25
279.09543
S
artifact
Unimod:490
PSI-MOD
Hep
Heptose
MOD:01198
From Unimod with no citation [JSG].
O-heptosyl-L-serine
A protein modification that effectively converts an L-serine residue to O-heptosyl-L-serine.
Unimod:490#S
Hep
Heptose
A protein modification that effectively converts an L-arginine residue to an N-heptosyl-L-arginine.
192.17
C 7 H 12 O 6
192.06339
C 13 H 24 N 4 O 7
348.36
348.1645
R
artifact
Unimod:490
PSI-MOD
Hep
Heptose
MOD:01199
From Unimod with no citation [JSG].
N-heptosyl-L-arginine
A protein modification that effectively converts an L-arginine residue to an N-heptosyl-L-arginine.
Unimod:490#R
Hep
Heptose
A protein modification that effectively converts an L-threonine residue to O-heptosyl-L-threonine.
192.17
C 7 H 12 O 6
192.06339
C 11 H 19 N 1 O 8
293.27
293.11105
T
artifact
Unimod:490
PSI-MOD
Hep
Heptose
MOD:01200
From Unimod with no citation [JSG].
O-heptosyl-L-threonine
A protein modification that effectively converts an L-threonine residue to O-heptosyl-L-threonine.
Unimod:490#T
Hep
Heptose
A protein modification that effectively converts an L-lysine residue to N6-heptosyl-L-lysine.
192.17
C 7 H 12 O 6
192.06339
C 13 H 24 N 2 O 7
320.34
320.15836
K
artifact
Unimod:490
PSI-MOD
Hep
Heptose
MOD:01201
From Unimod with no citation [JSG].
N6-heptosyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-heptosyl-L-lysine.
Unimod:490#K
Hep
Heptose
A protein modification that effectively converts an L-asparagine residue to N-heptosyl-L-asparagine.
192.17
C 7 H 12 O 6
192.06339
C 11 H 18 N 2 O 8
306.27
306.10632
N
artifact
Unimod:490
PSI-MOD
Hep
Heptose
MOD:01202
From Unimod with no citation [JSG].
N-heptosyl-L-asparagine
A protein modification that effectively converts an L-asparagine residue to N-heptosyl-L-asparagine.
Unimod:490#N
Hep
Heptose
A protein modification that effectively converts an L-lysine residue to N6-[(pyrid-3-yl)acetyl]lysine.
119.12
C 7 H 5 N 1 O 1
119.03712
C 13 H 17 N 3 O 2
247.3
247.13208
K
artifact
Unimod:25
PSI-MOD
Pyridylacetyl
pyridylacetyl
MOD:01203
Produced by reaction with N-[(pyrid-3-yl)acetyl]oxy-succinimide [JSG].
N6-(pyridylacetyl)lysine
A protein modification that effectively converts an L-lysine residue to N6-[(pyrid-3-yl)acetyl]lysine.
PubMed:9276974
Unimod:25#K
Pyridylacetyl
pyridylacetyl
modification from Unimod Artifact -
-48.1
C -1 H -4 S -1
-48.003372
C 4 H 5 N 1 O 1 S 0
83.09
83.03712
M
artifact
Unimod:526
PSI-MOD
Dethiomethyl
Prompt loss of side chain from oxidised Met
MOD:01204
prompt loss of methanethiol from oxidixed methionine
modification from Unimod Artifact -
PubMed:9004526
Unimod:526
Dethiomethyl
Prompt loss of side chain from oxidised Met
A protein modification that effectively replaces an O3 hydrogen atom of a serine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond.
947.85
C 36 H 57 N 3 O 26
947.32306
C 39 H 62 N 4 O 28
1034.93
1034.3551
S
natural
Unimod:160
PSI-MOD
Hex(1)HexNAc(1)NeuAc(2)
Hex1HexNAc1NeuAc2
MOD:01205
Hex1HexNAc1NeuAc2 O-glycosylated serine
A protein modification that effectively replaces an O3 hydrogen atom of a serine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond.
PubMed:7949339
Unimod:160#S
Hex(1)HexNAc(1)NeuAc(2)
Hex1HexNAc1NeuAc2
A protein modification that effectively replaces an O3 hydrogen atom of a threonine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond.
947.85
C 36 H 57 N 3 O 26
947.32306
C 40 H 64 N 4 O 28
1048.95
1048.3707
T
natural
Unimod:160
PSI-MOD
Hex(1)HexNAc(1)NeuAc(2)
Hex1HexNAc1NeuAc2
MOD:01206
Hex1HexNAc1NeuAc2 O-glycosylated threonine
A protein modification that effectively replaces an O3 hydrogen atom of a threonine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond.
Unimod:160#T
Hex(1)HexNAc(1)NeuAc(2)
Hex1HexNAc1NeuAc2
A protein modification that effectively replaces an N4 hydrogen atom of an asparagine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond.
947.85
C 36 H 57 N 3 O 26
947.32306
C 40 H 63 N 5 O 28
1061.95
1061.366
N
natural
Unimod:160
PSI-MOD
Hex(1)HexNAc(1)NeuAc(2)
Hex1HexNAc1NeuAc2
MOD:01207
Hex1HexNAc1NeuAc2 N4-glycosylated asparagine
A protein modification that effectively replaces an N4 hydrogen atom of an asparagine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond.
Unimod:160#N
Hex(1)HexNAc(1)NeuAc(2)
Hex1HexNAc1NeuAc2
A protein modification that effectively converts a C-terminal residue to the copper(1+) carboxylate salt.
62.54
Cu 1 H -1
61.921772
X
C-term
Unimod:531
cuprous salt
PSI-MOD
Cation:Cu[I]
Replacement of proton by copper
MOD:01208
copper(1+) carboxylate C-terminal residue
A protein modification that effectively converts a C-terminal residue to the copper(1+) carboxylate salt.
Unimod:531#C-term
cuprous salt
Cation:Cu[I]
Replacement of proton by copper
A protein modification that effectively converts an L-aspartic acid residue to the copper(1+) aspartate salt.
62.54
Cu 1 H -1
61.921772
C 4 Cu 1 H 4 N 1 O 3
177.63
176.94872
D
Unimod:531
cuprous salt
PSI-MOD
Cation:Cu[I]
Replacement of proton by copper
MOD:01209
copper(1+) L-aspartate
A protein modification that effectively converts an L-aspartic acid residue to the copper(1+) aspartate salt.
Unimod:531#D
cuprous salt
Cation:Cu[I]
Replacement of proton by copper
A protein modification that effectively converts an L-glutamic acid residue to the copper(1+) glutamate salt.
62.54
Cu 1 H -1
61.921772
C 5 Cu 1 H 6 N 1 O 3
191.65
190.96437
E
Unimod:531
cuprous salt
PSI-MOD
Cation:Cu[I]
Replacement of proton by copper
MOD:01210
copper(1+) L-glutamate
A protein modification that effectively converts an L-glutamic acid residue to the copper(1+) glutamate salt.
Unimod:531#E
cuprous salt
Cation:Cu[I]
Replacement of proton by copper
A protein modification that effectively converts an L-lysine residue to N6-(morpholine-2-acetyl)-lysine.
127.14
C 6 H 9 N 1 O 2
127.06333
C 12 H 21 N 3 O 3
255.32
255.1583
K
artifact
Unimod:29
N-succinimidylmorpholine-2-acetate N6-derivatized lysine
PSI-MOD
N-Succinimidyl-2-morpholine acetate
SMA
MOD:01211
The Unimod name "N-Succinimidyl-3-morpholine acetate" appears to have been a typographical error [JSG].
N6-(morpholine-2-acetyl)-lysine
A protein modification that effectively converts an L-lysine residue to N6-(morpholine-2-acetyl)-lysine.
PubMed:10446193
Unimod:29#K
N-succinimidylmorpholine-2-acetate N6-derivatized lysine
N-Succinimidyl-2-morpholine acetate
SMA
A protein modification that effectively converts an L-lysine residue to N6-(carboxamidomethyl)lysine.
57.05
C 2 H 3 N 1 O 1
57.021465
C 8 H 15 N 3 O 2
185.23
185.11642
K
artifact
Unimod:4
N6-(2-amino-2-oxoethyl)lysine
N6-(carbamoylmethyl)lysine
carbamidomethylk
PSI-MOD
Carbamidomethyl
Iodoacetamide derivative
MOD:01212
iodoacetamide N6-derivatized lysine
A protein modification that effectively converts an L-lysine residue to N6-(carboxamidomethyl)lysine.
OMSSA:27
PubMed:11510821
PubMed:12422359
PubMed:12686488
Unimod:4#K
N6-(2-amino-2-oxoethyl)lysine
N6-(carbamoylmethyl)lysine
carbamidomethylk
Carbamidomethyl
Iodoacetamide derivative
A protein modification that effectively converts an L-histidine residue to an iodoacetamide derivatized histidine, either 1'- or 3'-(carboxamidolmethyl)histidine.
57.05
C 2 H 3 N 1 O 1
57.021465
C 8 H 10 N 4 O 2
194.19
194.08038
H
artifact
Unimod:4
carbamidometylh
PSI-MOD
Carbamidomethyl
Iodoacetamide derivative
MOD:01213
iodoacetamide derivatized histidine
A protein modification that effectively converts an L-histidine residue to an iodoacetamide derivatized histidine, either 1'- or 3'-(carboxamidolmethyl)histidine.
OMSSA:28
PubMed:11510821
PubMed:12422359
PubMed:15627961
PubMed:2026710
Unimod:4#H
carbamidometylh
Carbamidomethyl
Iodoacetamide derivative
modification from Unimod Chemical derivative - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060.
MOD:01060
57.05
C 2 H 3 N 1 O 1
57.021465
C
artifact
Unimod:4
PSI-MOD
Carbamidomethyl
Iodoacetamide derivative
MOD:01214
iodoacetamide - site C
true
modification from Unimod Chemical derivative - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060.
PubMed:10504701
PubMed:11510821
PubMed:12422359
Unimod:4#C
Carbamidomethyl
Iodoacetamide derivative
A protein modification that effectively converts an L-aspartic acid residue to O4-(carboxamidomethyl)aspartate.
57.05
C 2 H 3 N 1 O 1
57.021465
C 6 H 8 N 2 O 4
172.14
172.0484
D
artifact
Unimod:4
carbamidomethyld
PSI-MOD
Carbamidomethyl
Iodoacetamide derivative
MOD:01215
iodoacetamide derivatized aspartic acid
A protein modification that effectively converts an L-aspartic acid residue to O4-(carboxamidomethyl)aspartate.
OMSSA:29
PubMed:11510821
PubMed:12422359
PubMed:16526082
Unimod:4#D
carbamidomethyld
Carbamidomethyl
Iodoacetamide derivative
A protein modification that effectively converts an L-glutamic acid residue to O5-(carboxamidomethyl)glutamate.
57.05
C 2 H 3 N 1 O 1
57.021465
C 7 H 10 N 2 O 4
186.17
186.06406
E
artifact
Unimod:4
carbamidomethyle
PSI-MOD
Carbamidomethyl
Iodoacetamide derivative
MOD:01216
iodoacetamide derivatized glutamic acid
A protein modification that effectively converts an L-glutamic acid residue to O5-(carboxamidomethyl)glutamate.
OMSSA:30
PubMed:11510821
PubMed:12422359
Unimod:4#E
carbamidomethyle
Carbamidomethyl
Iodoacetamide derivative
modification from Unimod Isotopic label -
155.0
(12)C 6 H 5 N 1 O 2 S 1
155.0041
(12)C 10 H 10 N 2 O 5 S 1
270.03
270.03104
D
artifact
Unimod:285
PSI-MOD
Light Sulfanilic Acid (SA) C12
SulfanilicAcid
MOD:01217
Sulfanilic Acid (SA), light C12 - site D
modification from Unimod Isotopic label -
PubMed:12872131
Unimod:285#D
Light Sulfanilic Acid (SA) C12
SulfanilicAcid
modification from Unimod Isotopic label -
155.0
(12)C 6 H 5 N 1 O 2 S 1
155.0041
(12)C 11 H 12 N 2 O 5 S 1
284.05
284.0467
E
artifact
Unimod:285
PSI-MOD
Light Sulfanilic Acid (SA) C12
SulfanilicAcid
MOD:01218
Sulfanilic Acid (SA), light C12 - site E
modification from Unimod Isotopic label -
PubMed:15283597
Unimod:285#E
Light Sulfanilic Acid (SA) C12
SulfanilicAcid
modification from Unimod Chemical derivative -
161.02
(13)C 6 H 5 N 1 O 2 S 1
161.02423
(12)C 4 (13)C 6 H 10 N 2 O 5 S 1
276.05
276.05118
D
artifact
Unimod:286
PSI-MOD
Heavy Sulfanilic Acid (SA) C13
SulfanilicAcid:13C(6)
MOD:01219
Sulfanilic Acid (SA), heavy C13 - site D
modification from Unimod Chemical derivative -
PubMed:9254591
PubMed:9750125
Unimod:286#D
Heavy Sulfanilic Acid (SA) C13
SulfanilicAcid:13C(6)
modification from Unimod Chemical derivative -
161.02
(13)C 6 H 5 N 1 O 2 S 1
161.02423
(12)C 5 (13)C 6 H 12 N 2 O 5 S 1
290.07
290.06683
E
artifact
Unimod:286
PSI-MOD
Heavy Sulfanilic Acid (SA) C13
SulfanilicAcid:13C(6)
MOD:01220
Sulfanilic Acid (SA), heavy C13 - site E
modification from Unimod Chemical derivative -
PubMed:15121203
PubMed:9254591
Unimod:286#E
Heavy Sulfanilic Acid (SA) C13
SulfanilicAcid:13C(6)
A protein modification that effectively converts an L-threonine residue to O-formyl-L-threonine.
28.01
C 1 O 1
27.994915
C 5 H 7 N 1 O 3
129.12
129.04259
T
artifact
Unimod:122
PSI-MOD
Formyl
Formylation
MOD:01221
From Unimod: Can occur under CNBr cleavage conditions (70% HCOOH).
O-formyl-L-threonine
A protein modification that effectively converts an L-threonine residue to O-formyl-L-threonine.
PubMed:11861642
PubMed:15799070
Unimod:122#T
Formyl
Formylation
A protein modification that effectively converts an L-serine residue to O-formyl-L-serine.
28.01
C 1 O 1
27.994915
C 4 H 5 N 1 O 3
115.09
115.02694
S
artifact
Unimod:122
PSI-MOD
Formyl
Formylation
MOD:01222
From Unimod: Can occur under CNBr cleavage conditions (70% HCOOH).
O-formyl-L-serine
A protein modification that effectively converts an L-serine residue to O-formyl-L-serine.
PubMed:15627961
PubMed:15799070
Unimod:122#S
Formyl
Formylation
modification from Unimod Other -
88.12
C 3 H 4 O 1 S 1
87.99828
X
artifact
N-term
Unimod:126
ntermpeptioacetyl
PSI-MOD
3,3-Dithio-bis-(sulfosuccinimidyl)propionate
Thioacyl
thioacylation of primary amines (N-term and Lys)
MOD:01223
This Unimod entry is misdescribed as "thioacylation" [JSG].
thioacylation of primary amines - site N-term
modification from Unimod Other -
OMSSA:41
PubMed:11710128
PubMed:3155470
PubMed:957432
Unimod:126#N-term
ntermpeptioacetyl
3,3-Dithio-bis-(sulfosuccinimidyl)propionate
Thioacyl
thioacylation of primary amines (N-term and Lys)
modification from Unimod Other -
88.12
C 3 H 4 O 1 S 1
87.99828
C 9 H 16 N 2 O 2 S 1
216.3
216.09325
K
artifact
Unimod:126
thioacetylk
PSI-MOD
3,3-Dithio-bis-(sulfosuccinimidyl)propionate
Thioacyl
thioacylation of primary amines (N-term and Lys)
MOD:01224
This Unimod entry is misdescribed as "thioacylation" [JSG].
thioacylation of primary amines - site K
modification from Unimod Other -
OMSSA:40
PubMed:11710128
PubMed:3155470
PubMed:957432
Unimod:126#K
thioacetylk
3,3-Dithio-bis-(sulfosuccinimidyl)propionate
Thioacyl
thioacylation of primary amines (N-term and Lys)
A protein modification that effectively converts an L-tyrosine residue into an L-fluorotyrosine.
17.99
F 1 H -1
17.990578
C 9 F 1 H 8 N 1 O 2
181.17
181.05391
Y
artifact
Unimod:127
phef
PSI-MOD
Fluoro
fluorophenylalanine replacement of phenylalanine
MOD:01225
From Unimod: the citation appears to be correct, but the PMID is not and has been corrected [JSG].
monofluorinated L-tyrosine
A protein modification that effectively converts an L-tyrosine residue into an L-fluorotyrosine.
OMSSA:46
PubMed:8069568
Unimod:127#Y
phef
Fluoro
fluorophenylalanine replacement of phenylalanine
A protein modification that effectively converts an L-tryptophan residue to an L-fluorotryptophan.
17.99
F 1 H -1
17.990578
C 11 F 1 H 9 N 2 O 1
204.2
204.06989
W
artifact
Unimod:127
PSI-MOD
Fluoro
fluorophenylalanine replacement of phenylalanine
MOD:01226
From Unimod: the citation appears to be correct, but the PMID is not and has been corrected [JSG].
monofluorinated L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to an L-fluorotryptophan.
PubMed:8069568
Unimod:127#W
Fluoro
fluorophenylalanine replacement of phenylalanine
A protein modification that effectively converts an L-phenylalanine residue to an L-fluorophenylalanine.
17.99
C 0 F 1 H -1 N 0 O 0
17.990578
C 9 F 1 H 8 N 1 O 1
165.17
165.05899
F
artifact
Unimod:127
phef
PSI-MOD
Fluoro
fluorophenylalanine replacement of phenylalanine
MOD:01227
From Unimod: the citation appears to be correct, but the PMID is not and has been corrected. From DeltaMass: (element abbreviation in formula incorrect, mass incorrect, and aggregate not delta) Average Mass: 149 Formula: C9H8O1N1Fl1 Average Mass Change: 149 References:PE Sciex with no citation [JSG].
monofluorinated L-phenylalanine
A protein modification that effectively converts an L-phenylalanine residue to an L-fluorophenylalanine.
DeltaMass:181
OMSSA:46
PubMed:8069568
Unimod:127#F
phef
Fluoro
fluorophenylalanine replacement of phenylalanine
A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one iodine atom.
125.9
H -1 I 1
125.896645
C 9 H 8 I 1 N 1 O 2
289.07
288.95996
Y
artifact
Unimod:129
I1Tyr
iodinationy
PSI-MOD
Iodination
Iodo
MOD:01228
From DeltaMass: Average Mass: 289 [name misspelled "monoiodated" - JSG].
monoiodinated tyrosine
A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one iodine atom.
DeltaMass:0
OMSSA:65
PubMed:1326520
PubMed:15627961
PubMed:2026710
Unimod:129#Y
I1Tyr
iodinationy
Iodination
Iodo
A protein modification that effectively converts an L-histidine residue to an L-iodohistidine.
125.9
C 0 H -1 I 1 N 0 O 0
125.896645
C 6 H 6 I 1 N 3 O 1
263.04
262.95557
H
artifact
Unimod:129
I1His
PSI-MOD
Iodination
Iodo
MOD:01229
L-iodohistidine
A protein modification that effectively converts an L-histidine residue to an L-iodohistidine.
PubMed:15627961
PubMed:2026710
Unimod:129#H
I1His
Iodination
Iodo
modification from Unimod Isotopic label -
105.02
(12)C 6 H 3 N 1 O 1
105.02146
(12)C 12 H 15 N 3 O 2
233.12
233.11642
K
artifact
Unimod:365
PSI-MOD
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form
ICPL
MOD:01230
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form - site K
modification from Unimod Isotopic label -
PubMed:15602776
Unimod:365#K
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form
ICPL
A protein modification that effectively converts an L-lysine residue to 3x(13)C labeled N6-propanoyl-L-lysine.
59.04
(13)C 3 H 4 O 1
59.036278
(12)C 6 (13)C 3 H 16 N 2 O 2
187.13
187.13124
K
artifact
Unimod:59
PSI-MOD
Propionate labeling reagent heavy form (+3amu), N-term & K
Propionyl:13C(3)
MOD:01231
3x(13)C labeled N6-propanoyl-L-lysine
A protein modification that effectively converts an L-lysine residue to 3x(13)C labeled N6-propanoyl-L-lysine.
PubMed:11857757
PubMed:11999733
PubMed:12175151
PubMed:12442261
Unimod:59#K
Propionate labeling reagent heavy form (+3amu), N-term & K
Propionyl:13C(3)
A protein modification that effectively converts an L-lysine residue to 3x(12)C labeled N6-propanoyl-L-lysine.
56.03
(12)C 3 H 4 O 1
56.026215
(12)C 9 H 16 N 2 O 2
184.12
184.12119
K
artifact
Unimod:58
PSI-MOD
Propionate labeling reagent light form (N-term & K)
Propionyl
MOD:01232
3x(12)C labeled N6-propanoyl-L-lysine
A protein modification that effectively converts an L-lysine residue to 3x(12)C labeled N6-propanoyl-L-lysine.
PubMed:11857757
PubMed:11999733
PubMed:12175151
Unimod:58#K
Propionate labeling reagent light form (N-term & K)
Propionyl
A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled N6-acetyl-L-lysine.
45.03
C 2 (1)H -1 (2)H 3 O 1
45.029396
C 8 (1)H 11 (2)H 3 N 2 O 2
173.12
173.12436
K
artifact
Unimod:56
PSI-MOD
Acetate labeling reagent (N-term & K) (heavy form, +3amu)
Acetyl:2H(3)
MOD:01233
3x(2)H labeled N6-acetyl-L-lysine
A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled N6-acetyl-L-lysine.
PubMed:11857757
PubMed:11999733
PubMed:12175151
Unimod:56#K
Acetate labeling reagent (N-term & K) (heavy form, +3amu)
Acetyl:2H(3)
modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate
2.0
(16)O -1 (18)O 1
2.004246
C 3 H 5 N 1 (16)O 1 (18)O 1
89.04
89.03628
S
artifact
Unimod:258
PSI-MOD
Label:18O(1)
O18 Labeling
MOD:01234
(18)O monosubstituted L-serine
modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate
PubMed:11467524
Unimod:258#S
Label:18O(1)
O18 Labeling
modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate
2.0
(16)O -1 (18)O 1
2.004246
C 4 H 7 N 1 (16)O 1 (18)O 1
103.05
103.051926
T
artifact
Unimod:258
PSI-MOD
Label:18O(1)
O18 Labeling
MOD:01235
(18)O monosubstituted L-threonine
modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate
PubMed:11467524
PubMed:15549660
Unimod:258#T
Label:18O(1)
O18 Labeling
modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate
2.0
(16)O -1 (18)O 1
2.004246
C 9 H 9 N 1 (16)O 1 (18)O 1
165.07
165.06758
Y
artifact
Unimod:258
PSI-MOD
Label:18O(1)
O18 Labeling
MOD:01236
(18)O monosubstituted L-tyrosine
modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate
PubMed:11467524
PubMed:15549660
Unimod:258#Y
Label:18O(1)
O18 Labeling
A protein modification produced by formation of an adduct of an L-cysteine residue with 4-hydroxynonenal.
156.22
C 9 H 16 O 2
156.11504
C 12 H 21 N 1 O 3 S 1
259.36
259.1242
C
artifact
Unimod:53
PSI-MOD
4-hydroxynonenal (HNE)
HNE
MOD:01237
4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG].
cysteine 4-hydroxynonenal adduct
A protein modification produced by formation of an adduct of an L-cysteine residue with 4-hydroxynonenal.
PubMed:11327326
PubMed:15133838
PubMed:9629898
Unimod:53#C
4-hydroxynonenal (HNE)
HNE
A protein modification produced by formation of an adduct of an L-lysine residue with 4-hydroxynonenal.
156.22
C 9 H 16 O 2
156.11504
C 15 H 28 N 2 O 3
284.4
284.21
K
artifact
Unimod:53
PSI-MOD
4-hydroxynonenal (HNE)
HNE
MOD:01238
4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG].
lysine 4-hydroxynonenal adduct
A protein modification produced by formation of an adduct of an L-lysine residue with 4-hydroxynonenal.
PubMed:11327326
PubMed:15133838
PubMed:9629898
Unimod:53#K
4-hydroxynonenal (HNE)
HNE
A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal.
156.22
C 9 H 16 O 2
156.11504
C 15 H 23 N 3 O 3
293.37
293.17395
H
artifact
Unimod:53
PSI-MOD
4-hydroxynonenal (HNE)
HNE
MOD:01239
4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG].
histidine 4-hydroxynonenal adduct
A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal.
PubMed:10717661
PubMed:11327326
PubMed:15133838
Unimod:53#H
4-hydroxynonenal (HNE)
HNE
A protein modification that crosslinks the N6-amino of a peptidyl lysine with the carboxyl of leucyl-arginyl-glycyl-glycine, the C-terminal tetrapeptide of ubiquitin.
383.45
C 16 H 29 N 7 O 4
383.2281
C 22 H 41 N 9 O 5
511.63
511.32306
K
artifact
Unimod:535
PSI-MOD
LeuArgGlyGly
Ubiquitination
MOD:01240
ubiquitination signature tetrapeptidyl lysine
A protein modification that crosslinks the N6-amino of a peptidyl lysine with the carboxyl of leucyl-arginyl-glycyl-glycine, the C-terminal tetrapeptide of ubiquitin.
PubMed:10504701
Unimod:535
LeuArgGlyGly
Ubiquitination
A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled L-aspartic acid 4-methyl ester.
17.03
C 1 (1)H -1 (2)H 3
17.03448
C 5 (1)H 4 (2)H 3 N 1 O 3
132.06
132.06142
D
artifact
Unimod:298
trideuteromethyld
PSI-MOD
Methyl:2H(3)
deuterated methyl ester
MOD:01241
3x(2)H labeled L-aspartic acid 4-methyl ester
A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled L-aspartic acid 4-methyl ester.
OMSSA:19
PubMed:12185208
Unimod:298#D
trideuteromethyld
Methyl:2H(3)
deuterated methyl ester
A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled L-glutamic acid 5-methyl ester.
17.03
C 1 (1)H -1 (2)H 3
17.03448
C 6 (1)H 6 (2)H 3 N 1 O 3
146.08
146.07707
E
artifact
Unimod:298
trideuteromethyle
PSI-MOD
Methyl:2H(3)
deuterated methyl ester
MOD:01242
3x(2)H labeled L-glutamic acid 5-methyl ester
A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled L-glutamic acid 5-methyl ester.
OMSSA:20
PubMed:1326520
Unimod:298#E
trideuteromethyle
Methyl:2H(3)
deuterated methyl ester
A protein modification that effectively converts a C-terminal residue to the potassium carboxylate salt.
38.09
H -1 K 1
37.955883
X
C-term
Unimod:530
PSI-MOD
Cation:K
Replacement of proton by potassium
MOD:01243
potassium carboxylate C-terminal residue
A protein modification that effectively converts a C-terminal residue to the potassium carboxylate salt.
Unimod:530#C-term
Cation:K
Replacement of proton by potassium
A protein modification that effectively converts an L-glutamioc acid residue to the potassium glutamate salt.
38.09
H -1 K 1
37.955883
C 5 H 6 K 1 N 1 O 3
167.21
166.99847
E
Unimod:530
PSI-MOD
Cation:K
Replacement of proton by potassium
MOD:01244
potassium L-glutamate
A protein modification that effectively converts an L-glutamioc acid residue to the potassium glutamate salt.
Unimod:530#E
Cation:K
Replacement of proton by potassium
A protein modification that effectively converts an L-aspartic acid residue to the potassium aspartate salt.
38.09
H -1 K 1
37.955883
C 4 H 4 K 1 N 1 O 3
153.18
152.98282
D
Unimod:530
PSI-MOD
Cation:K
Replacement of proton by potassium
MOD:01245
potassium L-aspartate
A protein modification that effectively converts an L-aspartic acid residue to the potassium aspartate salt.
Unimod:530#D
Cation:K
Replacement of proton by potassium
OBSOLETE because redundant and identical to MOD:00812 after formula correction. Remap to MOD:00812.
MOD:00812
147.15
C 6 H 11 O 4
147.06573
C 9 H 16 N 1 O 6
234.23
234.09776
S
natural
Unimod:295
PSI-MOD
Fucose
dHex
MOD:01246
fucosylated -site S
true
OBSOLETE because redundant and identical to MOD:00812 after formula correction. Remap to MOD:00812.
PubMed:11344537
PubMed:15189151
PubMed:3311742
PubMed:3578767
Unimod:295#S
Fucose
dHex
OBSOLETE because redundant and identical to MOD:00813 after formula correction. Remap to MOD:00813.
MOD:00813
147.15
C 6 H 11 O 4
147.06573
C 10 H 18 N 1 O 6
248.26
248.11342
T
natural
Unimod:295
PSI-MOD
Fucose
dHex
MOD:01247
fucosylated -site T
true
OBSOLETE because redundant and identical to MOD:00813 after formula correction. Remap to MOD:00813.
PubMed:11344537
PubMed:11857757
PubMed:15189151
Unimod:295#T
Fucose
dHex
A protein modification that is produced by reaction of iodouridine monophosphate with an L-tyrosine residue to form an ether linkage.
322.17
C 9 H 11 N 2 O 9 P 1
322.0202
C 18 H 20 N 3 O 11 P 1
485.34
485.08356
Y
artifact
Unimod:292
PSI-MOD
Cross-link of (Iodo)-uracil MP with W,F,Y
IodoU-AMP
MOD:01248
This has an ether linkage and not a phosphodiester linkage with UMP.
iodouridine monophosphate derivatized tyrosine
A protein modification that is produced by reaction of iodouridine monophosphate with an L-tyrosine residue to form an ether linkage.
PubMed:11112526
PubMed:11567090
PubMed:6540775
Unimod:292#Y
Cross-link of (Iodo)-uracil MP with W,F,Y
IodoU-AMP
A protein modification that is produced by reaction of iodouridine monophosphate with an L-tryptophan residue.
322.17
C 9 H 11 N 2 O 9 P 1
322.0202
C 20 H 21 N 4 O 10 P 1
508.38
508.09952
W
artifact
Unimod:292
PSI-MOD
Cross-link of (Iodo)-uracil MP with W,F,Y
IodoU-AMP
MOD:01249
This has a carbon-nitrogen linkage and not a phosphodiester linkage with UMP.
iodouridine monophosphate derivatized tryptophan
A protein modification that is produced by reaction of iodouridine monophosphate with an L-tryptophan residue.
PubMed:11112526
PubMed:11567090
PubMed:6540775
Unimod:292#W
Cross-link of (Iodo)-uracil MP with W,F,Y
IodoU-AMP
A protein modification that is produced by reaction of iodouridine monophosphate with an L-phenylalanine residue.
322.17
C 9 H 11 N 2 O 9 P 1
322.0202
C 18 H 20 N 3 O 10 P 1
469.34
469.08862
F
artifact
Unimod:292
PSI-MOD
Cross-link of (Iodo)-uracil MP with W,F,Y
IodoU-AMP
MOD:01250
This has a carbon-carbon linkage and not a phosphodiester linkage with UMP.
iodouridine monophosphate derivatized phenylalanine
A protein modification that is produced by reaction of iodouridine monophosphate with an L-phenylalanine residue.
PubMed:11112526
PubMed:11567090
PubMed:6540775
Unimod:292#F
Cross-link of (Iodo)-uracil MP with W,F,Y
IodoU-AMP
A protein modification that effectively converts an L-lysine residue to N6-[3-(carboxamidomethylthio)propanoyl]lysine.
145.18
C 5 H 7 N 1 O 2 S 1
145.01974
C 11 H 19 N 3 O 3 S 1
273.35
273.11472
K
artifact
Unimod:293
PSI-MOD
3-(carbamidomethylthio)propanoyl
CAMthiopropanoyl
MOD:01251
N6-[3-(carboxamidomethylthio)propanoyl]lysine
A protein modification that effectively converts an L-lysine residue to N6-[3-(carboxamidomethylthio)propanoyl]lysine.
PubMed:15121203
Unimod:293#K
3-(carbamidomethylthio)propanoyl
CAMthiopropanoyl
OBSOLETE because redundant and identical to MOD:00933. Remap to MOD:00933.
MOD:00933
54.05
C 3 H 2 O 1
54.010567
C 9 H 14 N 4 O 2
210.24
210.11168
R
artifact
Unimod:319
PSI-MOD
Delta:H(2)C(3)O(1)
MDA adduct +54
MOD:01252
5-hydro-5-methylimidazol-4-one, methylglyoxal arginine adduct (+54 amu)
true
OBSOLETE because redundant and identical to MOD:00933. Remap to MOD:00933.
PubMed:9448752
Unimod:319#R
Delta:H(2)C(3)O(1)
MDA adduct +54
modification from Unimod Chemical derivative - Malondialdehyde (MDA) adduct
54.05
C 3 H 2 O 1
54.010567
C 9 H 14 N 2 O 2
182.22
182.10553
K
artifact
Unimod:319
PSI-MOD
Delta:H(2)C(3)O(1)
MDA adduct +54
MOD:01253
malondialdehyde lysine adduct (+54 amu)
modification from Unimod Chemical derivative - Malondialdehyde (MDA) adduct
Unimod:319#K
Delta:H(2)C(3)O(1)
MDA adduct +54
A protein modification that effectively converts an L-lysine residue to 4x(2)H labeled dimethylated L-lysine.
32.06
C 2 (2)H 4
32.056408
C 8 H 12 (2)H 4 N 2 O 1
160.15
160.15137
K
artifact
Unimod:199
mod189
PSI-MOD
DiMethyl-CHD2
Dimethyl:2H(4)
MOD:01254
4x(2)H labeled dimethylated L-lysine
A protein modification that effectively converts an L-lysine residue to 4x(2)H labeled dimethylated L-lysine.
OMSSA:189
PubMed:14670044
Unimod:199#K
mod189
DiMethyl-CHD2
Dimethyl:2H(4)
A protein modification that effectively converts an L-serine residue to S-(2-sulfanylethyl)cysteine.
76.18
C 2 H 4 O -1 S 2
75.98053
C 5 H 9 N 1 O 1 S 2
163.25
163.01256
S
artifact
Unimod:200
S-(2-mercaptoethyl)cysteine
PSI-MOD
EDT
Ethanedithiol
MOD:01255
S-(2-sulfanylethyl)cysteine (Ser)
A protein modification that effectively converts an L-serine residue to S-(2-sulfanylethyl)cysteine.
PubMed:11507762
Unimod:200#S
S-(2-mercaptoethyl)cysteine
EDT
Ethanedithiol
A protein modification that effectively converts an L-threonine residue to 3-methyl-S-(2-sulfanylethyl)cysteine.
76.18
C 2 H 4 O -1 S 2
75.98053
C 6 H 11 N 1 O 1 S 2
177.28
177.02821
T
artifact
Unimod:200
beta-methyl-S-(2-mercaptoethyl)cysteine
PSI-MOD
EDT
Ethanedithiol
MOD:01256
3-methyl-S-(2-sulfanylethyl)cysteine (Thr)
A protein modification that effectively converts an L-threonine residue to 3-methyl-S-(2-sulfanylethyl)cysteine.
PubMed:11507762
Unimod:200#T
beta-methyl-S-(2-mercaptoethyl)cysteine
EDT
Ethanedithiol
modification from Unimod Chemical derivative -
170.17
C 10 H 6 N 2 O 1
170.04802
C 16 H 18 N 4 O 2
298.35
298.14297
K
artifact
Unimod:194
PSI-MOD
6-aminoquinolyl-N-hydroxysuccinimidyl carbamate
AccQTag
MOD:01257
6-aminoquinolyl-N-hydroxysuccinimidyl carbamate - site K
modification from Unimod Chemical derivative -
PubMed:12716131
PubMed:14997490
Unimod:194#K
6-aminoquinolyl-N-hydroxysuccinimidyl carbamate
AccQTag
modification from Unimod Chemical derivative -
111.1
C 5 H 5 N 1 O 2
111.03203
C 8 H 10 N 2 O 3 S 1
214.24
214.04121
C
artifact
Unimod:314
PSI-MOD
Nmethylmaleimide
MOD:01258
N-methylmaleimide modified L-cysteine
modification from Unimod Chemical derivative -
PubMed:9448752
Unimod:314#C
Nmethylmaleimide
Nmethylmaleimide
modification from Unimod Chemical derivative -
111.1
C 5 H 5 N 1 O 2
111.03203
C 11 H 17 N 3 O 3
239.27
239.12698
K
artifact
Unimod:314
PSI-MOD
Nmethylmaleimide
MOD:01259
N-methylmaleimide modified L-lysine
modification from Unimod Chemical derivative -
PubMed:9448752
Unimod:314#K
Nmethylmaleimide
Nmethylmaleimide
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
362.38
C 19 H 22 O 7
362.13657
C 28 H 31 N 1 O 9
525.55
525.1999
Y
artifact
Unimod:270
PSI-MOD
Cytopiloyne
nucleophilic addtion to cytopiloyne
MOD:01260
nucleophilic addtion to cytopiloyne - site Y
true
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
PubMed:15549660
Unimod:270#Y
Cytopiloyne
nucleophilic addtion to cytopiloyne
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
362.38
C 19 H 22 O 7
362.13657
C 22 H 27 N 1 O 9
449.46
449.16858
S
artifact
Unimod:270
PSI-MOD
Cytopiloyne
nucleophilic addtion to cytopiloyne
MOD:01261
nucleophilic addtion to cytopiloyne - site S
true
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
PubMed:15549660
Unimod:270#C
Cytopiloyne
nucleophilic addtion to cytopiloyne
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
362.38
C 19 H 22 O 7
362.13657
C 25 H 34 N 4 O 8
518.57
518.2377
R
artifact
Unimod:270
PSI-MOD
Cytopiloyne
nucleophilic addtion to cytopiloyne
MOD:01262
nucleophilic addition to cytopiloyne - site R
true
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
PubMed:12590383
PubMed:15549660
Unimod:270#R
Cytopiloyne
nucleophilic addtion to cytopiloyne
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
362.38
C 19 H 22 O 7
362.13657
C 25 H 34 N 2 O 8
490.55
490.2315
K
artifact
Unimod:270
PSI-MOD
Cytopiloyne
nucleophilic addtion to cytopiloyne
MOD:01263
nucleophilic addtion to cytopiloyne - site K
true
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
PubMed:15549660
Unimod:270#K
Cytopiloyne
nucleophilic addtion to cytopiloyne
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
362.38
C 19 H 22 O 7
362.13657
C 22 H 27 N 1 O 8 S 1
465.52
465.14575
C
artifact
Unimod:270
PSI-MOD
Cytopiloyne
nucleophilic addtion to cytopiloyne
MOD:01264
nucleophilic addtion to cytopiloyne - site C
true
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
PubMed:15549660
Unimod:270#C
Cytopiloyne
nucleophilic addtion to cytopiloyne
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
362.38
C 19 H 22 O 7
362.13657
C 24 H 29 N 1 O 8
459.5
459.18933
P
artifact
Unimod:270
PSI-MOD
Cytopiloyne
nucleophilic addtion to cytopiloyne
MOD:01265
nucleophilic addtion to cytopiloyne - site P
true
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
PubMed:15549660
Unimod:270#P
Cytopiloyne
nucleophilic addtion to cytopiloyne
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
380.39
C 19 H 24 O 8
380.14713
C 22 H 29 N 1 O 9 S 1
483.53
483.1563
C
artifact
Unimod:271
PSI-MOD
Cytopiloyne+water
nucleophilic addition to cytopiloyne+H2O
MOD:01266
nucleophilic addition to cytopiloyne+H2O - site C
true
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
PubMed:15549660
Unimod:271#C
Cytopiloyne+water
nucleophilic addition to cytopiloyne+H2O
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
380.39
C 19 H 24 O 8
380.14713
C 25 H 36 N 2 O 9
508.57
508.2421
K
artifact
Unimod:271
PSI-MOD
Cytopiloyne+water
nucleophilic addition to cytopiloyne+H2O
MOD:01267
nucleophilic addition to cytopiloyne+H2O - site K
true
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
PubMed:11746907
PubMed:15549660
Unimod:271#K
Cytopiloyne+water
nucleophilic addition to cytopiloyne+H2O
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
380.39
C 19 H 24 O 8
380.14713
C 23 H 31 N 1 O 10
481.5
481.1948
T
artifact
Unimod:271
PSI-MOD
Cytopiloyne+water
nucleophilic addition to cytopiloyne+H2O
MOD:01268
nucleophilic addition to cytopiloyne+H2O - site T
true
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
PubMed:15549660
Unimod:271#T
Cytopiloyne+water
nucleophilic addition to cytopiloyne+H2O
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
380.39
C 19 H 24 O 8
380.14713
C 25 H 36 N 4 O 9
536.58
536.2482
R
artifact
Unimod:271
PSI-MOD
Cytopiloyne+water
nucleophilic addition to cytopiloyne+H2O
MOD:01269
nucleophilic addition to cytopiloyne+H2O - site R
true
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
PubMed:15549660
Unimod:271#R
Cytopiloyne+water
nucleophilic addition to cytopiloyne+H2O
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
380.39
C 19 H 24 O 8
380.14713
C 22 H 29 N 1 O 10
467.47
467.17914
S
artifact
Unimod:271
PSI-MOD
Cytopiloyne+water
nucleophilic addition to cytopiloyne+H2O
MOD:01270
nucleophilic addition to cytopiloyne+H2O - site S
true
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
PubMed:14670044
PubMed:15549660
Unimod:271#S
Cytopiloyne+water
nucleophilic addition to cytopiloyne+H2O
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
380.39
C 19 H 24 O 8
380.14713
C 28 H 33 N 1 O 10
543.57
543.21045
Y
artifact
Unimod:271
PSI-MOD
Cytopiloyne+water
nucleophilic addition to cytopiloyne+H2O
MOD:01271
nucleophilic addition to cytopiloyne+H2O - site Y
true
OBSOLETE because there is no evidence in the literature of covalent modification of polypeptides with cytopiloyne or cytopiloyne+H2O. Modifications could potentially happen, but are not experimentally verified. [PMT] modification from Unimod Chemical derivative -
PubMed:15549660
Unimod:271#Y
Cytopiloyne+water
nucleophilic addition to cytopiloyne+H2O
modification from Unimod Chemical derivative -
225.31
C 10 H 15 N 3 O 1 S 1
225.09358
C 16 H 27 N 5 O 2 S 1
353.49
353.18854
K
artifact
Unimod:89
PSI-MOD
Iminobiotin
Iminobiotinylation
MOD:01272
iminobiotinylation - site K
modification from Unimod Chemical derivative -
PubMed:9750125
Unimod:89#K
Iminobiotin
Iminobiotinylation
A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-serine residue.
183.23
C 8 H 9 N 1 O 2 S 1
183.0354
C 11 H 14 N 2 O 4 S 1
270.3
270.0674
S
artifact
Unimod:276
PSI-MOD
AEBS
Aminoethylbenzenesulfonylation
MOD:01273
O-[4-(2-aminoethyl)benzenesulfonyl] serine
A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-serine residue.
PubMed:15283597
PubMed:8597590
Unimod:276#S
AEBS
Aminoethylbenzenesulfonylation
A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-histidine residue.
183.23
C 8 H 9 N 1 O 2 S 1
183.0354
C 14 H 16 N 4 O 3 S 1
320.37
320.0943
H
artifact
Unimod:276
PSI-MOD
AEBS
Aminoethylbenzenesulfonylation
MOD:01274
N'-[4-(2-aminoethyl)benzenesulfonyl] derivatized histidine
A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-histidine residue.
PubMed:8597590
Unimod:276#H
AEBS
Aminoethylbenzenesulfonylation
A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-lysine residue.
183.23
C 8 H 9 N 1 O 2 S 1
183.0354
C 14 H 21 N 3 O 3 S 1
311.4
311.13037
K
artifact
Unimod:276
PSI-MOD
AEBS
Aminoethylbenzenesulfonylation
MOD:01275
N6-[4-(2-aminoethyl)benzenesulfonyl]lysine
A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-lysine residue.
PubMed:8597590
Unimod:276#K
AEBS
Aminoethylbenzenesulfonylation
A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-tyrosine residue.
183.23
C 8 H 9 N 1 O 2 S 1
183.0354
C 17 H 18 N 2 O 4 S 1
346.4
346.09872
Y
artifact
Unimod:276
PSI-MOD
AEBS
Aminoethylbenzenesulfonylation
MOD:01276
O4'-[4-(2-aminoethyl)benzenesulfonyl]tyrosine
A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-tyrosine residue.
PubMed:10906242
PubMed:8597590
Unimod:276#Y
AEBS
Aminoethylbenzenesulfonylation
modification from Unimod Other -
70.09
C 4 H 6 O 1
70.04186
C 7 H 11 N 1 O 2 S 1
173.23
173.05106
C
artifact
Unimod:253
PSI-MOD
Crotonaldehyde
MOD:01277
crotonylated L-cysteine
modification from Unimod Other -
PubMed:11283024
Unimod:253#C
Crotonaldehyde
Crotonaldehyde
modification from Unimod Other -
70.09
C 4 H 6 O 1
70.04186
C 10 H 18 N 2 O 2
198.27
198.13683
K
artifact
Unimod:253
PSI-MOD
Crotonaldehyde
MOD:01278
crotonylated L-lysine
modification from Unimod Other -
PubMed:11283024
Unimod:253#K
Crotonaldehyde
Crotonaldehyde
modification from Unimod Other -
70.09
C 4 H 6 O 1
70.04186
C 10 H 13 N 3 O 2
207.23
207.10078
H
artifact
Unimod:253
PSI-MOD
Crotonaldehyde
MOD:01279
crotonylated L-histidine
modification from Unimod Other -
PubMed:11283024
PubMed:1443554
Unimod:253#H
Crotonaldehyde
Crotonaldehyde
modification from Unimod Chemical derivative -
490.7
C 20 H 34 N 4 O 4 S 3
490.17422
C 24 H 41 N 5 O 6 S 3
591.8
591.2219
T
artifact
Unimod:118
PSI-MOD
EDT-iodo-PEO-biotin
EDT-iodoacetyl-PEO-biotin
MOD:01280
EDT-iodo-PEO-biotin - site T
modification from Unimod Chemical derivative -
PubMed:11857757
PubMed:12175151
Unimod:118#T
EDT-iodo-PEO-biotin
EDT-iodoacetyl-PEO-biotin
modification from Unimod Chemical derivative -
490.7
C 20 H 34 N 4 O 4 S 3
490.17422
C 23 H 39 N 5 O 6 S 3
577.77
577.20624
S
artifact
Unimod:118
PSI-MOD
EDT-iodo-PEO-biotin
EDT-iodoacetyl-PEO-biotin
MOD:01281
EDT-iodo-PEO-biotin - site S
modification from Unimod Chemical derivative -
PubMed:16335955
Unimod:118#S
EDT-iodo-PEO-biotin
EDT-iodoacetyl-PEO-biotin
OBSOLETE because this modification is not supported by the linked literature [PMT]
56.06
C 3 H 4 O 1
56.026215
C 9 H 11 N 3 O 2
193.21
193.08513
H
artifact
Unimod:206
PSI-MOD
Acrolein addition +56
Delta:H(4)C(3)O(1)
MOD:01282
acrolein addition +56 - site H
true
OBSOLETE because this modification is not supported by the linked literature [PMT]
PubMed:10825247
PubMed:15541752
Unimod:206#H
Acrolein addition +56
Delta:H(4)C(3)O(1)
OBSOLETE because this modification is not supported by the linked literature [PMT]
56.06
C 3 H 4 O 1
56.026215
C 9 H 16 N 2 O 2
184.24
184.12119
K
artifact
Unimod:206
PSI-MOD
Acrolein addition +56
Delta:H(4)C(3)O(1)
MOD:01283
acrolein addition +56 - site K
true
OBSOLETE because this modification is not supported by the linked literature [PMT]
PubMed:10825247
PubMed:15541752
Unimod:206#K
Acrolein addition +56
Delta:H(4)C(3)O(1)
OBSOLETE because this modification is not supported by the linked literature [PMT]
56.06
C 3 H 4 O 1
56.026215
C 6 H 9 N 1 O 2 S 1
159.2
159.0354
C
artifact
Unimod:206
PSI-MOD
Acrolein addition +56
Delta:H(4)C(3)O(1)
MOD:01284
acrolein addition +56 - site C
true
OBSOLETE because this modification is not supported by the linked literature [PMT]
PubMed:10825247
PubMed:15541752
PubMed:9254591
Unimod:206#C
Acrolein addition +56
Delta:H(4)C(3)O(1)
A protein modification that effectively converts an L-leucine residue to 6x(13)C,1x(15)N isotope labeled L-leucine.
7.02
(12)C -6 (13)C 6 (14)N -1 (15)N 1
7.017164
(13)C 6 H 11 (15)N 1 O 1
120.1
120.10123
L
artifact
Unimod:695
PSI-MOD
13C(6) 15N(1) Silac label
Label:13C(6)15N(1)
MOD:01285
6x(13)C,1x(15)N labeled L-leucine
A protein modification that effectively converts an L-leucine residue to 6x(13)C,1x(15)N isotope labeled L-leucine.
PubMed:11857757
PubMed:11999733
PubMed:12175151
Unimod:695#L
13C(6) 15N(1) Silac label
Label:13C(6)15N(1)
A protein modification that effectively converts an L-isoleucine residue to 6x(13)C,1x(15)N isotope labeled L-isoleucine.
7.02
(12)C -6 (13)C 6 (14)N -1 (15)N 1
7.017164
(13)C 6 H 11 (15)N 1 O 1
120.1
120.10123
I
artifact
Unimod:695
PSI-MOD
13C(6) 15N(1) Silac label
Label:13C(6)15N(1)
MOD:01286
6x(13)C,1x(15)N labeled L-isoleucine
A protein modification that effectively converts an L-isoleucine residue to 6x(13)C,1x(15)N isotope labeled L-isoleucine.
PubMed:11857757
PubMed:11999733
PubMed:12175151
Unimod:695#I
13C(6) 15N(1) Silac label
Label:13C(6)15N(1)
modification from Unimod Isotopic label -
111.04
(13)C 6 H 3 N 1 O 1
111.041595
C 6 (13)C 6 H 15 N 3 O 2
239.14
239.13655
K
artifact
Unimod:364
PSI-MOD
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form
ICPL:13C(6)
MOD:01287
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form - site K
modification from Unimod Isotopic label -
PubMed:11857757
PubMed:15602776
Unimod:364#K
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form
ICPL:13C(6)
OBSOLETE because this is not supported by the literature [PMT]
28.05
C 2 H 4
28.0313
C 8 H 11 N 3 O 1
165.2
165.09021
H
artifact
Unimod:255
PSI-MOD
Acetaldehyde +28
Delta:H(4)C(2)
MOD:01288
acetaldehyde +28 - site H
true
OBSOLETE because this is not supported by the literature [PMT]
Unimod:255#H
Acetaldehyde +28
Delta:H(4)C(2)
OBSOLETE because this is not supported by the literature [PMT]
28.05
C 2 H 4
28.0313
C 8 H 16 N 2 O 1
156.23
156.12627
K
artifact
Unimod:255
PSI-MOD
Acetaldehyde +28
Delta:H(4)C(2)
MOD:01289
acetaldehyde +28 - site K
true
OBSOLETE because this is not supported by the literature [PMT]
Unimod:255#K
Acetaldehyde +28
Delta:H(4)C(2)
OBSOLETE because redundant and identical to MOD:00465. Remap to MOD:00465.
MOD:00465
32.0
O 2
31.989828
C 9 H 9 N 1 O 3
179.17
179.05824
F
artifact
Unimod:425
PSI-MOD
Dioxidation
dihydroxy
MOD:01290
dihydroxylated residue - site F
true
OBSOLETE because redundant and identical to MOD:00465. Remap to MOD:00465.
PubMed:11857757
PubMed:12175151
PubMed:12686488
PubMed:9252331
Unimod:425
Dioxidation
dihydroxy
OBSOLETE because redundant and identical to MOD:00464. Remap to MOD:00464.
MOD:00464
32.0
O 2
31.989828
C 11 H 10 N 2 O 3
218.21
218.06914
W
artifact
Unimod:425
PSI-MOD
Dioxidation
dihydroxy
MOD:01291
dihydroxylated residue - site W
true
OBSOLETE because redundant and identical to MOD:00464. Remap to MOD:00464.
PubMed:12643539
PubMed:12686488
PubMed:6273432
PubMed:9252331
Unimod:425
Dioxidation
dihydroxy
OBSOLETE because redundant and identical to MOD:00075. Map to MOD:00075.
MOD:00075
29.06
C 2 H 5
29.039125
P
natural
Unimod:529
PSI-MOD
Delta:H(5)C(2)
Dimethylation of proline residue
MOD:01292
dimethylation of proline residue
true
OBSOLETE because redundant and identical to MOD:00075. Map to MOD:00075.
Unimod:529
Delta:H(5)C(2)
Dimethylation of proline residue
A protein modification that effectively converts an L-asparagine residue to L-aspartic acid with one (18)O.
2.99
H -1 N -1 (18)O 1
2.988262
C 4 H 5 N 1 (16)O 2 (18)O 1
117.03
117.03119
N
artifact
Unimod:366
oxy18
PSI-MOD
Deamidated:18O(1)
Deamidation in presence of O18
MOD:01293
1x(18)O labeled deamidated L-asparagine
A protein modification that effectively converts an L-asparagine residue to L-aspartic acid with one (18)O.
OMSSA:139
PubMed:8382902
Unimod:366#N
oxy18
Deamidated:18O(1)
Deamidation in presence of O18
OBSOLETE identical and redundant with MOD:00791. Remap to MOD:00791.
MOD:00791
2.99
H -1 N -1 (18)O 1
2.988262
Q
artifact
PSI-MOD
Deamidated:18O(1)
Deamidation in presence of O18
MOD:01294
deamidation in presence of O18 -site Q
true
OBSOLETE identical and redundant with MOD:00791. Remap to MOD:00791.
PubMed:8382902
Deamidated:18O(1)
Deamidation in presence of O18
A protein modification that effectively converts an L-aspartic acid residue to monosodium L-aspartate.
21.98
H -1 Na 1
21.981943
C 4 H 4 N 1 Na 1 O 3
137.07
137.00888
D
artifact
Unimod:30
Na1Asp
PSI-MOD
Cation:Na
Sodium adduct
MOD:01295
monosodium L-aspartate
A protein modification that effectively converts an L-aspartic acid residue to monosodium L-aspartate.
PubMed:12216740
Unimod:30#D
Na1Asp
Cation:Na
Sodium adduct
A protein modification that effectively converts an L-glutamic acid residue to monosodium L-glutamate.
21.98
H -1 Na 1
21.981943
C 5 H 6 N 1 Na 1 O 3
151.1
151.02454
E
artifact
Unimod:30
MSG
Na1Glu
PSI-MOD
Cation:Na
Sodium adduct
MOD:01296
monosodium L-glutamate
A protein modification that effectively converts an L-glutamic acid residue to monosodium L-glutamate.
PubMed:12216740
Unimod:30#E
MSG
Na1Glu
Cation:Na
Sodium adduct
A protein modification that effectively converts an L-proline residue to 5x(13)C labeled L-proline.
5.02
(12)C -5 (13)C 5
5.016774
(13)C 5 H 7 N 1 O 1
102.07
102.069534
P
artifact
Unimod:772
PSI-MOD
13C(5) Silac label
Label:13C(5)
MOD:01297
In PubMed:12716131, fully (13)C labeled proline apparently resulted from the catabolic conversion of (13)C labeled L-arginine during SILAC.
5x(13)C labeled L-proline
A protein modification that effectively converts an L-proline residue to 5x(13)C labeled L-proline.
PubMed:12716131
Unimod:772#P
13C(5) Silac label
Label:13C(5)
A protein modification produced by formation of an adduct of an L-cysteine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4.
158.24
C 9 H 18 O 2
158.13068
C 12 H 23 N 1 O 3 S 1
261.38
261.13986
C
artifact
Unimod:335
PSI-MOD
HNE+Delta:H(2)
reduced 4-Hydroxynonenal
MOD:01298
4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG].
reduced cysteine 4-hydroxynonenal adduct
A protein modification produced by formation of an adduct of an L-cysteine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4.
PubMed:11910026
PubMed:15133838
Unimod:335#C
HNE+Delta:H(2)
reduced 4-Hydroxynonenal
A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4.
158.24
C 9 H 18 O 2
158.13068
C 15 H 30 N 2 O 3
286.42
286.22565
K
artifact
Unimod:335
PSI-MOD
HNE+Delta:H(2)
reduced 4-Hydroxynonenal
MOD:01299
4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG].
reduced lysine 4-hydroxynonenal adduct
A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4.
PubMed:11910026
PubMed:12148805
PubMed:15133838
Unimod:335#K
HNE+Delta:H(2)
reduced 4-Hydroxynonenal
A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4.
158.24
C 9 H 18 O 2
158.13068
C 15 H 25 N 3 O 3
295.38
295.1896
H
artifact
Unimod:335
PSI-MOD
HNE+Delta:H(2)
reduced 4-Hydroxynonenal
MOD:01300
4-hydroxynonenal, a toxic lipid aldehyde, is a product of the hydroperoxide beta-cleavage degradation of omega-6 polyunsaturated fatty acids, such as arachidonic and linoleic acids [JSG].
reduced histidine 4-hydroxynonenal adduct
A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4.
PubMed:11910026
PubMed:12148805
PubMed:15133838
Unimod:335#H
HNE+Delta:H(2)
reduced 4-Hydroxynonenal
A protein modification that effectively converts an L-threonine residue to 2-amino-3-(methylamino)butanoic acid.
13.04
C 1 H 3 N 1 O -1
13.031634
C 5 H 10 N 2 O 1
114.15
114.079315
T
artifact
Unimod:337
PSI-MOD
Methylamine
Michael addition with methylamine
MOD:01301
In PubMed:11743741 phosphothreonine is converted to dehydrobutyrine in base, then by Michael addition of methylamine to 2-amino-3-(methylamino)butanoic acid.
methylamine Michael addition derivatized threonine
A protein modification that effectively converts an L-threonine residue to 2-amino-3-(methylamino)butanoic acid.
PubMed:11743741
Unimod:337#T
Methylamine
Michael addition with methylamine
A protein modification that effectively converts an L-serine residue to 2-amino-3-(methylamino)propanoic acid.
13.04
C 1 H 3 N 1 O -1
13.031634
C 4 H 8 N 2 O 1
100.12
100.06366
S
artifact
Unimod:337
PSI-MOD
Methylamine
Michael addition with methylamine
MOD:01302
In PubMed:11743741 phosphoserine is converted to dehydroalanine in base, then by Michael addition of methylamine to 2-amino-3-(methylamino)propanoic acid.
methylamine Michael addition derivatized serine
A protein modification that effectively converts an L-serine residue to 2-amino-3-(methylamino)propanoic acid.
PubMed:11743741
Unimod:337#S
Methylamine
Michael addition with methylamine
A protein modification that effectively converts an L-asparagine residue to an N4-hexosaminyl-L-asparagine.
161.16
C 6 H 11 N 1 O 4
161.0688
C 10 H 17 N 3 O 6
275.26
275.11172
N
artifact
Unimod:454
PSI-MOD
HexN
Hexosamine
MOD:01303
The natural modifications are N4-(N-acetylamino)galactosyl-L-asparagine (MOD:00832) or N4-(N-acetylamino)glucosyl-L-asparagine (MOD:00831) [JSG].
N4-hexosaminylated asparagine
A protein modification that effectively converts an L-asparagine residue to an N4-hexosaminyl-L-asparagine.
PubMed:11467524
Unimod:454#N
HexN
Hexosamine
A protein modification that effectively converts an L-lysine residue to an N4-hexosaminyl-L-lysine, as a synthetic peptide protectting group.
161.16
C 6 H 11 N 1 O 4
161.0688
C 12 H 23 N 3 O 5
289.33
289.16376
K
artifact
Unimod:454
PSI-MOD
HexN
Hexosamine
MOD:01304
N6-hexosaminylated lysine
A protein modification that effectively converts an L-lysine residue to an N4-hexosaminyl-L-lysine, as a synthetic peptide protectting group.
Unimod:454#K
HexN
Hexosamine
A protein modification that effectively converts an L-tryptophan residue to N1'-hexosaminyl-L-tryptophan.
161.16
C 6 H 11 N 1 O 4
161.0688
C 17 H 21 N 3 O 5
347.37
347.14813
W
artifact
Unimod:454
PSI-MOD
HexN
Hexosamine
MOD:01305
The natural modification is N1'-mannosyl-L-tryptophan (MOD:00165) [JSG].
N1'-hexosaminylated tryptophan
A protein modification that effectively converts an L-tryptophan residue to N1'-hexosaminyl-L-tryptophan.
Unimod:454#W
HexN
Hexosamine
A protein modification that effectively converts an L-threonine residue to O-hexosaminyl-L-threonine.
161.16
C 6 H 11 N 1 O 4
161.0688
C 10 H 18 N 2 O 6
262.26
262.1165
T
natural
Unimod:454
PSI-MOD
HexN
Hexosamine
MOD:01306
The natural modifications are O-(N-acetylaminogalactosyl)-L-threonine (MOD:00164) or O-(N-acetylaminoglucosyl)-L-threonine (MOD:00806) [JSG].
O-hexosaminylated threonine
A protein modification that effectively converts an L-threonine residue to O-hexosaminyl-L-threonine.
Unimod:454#T
HexN
Hexosamine
modification from Unimod Chemical derivative -
525.66
C 19 H 34 N 4 O 5 P 1 S 3
525.1429
C 22 H 39 N 5 O 7 P 1 S 3
612.74
612.1749
S
artifact
Unimod:332
PSI-MOD
Thiophos-S-S-biotin
thiophosphate labeled with biotin-HPDP
MOD:01307
thiophosphate labeled with biotin-HPDP -site S
modification from Unimod Chemical derivative -
Unimod:332#S
Thiophos-S-S-biotin
thiophosphate labeled with biotin-HPDP
modification from Unimod Chemical derivative -
525.66
C 19 H 34 N 4 O 5 P 1 S 3
525.1429
C 23 H 41 N 5 O 7 P 1 S 3
626.76
626.19055
T
artifact
Unimod:332
PSI-MOD
Thiophos-S-S-biotin
thiophosphate labeled with biotin-HPDP
MOD:01308
thiophosphate labeled with biotin-HPDP -site T
modification from Unimod Chemical derivative -
Unimod:332#T
Thiophos-S-S-biotin
thiophosphate labeled with biotin-HPDP
modification from Unimod Chemical derivative -
525.66
C 19 H 34 N 4 O 5 P 1 S 3
525.1429
C 28 H 43 N 5 O 7 P 1 S 3
688.83
688.20624
Y
artifact
Unimod:332
PSI-MOD
Thiophos-S-S-biotin
thiophosphate labeled with biotin-HPDP
MOD:01309
thiophosphate labeled with biotin-HPDP - site Y
modification from Unimod Chemical derivative -
Unimod:332#Y
Thiophos-S-S-biotin
thiophosphate labeled with biotin-HPDP
A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent light form group.
59.07
C 3 (1)H 9 N 1
59.073498
C 9 (1)H 21 N 3 O 1
187.17
187.16846
K
artifact
Unimod:60
PSI-MOD
GIST-Quat
Quaternary amine labeling reagent light form (N-term & K)
MOD:01310
quaternary amine labeling reagent light form N6-L-lysine
A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent light form group.
PubMed:11857757
Unimod:60#K
GIST-Quat
Quaternary amine labeling reagent light form (N-term & K)
A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+3amu) form group.
62.09
C 3 (1)H 6 (2)H 3 N 1
62.09233
C 9 (1)H 18 (2)H 3 N 3 O 1
190.19
190.18729
K
artifact
Unimod:61
PSI-MOD
GIST-Quat:2H(3)
Quaternary amine labeling reagent heavy (+3amu) form, N-term & K
MOD:01311
quaternary amine labeling reagent heavy form (+3amu) N6-L-lysine
A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+3amu) form group.
PubMed:11698400
PubMed:11857757
PubMed:11914093
Unimod:61#K
GIST-Quat:2H(3)
Quaternary amine labeling reagent heavy (+3amu) form, N-term & K
A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+6amu) form group.
65.11
C 3 (1)H 3 (2)H 6 N 1
65.11116
C 9 (1)H 15 (2)H 6 N 3 O 1
193.21
193.20612
K
artifact
Unimod:62
PSI-MOD
GIST-Quat:2H(6)
Quaternary amine labeling reagent heavy form (+6amu), N-term & K
MOD:01312
Apparently incorrect parent [JSG].
quaternary amine labeling reagent heavy form (+6amu) N6-L-lysine
A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+6amu) form group.
PubMed:11857757
Unimod:62#K
GIST-Quat:2H(6)
Quaternary amine labeling reagent heavy form (+6amu), N-term & K
A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+9amu) form group.
68.13
C 3 (2)H 9 N 1
68.12999
C 9 (1)H 12 (2)H 9 N 3 O 1
196.22
196.22496
K
artifact
Unimod:63
PSI-MOD
GIST-Quat:2H(9)
Quaternary amine labeling reagent heavy form (+9amu), N-term & K
MOD:01313
quaternary amine labeling reagent heavy form (+9amu) N6-L-lysine
A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+9amu) form group.
PubMed:11857757
Unimod:63#K
GIST-Quat:2H(9)
Quaternary amine labeling reagent heavy form (+9amu), N-term & K
A protein modification that effectively converts an L-lysine residue to 4x(1)H,4x(12)C-labeled N6-succinyl-L-lysine.
100.02
(12)C 4 (1)H 4 O 3
100.016045
(12)C 10 H 16 N 2 O 4
228.11
228.11101
K
artifact
Unimod:64
PSI-MOD
Succinic anhydride labeling reagent light form (K)
Succinyl
MOD:01314
4x(1)H,4x(12)C-labeled N6-succinyl-L-lysine
A protein modification that effectively converts an L-lysine residue to 4x(1)H,4x(12)C-labeled N6-succinyl-L-lysine.
PubMed:11857757
PubMed:12175151
PubMed:12716131
Unimod:64#K
Succinic anhydride labeling reagent light form (K)
Succinyl
A protein modification that effectively converts an L-lysine residue to 4x(2)H-labeled N6-succinyl-L-lysine.
104.04
C 4 (2)H 4 O 3
104.04115
C 10 (1)H 12 (2)H 4 N 2 O 4
232.14
232.13611
K
artifact
Unimod:65
PSI-MOD
Succinic anhydride labeling reagent, heavy form (+4amu, 4H2), N-term & K
Succinyl:2H(4)
MOD:01315
4x(2)H labeled N6-succinyl-L-lysine
A protein modification that effectively converts an L-lysine residue to 4x(2)H-labeled N6-succinyl-L-lysine.
PubMed:11344537
PubMed:11857757
PubMed:12175151
PubMed:15189151
Unimod:65#K
Succinic anhydride labeling reagent, heavy form (+4amu, 4H2), N-term & K
Succinyl:2H(4)
A protein modification that effectively converts an L-lysine residue to 4x(13)C labeled N6-succinyl-L-lysine.
104.03
(13)C 4 H 4 O 3
104.029465
(12)C 6 (13)C 4 H 16 N 2 O 4
232.12
232.12442
K
artifact
Unimod:66
PSI-MOD
Succinic anhydride labeling reagent, heavy form (+4amu, 4C13), K
Succinyl:13C(4)
MOD:01316
4x(13)C labeled N6-succinyl-L-lysine
A protein modification that effectively converts an L-lysine residue to 4x(13)C labeled N6-succinyl-L-lysine.
PubMed:11344537
PubMed:11857757
PubMed:12175151
PubMed:15189151
Unimod:66#K
Succinic anhydride labeling reagent, heavy form (+4amu, 4C13), K
Succinyl:13C(4)
modification from Unimod Chemical derivative -
87.18
C 4 H 9 N 1 O -1 S 1
87.05066
C 8 H 16 N 2 O 1 S 1
188.29
188.09833
T
artifact
Unimod:178
PSI-MOD
DAET
phosphorylation to amine thiol
MOD:01317
phosphorylation to amine thiol - site T
modification from Unimod Chemical derivative -
PubMed:12216740
Unimod:178#T
DAET
phosphorylation to amine thiol
modification from Unimod Chemical derivative -
87.18
C 4 H 9 N 1 O -1 S 1
87.05066
C 7 H 14 N 2 O 1 S 1
174.26
174.08269
S
artifact
Unimod:178
PSI-MOD
DAET
phosphorylation to amine thiol
MOD:01318
phosphorylation to amine thiol - site S
modification from Unimod Chemical derivative -
PubMed:11510821
PubMed:12216740
PubMed:12422359
Unimod:178#S
DAET
phosphorylation to amine thiol
modification from Unimod Other
218.34
C 15 H 22 O 1
218.16707
C 21 H 29 N 3 O 2
355.48
355.22598
H
artifact
Unimod:176
PSI-MOD
BHT
Michael addition of BHT quinone methide to Cysteine and Lysine
MOD:01319
Secondary adduct, much less common than cysteine. [Unimod]
Michael addition of BHT quinone methide to histidine
modification from Unimod Other
PubMed:11510821
PubMed:12422359
PubMed:9448752
Unimod:176#H
BHT
Michael addition of BHT quinone methide to Cysteine and Lysine
modification from Unimod Other
218.34
C 15 H 22 O 1
218.16707
C 21 H 34 N 2 O 2
346.51
346.26202
K
artifact
Unimod:176
PSI-MOD
BHT
Michael addition of BHT quinone methide to Cysteine and Lysine
MOD:01320
Secondary adduct, much less common than cysteine. [Unimod]
Michael addition of BHT quinone methide to lysine
modification from Unimod Other
PubMed:16078144
PubMed:9448752
Unimod:176#K
BHT
Michael addition of BHT quinone methide to Cysteine and Lysine
modification from Unimod Other
218.34
C 15 H 22 O 1
218.16707
C 18 H 27 N 1 O 2 S 1
321.48
321.17624
C
artifact
Unimod:176
PSI-MOD
BHT
Michael addition of BHT quinone methide to Cysteine and Lysine
MOD:01321
Primary adduct formed. [Unimod]
Michael addition of BHT quinone methide to cysteine
modification from Unimod Other
PubMed:11510821
PubMed:12422359
PubMed:9448752
Unimod:176#C
BHT
Michael addition of BHT quinone methide to Cysteine and Lysine
OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other -
40.06
C 3 H 4
40.0313
C 9 H 16 N 2 O 1
168.24
168.12627
K
artifact
Unimod:256
PSI-MOD
Delta:H(4)C(3)
Propionaldehyde +40
MOD:01322
propionaldehyde +40 - site K
true
OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other -
PubMed:15549660
Unimod:256#K
Delta:H(4)C(3)
Propionaldehyde +40
OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other -
40.06
C 3 H 4
40.0313
C 9 H 11 N 3 O 1
177.21
177.09021
H
artifact
Unimod:256
PSI-MOD
Delta:H(4)C(3)
Propionaldehyde +40
MOD:01323
propionaldehyde +40 - site H
true
OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other -
Unimod:256#H
Delta:H(4)C(3)
Propionaldehyde +40
OBSOLETE because this is not supported by the linked literature [PMT]
26.04
C 2 H 2
26.01565
C 8 H 9 N 3 O 1
163.18
163.07455
H
artifact
Unimod:254
PSI-MOD
Acetaldehyde +26
Delta:H(2)C(2)
MOD:01324
acetaldehyde +26 - site H
true
OBSOLETE because this is not supported by the linked literature [PMT]
PubMed:7744761
Unimod:254#H
Acetaldehyde +26
Delta:H(2)C(2)
OBSOLETE because this is not supported by the linked literature [PMT]
26.04
C 2 H 2
26.01565
C 8 H 14 N 2 O 1
154.21
154.11061
K
artifact
Unimod:254
PSI-MOD
Acetaldehyde +26
Delta:H(2)C(2)
MOD:01325
acetaldehyde +26 - site K
true
OBSOLETE because this is not supported by the linked literature [PMT]
PubMed:7744761
Unimod:254#K
Acetaldehyde +26
Delta:H(2)C(2)
A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-tyrosine.
9.03
(12)C -9 (13)C 9
9.030194
(13)C 9 H 9 N 1 O 2
172.09
172.09352
Y
artifact
Unimod:184
PSI-MOD
13C(9) Silac label
Label:13C(9)
MOD:01326
9x(13)C labeled L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-tyrosine.
PubMed:11510821
PubMed:12422359
PubMed:12716131
Unimod:184#Y
13C(9) Silac label
Label:13C(9)
A protein modification that effectively converts an L-phenylalanine residue to 9x(13)C labeled L-phenylalanine.
9.03
(12)C -9 (13)C 9
9.030194
(13)C 9 H 9 N 1 O 1
156.1
156.0986
F
artifact
Unimod:184
PSI-MOD
13C(9) Silac label
Label:13C(9)
MOD:01327
9x(13)C labeled L-phenylalanine
A protein modification that effectively converts an L-phenylalanine residue to 9x(13)C labeled L-phenylalanine.
PubMed:12716131
Unimod:184#F
13C(9) Silac label
Label:13C(9)
modification from Unimod Chemical derivative - hydroxylethanone
58.04
C 2 H 2 O 2
58.005478
C 13 H 12 N 2 O 3
244.25
244.0848
W
artifact
Unimod:6
PSI-MOD
Carboxymethyl
Iodoacetic acid derivative
MOD:01328
There is no citation for this Unimod entry. Iodoacetic acid derivatization of tryptophan is not mentioned in the citation [JSG].
iodoacetic acid - site W
modification from Unimod Chemical derivative - hydroxylethanone
PubMed:17525468
Unimod:6#W
Carboxymethyl
Iodoacetic acid derivative
OBSOLETE because duplicate and redundant with MOD:01061. Remap to MOD:01061
MOD:01061
58.04
C 2 H 2 O 2
58.005478
C
artifact
Unimod:6
PSI-MOD
Carboxymethyl
Iodoacetic acid derivative
MOD:01329
Modification from Unimod Chemical derivative, Unimod:6 site C
iodoacetic acid - site C
true
OBSOLETE because duplicate and redundant with MOD:01061. Remap to MOD:01061
DeltaMass:197
Carboxymethyl
Iodoacetic acid derivative
OBSOLETE because identical with MOD:01094. Remap to MOD:01094
MOD:01094
58.04
C 2 H 2 O 2
58.005478
K
artifact
Unimod:6
PSI-MOD
Carboxymethyl
Iodoacetic acid derivative
MOD:01330
a modification from Unimod:6
iodoacetic acid -site K
true
OBSOLETE because identical with MOD:01094. Remap to MOD:01094
PubMed:18688235
Carboxymethyl
Iodoacetic acid derivative
A protein modification that effectively converts an L-arginine residue to 6x(13)C labeled L-arginine.
6.02
(12)C -6 (13)C 6
6.020129
(13)C 6 H 12 N 4 O 1
162.12
162.12125
R
artifact
Unimod:188
arg-13c6
PSI-MOD
13C(6) Silac label
Label:13C(6)
MOD:01331
6x(13)C labeled L-arginine
A protein modification that effectively converts an L-arginine residue to 6x(13)C labeled L-arginine.
OMSSA:136
PubMed:12716131
Unimod:188#R
arg-13c6
13C(6) Silac label
Label:13C(6)
A protein modification that effectively converts an L-leucine residue to 6x(13)C labeled L-leucine.
6.02
(12)C -6 (13)C 6
6.020129
(13)C 6 H 11 N 1 O 1
119.1
119.104195
L
artifact
Unimod:188
PSI-MOD
13C(6) Silac label
Label:13C(6)
MOD:01332
6x(13)C labeled L-leucine
A protein modification that effectively converts an L-leucine residue to 6x(13)C labeled L-leucine.
PubMed:12716131
Unimod:188#L
13C(6) Silac label
Label:13C(6)
A protein modification that effectively converts an L-isoleucine residue to 6x(13)C labeled L-isoleucine.
6.02
(12)C -6 (13)C 6
6.020129
(13)C 6 H 11 N 1 O 1
119.1
119.104195
I
artifact
Unimod:188
PSI-MOD
13C(6) Silac label
Label:13C(6)
MOD:01333
6x(13)C labeled L-isoleucine
A protein modification that effectively converts an L-isoleucine residue to 6x(13)C labeled L-isoleucine.
PubMed:12716131
PubMed:12766232
Unimod:188#I
13C(6) Silac label
Label:13C(6)
A protein modification that effectively converts an L-lysine residue to 6x(13)C labeled L-lysine.
6.02
(12)C -6 (13)C 6
6.020129
(13)C 6 H 12 N 2 O 1
134.12
134.1151
K
artifact
Unimod:188
lys-13c6
PSI-MOD
13C(6) Silac label
Label:13C(6)
MOD:01334
6x(13)C labeled L-lysine
A protein modification that effectively converts an L-lysine residue to 6x(13)C labeled L-lysine.
OMSSA:138
PubMed:11857757
PubMed:11999733
PubMed:12175151
PubMed:12716131
Unimod:188#K
lys-13c6
13C(6) Silac label
Label:13C(6)
modification from Unimod Chemical derivative -
220.99
(12)C 1 (13)C 6 H 5 N 1 O 3 S 2
220.99121
(12)C 7 (13)C 6 H 17 N 3 O 4 S 2
349.09
349.08618
K
artifact
Unimod:464
PSI-MOD
4-sulfophenyl isothiocyanate (Heavy C13)
SPITC:13C(6)
MOD:01335
6x(13)C labeled 4-sulfophenyl isothiocyanate derivatized lysine
modification from Unimod Chemical derivative -
PubMed:11467524
PubMed:16526082
Unimod:464#K
4-sulfophenyl isothiocyanate (Heavy C13)
SPITC:13C(6)
OBSOLETE - identical and redundant with MOD:00657. Remap to MOD:00657.
MOD:00657
15.01
C 1 H 1 N -1 O 1
14.999666
Q
natural
Unimod:528
PSI-MOD
Deamidation followed by a methylation
Methyl+Deamidated
MOD:01336
Modification from Unimod Post-translational - Unimod:528.
deamidation followed by a methylation -site Q
true
OBSOLETE - identical and redundant with MOD:00657. Remap to MOD:00657.
PubMed:18688235
Deamidation followed by a methylation
Methyl+Deamidated
A protein modification that effectively converts an L-asparagine residue to L-aspartate 4-methyl ester.
15.01
C 1 H 1 N -1 O 1
14.999666
C 5 H 7 N 1 O 3
129.12
129.04259
N
artifact
Unimod:528
PSI-MOD
Deamidation followed by a methylation
Methyl+Deamidated
MOD:01337
The deamidation and methylation of L-asparagine has not been reported as a natural modification. It is extremely unlikely that eukaryotes produce this modification, because a natural process that would form L-aspartic acid 4-methyl ester from either L-aspartic acid or L-asparagine would interfere with the D-aspartyl peptide repair mechanism [JSG].
deamidated 4-methyl esterified asparagine
A protein modification that effectively converts an L-asparagine residue to L-aspartate 4-methyl ester.
Unimod:528#N
Deamidation followed by a methylation
Methyl+Deamidated
A protein modification that effectively converts an L-lysine residue to N6-ethyl-L-lysine.
28.05
C 2 H 4
28.0313
C 8 H 16 N 2 O 1
156.23
156.12627
K
hypothetical
Unimod:280
PSI-MOD
Ethyl
Ethylation
MOD:01338
The Unimod citation refers to the formation of glutamate ethyl ester and not to either lysine or N-terminal alkylation [JSG].
N6-ethyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-ethyl-L-lysine.
PubMed:9629898
Unimod:280#K
Ethyl
Ethylation
A protein modification that effectively replaces a hydrogen atom with an ethyl group.
28.05
C 2 H 4
28.0313
X
artifact
Unimod:280
EtRes
PSI-MOD
Ethyl
Ethylation
MOD:01339
From DeltaMass: Average Mass: 28 with no citation. The Unimod citation refers to the formation of glutamate ethyl ester and not to either lysine or N-terminal alkylation [JSG].
ethylated residue
A protein modification that effectively replaces a hydrogen atom with an ethyl group.
PubMed:9629898
Unimod:280
EtRes
Ethyl
Ethylation
modification from Unimod Isotopic label -
348.24
C 16 (1)H 16 (2)H 10 N 4 O 2 S 1
348.24042
C 22 (1)H 28 (2)H 10 N 6 O 3 S 1
476.34
476.3354
K
artifact
Unimod:91
PSI-MOD
ESP-Tag heavy d10
ESP:2H(10)
MOD:01340
ESP-Tag heavy d10 - site K
modification from Unimod Isotopic label -
PubMed:11078590
PubMed:11085420
PubMed:11821862
Unimod:91#K
ESP-Tag heavy d10
ESP:2H(10)
modification from Unimod Isotopic label -
338.47
C 16 H 26 N 4 O 2 S 1
338.17764
C 22 H 38 N 6 O 3 S 1
466.64
466.2726
K
artifact
Unimod:90
PSI-MOD
ESP
ESP-Tag light d0
MOD:01341
ESP-Tag light d0 - site K
modification from Unimod Isotopic label -
Unimod:90#K
ESP
ESP-Tag light d0
OBSOLETE because redundant and identical to MOD:00530. Remap to MOD:00530.
MOD:00530
46.91
S -1 Se 1
47.94445
C 5 H 9 N 1 O 1 S 0 Se 1
178.1
178.98494
M
artifact
Unimod:162
PSI-MOD
Delta:S(-1)Se(1)
Selenium replaces sulphur
MOD:01342
selenium substitution for sulfur - site M
true
OBSOLETE because redundant and identical to MOD:00530. Remap to MOD:00530.
PubMed:12148805
Unimod:162
Delta:S(-1)Se(1)
Selenium replaces sulphur
OBSOLETE because redundant and identical to MOD:00686. Remap to MOD:00686.
MOD:00686
46.91
S -1 Se 1
47.94445
C 3 H 5 N 1 O 1 S 0 Se 1
150.05
150.95363
C
artifact
Unimod:162
PSI-MOD
Delta:S(-1)Se(1)
Selenium replaces sulphur
MOD:01343
selenium substitution for sulfur - site C
true
OBSOLETE because redundant and identical to MOD:00686. Remap to MOD:00686.
PubMed:12148805
Unimod:162
Delta:S(-1)Se(1)
Selenium replaces sulphur
OBSOLETE because redundant and identical with MOD:00835. Remap to MOD:00835.
MOD:00835
-2.02
H -2
-2.01565
S
natural
Unimod:401
PSI-MOD
2-amino-3-oxo-butanoic_acid
Didehydro
MOD:01344
dehydrogenated residue - site S
true
OBSOLETE because redundant and identical with MOD:00835. Remap to MOD:00835.
PubMed:9252331
PubMed:9276974
Unimod:401
2-amino-3-oxo-butanoic_acid
Didehydro
A protein modification that effectively converts an L-threonine residue to 2-amino-3-oxobutanoic acid.
-2.02
H -2
-2.01565
C 4 H 5 N 1 O 2
99.09
99.03203
T
artifact
Unimod:401
2-amino-3-ketobutyric acid
3-ketobutyrine
twoamino3oxobutanoicacid
PSI-MOD
2-amino-3-oxo-butanoic_acid
Didehydro
MOD:01345
There is no citation for this modification in the Unimod entry. Although mentioned in PubMed:9252331, there is no citation for it there [JSG].
2-amino-3-oxobutanoic acid
A protein modification that effectively converts an L-threonine residue to 2-amino-3-oxobutanoic acid.
OMSSA:23
PubMed:12716131
PubMed:9252331
Unimod:401#T
2-amino-3-ketobutyric acid
3-ketobutyrine
twoamino3oxobutanoicacid
2-amino-3-oxo-butanoic_acid
Didehydro
A protein modification that effectively converts an L-asparagine residue to an N4-hexosyl-L-asparagine.
162.14
C 6 H 10 O 5
162.05283
C 10 H 16 N 2 O 7
276.25
276.09576
N
natural
Unimod:41
PSI-MOD
Hex
Hexose
MOD:01346
N4-hexosylated asparagine
A protein modification that effectively converts an L-asparagine residue to an N4-hexosyl-L-asparagine.
PubMed:11112526
PubMed:11567090
PubMed:15279557
PubMed:6540775
Unimod:41#N
Hex
Hexose
A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and an L-lysine residue to form a Schiff-base or an Amadori ketosamine lysine adduct.
162.14
C 6 H 10 O 5
162.05283
C 12 H 22 N 2 O 6
290.32
290.1478
K
natural
Unimod:41
PSI-MOD
Hex
Hexose
MOD:01347
hexose glycated L-lysine
A modification produced in a non-enzymatic reaction between a carbohydrate carbonyl group (C1 of aldohexose or C2 of fructose) and an L-lysine residue to form a Schiff-base or an Amadori ketosamine lysine adduct.
DeltaMass:0
PubMed:15279557
Unimod:41#K
Hex
Hexose
A protein modification that effectively converts an L-threonine residue to an O-hexosyl-L-threonine.
162.14
C 6 H 10 O 5
162.05283
C 10 H 17 N 1 O 7
263.25
263.1005
T
natural
Unimod:41
PSI-MOD
Hex
Hexose
MOD:01348
O-hexosylated threonine
A protein modification that effectively converts an L-threonine residue to an O-hexosyl-L-threonine.
PubMed:15279557
PubMed:8597590
Unimod:41#T
Hex
Hexose
modification from Unimod Chemical derivative -
143.14
C 6 H 9 N 1 O 3
143.05824
C 9 H 14 N 2 O 4 S 1
246.28
246.06743
C
artifact
Unimod:320
PSI-MOD
Nethylmaleimide+water
Nethylmaleimidehydrolysis
MOD:01349
Hydolyzed N-ethylmaeimide adduct, a mixture of isobaric 2- and 3-(S-cysteinyl)-4-(ethylamino)-4-oxobutanoic acid [JSG].
hydrolyzed N-ethylmaleimide cysteine adduct
modification from Unimod Chemical derivative -
Unimod:320#C
Nethylmaleimide+water
Nethylmaleimidehydrolysis
modification from Unimod Chemical derivative -
143.14
C 6 H 9 N 1 O 3
143.05824
C 12 H 21 N 3 O 4
271.32
271.1532
K
artifact
Unimod:320
PSI-MOD
Nethylmaleimide+water
Nethylmaleimidehydrolysis
MOD:01350
Hydolyzed N-ethylmaeimide adduct, a mixture of isobaric 2- and 3-(N6-lysyl)-4-(ethylamino)-4-oxobutanoic acid [JSG].
hydrolyzed N-ethylmaleimide lysine adduct
modification from Unimod Chemical derivative -
Unimod:320#K
Nethylmaleimide+water
Nethylmaleimidehydrolysis
A protein modification that effectively converts an L-tryptophan residue to a nitrated L-tryptophan.
45.0
H -1 N 1 O 2
44.985077
C 11 H 9 N 3 O 3
231.21
231.06439
W
artifact
Unimod:354
nitrow
PSI-MOD
Nitro
Oxidation to nitro
MOD:01351
One or more isobaric isomers are produced by nitration with peroxynitrite reagent [JSG].
nitrated L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to a nitrated L-tryptophan.
OMSSA:85
PubMed:8839040
PubMed:9252331
Unimod:354#W
nitrow
Nitro
Oxidation to nitro
A protein modification that effectively converts an L-tyrosine residue to a nitrated L-tyrosine.
45.0
H -1 N 1 O 2
44.985077
C 9 H 8 N 2 O 4
208.17
208.0484
Y
artifact
Unimod:354
uniprot.ptm:PTM-0213
nitroy
PSI-MOD
Nitro
Oxidation to nitro
MOD:01352
One or more isobaric isomers are produced by nitration with peroxynitrite reagent [JSG].
nitrated L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to a nitrated L-tyrosine.
OMSSA:86
PubMed:14678012
PubMed:8839040
PubMed:9252331
Unimod:354#Y
nitroy
Nitro
Oxidation to nitro
modification from Unimod Chemical derivative -
41.05
C 2 H 3 N 1
41.02655
C 8 H 15 N 3 O 1
169.23
169.1215
K
artifact
Unimod:141
PSI-MOD
Amidine
amidination of lysines or N-terminal amines with methyl acetimidate
MOD:01353
amidination of lysines or N-terminal amines with methyl acetimidate - site K
modification from Unimod Chemical derivative -
PubMed:12643539
PubMed:15602776
PubMed:6273432
Unimod:141#K
Amidine
amidination of lysines or N-terminal amines with methyl acetimidate
A protein modification that effectively replaces an N4 hydrogen atom of an asparagine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond.
657.6
C 25 H 41 N 2 O 18
657.2354
C 29 H 47 N 4 O 20
771.7
771.2784
N
natural
Unimod:149
PSI-MOD
Hex(1)HexNAc(1)NeuAc(1)
Hex1HexNAc1NeuAc1
MOD:01354
Hex1HexNAc1NeuAc1 N4-glycosylated asparagine
A protein modification that effectively replaces an N4 hydrogen atom of an asparagine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond.
PubMed:11698400
Unimod:149#N
Hex(1)HexNAc(1)NeuAc(1)
Hex1HexNAc1NeuAc1
A protein modification that effectively replaces an O3 hydrogen atom of a threonine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond.
657.6
C 25 H 41 N 2 O 18
657.2354
C 29 H 48 N 3 O 20
758.7
758.28314
T
natural
Unimod:149
PSI-MOD
Hex(1)HexNAc(1)NeuAc(1)
Hex1HexNAc1NeuAc1
MOD:01355
Hex1HexNAc1NeuAc1 O-glycosylated threonine
A protein modification that effectively replaces an O3 hydrogen atom of a threonine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond.
Unimod:149#T
Hex(1)HexNAc(1)NeuAc(1)
Hex1HexNAc1NeuAc1
A protein modification that effectively replaces an O3 hydrogen atom of a serine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond.
657.6
C 25 H 41 N 2 O 18
657.2354
C 28 H 46 N 3 O 20
744.68
744.26746
S
natural
Unimod:149
PSI-MOD
Hex(1)HexNAc(1)NeuAc(1)
Hex1HexNAc1NeuAc1
MOD:01356
Hex1HexNAc1NeuAc1 O-glycosylated serine
A protein modification that effectively replaces an O3 hydrogen atom of a serine residue with a carbohydrate-like group composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond.
PubMed:7856876
Unimod:149#S
Hex(1)HexNAc(1)NeuAc(1)
Hex1HexNAc1NeuAc1
A protein modification that effectively replaces two hydrogen atoms of an L-lysine residue containing common isotopes with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated L-lysine.
34.06
(13)C 2 (2)H 4
34.063118
(12)C 6 (13)C 2 (1)H 12 (2)H 4 N 2 O 1
162.16
162.15808
K
artifact
Unimod:510
PSI-MOD
DiMethyl-C13HD2
Dimethyl:2H(4)13C(2)
MOD:01357
2x(13)C,4x(2)H labeled dimethylated L-lysine
A protein modification that effectively replaces two hydrogen atoms of an L-lysine residue containing common isotopes with two (13)C,3x(2)H labeled methyl groups to form a 2x(13)C,6x(2)H labeled dimethylated L-lysine.
PubMed:12686488
PubMed:16335955
Unimod:510#K
DiMethyl-C13HD2
Dimethyl:2H(4)13C(2)
modification from Unimod Isotopic label - Use when labelling post-digest
109.05
C 6 (1)H -1 (2)H 4 N 1 O 1
109.04657
X
artifact
N-term
Unimod:687
PSI-MOD
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form
ICPL:2H(4)
MOD:01358
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form - site N-term
modification from Unimod Isotopic label - Use when labelling post-digest
PubMed:15602776
Unimod:687#N-term
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form
ICPL:2H(4)
modification from Unimod Isotopic label - Use when labelling post-digest
109.05
C 6 (1)H -1 (2)H 4 N 1 O 1
109.04657
C 12 (1)H 11 (2)H 4 N 3 O 2
237.14
237.14154
K
artifact
Unimod:687
PSI-MOD
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form
ICPL:2H(4)
MOD:01359
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form - site K
modification from Unimod Isotopic label - Use when labelling post-digest
PubMed:15602776
Unimod:687#K
Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form
ICPL:2H(4)
A protein modification that effectively converts an L-lysine residue to the 4-sulfophenyl isothiocyanate adduct, N6-[(4-sulfophenyl)carbamothioyl]lysine.
215.24
C 7 H 5 N 1 O 3 S 2
214.97108
C 13 H 17 N 3 O 4 S 2
343.42
343.06604
K
artifact
Unimod:261
N6-[(4-sulfophenyl)carbamothioyl]lysine
PSI-MOD
4-sulfophenyl isothiocyanate
SPITC
MOD:01360
4-sulfophenyl isothiocyanate N6-derivatized lysine
A protein modification that effectively converts an L-lysine residue to the 4-sulfophenyl isothiocyanate adduct, N6-[(4-sulfophenyl)carbamothioyl]lysine.
PubMed:14689565
PubMed:14745769
PubMed:15549660
PubMed:16526082
Unimod:261#K
N6-[(4-sulfophenyl)carbamothioyl]lysine
4-sulfophenyl isothiocyanate
SPITC
A protein modification that effectively converts an L-threonine residue to O-thiophospho-L-threonine.
96.04
H 1 O 2 P 1 S 1
95.94349
C 4 H 8 N 1 O 4 P 1 S 1
197.14
196.99117
T
artifact
Unimod:260
PSI-MOD
Thiophospho
Thiophosphorylation
MOD:01361
O-thiophospho-L-threonine
A protein modification that effectively converts an L-threonine residue to O-thiophospho-L-threonine.
PubMed:11507762
PubMed:12110917
Unimod:260#T
Thiophospho
Thiophosphorylation
A protein modification that effectively converts an L-serine residue to O-thiophospho-L-serine.
96.04
H 1 O 2 P 1 S 1
95.94349
C 3 H 6 N 1 O 4 P 1 S 1
183.12
182.97551
S
artifact
Unimod:260
PSI-MOD
Thiophospho
Thiophosphorylation
MOD:01362
O-thiophospho-L-serine
A protein modification that effectively converts an L-serine residue to O-thiophospho-L-serine.
PubMed:11507762
PubMed:12110917
Unimod:260#S
Thiophospho
Thiophosphorylation
A protein modification that effectively converts an L-tyrosine residue to O4'-thiophospho-L-tyrosine.
96.04
H 1 O 2 P 1 S 1
95.94349
C 9 H 10 N 1 O 4 P 1 S 1
259.22
259.0068
Y
artifact
Unimod:260
PSI-MOD
Thiophospho
Thiophosphorylation
MOD:01363
O4'-thiophospho-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to O4'-thiophospho-L-tyrosine.
PubMed:12110917
PubMed:15549660
Unimod:260#Y
Thiophospho
Thiophosphorylation
modification from Unimod Chemical derivative -
421.43
C 21 H 15 N 3 O 5 S 1
421.07324
C 24 H 20 N 4 O 7 S 1
508.51
508.10526
S
artifact
Unimod:478
PSI-MOD
FTC
fluorescein-5-thiosemicarbazide
MOD:01364
fluorescein-5-thiosemicarbazide - site S
modification from Unimod Chemical derivative -
PubMed:11467524
Unimod:478#S
FTC
fluorescein-5-thiosemicarbazide
modification from Unimod Chemical derivative -
421.43
C 21 H 15 N 3 O 5 S 1
421.07324
C 24 H 20 N 4 O 6 S 2
524.57
524.0824
C
artifact
Unimod:478
PSI-MOD
FTC
fluorescein-5-thiosemicarbazide
MOD:01365
fluorescein-5-thiosemicarbazide - site C
modification from Unimod Chemical derivative -
Unimod:478#C
FTC
fluorescein-5-thiosemicarbazide
modification from Unimod Chemical derivative -
421.43
C 21 H 15 N 3 O 5 S 1
421.07324
C 27 H 27 N 5 O 6 S 1
549.6
549.1682
K
artifact
Unimod:478
PSI-MOD
FTC
fluorescein-5-thiosemicarbazide
MOD:01366
fluorescein-5-thiosemicarbazide - site K
modification from Unimod Chemical derivative -
Unimod:478#K
FTC
fluorescein-5-thiosemicarbazide
modification from Unimod Chemical derivative -
421.43
C 21 H 15 N 3 O 5 S 1
421.07324
C 26 H 22 N 4 O 6 S 1
518.54
518.126
P
artifact
Unimod:478
PSI-MOD
FTC
fluorescein-5-thiosemicarbazide
MOD:01367
fluorescein-5-thiosemicarbazide - site P
modification from Unimod Chemical derivative -
Unimod:478#P
FTC
fluorescein-5-thiosemicarbazide
modification from Unimod Chemical derivative -
421.43
C 21 H 15 N 3 O 5 S 1
421.07324
C 27 H 27 N 7 O 6 S 1
577.62
577.1744
R
artifact
Unimod:478
PSI-MOD
FTC
fluorescein-5-thiosemicarbazide
MOD:01368
fluorescein-5-thiosemicarbazide - site R
modification from Unimod Chemical derivative -
PubMed:15525938
Unimod:478#R
FTC
fluorescein-5-thiosemicarbazide
A protein modification that effectively replaces a carboxamido group with a carboxyl methyl ester group.
15.01
C 1 H 1 N -1 O 1
14.999666
X
Unimod:528
PSI-MOD
Deamidation followed by a methylation
Methyl+Deamidated
MOD:01369
deamidated and methyl esterified residue
A protein modification that effectively replaces a carboxamido group with a carboxyl methyl ester group.
Unimod:528
Deamidation followed by a methylation
Methyl+Deamidated
A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C,1x(15)N labeled residue.
7.02
(12)C -6 (13)C 6 (14)N -1 (15)N 1
7.017164
X
artifact
Unimod:695
PSI-MOD
13C(6) 15N(1) Silac label
Label:13C(6)15N(1)
MOD:01370
6x(13)C,1x(15)N labeled residue
A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C,1x(15)N labeled residue.
PubMed:11857757
PubMed:11999733
PubMed:12175151
Unimod:695
13C(6) 15N(1) Silac label
Label:13C(6)15N(1)
OBSOLETE bcecause identical and redundant with MOD:00851. Remap to MOD:00851.
MOD:00851
2.99
H -1 N -1 (18)O 1
2.988262
X
artifact
PSI-MOD
Deamidated:18O(1)
Deamidation in presence of O18
MOD:01371
deamidation in presence of O18
true
OBSOLETE bcecause identical and redundant with MOD:00851. Remap to MOD:00851.
PubMed:8382902
Deamidated:18O(1)
Deamidation in presence of O18
A protein modification that effectively converts an L-leucine residue to a (2S)-4-hydroxyleucine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 6 H 11 N 1 O 2
129.16
129.07898
L
natural
uniprot.ptm:PTM-0665
(2S)-2-amino-4-hydroxy-4-methylpentanoic acid
(2S)-4-hydroxyleucine
MOD_RES (2S)-4-hydroxyleucine
gamma-hydroxyleucine
PSI-MOD
MOD:01372
(2S)-4-hydroxyleucine
A protein modification that effectively converts an L-leucine residue to a (2S)-4-hydroxyleucine.
ChEBI:141825
PubMed:363352
PubMed:9164839
RESID:AA0442
(2S)-2-amino-4-hydroxy-4-methylpentanoic acid
(2S)-4-hydroxyleucine
MOD_RES (2S)-4-hydroxyleucine
gamma-hydroxyleucine
A protein modification that effectively converts an L-leucine residue to a (2S,4R)-5-hydroxyleucine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 6 H 11 N 1 O 2
129.16
129.07898
L
hypothetical
uniprot.ptm:PTM-0491
(2S,4R)-2-amino-5-hydroxy-4-methylpentanoic acid
(2S,4R)-5-hydroxyleucine
(4R)-5-hydroxyleucine
MOD_RES (4R)-5-hydroxyleucine
delta-hydroxyleucine
PSI-MOD
MOD:01373
(2S,4R)-5-hydroxyleucine
A protein modification that effectively converts an L-leucine residue to a (2S,4R)-5-hydroxyleucine.
ChEBI:141824
PubMed:16858410
PubMed:7690768
PubMed:9164839
RESID:AA0443
(2S,4R)-2-amino-5-hydroxy-4-methylpentanoic acid
(2S,4R)-5-hydroxyleucine
(4R)-5-hydroxyleucine
MOD_RES (4R)-5-hydroxyleucine
delta-hydroxyleucine
A modification that effectively oxygenates C5 of an L-leucine residue to form a (2S,4R)-5-oxoleucine.
13.98
C 0 H -2 N 0 O 1
13.979265
C 6 H 9 N 1 O 2
127.14
127.06333
L
hypothetical
uniprot.ptm:PTM-0492
(2S,4R)-2-amino-4-methyl-5-oxopentanoic acid
(2S,4R)-5-oxoleucine
(4R)-5-oxo-L-leucine
PSI-MOD
MOD:01374
(2S,4R)-5-oxoleucine
A modification that effectively oxygenates C5 of an L-leucine residue to form a (2S,4R)-5-oxoleucine.
ChEBI:43739
PubMed:16858410
RESID:AA0444
(2S,4R)-2-amino-4-methyl-5-oxopentanoic acid
(2S,4R)-5-oxoleucine
(4R)-5-oxo-L-leucine
A protein modification that effectively converts an L-leucine residue to a (2S,4R)-4,5-dihydroxyleucine.
32.0
C 0 H 0 N 0 O 2
31.989828
C 6 H 11 N 1 O 3
145.16
145.0739
L
natural
uniprot.ptm:PTM-0340
(2S,4R)-2-amino-4,5-dihydroxy-4-methylpentanoic acid
(2S,4R)-4,5-dihydroxyleucine
(4R)-4,5-dihydroxyleucine
MOD_RES (4R)-4,5-dihydroxyleucine
gamma,delta-dihydroxyleucine
PSI-MOD
MOD:01375
(2S,4R)-4,5-dihydroxyleucine
A protein modification that effectively converts an L-leucine residue to a (2S,4R)-4,5-dihydroxyleucine.
ChEBI:141823
PubMed:6010785
PubMed:6893271
RESID:AA0445
(2S,4R)-2-amino-4,5-dihydroxy-4-methylpentanoic acid
(2S,4R)-4,5-dihydroxyleucine
(4R)-4,5-dihydroxyleucine
MOD_RES (4R)-4,5-dihydroxyleucine
gamma,delta-dihydroxyleucine
A protein modification that effectively converts an L-isoleucine residue to a (2S,3S,4R)-3,4-dihydroxyisoleucine.
32.0
C 0 H 0 N 0 O 2
31.989828
C 6 H 11 N 1 O 3
145.16
145.0739
I
natural
uniprot.ptm:PTM-0343
(2S,3S,4R)-2-amino-3,4-dihydroxy-3-methylpentanoic acid
(2S,3S,4R)-3,4-dihydroxyisoleucine
(3S,4R)-3,4-dihydroxyisoleucine
MOD_RES (3S,4R)-3,4-dihydroxyisoleucine
beta,gamma-dihydroxyisoleucine
PSI-MOD
MOD:01376
(2S,3S,4R)-3,4-dihydroxyisoleucine
A protein modification that effectively converts an L-isoleucine residue to a (2S,3S,4R)-3,4-dihydroxyisoleucine.
ChEBI:141827
PubMed:11320328
RESID:AA0447
(2S,3S,4R)-2-amino-3,4-dihydroxy-3-methylpentanoic acid
(2S,3S,4R)-3,4-dihydroxyisoleucine
(3S,4R)-3,4-dihydroxyisoleucine
MOD_RES (3S,4R)-3,4-dihydroxyisoleucine
beta,gamma-dihydroxyisoleucine
A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4S)-4-hydroxyisoleucine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 6 H 11 N 1 O 2
129.16
129.07898
I
natural
uniprot.ptm:PTM-0337
(2S,3R,4S)-2-amino-3-methyl-4-hydroxyvaleric acid
(2S,3R,4S)-2-amino-4-hydroxy-3-methylpentanoic acid
(2S,3R,4S)-4-hydroxyisoleucine
(3R,4S)-4-hydroxyisoleucine
MOD_RES (3R,4S)-4-hydroxyisoleucine
gamma-hydroxyisoleucine
PSI-MOD
MOD:01377
(2S,3R,4S)-4-hydroxyisoleucine
A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4S)-4-hydroxyisoleucine.
ChEBI:141844
PubMed:363352
RESID:AA0448
(2S,3R,4S)-2-amino-3-methyl-4-hydroxyvaleric acid
(2S,3R,4S)-2-amino-4-hydroxy-3-methylpentanoic acid
(2S,3R,4S)-4-hydroxyisoleucine
(3R,4S)-4-hydroxyisoleucine
MOD_RES (3R,4S)-4-hydroxyisoleucine
gamma-hydroxyisoleucine
A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4R)-4,5-dihydroxyisoleucine.
32.0
C 0 H 0 N 0 O 2
31.989828
C 6 H 11 N 1 O 3
145.16
145.0739
I
natural
uniprot.ptm:PTM-0336
(2S,3R,4R)-2-amino-4,5-dihydroxy-3-methylpentanoic acid
(2S,3R,4R)-4,5-dihydroxyisoleucine
(3R,4R)-4,5-dihydroxyisoleucine
MOD_RES (3R,4R)-4,5-dihydroxyisoleucine
gamma,delta-dihydroxyisoleucine
PSI-MOD
MOD:01378
(2S,3R,4R)-4,5-dihydroxyisoleucine
A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4R)-4,5-dihydroxyisoleucine.
ChEBI:141826
PubMed:11805306
PubMed:18552824
PubMed:363352
RESID:AA0449
(2S,3R,4R)-2-amino-4,5-dihydroxy-3-methylpentanoic acid
(2S,3R,4R)-4,5-dihydroxyisoleucine
(3R,4R)-4,5-dihydroxyisoleucine
MOD_RES (3R,4R)-4,5-dihydroxyisoleucine
gamma,delta-dihydroxyisoleucine
A protein modification that effectively converts an L-tryptophan residue to 2'-methylsulfonyl-L-tryptophan.
78.09
C 1 H 2 N 0 O 2 S 1
77.97755
C 12 H 12 N 2 O 3 S 1
264.3
264.05685
W
natural
uniprot.ptm:PTM-0304
2'-methylsulfonyl-L-tryptophan
2-methylsulfonyl-3-((2S)-2-amino-2-carboxyethyl)-1H-indole
MOD_RES 2'-methylsulfonyltryptophan
PSI-MOD
MOD:01379
2'-methylsulfonyl-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to 2'-methylsulfonyl-L-tryptophan.
PubMed:6893271
RESID:AA0450
2'-methylsulfonyl-L-tryptophan
2-methylsulfonyl-3-((2S)-2-amino-2-carboxyethyl)-1H-indole
MOD_RES 2'-methylsulfonyltryptophan
A protein modification that effectively cross-links an L-cysteine residue and an L-tryptophan residue by a thioether bond to form 2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide.
29.98
C 0 H -2 N 0 O 2 S 0
29.974178
C 14 H 13 N 3 O 4 S 1
319.33
319.06268
C, W
natural
uniprot.ptm:PTM-0338
2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide
2-((2R)-2-amino-2carboxyethyl)sulfinyl-3-((2S)-2-amino-2-carboxyethyl)-1H-indole
6'-hydroxy-S-oxo-tryptathionine
CROSSLNK 2'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys)
PSI-MOD
MOD:01380
Cross-link 2.
2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide
A protein modification that effectively cross-links an L-cysteine residue and an L-tryptophan residue by a thioether bond to form 2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide.
PubMed:11805306
PubMed:18552824
PubMed:363352
PubMed:4865716
RESID:AA0451
2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide
2-((2R)-2-amino-2carboxyethyl)sulfinyl-3-((2S)-2-amino-2-carboxyethyl)-1H-indole
6'-hydroxy-S-oxo-tryptathionine
CROSSLNK 2'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys)
A protein modification that effectively converts an L-serine residue to O-palmitoleyl-L-serine.
236.4
C 16 H 28 N 0 O 1
236.21402
C 19 H 33 N 1 O 3
323.48
323.24603
S
natural
uniprot.ptm:PTM-0493
(2S)-2-amino-3-((9Z)-9-hexadecenoyloxy)propanoic acid
L-serine cis-9-hexadecenoate ester
LIPID O-palmitoleyl serine
O-palmitoleyl-L-serine
O3-palmitoleyl-serine
mod186
PSI-MOD
MOD:01381
O-palmitoleyl-L-serine
A protein modification that effectively converts an L-serine residue to O-palmitoleyl-L-serine.
OMSSA:186
PubMed:17141155
RESID:AA0455
(2S)-2-amino-3-((9Z)-9-hexadecenoyloxy)propanoic acid
L-serine cis-9-hexadecenoate ester
LIPID O-palmitoleyl serine
O-palmitoleyl-L-serine
O3-palmitoleyl-serine
mod186
A protein modification that effectively converts an L-methionine residue to N,N,N-trimethyl-L-methionine.
43.09
C 3 H 7 N 0 O 0 S 0
43.054226
1+
C 8 H 17 N 1 O 1 S 1
175.29
175.10254
M
natural
N-term
uniprot.ptm:PTM-0503
(1S)-1-carboxy-N,N,N-trimethyl-3-(methylsulfanyl)propanaminium
(1S)-1-carboxy-N,N,N-trimethyl-3-(methylsulfanyl)propanazanium
2-trimethylammonio-4-(methylthio)butanoic acid
MOD_RES N,N,N-trimethylmethionine
N,N,N-trimethyl-L-methionine
N,N,N-trimethylmethionine cation
N,N,N-trimethylmethioninium
N2Me3+Met
PSI-MOD
MOD:01382
N,N,N-trimethyl-L-methionine
A protein modification that effectively converts an L-methionine residue to N,N,N-trimethyl-L-methionine.
PubMed:18611379
RESID:AA0456
(1S)-1-carboxy-N,N,N-trimethyl-3-(methylsulfanyl)propanaminium
(1S)-1-carboxy-N,N,N-trimethyl-3-(methylsulfanyl)propanazanium
2-trimethylammonio-4-(methylthio)butanoic acid
MOD_RES N,N,N-trimethylmethionine
N,N,N-trimethyl-L-methionine
N,N,N-trimethylmethionine cation
N,N,N-trimethylmethioninium
N2Me3+Met
A protein modification that effectively cross-links two L-cysteine residues and oxidizes a sulfur to form L-cystine S-oxide.
13.98
C 0 H -2 N 0 O 1 S 0
13.979265
C 6 H 8 N 2 O 3 S 2
220.26
219.99763
C, C
hypothetical
uniprot.ptm:PTM-0324
(2R)-2-amino-3-[([(2R)-2-amino-2-carboxyethyl]sulfanyl)sulfinyl]propanoic acid
CROSSLNK S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)
L-cystine S-oxide
S-[(2R)-2-amino-3-oxopropyl] (2R)-2-amino-3-oxopropane-1-sulfinothioate
S-cysteinyl 3-(oxidosulfanyl)alanine
cystine sulfoxide
PSI-MOD
MOD:01383
Cross-link 2.
L-cystine S-oxide
A protein modification that effectively cross-links two L-cysteine residues and oxidizes a sulfur to form L-cystine S-oxide.
RESID:AA0457
(2R)-2-amino-3-[([(2R)-2-amino-2-carboxyethyl]sulfanyl)sulfinyl]propanoic acid
CROSSLNK S-cysteinyl 3-(oxidosulfanyl)alanine (Cys-Cys)
L-cystine S-oxide
S-[(2R)-2-amino-3-oxopropyl] (2R)-2-amino-3-oxopropane-1-sulfinothioate
S-cysteinyl 3-(oxidosulfanyl)alanine
cystine sulfoxide
A protein modification that effectively converts an L-serine residue to an aminomalonic acid.
13.98
C 0 H -2 N 0 O 1 S 0
13.979265
C 3 H 3 N 1 O 3
101.06
101.01129
S
hypothetical
uniprot.ptm:PTM-0321
2-carboxyglycine
Ama
MOD_RES Aminomalonic acid (Ser)
aminomalonic acid
aminopropanedioic acid
PSI-MOD
MOD:01384
aminomalonic acid (Ser)
A protein modification that effectively converts an L-serine residue to an aminomalonic acid.
PubMed:1621954
PubMed:5415959
PubMed:6366787
PubMed:7457858
RESID:AA0458
2-carboxyglycine
Ama
MOD_RES Aminomalonic acid (Ser)
aminomalonic acid
aminopropanedioic acid
A protein modification that effectively converts an L-phenylalanine residue to 3-hydroxy-L-phenylalanine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 9 H 9 N 1 O 2
163.18
163.06332
F
natural
uniprot.ptm:PTM-0346
(2S,3S)-2-amino-3-hydroxy-3-phenylpropanoic acid
3-hydoxyphenylalanine
3-hydroxy-L-phenylalanine
3-phenyl-L-serine
3HyPhe
L-threo-3-phenylserine
MOD_RES 3-hydroxyphenylalanine
beta-hydroxyphenylalanine
beta-phenylserine
hydroxylationf
PSI-MOD
MOD:01385
3-hydroxy-L-phenylalanine
A protein modification that effectively converts an L-phenylalanine residue to 3-hydroxy-L-phenylalanine.
ChEBI:16795
OMSSA:63
PubMed:10625477
PubMed:15651011
PubMed:16734421
PubMed:1880060
PubMed:7398618
PubMed:7844053
RESID:AA0462
(2S,3S)-2-amino-3-hydroxy-3-phenylpropanoic acid
3-hydoxyphenylalanine
3-hydroxy-L-phenylalanine
3-phenyl-L-serine
3HyPhe
L-threo-3-phenylserine
MOD_RES 3-hydroxyphenylalanine
beta-hydroxyphenylalanine
beta-phenylserine
hydroxylationf
A protein modification that effectively converts an L-valine residue to 3-hydroxy-L-valine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 5 H 9 N 1 O 2
115.13
115.06333
V
natural
uniprot.ptm:PTM-0347
(2S)-2-amino-3-hydroxy-3-methylbutanoic acid
3-hydroxy-L-valine
3-hydroxyvaline
3HyVal
MOD_RES 3-hydroxyvaline
PSI-MOD
MOD:01386
3-hydroxy-L-valine
A protein modification that effectively converts an L-valine residue to 3-hydroxy-L-valine.
ChEBI:141793
PubMed:7328054
RESID:AA0463
(2S)-2-amino-3-hydroxy-3-methylbutanoic acid
3-hydroxy-L-valine
3-hydroxyvaline
3HyVal
MOD_RES 3-hydroxyvaline
A protein modification that effectively converts an L-threonine residue to O-methyl-L-threonine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 5 H 9 N 1 O 2
115.13
115.06333
T
natural
uniprot.ptm:PTM-0356
(2S,3R)-2-amino-3-methoxybutanoic acid
MOD_RES O-methylthreonine
O-methyl threonine
O-methyl-L-threonine
OMeThr
threonine methyl ether
PSI-MOD
MOD:01387
O-methyl-L-threonine
A protein modification that effectively converts an L-threonine residue to O-methyl-L-threonine.
PubMed:7328054
RESID:AA0464
(2S,3R)-2-amino-3-methoxybutanoic acid
MOD_RES O-methylthreonine
O-methyl threonine
O-methyl-L-threonine
OMeThr
threonine methyl ether
A protein modification that effectively converts an L-threonine residue into 1-amino-2-propanol.
-44.01
C -1 H 0 N 0 O -2
-43.98983
C 3 H 8 N 1 O 1
74.1
74.06059
T
natural
C-term
uniprot.ptm:PTM-0354
(2R)-1-aminopropan-2-ol
1-amino-2-hydroxypropane
1-amino-2-propanol
1-methyl-2-aminoethanol
2-amino-1-methylethanol
2-hydroxy-1-propylamine
2-hydroxypropanamine
2-hydroxypropylamine
MOD_RES Decarboxylated threonine
alpha-aminoisopropyl alcohol
dCbxThr
decarboxylated threonine
isopropanolamine
threamine
PSI-MOD
MOD:01388
1-amino-2-propanol
A protein modification that effectively converts an L-threonine residue into 1-amino-2-propanol.
ChEBI:15675
PubMed:7328054
RESID:AA0465
(2R)-1-aminopropan-2-ol
1-amino-2-hydroxypropane
1-amino-2-propanol
1-methyl-2-aminoethanol
2-amino-1-methylethanol
2-hydroxy-1-propylamine
2-hydroxypropanamine
2-hydroxypropylamine
MOD_RES Decarboxylated threonine
alpha-aminoisopropyl alcohol
dCbxThr
decarboxylated threonine
isopropanolamine
threamine
A protein modification that effectively crosslinks an L-cysteine residue and an L-isoleucine residue to form L-isoleucine thiazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 9 H 12 N 2 O 1 S 1
196.27
196.06703
C, I
natural
uniprot.ptm:PTM-0361
2-[(1S,2S)-1-amino-2-methylbutyl]-1,3-thiazole-4-carboxylic acid
2-[1-zanyl-2-methylbutyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Ile-Cys)
L-isoleucine thiazole-4-carboxylic acid
PSI-MOD
MOD:01389
Cross-link 2.
L-isoleucine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-isoleucine residue to form L-isoleucine thiazole-4-carboxylic acid.
PubMed:11320328
RESID:AA0466
2-[(1S,2S)-1-amino-2-methylbutyl]-1,3-thiazole-4-carboxylic acid
2-[1-zanyl-2-methylbutyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Ile-Cys)
L-isoleucine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-valine residue to form L-valine thiazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 8 H 10 N 2 O 1 S 1
182.24
182.05139
C, V
natural
uniprot.ptm:PTM-0365
2-[(1S)-1-amino-2-methylpropyl]-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-methylpropyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Val-Cys)
L-valine thiazole-4-carboxylic acid
PSI-MOD
MOD:01390
Cross-link 2.
L-valine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-valine residue to form L-valine thiazole-4-carboxylic acid.
PubMed:7328054
RESID:AA0467
2-[(1S)-1-amino-2-methylpropyl]-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-methylpropyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Val-Cys)
L-valine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-valine residue, and C-5 methoxymethylates to form L-valine 5-(methoxymethyl)thiazole-4-carboxylic acid.
24.02
C 2 H 0 N 0 O 0 S 0
24.0
C 10 H 14 N 2 O 2 S 1
226.29
226.0776
C, V
natural
uniprot.ptm:PTM-0373
2-[(1S)-1-amino-2-methylpropyl]-5-(methoxymethyl)-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-methylpropyl]-5-(methoxymethyl)-1,3-thiazole-4-carboxylic acid
CROSSLNK 5-(methoxymethyl)thiazole-4-carboxylic acid (Val-Cys)
L-valine 5-(methoxymethyl)thiazole-4-carboxylic acid
PSI-MOD
MOD:01391
Cross-link 2.
L-valine 5-(methoxymethyl)thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-valine residue, and C-5 methoxymethylates to form L-valine 5-(methoxymethyl)thiazole-4-carboxylic acid.
PubMed:10625477
PubMed:1880060
PubMed:7844053
RESID:AA0468
2-[(1S)-1-amino-2-methylpropyl]-5-(methoxymethyl)-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-methylpropyl]-5-(methoxymethyl)-1,3-thiazole-4-carboxylic acid
CROSSLNK 5-(methoxymethyl)thiazole-4-carboxylic acid (Val-Cys)
L-valine 5-(methoxymethyl)thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-asparagine residue, and C-4 methylates to form L-asparagine 5-methylthiazole-4-carboxylic acid.
-6.0
C 1 H -2 N 0 O -1 S 0
-6.010565
C 8 H 9 N 3 O 2 S 1
211.24
211.04155
C, N
natural
uniprot.ptm:PTM-0352
2-[(1S)-1,3-bisazanyl-3-oxopropyl]-5-methyl-1,3-thiazole-4-carboxylic acid
2-[(1S)-1,3-diamino-3-oxopropyl]-5-methyl-1,3-thiazole-4-carboxylic acid
CROSSLNK 5-methylthiazole-4-carboxylic acid (Asn-Cys)
L-asparagine 5-methylthiazole-4-carboxylic acid
PSI-MOD
MOD:01392
Cross-link 2.
L-asparagine 5-methylthiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-asparagine residue, and C-4 methylates to form L-asparagine 5-methylthiazole-4-carboxylic acid.
PubMed:10625477
PubMed:1880060
PubMed:7844053
RESID:AA0469
2-[(1S)-1,3-bisazanyl-3-oxopropyl]-5-methyl-1,3-thiazole-4-carboxylic acid
2-[(1S)-1,3-diamino-3-oxopropyl]-5-methyl-1,3-thiazole-4-carboxylic acid
CROSSLNK 5-methylthiazole-4-carboxylic acid (Asn-Cys)
L-asparagine 5-methylthiazole-4-carboxylic acid
A protein modification that crosslinks two serine residues and a cysteine residue by formation of a pyridine-2,5-dicarboxylic acid.
-70.07
C 0 H -8 N -1 O -3 S 0
-70.050415
C 9 H 7 N 2 O 2 S 1
207.23
207.02283
C, S, S
natural
uniprot.ptm:PTM-0358
6-[(1R)-1-amino-2-sulfanylethyl]pyridine-2,5-dicarboxylic acid
L-cysteine pyridine-2,5-dicarboxylic acid
PSI-MOD
MOD:01393
Cross-link 3.
L-cysteine pyridine-2,5-dicarboxylic acid
A protein modification that crosslinks two serine residues and a cysteine residue by formation of a pyridine-2,5-dicarboxylic acid.
PubMed:10625477
PubMed:1880060
PubMed:7844053
RESID:AA0470
6-[(1R)-1-amino-2-sulfanylethyl]pyridine-2,5-dicarboxylic acid
L-cysteine pyridine-2,5-dicarboxylic acid
A protein modification that crosslinks two serine residues and a cysteine residue by formation of a 5-amino-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid.
-53.04
C 0 H -5 N 0 O -3 S 0
-53.02387
C 9 H 11 N 3 O 2 S 1
225.27
225.0572
C, S, S
natural
N-term
uniprot.ptm:PTM-0348
(5R,6R)-5-amino-6-[(1R)-1-amino-2-sulfanylethyl]-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid
L-cysteine 5-amino-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid
L-cysteine 5-aminopiperideine-2,5-dicarboxylic acid
PSI-MOD
CROSSLNK 5-amino-piperideine-2,5-dicarboxylic acid
MOD:01394
Cross-link 3.
L-cysteine 5-amino-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid
A protein modification that crosslinks two serine residues and a cysteine residue by formation of a 5-amino-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid.
PubMed:11320328
RESID:AA0471
(5R,6R)-5-amino-6-[(1R)-1-amino-2-sulfanylethyl]-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid
L-cysteine 5-amino-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid
L-cysteine 5-aminopiperideine-2,5-dicarboxylic acid
CROSSLNK 5-amino-piperideine-2,5-dicarboxylic acid
A protein modification that effectively results from forming an adduct between an isoleucine residue, a threonine residue and the quinaldate compound 2-carboxy-4-(1-hydroxyethyl)--7,8-dihydroquinolin-8-ol.
215.21
C 12 H 9 N 1 O 3
215.05824
C 22 H 28 N 3 O 6
430.48
430.1978
I, T
natural
N-term
(7R,8S)-7-[(1S,2S)-1-carboxy-2-methylbutyl]amino-2-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)carbonyl-8-hydroxy-4-[(1S)-1-hydroxyethyl]-7,8-dihydroquinoline
4-(1-hydroxyethyl)-7-isoleucino-2-(threonin-O3-ylcarbonyl)-7,8-dihydroquinolin-8-ol
BINDING 4-(1-hydroxyethyl)-7,8-dihydroquinolin-8-ol (covalent; via 2 links)
PSI-MOD
MOD:01395
Cross-link 2.
4-(1-hydroxyethyl)-7-isoleucino-2-(threonin-O3-ylcarbonyl)-7,8-dihydroquinolin-8-ol
A protein modification that effectively results from forming an adduct between an isoleucine residue, a threonine residue and the quinaldate compound 2-carboxy-4-(1-hydroxyethyl)--7,8-dihydroquinolin-8-ol.
PubMed:11320328
RESID:AA0472
(7R,8S)-7-[(1S,2S)-1-carboxy-2-methylbutyl]amino-2-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)carbonyl-8-hydroxy-4-[(1S)-1-hydroxyethyl]-7,8-dihydroquinoline
4-(1-hydroxyethyl)-7-isoleucino-2-(threonin-O3-ylcarbonyl)-7,8-dihydroquinolin-8-ol
BINDING 4-(1-hydroxyethyl)-7,8-dihydroquinolin-8-ol (covalent; via 2 links)
A protein modification that effectively converts an L-proline residue to a 5-hydroxy-3-methyl-L-proline.
30.03
C 1 H 2 N 0 O 1
30.010565
C 6 H 9 N 1 O 2
127.14
127.06333
P
artifactual
(2S,3S,5Xi)-5-hydroxy-3-methylpyrrolidine-2-carboxylic acid
5-hydroxy-3-methyl-L-proline
5-hydroxy-3-methylproline
5Hy3MePro
MOD_RES 5-hydroxy-3-methylproline (Ile)
beta-methyl-delta-hydroxyproline
PSI-MOD
MOD:01396
This entry is for the hypothetical formation of 5-hydroxy-3-methyl-L-proline from proline. For the natural production from L-isoleucine, use MOD:01897 [JSG].
5-hydroxy-3-methyl-L-proline (Pro)
A protein modification that effectively converts an L-proline residue to a 5-hydroxy-3-methyl-L-proline.
PubMed:7592021
PubMed:8557573
RESID:AA0473
(2S,3S,5Xi)-5-hydroxy-3-methylpyrrolidine-2-carboxylic acid
5-hydroxy-3-methyl-L-proline
5-hydroxy-3-methylproline
5Hy3MePro
MOD_RES 5-hydroxy-3-methylproline (Ile)
beta-methyl-delta-hydroxyproline
A protein modification that effectively crosslinks an L-serine residue and an L-threonine residue to form L-serine 5-methyloxazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1
-20.026215
C 7 H 8 N 2 O 3
168.15
168.0535
S, T
natural
uniprot.ptm:PTM-0386
2-[(1S)-1-amino-2-hydroxyethyl]-5-methyl-1,3-oxazole-4-carboxylic acid
2-[1-azanyl-2-hydroxyethyl]-5-methyl-1,3-oxazole-4-carboxylic acid
CROSSLNK 5-methyloxazole-4-carboxylic acid (Ser-Thr)
L-serine 5-methyloxazole-4-carboxylic acid
PSI-MOD
MOD:01397
Cross-link 2.
L-serine 5-methyloxazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-serine residue and an L-threonine residue to form L-serine 5-methyloxazole-4-carboxylic acid.
PubMed:7592021
PubMed:8557573
RESID:AA0474
2-[(1S)-1-amino-2-hydroxyethyl]-5-methyl-1,3-oxazole-4-carboxylic acid
2-[1-azanyl-2-hydroxyethyl]-5-methyl-1,3-oxazole-4-carboxylic acid
CROSSLNK 5-methyloxazole-4-carboxylic acid (Ser-Thr)
L-serine 5-methyloxazole-4-carboxylic acid
A protein modification that effectively converts an L-lysine residue to N6-propanoyl-L-lysine.
56.06
C 3 H 4 N 0 O 1
56.026215
C 9 H 16 N 2 O 2
184.24
184.12119
K
natural
Unimod:58
uniprot.ptm:PTM-0642
(2S)-2-amino-6-(propanoylamino)hexanoic acid
2-amino-6-propionylaminocaproic acid
MOD_RES N6-propionyllysine
N(zeta)-propanoyllysine
N6-(1-oxopropyl)-L-lysine
N6-propanoyl-L-lysine
N6-propionyllysine
epsilon-propanoyl-L-lysine
epsilon-propionyl-L-lysine
PSI-MOD
MOD:01398
The binding of histone peptides with propanoylated lysine to nuclear bromodomain proteins is non-specific and weaker than binding to the corresponding acetylated lysine peptides [JSG].
N6-propanoyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-propanoyl-L-lysine.
PubMed:17267393
PubMed:17684016
PubMed:20715035
RESID:AA0475
Unimod:58#K
(2S)-2-amino-6-(propanoylamino)hexanoic acid
2-amino-6-propionylaminocaproic acid
MOD_RES N6-propionyllysine
N(zeta)-propanoyllysine
N6-(1-oxopropyl)-L-lysine
N6-propanoyl-L-lysine
N6-propionyllysine
epsilon-propanoyl-L-lysine
epsilon-propionyl-L-lysine
A protein modification that effectively converts an L-lysine residue to an N6-(ADP-ribosyl)-L-lysine.
541.3
C 15 H 21 N 5 O 13 P 2
541.0611
C 21 H 33 N 7 O 14 P 2
669.48
669.15607
K
hypothetical
uniprot.ptm:PTM-0355
(S)-2-amino-6-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)hexanoic acid
2-amino-6-(ADP-ribosyl)amino-hexanoic acid
MOD_RES N6-(ADP-ribosyl)lysine
N(zeta)-ADP-ribosyllysine
N6-(ADP-ribosyl)-L-lysine
N6-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-lysine
N6-alpha-D-ribofuranosyl-L-lysine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
epsilon-ADP-ribosyllysine
PSI-MOD
MOD:01399
N6-(ADP-ribosyl)-L-lysine
A protein modification that effectively converts an L-lysine residue to an N6-(ADP-ribosyl)-L-lysine.
PubMed:18436469
RESID:AA0476
(S)-2-amino-6-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)hexanoic acid
2-amino-6-(ADP-ribosyl)amino-hexanoic acid
MOD_RES N6-(ADP-ribosyl)lysine
N(zeta)-ADP-ribosyllysine
N6-(ADP-ribosyl)-L-lysine
N6-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-lysine
N6-alpha-D-ribofuranosyl-L-lysine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
epsilon-ADP-ribosyllysine
A protein modification that effectively converts an L-lysine residue to an L-lysyl-poly(ADP-ribose).
K
natural
C-term
L-lysyl-poly(ADP-ribose)
MOD_RES Lysyl poly(ADP-ribose)
poly[2'-adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with 1alpha-D-ribofuranosyl] (2S)-2,6-diaminohexanoate
PSI-MOD
MOD:01400
L-lysyl-poly(ADP-ribose)
A protein modification that effectively converts an L-lysine residue to an L-lysyl-poly(ADP-ribose).
PubMed:6772638
RESID:AA0477
L-lysyl-poly(ADP-ribose)
MOD_RES Lysyl poly(ADP-ribose)
poly[2'-adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with 1alpha-D-ribofuranosyl] (2S)-2,6-diaminohexanoate
A protein modification that effectively converts an L-asparagine residue to a (2S,3S)-3-hydroxyasparagine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 4 H 6 N 2 O 3
130.1
130.03784
N
natural
uniprot.ptm:PTM-0370
(2S,3S)-2,4-diamino-3-hydroxy-4-oxobutanoic acid
(2S,3S)-2-amino-3-hydroxy-4-butanediamic acid
(2S,3S)-3-hydroxyasparagine
(3S)3HyAsn
L-threo-beta-hydroxyasparagine
MOD_RES (3S)-3-hydroxyasparagine
PSI-MOD
MOD:01401
(2S,3S)-3-hydroxyasparagine
A protein modification that effectively converts an L-asparagine residue to a (2S,3S)-3-hydroxyasparagine.
ChEBI:138107
ChEBI:50789
PubMed:11823643
PubMed:12042299
PubMed:12215170
PubMed:17573339
RESID:AA0478
(2S,3S)-2,4-diamino-3-hydroxy-4-oxobutanoic acid
(2S,3S)-2-amino-3-hydroxy-4-butanediamic acid
(2S,3S)-3-hydroxyasparagine
(3S)3HyAsn
L-threo-beta-hydroxyasparagine
MOD_RES (3S)-3-hydroxyasparagine
A protein modification that effectively converts an L-proline residue to a (2S,3R,4R)-3,4-dihydroxyproline.
32.0
C 0 H 0 N 0 O 2
31.989828
C 5 H 7 N 1 O 3
129.12
129.04259
P
natural
uniprot.ptm:PTM-0368
(2S,3R,4R)-3,4-dihydroxyproline
(2S,3R,4R)-3,4-dihydroxypyrrolidine-2-carboxylic acid
2,3-trans-3,4-trans-3,4-dihydroxy-L-proline
2-alpha-3-beta-4-alpha-3,4-dihydroxyproline
MOD_RES (3R,4R)-3,4-dihydroxyproline
PSI-MOD
MOD:01402
(2S,3R,4R)-3,4-dihydroxyproline
A protein modification that effectively converts an L-proline residue to a (2S,3R,4R)-3,4-dihydroxyproline.
ChEBI:141805
PubMed:6893271
RESID:AA0479
(2S,3R,4R)-3,4-dihydroxyproline
(2S,3R,4R)-3,4-dihydroxypyrrolidine-2-carboxylic acid
2,3-trans-3,4-trans-3,4-dihydroxy-L-proline
2-alpha-3-beta-4-alpha-3,4-dihydroxyproline
MOD_RES (3R,4R)-3,4-dihydroxyproline
A protein modification that effectively converts an L-leucine residue to a (2S)-4,5,5'-trihydroxyleucine.
48.0
C 0 H 0 N 0 O 3
47.984745
C 6 H 11 N 1 O 4
161.16
161.0688
L
natural
uniprot.ptm:PTM-0372
(2S)-2-amino-4,5-dihydroxy-4-(hydroxymethyl)pentanoic acid
(2S)-4,5,5'-trihydroxyleucine
4,5,5'-trihydroxyleucine
MOD_RES 4,5,4'-trihydroxyleucine
gamma,delta,delta'-trihydroxyleucine
PSI-MOD
MOD:01403
(2S)-4,5,5'-trihydroxyleucine
A protein modification that effectively converts an L-leucine residue to a (2S)-4,5,5'-trihydroxyleucine.
PubMed:6893271
RESID:AA0480
(2S)-2-amino-4,5-dihydroxy-4-(hydroxymethyl)pentanoic acid
(2S)-4,5,5'-trihydroxyleucine
4,5,5'-trihydroxyleucine
MOD_RES 4,5,4'-trihydroxyleucine
gamma,delta,delta'-trihydroxyleucine
A protein modification that effectively crosslinks an L-cysteine residue and an L-asparagine residue to form L-asparagine thiazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 7 H 7 N 3 O 2 S 1
197.21
197.0259
C, N
natural
uniprot.ptm:PTM-0359
2-[(1S)-1,3-diamino-3-oxopropyl]-1,3-thiazole-4-carboxylic acid
2-[1,3-bisazanyl-3-oxopropyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Asn-Cys)
L-asparagine thiazole-4-carboxylic acid
PSI-MOD
MOD:01404
Cross-link 2.
L-asparagine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-asparagine residue to form L-asparagine thiazole-4-carboxylic acid.
PubMed:7592021
PubMed:8557573
RESID:AA0481
2-[(1S)-1,3-diamino-3-oxopropyl]-1,3-thiazole-4-carboxylic acid
2-[1,3-bisazanyl-3-oxopropyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Asn-Cys)
L-asparagine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-proline residue to form L-proline thiazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 8 H 8 N 2 O 1 S 1
180.22
180.03574
C, P
natural
2-[(2S)-pyrrolidin-2-yl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Pro-Cys)
L-proline thiazole-4-carboxylic acid
PSI-MOD
MOD:01405
Cross-link 2.
L-proline thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-proline residue to form L-proline thiazole-4-carboxylic acid.
PubMed:7592021
PubMed:8557573
RESID:AA0482
2-[(2S)-pyrrolidin-2-yl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Pro-Cys)
L-proline thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-threonine thiazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 7 H 8 N 2 O 2 S 1
184.21
184.03065
C, T
natural
uniprot.ptm:PTM-0364
2-[(1S,2R)-1-amino-2-hydroxypropyl]-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-hydroxypropyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Thr-Cys)
L-threonine thiazole-4-carboxylic acid
PSI-MOD
MOD:01406
Cross-link 2.
L-threonine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-threonine thiazole-4-carboxylic acid.
PubMed:11320328
RESID:AA0483
2-[(1S,2R)-1-amino-2-hydroxypropyl]-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-hydroxypropyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Thr-Cys)
L-threonine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazoline-4-carboxylic acid.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 12 H 12 N 2 O 1 S 1
232.3
232.06703
C, F
natural
uniprot.ptm:PTM-0366
(4R)-2-[(1S)-1-amino-2-phenylethyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-phenylethyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazoline-4-carboxylic acid (Phe-Cys)
L-phenylalanine thiazoline-4-carboxylic acid
PSI-MOD
MOD:01407
Cross-link 2.
L-phenylalanine thiazoline-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazoline-4-carboxylic acid.
PubMed:7592021
PubMed:8557573
RESID:AA0484
(4R)-2-[(1S)-1-amino-2-phenylethyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-phenylethyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazoline-4-carboxylic acid (Phe-Cys)
L-phenylalanine thiazoline-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-threonine thiazoline-4-carboxylic acid.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 7 H 10 N 2 O 2 S 1
186.23
186.0463
C, T
natural
uniprot.ptm:PTM-0392
(4S)-2-[(1S,2R)-1-amino-2-hydroxypropyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-hydroxypropyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid
CROSSLNK (4S)-thiazoline-4-carboxylic acid (Thr-Cys)
L-threonine (4S)-thiazoline-4-carboxylic acid
PSI-MOD
MOD:01408
Cross-link 2.
L-threonine thiazoline-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-threonine thiazoline-4-carboxylic acid.
PubMed:11320328
RESID:AA0485
(4S)-2-[(1S,2R)-1-amino-2-hydroxypropyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid
2-[1-azanyl-2-hydroxypropyl]-4,5-dihydro-1,3-thiazole-4-carboxylic acid
CROSSLNK (4S)-thiazoline-4-carboxylic acid (Thr-Cys)
L-threonine (4S)-thiazoline-4-carboxylic acid
A protein modification that effectively replaces three hydrogen atoms with three hydroxyl groups.
48.0
C 0 H 0 N 0 O 3
47.984745
X
Hy3Res
PSI-MOD
MOD:01409
trihydroxylated residue
A protein modification that effectively replaces three hydrogen atoms with three hydroxyl groups.
PubMed:18688235
Hy3Res
A protein modification that effectively converts an L-leucine residue to an hydroxylated leucine.
L
HyLeu
PSI-MOD
MOD:01410
hydroxylated leucine
A protein modification that effectively converts an L-leucine residue to an hydroxylated leucine.
PubMed:18688235
HyLeu
A protein modification that effectively converts an L-leucine residue to a monohydroxylated leucine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 6 H 11 N 1 O 2
129.16
129.07898
L
natural
Hy1Leu
PSI-MOD
MOD:01411
monohydroxylated leucine
A protein modification that effectively converts an L-leucine residue to a monohydroxylated leucine.
PubMed:18688235
Hy1Leu
A protein modification that effectively converts an L-leucine residue to a dihydroxylated leucine.
32.0
C 0 H 0 N 0 O 2
31.989828
C 6 H 11 N 1 O 3
145.16
145.0739
L
natural
Hy2Leu
PSI-MOD
MOD:01412
dihydroxylated leucine
A protein modification that effectively converts an L-leucine residue to a dihydroxylated leucine.
PubMed:18688235
Hy2Leu
A protein modification that effectively converts an L-leucine residue to a trihydroxylated leucine.
48.0
C 0 H 0 N 0 O 3
47.984745
C 6 H 11 N 1 O 4
161.16
161.0688
L
natural
Hy3Leu
PSI-MOD
MOD:01413
trihydroxylated leucine
A protein modification that effectively converts an L-leucine residue to a trihydroxylated leucine.
PubMed:18688235
Hy3Leu
A protein modification that effectively converts an L-isoleucine residue to an hydroxylated isoleucine.
I
HyIle
PSI-MOD
MOD:01414
hydroxylated isoleucine
A protein modification that effectively converts an L-isoleucine residue to an hydroxylated isoleucine.
PubMed:18688235
HyIle
A protein modification that effectively converts an L-isoleucine residue to a monohydroxylated isoleucine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 6 H 11 N 1 O 2
129.16
129.07898
I
natural
Hy1Ile
PSI-MOD
MOD:01415
monohydroxylated isoleucine
A protein modification that effectively converts an L-isoleucine residue to a monohydroxylated isoleucine.
PubMed:18688235
Hy1Ile
A protein modification that effectively converts an L-isoleucine residue to a dihydroxylated isoleucine.
32.0
C 0 H 0 N 0 O 2
31.989828
C 6 H 11 N 1 O 3
145.16
145.0739
I
natural
Hy2Ile
PSI-MOD
MOD:01416
dihydroxylated isoleucine
A protein modification that effectively converts an L-isoleucine residue to a dihydroxylated isoleucine.
PubMed:18688235
Hy2Ile
A protein modification that effectively converts an L-proline residue to a monomethylated proline.
14.03
C 1 H 2 N 0 O 0
14.01565
C 6 H 10 N 1 O 1
112.15
112.07624
P
natural
Me1Pro
PSI-MOD
MOD:01417
monomethylated proline
A protein modification that effectively converts an L-proline residue to a monomethylated proline.
PubMed:18688235
Me1Pro
A protein modification that effectively converts an L-threonine residue to a methylated threonine, such as O-methyl-L-threonine.
T
natural
MeThr
PSI-MOD
MOD:01418
methylated threonine
A protein modification that effectively converts an L-threonine residue to a methylated threonine, such as O-methyl-L-threonine.
PubMed:18688235
MeThr
A protein modification that crosslinks two residues by condensation of a serine or threonine hydroxyl with the carbonyl of the preceding residue to form an oxazole or oxazoline ring, or by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 1,3-oxazole-4-carbothionic acid.
PSI-MOD
MOD:01419
oxazole/oxazoline ring crosslinked residues
A protein modification that crosslinks two residues by condensation of a serine or threonine hydroxyl with the carbonyl of the preceding residue to form an oxazole or oxazoline ring, or by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 1,3-oxazole-4-carbothionic acid.
PubMed:18688235
A protein modification that crosslinks two residues by condensation of a cysteine thiol with the carbonyl of the preceding residue to form a thiazole or thiazoline ring.
C
natural
PSI-MOD
MOD:01420
thiazole/thiazoline ring crosslinked residues
A protein modification that crosslinks two residues by condensation of a cysteine thiol with the carbonyl of the preceding residue to form a thiazole or thiazoline ring.
PubMed:18688235
A protein modification that crosslinks two residues by condensation of a serine hydroxyl with the carbonyl of the preceding residue to form an oxazole or oxazoline ring.
S
natural
PSI-MOD
MOD:01421
oxazole/oxazoline ring crosslinked residues (Ser)
A protein modification that crosslinks two residues by condensation of a serine hydroxyl with the carbonyl of the preceding residue to form an oxazole or oxazoline ring.
PubMed:18688235
A protein modification that crosslinks two residues by condensation of a threonine hydroxyl with the carbonyl of the preceding residue to form a 5-methyloxazole or 5-methyloxazoline ring.
T
natural
PSI-MOD
MOD:01422
oxazole/oxazoline ring crosslinked residues (Thr)
A protein modification that crosslinks two residues by condensation of a threonine hydroxyl with the carbonyl of the preceding residue to form a 5-methyloxazole or 5-methyloxazoline ring.
PubMed:18688235
A protein modification that effectively replaces a hydrogen atom with a palmitoleyl group.
236.4
C 16 H 28 N 0 O 1
236.21402
X
natural
Unimod:431
PSI-MOD
MOD:01423
palmitoleylated residue
A protein modification that effectively replaces a hydrogen atom with a palmitoleyl group.
Unimod:431
A protein modification that effectively results from forming an adduct with a compound containing a quinaldate, kynurenate, or xanthurenate group.
PSI-MOD
MOD:01424
quinaldate modified residue
A protein modification that effectively results from forming an adduct with a compound containing a quinaldate, kynurenate, or xanthurenate group.
PubMed:18688235
A protein modification that crosslinks three residues by formation of a pyridinyl ring, such as pyridine-2,5-dicarboxylic acid or 5-aminopiperideine-2,5-dicarboxylic acid.
X
natural
PSI-MOD
MOD:01425
Cross-link 3.
pyridinyl ring crosslinked residues
A protein modification that crosslinks three residues by formation of a pyridinyl ring, such as pyridine-2,5-dicarboxylic acid or 5-aminopiperideine-2,5-dicarboxylic acid.
PubMed:18688235
A protein modification that forms an adduct with a particular isotope labeled compound used as a reagent.
PSI-MOD
MOD:01426
isotope tagged reagent derivatized residue
A protein modification that forms an adduct with a particular isotope labeled compound used as a reagent.
PubMed:18688235
OBSOLETE because redundant and identical to MOD:00819. Remap to MOD:00819.
MOD:00819
C 4 H 7 N 1 O 1
85.11
85.052765
X
artifact
Abu
PSI-MOD
MOD:01427
2-aminobutanoic acid (Abu)
true
OBSOLETE because redundant and identical to MOD:00819. Remap to MOD:00819.
PubMed:18688235
Abu
A protein modification that forms an adduct with a (13)C labeled compound used as a reagent.
PSI-MOD
MOD:01428
(13)C isotope tagged reagent
A protein modification that forms an adduct with a (13)C labeled compound used as a reagent.
PubMed:18688235
A protein modification that forms an adduct with a (15)N labeled compound used as a reagent.
PSI-MOD
MOD:01429
(15)N isotope tagged reagent
A protein modification that forms an adduct with a (15)N labeled compound used as a reagent.
PubMed:18688235
A protein modification that forms an adduct with a (13)C labeled compound used as a reagent.
PSI-MOD
MOD:01430
(18)O isotope tagged reagent
A protein modification that forms an adduct with a (13)C labeled compound used as a reagent.
PubMed:18688235
A protein modification that forms an adduct with a (2)H labeled compound used as a reagent.
PSI-MOD
MOD:01431
(2)H deuterium tagged reagent
A protein modification that forms an adduct with a (2)H labeled compound used as a reagent.
PubMed:18688235
A protein modification that effectively converts an L-leucine residue to a (2S,4S)-4,5-dihydroxyleucine.
32.0
C 0 H 0 N 0 O 2
31.989828
C 6 H 11 N 1 O 3
145.16
145.0739
L
natural
uniprot.ptm:PTM-0666
(2S,4S)-2-amino-4,5-dihydroxy-4-methylpentanoic acid
(2S,4S)-4,5-dihydroxyleucine
(4S)-4,5-dihydroxyleucine
MOD_RES (4S)-4,5-dihydroxyleucine
gamma,delta-dihydroxyleucine
PSI-MOD
MOD:01432
(2S,4S)-4,5-dihydroxyleucine
A protein modification that effectively converts an L-leucine residue to a (2S,4S)-4,5-dihydroxyleucine.
ChEBI:141819
PubMed:3718926
RESID:AA0446
(2S,4S)-2-amino-4,5-dihydroxy-4-methylpentanoic acid
(2S,4S)-4,5-dihydroxyleucine
(4S)-4,5-dihydroxyleucine
MOD_RES (4S)-4,5-dihydroxyleucine
gamma,delta-dihydroxyleucine
A protein modification that effectively converts an L-threonine residue into 1-amino-2-propanone.
-46.03
C -1 H -2 N 0 O -2
-46.005478
C 3 H 6 N 1 O 1
72.09
72.04494
T
natural
C-term
uniprot.ptm:PTM-0379
1-amino-2-propanone
1-aminopropan-2-one
1-aminopropanone
MOD_RES 1-amino-2-propanone
aminoacetone
PSI-MOD
MOD:01433
1-amino-2-propanone
A protein modification that effectively converts an L-threonine residue into 1-amino-2-propanone.
ChEBI:17906
PubMed:12715872
PubMed:19196969
RESID:AA0486
1-amino-2-propanone
1-aminopropan-2-one
1-aminopropanone
MOD_RES 1-amino-2-propanone
aminoacetone
A protein modification that effectively converts an L-glutamic acid residue to a 4-hydroxy-L-glutamic acid.
16.0
C 0 H 0 N 0 O 1
15.994915
C 5 H 7 N 1 O 4
145.11
145.0375
E
natural
uniprot.ptm:PTM-0453
(2S,4Xi)-2-amino-4-hydroxypentanedioic acid
4-hydroxy-L-glutamic acid
MOD_RES 4-hydroxyglutamate
gamma-hydroxy glutaminic acid
threo-4-hydroxy-L-glutamic acid
PSI-MOD
MOD:01434
4-hydroxy-L-glutamic acid
A protein modification that effectively converts an L-glutamic acid residue to a 4-hydroxy-L-glutamic acid.
ChEBI:141845
PubMed:893891
RESID:AA0487
(2S,4Xi)-2-amino-4-hydroxypentanedioic acid
4-hydroxy-L-glutamic acid
MOD_RES 4-hydroxyglutamate
gamma-hydroxy glutaminic acid
threo-4-hydroxy-L-glutamic acid
A protein modification that effectively results from forming an adduct between a cysteine residue, a glutamic acid residue and the indole compound 2-carboxy-3-methyl-4-hydroxymethyl--indole.
169.18
C 11 H 7 N 1 O 1 S 0
169.05276
C 19 H 19 N 3 O 5 S 1
401.44
401.10455
C, E
natural
2-([(1R)-1-amino-1-carboxyeth-2-yl]sulfanyl)carbonyl-3-methyl-4-([(1S)-1-amino-1-carboxy-4-oxobutan-4-yl]oxy)methyl-1H-indole
2-(cystein-S-ylcarbonyl)-3-methyl-4-(glutam-5-yloxy)methylindole
2-(cystein-S-ylcarbonyl)-4-[(glutam-5-yloxy)methyl]-3-methyl-1H-indole
BINDING 3-methyl-4-hydroxymethylindole-2-carboxylic acid (covalent; via 2 links)
PSI-MOD
MOD:01435
Cross-link 2.
2-(cystein-S-ylcarbonyl)-3-methyl-4-(glutam-5-yloxy)methylindole
A protein modification that effectively results from forming an adduct between a cysteine residue, a glutamic acid residue and the indole compound 2-carboxy-3-methyl-4-hydroxymethyl--indole.
PubMed:893891
RESID:AA0488
2-([(1R)-1-amino-1-carboxyeth-2-yl]sulfanyl)carbonyl-3-methyl-4-([(1S)-1-amino-1-carboxy-4-oxobutan-4-yl]oxy)methyl-1H-indole
2-(cystein-S-ylcarbonyl)-3-methyl-4-(glutam-5-yloxy)methylindole
2-(cystein-S-ylcarbonyl)-4-[(glutam-5-yloxy)methyl]-3-methyl-1H-indole
BINDING 3-methyl-4-hydroxymethylindole-2-carboxylic acid (covalent; via 2 links)
A protein modification that effectively converts an L-cysteine residue to cyclo[(prolylserin)-O-yl] cysteinate.
166.18
C 8 H 10 N 2 O 2 S 0
166.07423
C 11 H 16 N 3 O 4 S 1
286.33
286.08615
C
natural
C-term
(3,6-dioxopyrrolo[4,5-a]piperazin-2-yl)methyl cysteinate
MOD_RES Cyclo[(prolylserin)-O-yl] cysteinate
[(3S,8aS)-1,4-dioxooctahydropyrrolo[1,2-a]pyrazin-3-yl]methyl (2R)-2-amino-3-sulfanylpropanoate
cyclo[(prolylserin)-O-yl] cysteinate
PSI-MOD
MOD:01436
cyclo[(prolylserin)-O-yl] cysteinate (Cys)
A protein modification that effectively converts an L-cysteine residue to cyclo[(prolylserin)-O-yl] cysteinate.
PubMed:7961166
RESID:AA0489#CYS
(3,6-dioxopyrrolo[4,5-a]piperazin-2-yl)methyl cysteinate
MOD_RES Cyclo[(prolylserin)-O-yl] cysteinate
[(3S,8aS)-1,4-dioxooctahydropyrrolo[1,2-a]pyrazin-3-yl]methyl (2R)-2-amino-3-sulfanylpropanoate
cyclo[(prolylserin)-O-yl] cysteinate
A protein modification that effectively converts an L-cysteine residue, an L-proline residue, and an L-serine residue to cyclo[(prolylserin)-O-yl] cysteinate.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 11 H 16 N 3 O 4 S 1
286.33
286.08615
C, P, S
natural
C-term
uniprot.ptm:PTM-0380
(3,6-dioxopyrrolo[4,5-a]piperazin-2-yl)methyl cysteinate
MOD_RES Cyclo[(prolylserin)-O-yl] cysteinate
[(3S,8aS)-1,4-dioxooctahydropyrrolo[1,2-a]pyrazin-3-yl]methyl (2R)-2-amino-3-sulfanylpropanoate
cyclo[(prolylserin)-O-yl] cysteinate
PSI-MOD
MOD:01437
Cross-link 3.
cyclo[(prolylserin)-O-yl] cysteinate (Cys-Pro-Ser cross-link)
A protein modification that effectively converts an L-cysteine residue, an L-proline residue, and an L-serine residue to cyclo[(prolylserin)-O-yl] cysteinate.
PubMed:7961166
RESID:AA0489#TRI
(3,6-dioxopyrrolo[4,5-a]piperazin-2-yl)methyl cysteinate
MOD_RES Cyclo[(prolylserin)-O-yl] cysteinate
[(3S,8aS)-1,4-dioxooctahydropyrrolo[1,2-a]pyrazin-3-yl]methyl (2R)-2-amino-3-sulfanylpropanoate
cyclo[(prolylserin)-O-yl] cysteinate
A protein modification that effectively converts an L-cysteine residue to S-[2-(pyridin-2-yl)ethyl]-L-cysteine.
105.14
C 7 H 7 N 1
105.057846
C 10 H 12 N 2 O 1 S 1
208.28
208.06703
C
artifact
2-PEC
2-vinylpyridine derivatized cysteine residue
Pyridylethyl Cystenyl
S-(pyridin-2-ylethyl)-L-cysteine
PSI-MOD
Pyridylethyl
S-pyridylethylation
MOD:01438
From DeltaMass: (name misspelled "Pyridylethyl Cystenyl", and formula incorrect, N and O reversed) Formula: C10H12O2N1S1 Monoisotopic Mass Change: 208.067 Average Mass Change: 208.286
S-[2-(pyridin-2-yl)ethyl]-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-[2-(pyridin-2-yl)ethyl]-L-cysteine.
PubMed:18369855
PubMed:18688235
2-PEC
2-vinylpyridine derivatized cysteine residue
Pyridylethyl Cystenyl
S-(pyridin-2-ylethyl)-L-cysteine
Pyridylethyl
S-pyridylethylation
A protein modification that effectively converts an L-cysteine residue to S-[2-(pyridin-4-yl)ethyl]-L-cysteine.
C
artifact
4-PEC
Pyridylethyl Cystenyl
S-(pyridin-4-ylethyl)-L-cysteine
PSI-MOD
Pyridylethyl
S-pyridylethylation
MOD:01439
S-[2-(pyridin-4-yl)ethyl]-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-[2-(pyridin-4-yl)ethyl]-L-cysteine.
PubMed:18688235
PubMed:6528972
4-PEC
Pyridylethyl Cystenyl
S-(pyridin-4-ylethyl)-L-cysteine
Pyridylethyl
S-pyridylethylation
A protein modification that effectively converts a source amino acid residue to an L-glutamyl semialdehyde.
C 5 H 7 N 1 O 2
113.12
113.047676
X
artifact
(S)-2-amino-5-oxopentanoic acid
L-glutamic gamma-semialdehyde
PSI-MOD
MOD:01440
glutamyl semialdehyde
A protein modification that effectively converts a source amino acid residue to an L-glutamyl semialdehyde.
PubMed:18688235
(S)-2-amino-5-oxopentanoic acid
L-glutamic gamma-semialdehyde
A protein modification that inserts or replaces a residue with a natural, standard, encoded residue.
X
natural
PSI-MOD
MOD:01441
natural, standard, encoded residue
A protein modification that inserts or replaces a residue with a natural, standard, encoded residue.
PubMed:18688235
PubMed:6692818
A protein modification that effectively cross-links an L-valine residue and an L-tyrosine residue by an ether bond to form 3-(O4'-L-tyrosyl)-L-valine.
-2.02
C 0 H -2 N 0 O 0
-2.01565
C 14 H 16 N 2 O 3
260.29
260.1161
V, Y
natural
uniprot.ptm:PTM-0390
(2S)-2-amino-3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-3-methylbutanoic acid
3-(O4'-L-tyrosyl)-L-valine
CROSSLNK 3-(O4'-tyrosyl)-valine (Val-Tyr)
PSI-MOD
MOD:01442
Cross-link 2.
3-(O4'-L-tyrosyl)-L-valine
A protein modification that effectively cross-links an L-valine residue and an L-tyrosine residue by an ether bond to form 3-(O4'-L-tyrosyl)-L-valine.
PubMed:19321420
RESID:AA0490
(2S)-2-amino-3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-3-methylbutanoic acid
3-(O4'-L-tyrosyl)-L-valine
CROSSLNK 3-(O4'-tyrosyl)-valine (Val-Tyr)
A protein modification that effectively converts four L-glutamic acid residues and two L-histidine residues to tetrakis-L-glutamato bis-L-N1'-histidino lipid carboxylato manganese iron oxide.
350.12
C 14 Fe 1 H 23 Mn 1 N 0 O 3
350.03824
1-
C 46 Fe 1 H 65 Mn 1 N 10 O 17
1140.86
1140.3264
E, E, E, E, H, H
natural
PSI-MOD
MOD:01443
Cross-link 6. It is not clear whether the lipid carboxylate is a cofactor or a substrate, and its identity is not certain. It was modeled as myristic acid [JSG].
tetrakis-L-glutamato bis-L-N1'-histidino lipid carboxylato manganese iron oxide
A protein modification that effectively converts four L-glutamic acid residues and two L-histidine residues to tetrakis-L-glutamato bis-L-N1'-histidino lipid carboxylato manganese iron oxide.
PubMed:19321420
RESID:AA0491
A protein modification that effectively converts an L-cysteine residue to L-3,3-dihydroxyoalanine.
-0.06
C 0 H 0 N 0 O 2 S -1
0.017758
C 3 H 5 N 1 O 3
103.08
103.02694
C
natural
(S)-2-amino-3,3-dihydroxypropanoic acid
2-(dihydroxymethyl)glycine
3,3-dihydroxy-L-alanine
3,3-dihydroxyalanine
3-hydroxy-L-serine
3-oxoalanine hydrate
PSI-MOD
C(alpha)-formylglycine hydrate
MOD:01444
L-3,3-dihydroxyoalanine (Cys)
A protein modification that effectively converts an L-cysteine residue to L-3,3-dihydroxyoalanine.
PubMed:11435113
PubMed:17558559
RESID:AA0492#CYS
(S)-2-amino-3,3-dihydroxypropanoic acid
2-(dihydroxymethyl)glycine
3,3-dihydroxy-L-alanine
3,3-dihydroxyalanine
3-hydroxy-L-serine
3-oxoalanine hydrate
C(alpha)-formylglycine hydrate
A protein modification that effectively converts an L-serine residue to L-3,3-dihydroxyoalanine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 3 H 5 N 1 O 3
103.08
103.02694
S
natural
(S)-2-amino-3,3-dihydroxypropanoic acid
2-(dihydroxymethyl)glycine
3,3-dihydroxy-L-alanine
3,3-dihydroxyalanine
3-hydroxy-L-serine
3-oxoalanine hydrate
PSI-MOD
C(alpha)-formylglycine hydrate
MOD:01445
L-3,3-dihydroxyoalanine (Ser)
A protein modification that effectively converts an L-serine residue to L-3,3-dihydroxyoalanine.
PubMed:11435113
PubMed:17558559
RESID:AA0492#SER
(S)-2-amino-3,3-dihydroxypropanoic acid
2-(dihydroxymethyl)glycine
3,3-dihydroxy-L-alanine
3,3-dihydroxyalanine
3-hydroxy-L-serine
3-oxoalanine hydrate
C(alpha)-formylglycine hydrate
A protein modification that effectively converts an N-formyl-Lmethionine residue to N-(dihydroxymethyl)-L-methionine.
18.02
C 0 H 2 N 0 O 1 S 0
18.010565
C 6 H 12 N 1 O 3 S 1
178.23
178.05379
MOD:00030
hypothetical
N-term
(2S)-2-[(dihydroxymethyl)amino]-4-(methylsulfanyl)butanoic acid
N-(dihydroxymethyl)-L-methionine
N-formyl-L-methionine hydrate
N-orthoformylmethionine
PSI-MOD
MOD:01446
N-(dihydroxymethyl)-L-methionine (fMet)
A protein modification that effectively converts an N-formyl-Lmethionine residue to N-(dihydroxymethyl)-L-methionine.
PubMed:12595263
PubMed:9159480
RESID:AA0493
(2S)-2-[(dihydroxymethyl)amino]-4-(methylsulfanyl)butanoic acid
N-(dihydroxymethyl)-L-methionine
N-formyl-L-methionine hydrate
N-orthoformylmethionine
A protein modification that effectively converts an L-methionine residue to N-(dihydroxymethyl)-L-methionine (not known as a natural, post-translational modification process).
46.03
C 1 H 2 N 0 O 2 S 0
46.005478
C 6 H 12 N 1 O 3 S 1
178.23
178.05379
M
hypothetical
N-term
(2S)-2-[(dihydroxymethyl)amino]-4-(methylsulfanyl)butanoic acid
N-(dihydroxymethyl)-L-methionine
N-formyl-L-methionine hydrate
N-orthoformylmethionine
PSI-MOD
MOD:01447
This entry is for the artifactual formation of N-(dihydroxymethyl)-L-methionine from methionine. For N-(dihydroxymethyl)-L-methionine derived from encoded N-formyl-L-methionine, use MOD:01446.
N-(dihydroxymethyl)-L-methionine (Met)
A protein modification that effectively converts an L-methionine residue to N-(dihydroxymethyl)-L-methionine (not known as a natural, post-translational modification process).
PubMed:12595263
PubMed:9159480
RESID:AA0493
(2S)-2-[(dihydroxymethyl)amino]-4-(methylsulfanyl)butanoic acid
N-(dihydroxymethyl)-L-methionine
N-formyl-L-methionine hydrate
N-orthoformylmethionine
A protein modification that effectively converts a source amino acid residue to L-3,3-dihydroxyoalanine.
C 3 H 5 N 1 O 3
103.08
103.02694
X
natural
(S)-2-amino-3,3-dihydroxypropanoic acid
2-(dihydroxymethyl)glycine
3,3-dihydroxy-L-alanine
3,3-dihydroxyalanine
3-hydroxy-L-serine
3-oxoalanine hydrate
PSI-MOD
C(alpha)-formylglycine hydrate
MOD:01448
L-3,3-dihydroxyoalanine
A protein modification that effectively converts a source amino acid residue to L-3,3-dihydroxyoalanine.
PubMed:11435113
PubMed:17558559
RESID:AA0492
(S)-2-amino-3,3-dihydroxypropanoic acid
2-(dihydroxymethyl)glycine
3,3-dihydroxy-L-alanine
3,3-dihydroxyalanine
3-hydroxy-L-serine
3-oxoalanine hydrate
C(alpha)-formylglycine hydrate
A protein modification that effectively converts an L-3-oxoalanine residue to L-3,3-dihydroxyoalanine.
18.02
C 0 H 2 N 0 O 1
18.010565
C 3 H 5 N 1 O 3
103.08
103.02694
MOD:01169
natural
PSI-MOD
MOD:01449
L-3,3-dihydroxyoalanine (Oxoalanine)
A protein modification that effectively converts an L-3-oxoalanine residue to L-3,3-dihydroxyoalanine.
PubMed:11435113
PubMed:17558559
PubMed:18688235
A protein modification that modifies an N-formyl-L-methionine residue.
MOD:00030
N-term
PSI-MOD
MOD:01450
modified N-formyl-L-methionine residue
A protein modification that modifies an N-formyl-L-methionine residue.
PubMed:18688235
A protein modification that converts an L-serine residue to O-phosphopantetheine-L-serine with secondary neutral loss of pantetheine resulting in O-phospho-L-serine.
79.98
C 0 H 1 N 0 O 3 P 1
79.96633
C 3 H 6 N 1 O 5 P 1
167.06
166.99835
S
artifact
PSI-MOD
MOD:01451
Phosphoserine is generated and detected after the facile elimination of pantetheine from the phosphopantetheine tertiary phosphodiester. See MOD:01452 for alternate origin.
O-phospho-L-serine arising from O-phosphopantetheine-L-serine after neutral loss of pantetheine
A protein modification that converts an L-serine residue to O-phosphopantetheine-L-serine with secondary neutral loss of pantetheine resulting in O-phospho-L-serine.
PubMed:17042494
PubMed:18688235
Covalent modification of a peptide or protein amino acid O-phosphopantetheine-L-serine with secondary neutral loss of pantetheine resulting in O-phospho-L-serine.
-260.35
C -11 H -20 N -2 O -3 P 0 S -1
-260.11948
C 3 H 6 N 1 O 5 P 1
167.06
166.99835
MOD:00159
artifact
PSI-MOD
MOD:01452
Phosphoserine is generated and detected after the facile elimination of pantethiene from the phosphopantethiene tertiary phosphodiester. See MOD:01451 for alternate origin.
O-phosphopantetheine-L-serine with neutral loss of pantetheine
Covalent modification of a peptide or protein amino acid O-phosphopantetheine-L-serine with secondary neutral loss of pantetheine resulting in O-phospho-L-serine.
PubMed:17042494
PubMed:18688235
A protein modification that effectively converts a source amino acid residue to L-glutamate 5-methyl ester.
C 6 H 9 N 1 O 3
143.14
143.05824
X
natural
(2S)-2-amino-5-methoxy-5-oxopentanoic acid
(5)-methyl L-hydrogen glutamate
2-aminopentanedioic acid 5-methyl ester
5-methyl L-2-aminoglutarate
5-methyl L-glutamate
5-methyl esterified L-glutamic acid
L-glutamic acid 5-methyl ester
O-methyl Glutamyl
O5MeGlu
glutamic acid 5-methyl ester
glutamic acid gamma-methyl ester
PSI-MOD
MOD:01453
L-glutamic acid 5-methyl ester
A protein modification that effectively converts a source amino acid residue to L-glutamate 5-methyl ester.
RESID:AA0072
(2S)-2-amino-5-methoxy-5-oxopentanoic acid
(5)-methyl L-hydrogen glutamate
2-aminopentanedioic acid 5-methyl ester
5-methyl L-2-aminoglutarate
5-methyl L-glutamate
5-methyl esterified L-glutamic acid
L-glutamic acid 5-methyl ester
O-methyl Glutamyl
O5MeGlu
glutamic acid 5-methyl ester
glutamic acid gamma-methyl ester
A protein modification that effectively crosslinks an N-terminal L-proline residue and a strand of DNA at the C-1 of a ribose, freeing the nucleotide base and forming N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium.
1+
P
natural
N-term
(1Z,2S)-2-carboxy-1-[(3R,4R)-3,4-dihydroxy-5-(phosphonooxy)pentylidene]pyrrolidinium
N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium
PSI-MOD
DNA glycosylase proline Schiff base intermediate
MOD:01454
This linkage is not a Schiff-base [JSG].
N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium
A protein modification that effectively crosslinks an N-terminal L-proline residue and a strand of DNA at the C-1 of a ribose, freeing the nucleotide base and forming N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium.
PubMed:10833024
PubMed:11847126
PubMed:9030608
RESID:AA0494
(1Z,2S)-2-carboxy-1-[(3R,4R)-3,4-dihydroxy-5-(phosphonooxy)pentylidene]pyrrolidinium
N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium
DNA glycosylase proline Schiff base intermediate
A protein modification that effectively replaces a residue hydroxyl or carboxyl hydrogen with a phosphono group (H2PO3 or 'phosphate').
79.98
H 1 O 3 P 1
79.96633
X
OPhosRes
PSI-MOD
MOD:01455
O-phosphorylated residue
A protein modification that effectively replaces a residue hydroxyl or carboxyl hydrogen with a phosphono group (H2PO3 or 'phosphate').
PubMed:18688235
OPhosRes
A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with a phosphono group (H2PO3 or 'phosphate').
79.98
H 1 O 3 P 1
79.96633
X
NPhosRes
PSI-MOD
MOD:01456
N-phosphorylated residue
A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with a phosphono group (H2PO3 or 'phosphate').
PubMed:18688235
NPhosRes
A protein modification that effectively converts an L-serine residue to L-cysteine (not known as a natural, post-translational modification process).
-16.06
C 0 H 0 N 0 O 1 S -1
-15.977156
C 3 H 5 N 1 O 1 S 1
103.14
103.009186
C
artifact
Cys(Ser)
PSI-MOD
MOD:01457
L-cysteine (Ser)
A protein modification that effectively converts an L-serine residue to L-cysteine (not known as a natural, post-translational modification process).
PubMed:1849824
PubMed:18688235
Cys(Ser)
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acetyl group.
42.04
C 2 H 2 N 0 O 1
42.010567
X
natural
N-term
Unimod:1
N2AcRes
ntermacetyl
PSI-MOD
MOD:01458
alpha-amino acetylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acetyl group.
OMSSA:10
Unimod:1#N-term
N2AcRes
ntermacetyl
A protein modification that effectively converts an N-terminal residue to an 4x(2)H labeled alpha-dimethylamino N-terminal residue.
32.06
C 2 (2)H 4
32.056408
X
artifact
N-term
Unimod:199
mod190
PSI-MOD
DiMethyl-CHD2
Dimethyl:2H(4)
MOD:01459
Supposed to be alpha-amino and Lys-N6 derivatized by C(2)H2O and reduction.
4x(2)H labeled alpha-dimethylamino N-terminal residue
A protein modification that effectively converts an N-terminal residue to an 4x(2)H labeled alpha-dimethylamino N-terminal residue.
OMSSA:190
PubMed:14670044
Unimod:199#N-term
mod190
DiMethyl-CHD2
Dimethyl:2H(4)
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a methyl group.
X
natural
N-term
N2MeRes
PSI-MOD
MOD:01460
alpha-amino methylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a methyl group.
PubMed:18688235
N2MeRes
A protein modification that effectively replaces an L-alanine alpha amino hydrogen with a methyl group.
A
natural
PSI-MOD
MOD:01461
N-methylated alanine
A protein modification that effectively replaces an L-alanine alpha amino hydrogen with a methyl group.
PubMed:18688235
A protein modification that effectively replaces an L-proline alpha imino hydrogen with a methyl group.
P
natural
N-term
PSI-MOD
MOD:01462
N-methylated proline
A protein modification that effectively replaces an L-proline alpha imino hydrogen with a methyl group.
PubMed:18688235
A protein modification that effectively replaces an L-methionine alpha amino hydrogen with a methyl group.
M
natural
N-term
PSI-MOD
MOD:01463
N-methylated methionine
A protein modification that effectively replaces an L-methionine alpha amino hydrogen with a methyl group.
PubMed:18688235
A protein modification that effectively converts an L-methionine residue to an L-methioninium (protonated L-methionine).
1.01
C 0 H 1 N 0 O 0 S 0
1.007276
1+
C 5 H 11 N 1 O 1 S 1
133.21
133.05559
M
natural
N-term
PSI-MOD
MOD:01464
protonated L-methionine (L-methioninium) residue
A protein modification that effectively converts an L-methionine residue to an L-methioninium (protonated L-methionine).
PubMed:18688235
A protein modification that effectively converts an L-methioninium (protonated L-methionine) residue to an N6,N6,N6-trimethyl-L-methionine.
42.08
C 3 H 6 N 0 O 0 S 0
42.046402
1+
C 8 H 17 N 1 O 1 S 1
175.29
175.10254
MOD:001464
natural
N-term
N2Me3Met
PSI-MOD
MOD:01465
For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative N2Me3+Met process (MOD:01382) accounts for both protonation and trimethylation.
N,N,N-trimethyl-L-methionine (from L-methioninium)
A protein modification that effectively converts an L-methioninium (protonated L-methionine) residue to an N6,N6,N6-trimethyl-L-methionine.
PubMed:18688235
N2Me3Met
modification from Unimod Chemical derivative
170.17
C 11 H 6 O 2
170.03677
C 14 H 11 N 1 O 3 S 1
273.31
273.04596
C
artifact
Unimod:302
PSI-MOD
Menadione
Menadione quinone derivative
MOD:01466
menadione quinone derivative - site C
modification from Unimod Chemical derivative
PubMed:15939799
Unimod:302#K
Menadione
Menadione quinone derivative
modification from Unimod Chemical derivative
170.17
C 11 H 6 O 2
170.03677
C 17 H 18 N 2 O 3
298.34
298.13174
K
artifact
Unimod:302
PSI-MOD
Menadione
Menadione quinone derivative
MOD:01467
menadione quinone derivative - site K
modification from Unimod Chemical derivative
PubMed:15939799
Unimod:302#K
Menadione
Menadione quinone derivative
A protein modification that effectively converts an L-cysteine residue to L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (not known as a natural, post-translational modification process).
1618.93
C 40 H 47 Mo 1 N 20 O 26 P 4 S 3 Se 1
1620.9302
C 43 H 52 Mo 1 N 21 O 27 P 4 S 4 Se 1
1722.07
1723.9395
C
artifact
Unimod:415
2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide
L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide)
bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-selenocysteinyl-Se-molybdenum
formate dehydrogenase selenocysteine molybdenum cofactor
PSI-MOD
L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide)
MolybdopterinGD+Delta:S(-1)Se(1)
molybdopterin-se
MOD:01468
This entry is for the artifactual formation of L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) from cysteine. For natural formation from L-selenocysteine, use MOD:00253.
L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (Cys)
A protein modification that effectively converts an L-cysteine residue to L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (not known as a natural, post-translational modification process).
PubMed:14235557
PubMed:2211698
PubMed:8052647
PubMed:9036855
RESID:AA0248#CYS
Unimod:415
2-amino-5,6-dimercapto-7-methyl-3,7,8a,9-tetrahydro-8-oxa-1,3,9,10-tetraazaanthracen-4-one guanosine dinucleotide
L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide)
bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-selenocysteinyl-Se-molybdenum
formate dehydrogenase selenocysteine molybdenum cofactor
L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide)
MolybdopterinGD+Delta:S(-1)Se(1)
molybdopterin-se
A protein modification that effectively converts an L-cysteine residue to L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (not known as a natural, post-translational modification process).
1738.88
C 40 H 47 N 20 O 26 P 4 S 4 Se 1 W 1
1738.9479
C 43 H 52 N 21 O 27 P 4 S 5 Se 1 W 1
1842.02
1841.957
C
artifact
PSI-MOD
MOD:01469
This entry is for the artifactual formation of L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) from cysteine. For natural formation from L-selenocysteine, use MOD:00381.
L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (Cys)
A protein modification that effectively converts an L-cysteine residue to L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (not known as a natural, post-translational modification process).
PubMed:11372198
PubMed:12220497
RESID:AA0376#CYS
A protein modification that effectively converts an L-threonine residue to (E)-dehydrobutyrine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 4 H 5 N 1 O 1
83.09
83.03712
T
natural
uniprot.ptm:PTM-0441
(2E)-2-aminobut-2-enoic acid
(E)-2-amino-2-butenoic acid
(E)-2-aminobutenoic acid
(E)-dehydrobutyrine
(E)dHAbu
2,3-didehydrobutyrine
3-methyldehydroalanine
Dehydroamino butyric acid
Dhb
MOD_RES (E)-2,3-didehydrobutyrine
alpha,beta-dehydroaminobutyric acid
anhydrothreonine
methyl-dehydroalanine
PSI-MOD
Dehydrated
Dehydration
MOD:01470
(E)-dehydrobutyrine (Thr)
A protein modification that effectively converts an L-threonine residue to (E)-dehydrobutyrine.
DeltaMass:0
PubMed:1547888
PubMed:20805503
PubMed:3769923
RESID:AA0547
(2E)-2-aminobut-2-enoic acid
(E)-2-amino-2-butenoic acid
(E)-2-aminobutenoic acid
(E)-dehydrobutyrine
(E)dHAbu
2,3-didehydrobutyrine
3-methyldehydroalanine
Dehydroamino butyric acid
Dhb
MOD_RES (E)-2,3-didehydrobutyrine
alpha,beta-dehydroaminobutyric acid
anhydrothreonine
methyl-dehydroalanine
Dehydrated
Dehydration
A protein modification that effectively converts an L-threonine residue to (Z)-dehydrobutyrine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 4 H 5 N 1 O 1
83.09
83.03712
T
natural
uniprot.ptm:PTM-0440
(2Z)-2-aminobut-2-enoic acid
(Z)-2-amino-2-butenoic acid
(Z)-2-aminobutenoic acid
(Z)-dehydrobutyrine
(Z)dHAbu
2,3-didehydrobutyrine
3-methyldehydroalanine
Dehydroamino butyric acid
Dhb
MOD_RES (Z)-2,3-didehydrobutyrine
alpha,beta-dehydroaminobutyric acid
anhydrothreonine
methyl-dehydroalanine
PSI-MOD
Dehydrated
Dehydration
MOD:01471
(Z)-dehydrobutyrine (Thr)
A protein modification that effectively converts an L-threonine residue to (Z)-dehydrobutyrine.
DeltaMass:0
PubMed:1547888
PubMed:3769923
RESID:AA0182
(2Z)-2-aminobut-2-enoic acid
(Z)-2-amino-2-butenoic acid
(Z)-2-aminobutenoic acid
(Z)-dehydrobutyrine
(Z)dHAbu
2,3-didehydrobutyrine
3-methyldehydroalanine
Dehydroamino butyric acid
Dhb
MOD_RES (Z)-2,3-didehydrobutyrine
alpha,beta-dehydroaminobutyric acid
anhydrothreonine
methyl-dehydroalanine
Dehydrated
Dehydration
A protein modification that effectively either adds neutral hydrogen atoms (proton and electron), or removes oxygen atoms from a residue with or without the addition of hydrogen atoms.
RedRes
PSI-MOD
MOD:01472
reduced residue
A protein modification that effectively either adds neutral hydrogen atoms (proton and electron), or removes oxygen atoms from a residue with or without the addition of hydrogen atoms.
PubMed:18688235
RedRes
A protein modification that effectively adds neutral hydrogen atoms (proton and electron) to a residue.
HRes
PSI-MOD
MOD:01473
hydrogenated residue
A protein modification that effectively adds neutral hydrogen atoms (proton and electron) to a residue.
PubMed:18688235
HRes
A protein modification that effectively converts an L-serine residue to O-[S-(carboxymethyl)phosphopantetheine]-L-serine.
398.37
C 13 H 23 N 2 O 8 P 1 S 1
398.09128
C 16 H 28 N 3 O 10 P 1 S 1
485.44
485.1233
S
artifact
PSI-MOD
MOD:01474
This modification results from the derivatization of the pantetheine sulfhydryl with iodoacetic acid [JSG].
O-[S-(carboxymethyl)phosphopantetheine]-L-serine
A protein modification that effectively converts an L-serine residue to O-[S-(carboxymethyl)phosphopantetheine]-L-serine.
PubMed:18688235
A protein modification that effectively converts an L-serine residue to O-[S-(carboxamidomethyl)phosphopantetheine]-L-serine.
397.38
C 13 H 24 N 3 O 7 P 1 S 1
397.10727
C 16 H 29 N 4 O 9 P 1 S 1
484.46
484.13928
S
artifact
PSI-MOD
MOD:01475
This modification results from the derivatization of the pantetheine sulfhydryl with iodoacetamide [JSG].
O-[S-(carboxamidomethyl)phosphopantetheine]-L-serine
A protein modification that effectively converts an L-serine residue to O-[S-(carboxamidomethyl)phosphopantetheine]-L-serine.
PubMed:18688235
A protein modification that effectively converts an L-phenylalanine residue to an 2'-fluoro-L-fluorophenylalanine.
17.99
C 0 F 1 H -1 N 0 O 0
17.990578
C 9 F 1 H 8 N 1 O 1
165.17
165.05899
F
artifact
2-fluorophenylalanine
o-fluorophenylalanine
ortho-fluorophenylalanine
PSI-MOD
MOD:01476
2'-fluoro-L-phenylalanine
A protein modification that effectively converts an L-phenylalanine residue to an 2'-fluoro-L-fluorophenylalanine.
PubMed:18688235
PubMed:8172898
2-fluorophenylalanine
o-fluorophenylalanine
ortho-fluorophenylalanine
A protein modification that effectively converts an L-phenylalanine residue to an 3'-fluoro-L-fluorophenylalanine.
17.99
C 0 F 1 H -1 N 0 O 0
17.990578
C 9 F 1 H 8 N 1 O 1
165.17
165.05899
F
artifact
3-fluorophenylalanine
m-fluorophenylalanine
meta-fluorophenylalanine
PSI-MOD
MOD:01477
3'-fluoro-L-phenylalanine
A protein modification that effectively converts an L-phenylalanine residue to an 3'-fluoro-L-fluorophenylalanine.
PubMed:18688235
PubMed:8172898
3-fluorophenylalanine
m-fluorophenylalanine
meta-fluorophenylalanine
A protein modification that effectively converts an L-phenylalanine residue into an 4'-fluoro-L-fluorophenylalanine.
17.99
C 0 F 1 H -1 N 0 O 0
17.990578
C 9 F 1 H 8 N 1 O 1
165.17
165.05899
F
artifact
4-fluorophenylalanine
p-fluorophenylalanine
para-fluorophenylalanine
rho-fluorophenylalanine
PSI-MOD
MOD:01478
4'-fluoro-L-phenylalanine
A protein modification that effectively converts an L-phenylalanine residue into an 4'-fluoro-L-fluorophenylalanine.
PubMed:18688235
PubMed:8172898
4-fluorophenylalanine
p-fluorophenylalanine
para-fluorophenylalanine
rho-fluorophenylalanine
A protein modification that effectively converts an L-tryptophan residue into an 4'-fluoro-L-tryptophan.
17.99
F 1 H -1
17.990578
C 11 F 1 H 9 N 2 O 1
204.2
204.06989
W
artifact
4-fluorotryptophan
PSI-MOD
MOD:01479
4'-fluoro-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue into an 4'-fluoro-L-tryptophan.
PubMed:18688235
PubMed:8172898
4-fluorotryptophan
A protein modification that effectively converts an L-tryptophan residue into an 5'-fluoro-L-tryptophan.
17.99
F 1 H -1
17.990578
C 11 F 1 H 9 N 2 O 1
204.2
204.06989
W
artifact
5-fluorotryptophan
PSI-MOD
MOD:01480
5'-fluoro-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue into an 5'-fluoro-L-tryptophan.
PubMed:18688235
PubMed:8172898
5-fluorotryptophan
A protein modification that effectively converts an L-tryptophan residue into an 6'-fluoro-L-tryptophan.
17.99
F 1 H -1
17.990578
C 11 F 1 H 9 N 2 O 1
204.2
204.06989
W
artifact
6-fluorotryptophan
PSI-MOD
MOD:01481
6'-fluoro-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue into an 6'-fluoro-L-tryptophan.
PubMed:18688235
PubMed:8172898
6-fluorotryptophan
A protein modification that effectively substitutes a calcium atom or a cluster containing calcium for hydrogen atoms, or that coordinates a calcium ion.
CaRes
PSI-MOD
MOD:01482
calcium containing modified residue
A protein modification that effectively substitutes a calcium atom or a cluster containing calcium for hydrogen atoms, or that coordinates a calcium ion.
PubMed:18688235
CaRes
A protein modification that effectively replaces a residue hydroxyl group with a formyloxy group.
28.01
C 1 O 1
27.994915
X
artifact
OFoRes
PSI-MOD
MOD:01483
O-formylated residue
A protein modification that effectively replaces a residue hydroxyl group with a formyloxy group.
PubMed:18688235
OFoRes
A protein modification that effectively crosslinks an L-glutamic acid residue and an L-lysine residue by an isopeptide bond to form N6-(L-isoglutamyl)-L-lysine and the release of water.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 11 H 17 N 3 O 3
239.27
239.12698
K, E
natural
(2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid
2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid
5-glutamyl N6-lysine
N alpha -(gamma-Glutamyl)-lysine
N(epsilon)-(gamma-glutamyl)lysine
N6-(L-isoglutamyl)-L-lysine
PSI-MOD
MOD:01484
Cross-link 2. This cross-link is usually made by glutamine and releases ammonia, rather than glutamic acid and requiring the consumption of ATP.
N6-(L-isoglutamyl)-L-lysine (Glu)
A protein modification that effectively crosslinks an L-glutamic acid residue and an L-lysine residue by an isopeptide bond to form N6-(L-isoglutamyl)-L-lysine and the release of water.
ChEBI:21863
PubMed:19015515
RESID:AA0124#GLU
(2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid
2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid
5-glutamyl N6-lysine
N alpha -(gamma-Glutamyl)-lysine
N(epsilon)-(gamma-glutamyl)lysine
N6-(L-isoglutamyl)-L-lysine
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
144.11
(12)C 5 (13)C 2 H 12 N 2 (18)O 1
144.10593
X
artifact
Unimod:532
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 114
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ114
iTRAQ4plex114
MOD:01485
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-114 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
Unimod:532
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 114
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ114
iTRAQ4plex114
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
144.11
(12)C 5 (13)C 2 H 12 N 2 (18)O 1
144.10593
X
artifact
N-term
Unimod:532
(4-methylpiperazin-1-yl)acetyl
iTRAQ114nterm
PSI-MOD
Accurate mass for 114
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ114
iTRAQ4plex114
MOD:01486
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-114 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
OMSSA:167
Unimod:532#N-term
(4-methylpiperazin-1-yl)acetyl
iTRAQ114nterm
Accurate mass for 114
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ114
iTRAQ4plex114
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
144.11
(12)C 5 (13)C 2 H 12 N 2 (18)O 1
144.10593
(12)C 11 (13)C 2 H 24 N 4 (16)O 1 (18)O 1
272.2
272.2009
K
artifact
Unimod:532
(4-methylpiperazin-1-yl)acetyl
iTRAQ114K
PSI-MOD
Accurate mass for 114
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ114
iTRAQ4plex114
MOD:01487
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-114 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
OMSSA:168
Unimod:532#K
(4-methylpiperazin-1-yl)acetyl
iTRAQ114K
Accurate mass for 114
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ114
iTRAQ4plex114
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
144.11
(12)C 5 (13)C 2 H 12 N 2 (18)O 1
144.10593
(12)C 14 (13)C 2 H 21 N 3 (16)O 2 (18)O 1
307.17
307.16925
Y
artifact
Unimod:532
(4-methylpiperazin-1-yl)acetyl
iTRAQ114Y
PSI-MOD
Accurate mass for 114
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ114
iTRAQ4plex114
MOD:01488
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-114 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
OMSSA:169
Unimod:532#Y
(4-methylpiperazin-1-yl)acetyl
iTRAQ114Y
Accurate mass for 114
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ114
iTRAQ4plex114
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
144.11
(12)C 5 (13)C 2 H 12 N 2 (18)O 1
144.10593
(12)C 11 (13)C 2 H 19 N 5 O 1 (18)O 1
281.16
281.16483
H
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
iTRAQ4plex114
MOD:01489
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-114 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
iTRAQ4plex114
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
144.11
(12)C 5 (13)C 2 H 12 N 2 (18)O 1
144.10593
(12)C 8 (13)C 2 H 17 N 3 O 2 (18)O 1
231.14
231.13794
S
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
iTRAQ4plex114
MOD:01490
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-114 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
iTRAQ4plex114
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
144.11
(12)C 5 (13)C 2 H 12 N 2 (18)O 1
144.10593
(12)C 9 (13)C 2 H 19 N 3 O 2 (18)O 1
245.15
245.1536
T
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
iTRAQ4plex114
MOD:01491
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-114 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
iTRAQ4plex114
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
144.1
(12)C 6 (13)C 1 H 12 (14)N 1 (15)N 1 (18)O 1
144.0996
X
artifact
Unimod:533
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ115
iTRAQ4plex115
MOD:01492
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-115 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
Unimod:533
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ115
iTRAQ4plex115
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
144.1
(12)C 6 (13)C 1 H 12 (14)N 1 (15)N 1 (18)O 1
144.0996
X
artifact
N-term
Unimod:533
(4-methylpiperazin-1-yl)acetyl
iTRAQ115nterm
PSI-MOD
Accurate mass for 115
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ115
iTRAQ4plex115
MOD:01493
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-115 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
OMSSA:170
Unimod:533#N-term
(4-methylpiperazin-1-yl)acetyl
iTRAQ115nterm
Accurate mass for 115
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ115
iTRAQ4plex115
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
144.1
(12)C 6 (13)C 1 H 12 (14)N 1 (15)N 1 (18)O 1
144.0996
(12)C 12 (13)C 1 H 24 (14)N 3 (15)N 1 (16)O 1 (18)O 1
272.19
272.19455
K
artifact
Unimod:533
(4-methylpiperazin-1-yl)acetyl
iTRAQ115K
PSI-MOD
Accurate mass for 115
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ115
iTRAQ4plex115
MOD:01494
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-115 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
OMSSA:171
Unimod:533#K
(4-methylpiperazin-1-yl)acetyl
iTRAQ115K
Accurate mass for 115
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ115
iTRAQ4plex115
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
144.1
(12)C 6 (13)C 1 H 12 (14)N 1 (15)N 1 (18)O 1
144.0996
(12)C 15 (13)C 1 H 21 (14)N 2 (15)N 1 (16)O 2 (18)O 1
307.16
307.16293
Y
artifact
Unimod:533
(4-methylpiperazin-1-yl)acetyl
iTRAQ115Y
PSI-MOD
Accurate mass for 115
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ115
iTRAQ4plex115
MOD:01495
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-115 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
OMSSA:172
Unimod:533#Y
(4-methylpiperazin-1-yl)acetyl
iTRAQ115Y
Accurate mass for 115
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ115
iTRAQ4plex115
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
144.1
(12)C 6 (13)C 1 H 12 (14)N 1 (15)N 1 (18)O 1
144.0996
(12)C 12 (13)C 1 H 19 (14)N 4 (15)N 1 (16)O 1 (18)O 1
281.16
281.1585
H
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
iTRAQ4plex115
MOD:01496
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-115 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
iTRAQ4plex115
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
144.1
(12)C 6 (13)C 1 H 12 (14)N 1 (15)N 1 (18)O 1
144.0996
(12)C 9 (13)C 1 H 17 N 1 (14)N 1 (15)N 1 (16)O 2 (18)O 1
231.13
231.13162
S
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
iTRAQ4plex115
MOD:01497
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-115 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
iTRAQ4plex115
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
144.1
(12)C 6 (13)C 1 H 12 (14)N 1 (15)N 1 (18)O 1
144.0996
(12)C 10 (13)C 1 H 19 (14)N 2 (15)N 1 (16)O 2 (18)O 1
245.15
245.14728
T
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
iTRAQ4plex115
MOD:01498
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-115 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
iTRAQ4plex115
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
144.1
(12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1
144.10207
X
artifact
Unimod:214
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
MOD:01499
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-116 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
Unimod:214
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
144.1
(12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1
144.10207
X
artifact
N-term
Unimod:214
(4-methylpiperazin-1-yl)acetyl
iTRAQ116nterm
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
MOD:01500
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-116 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
OMSSA:173
Unimod:214#N-term
(4-methylpiperazin-1-yl)acetyl
iTRAQ116nterm
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
144.1
(12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1
144.10207
(12)C 10 (13)C 3 H 24 N 2 (14)N 1 (15)N 1 O 1 (16)O 1
272.2
272.19702
K
artifact
Unimod:214
(4-methylpiperazin-1-yl)acetyl
iTRAQ116K
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
MOD:01501
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-116 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
OMSSA:174
Unimod:214#K
(4-methylpiperazin-1-yl)acetyl
iTRAQ116K
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
144.1
(12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1
144.10207
(12)C 13 (13)C 3 H 21 N 1 (14)N 1 (15)N 1 O 2 (16)O 1
307.17
307.1654
Y
artifact
Unimod:214
(4-methylpiperazin-1-yl)acetyl
iTRAQ116Y
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
MOD:01502
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-116 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
OMSSA:175
Unimod:214#Y
(4-methylpiperazin-1-yl)acetyl
iTRAQ116Y
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
144.1
(12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1
144.10207
(12)C 10 (13)C 3 H 19 N 3 (14)N 1 (15)N 1 (16)O 2
281.16
281.16098
H
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
iTRAQ4plex
MOD:01503
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-116 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
iTRAQ4plex
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
144.1
(12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1
144.10207
(12)C 7 (13)C 3 H 17 (14)N 2 (15)N 1 (16)O 3
231.13
231.1341
S
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
iTRAQ4plex
MOD:01504
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-116 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
iTRAQ4plex
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
144.1
(12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1
144.10207
(12)C 8 (13)C 3 H 19 (14)N 2 (15)N 1 (16)O 3
245.15
245.14973
T
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
iTRAQ4plex
MOD:01505
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-116 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
iTRAQ4plex
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
144.1
(12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1
144.10207
X
artifact
Unimod:214
Unimod:889
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Applied Biosystems mTRAQ(TM) reagent
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
mTRAQ heavy
MOD:01506
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
Unimod:214
Unimod:889
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Applied Biosystems mTRAQ(TM) reagent
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
mTRAQ heavy
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
144.1
(12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1
144.10207
X
artifact
N-term
Unimod:214
Unimod:889
(4-methylpiperazin-1-yl)acetyl
iTRAQ117nterm
mTRAQ heavy on nterm
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Applied Biosystems mTRAQ(TM) reagent
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
mTRAQ heavy
MOD:01507
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
OMSSA:176
OMSSA:211
Unimod:214#N-term
Unimod:889#N-term
(4-methylpiperazin-1-yl)acetyl
iTRAQ117nterm
mTRAQ heavy on nterm
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Applied Biosystems mTRAQ(TM) reagent
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
mTRAQ heavy
A protein modification that effectively replaces the N6-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
144.1
(12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1
144.10207
(12)C 10 (13)C 3 H 24 N 2 (14)N 1 (15)N 1 O 1 (16)O 1
272.2
272.19702
K
artifact
Unimod:214
(4-methylpiperazin-1-yl)acetyl
iTRAQ117K
mTRAQ heavy on K
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Applied Biosystems mTRAQ(TM) reagent
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
mTRAQ heavy
MOD:01508
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
OMSSA:177
OMSSA:212
Unimod:214#K
Unimod:889#K
(4-methylpiperazin-1-yl)acetyl
iTRAQ117K
mTRAQ heavy on K
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Applied Biosystems mTRAQ(TM) reagent
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
mTRAQ heavy
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
144.1
(12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1
144.10207
(12)C 13 (13)C 3 H 21 N 1 (14)N 1 (15)N 1 O 2 (16)O 1
307.17
307.1654
Y
artifact
Unimod:214
Unimod:889
(4-methylpiperazin-1-yl)acetyl
iTRAQ117Y
mTRAQ heavy on Y
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Applied Biosystems mTRAQ(TM) reagent
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
mTRAQ heavy
MOD:01509
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
OMSSA:178
OMSSA:213
Unimod:214#Y
Unimod:889#Y
(4-methylpiperazin-1-yl)acetyl
iTRAQ117Y
mTRAQ heavy on Y
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Applied Biosystems mTRAQ(TM) reagent
Representative mass and accurate mass for 116 & 117
iTRAQ
iTRAQ4plex
mTRAQ heavy
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
144.1
(12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1
144.10207
(12)C 10 (13)C 3 H 19 (14)N 4 (15)N 1 (16)O 2
281.16
281.16098
H
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
iTRAQ4plex
MOD:01510
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-117 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
iTRAQ4plex
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
144.1
(12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1
144.10207
(12)C 7 (13)C 3 H 17 (14)N 2 (15)N 1 (16)O 3
231.13
231.1341
S
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
iTRAQ4plex
MOD:01511
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-117 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
iTRAQ4plex
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
144.1
(12)C 4 (13)C 3 H 12 (14)N 1 (15)N 1 (16)O 1
144.10207
(12)C 8 (13)C 3 H 19 (14)N 2 (15)N 1 (16)O 3
245.15
245.14973
T
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
iTRAQ4plex
MOD:01512
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex-117 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
iTRAQ4plex
Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.1 Da.
PSI-MOD
MOD:01513
modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.1 Da
Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.1 Da.
PubMed:18688235
Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.01 Da.
PSI-MOD
MOD:01514
modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.01 Da
Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.01 Da.
PubMed:18688235
Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.000001 Da.
PSI-MOD
MOD:01515
modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.000001 Da
Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.000001 Da.
PubMed:18688235
Modifications that have monoisotopic mass differences from their respective origins of 144.099-144.106 Da.
PSI-MOD
MOD:01516
modifications with monoisotopic mass diferences that are nominally equal at 144.099-144.106 Da.
Modifications that have monoisotopic mass differences from their respective origins of 144.099-144.106 Da.
PubMed:18688235
Modifications that have monoisotopic mass differences from their respective origins of 144.102062 Da.
PSI-MOD
MOD:01517
modifications with monoisotopic mass differences that are nominally equal at 144.102062 Da
Modifications that have monoisotopic mass differences from their respective origins of 144.102062 Da.
PubMed:18688235
A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups.
X
artifact
Unimod:214
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01518
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups.
Unimod:214
(4-methylpiperazin-1-yl)acetyl
A distinct molecular entity produced from a protein or a protein modification as the result of a fragmentation process.
PSI-MOD
MOD:01519
The reporter fragment is either itself a modification consisting of atoms derived from the original amino acid residues, or its detection can be taken as evidence that particular modified residues had been present.
reporter fragment
A distinct molecular entity produced from a protein or a protein modification as the result of a fragmentation process.
PubMed:18688235
A distinct molecular entity produced as the result of a fragmentation process performed on a particular modified residue.
PSI-MOD
MOD:01520
modification reporter fragment
A distinct molecular entity produced as the result of a fragmentation process performed on a particular modified residue.
PubMed:18688235
A protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex reagent derivatized residue.
PSI-MOD
MOD:01521
iTRAQ4plex reporter fragment
A protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex reagent derivatized residue.
PubMed:18688235
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 114 reagent derivatized residue.
1+
(12)C 5 (13)C 1 H 13 (14)N 2
114.11
114.11068
X
artifact
4-methyl-1-methylidenepiperazin-1-ium
PSI-MOD
MOD:01522
iTRAQ4plex-114 reporter fragment
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 114 reagent derivatized residue.
PubMed:18688235
4-methyl-1-methylidenepiperazin-1-ium
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 115 reagent derivatized residue.
1+
(12)C 5 (13)C 1 H 13 (14)N 1 (15)N 1
115.11
115.10771
X
artifact
4-methyl-1-methylidenepiperazin-1-ium
PSI-MOD
MOD:01523
iTRAQ4plex-115 reporter fragment
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 115 reagent derivatized residue.
PubMed:18688235
4-methyl-1-methylidenepiperazin-1-ium
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 116 reagent derivatized residue.
1+
(12)C 4 (13)C 2 H 13 (14)N 1 (15)N 1
116.11
116.11107
X
artifact
4-methyl-1-methylidenepiperazin-1-ium
PSI-MOD
MOD:01524
iTRAQ4plex-116 reporter fragment
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 116 reagent derivatized residue.
PubMed:18688235
4-methyl-1-methylidenepiperazin-1-ium
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 117 reagent derivatized residue.
1+
(12)C 3 (13)C 3 H 13 (14)N 1 (15)N 1
117.11
117.114426
X
artifact
4-methyl-1-methylidenepiperazin-1-ium
PSI-MOD
MOD:01525
iTRAQ4plex-117, mTRAQ heavy, reporter fragment
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 117 reagent derivatized residue.
PubMed:18688235
4-methyl-1-methylidenepiperazin-1-ium
A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups.
X
artifact
Unimod:730
PSI-MOD
MOD:01526
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups.
Unimod:730
A distinct molecular entity produced from a particular amino acid residue as the result of a fragmentation process.
PSI-MOD
MOD:01527
residue reporter fragment
A distinct molecular entity produced from a particular amino acid residue as the result of a fragmentation process.
PubMed:18688235
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
X
artifact
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01528
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-113 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
Unimod:730
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
X
artifact
N-term
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01529
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-113 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
Unimod:730#N-term
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 13 (13)C 7 H 36 (14)N 5 (15)N 1 (16)O 4
432.3
432.30032
K
artifact
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01530
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-113 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
Unimod:730#K
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 16 (13)C 7 H 33 (14)N 4 (15)N 1 (16)O 5
467.27
467.26868
Y
artifact
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01531
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-113 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
Unimod:730#Y
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 13 (13)C 7 H 31 (14)N 6 (15)N 1 (16)O 4
441.26
441.26428
H
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01532
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-113 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 10 (13)C 7 H 29 (14)N 4 (15)N 1 (16)O 5
391.24
391.2374
S
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01533
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-113 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 11 (13)C 7 H 31 (14)N 4 (15)N 1 (16)O 5
405.25
405.25305
T
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01534
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-113 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
X
artifact
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01535
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-114 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
Unimod:730
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
X
artifact
N-term
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01536
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-114 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
Unimod:730#N-term
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 13 (13)C 7 H 36 (14)N 5 (15)N 1 (16)O 4
432.3
432.30032
K
artifact
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01537
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-114 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
Unimod:730#K
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 16 (13)C 7 H 33 (14)N 4 (15)N 1 (16)O 5
467.27
467.26868
Y
artifact
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01538
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-114 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
Unimod:730#Y
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 13 (13)C 7 H 31 (14)N 6 (15)N 1 (16)O 4
441.26
441.26428
H
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01539
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-114 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 10 (13)C 7 H 29 (14)N 4 (15)N 1 (16)O 5
391.24
391.2374
S
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01540
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-114 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 11 (13)C 7 H 31 (14)N 4 (15)N 1 (16)O 5
405.25
405.25305
T
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01541
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-114 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
X
artifact
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01542
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-115 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
Unimod:731
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
X
artifact
N-term
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01543
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-115 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
Unimod:731#N-term
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 14 (13)C 6 H 36 (14)N 4 (15)N 2 (16)O 4
432.29
432.294
K
artifact
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01544
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-115 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
Unimod:731#K
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 17 (13)C 6 H 33 (14)N 3 (15)N 2 (16)O 5
467.26
467.26236
Y
artifact
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01545
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-115 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
Unimod:731#Y
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 14 (13)C 6 H 31 (14)N 5 (15)N 2 (16)O 4
441.26
441.25797
H
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01546
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-115 reporter+balance reagent N'-derivatized histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 11 (13)C 6 H 29 (14)N 3 (15)N 2 (16)O 5
391.23
391.23108
S
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01547
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-115 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 12 (13)C 6 H 31 (14)N 3 (15)N 2 (16)O 5
405.25
405.2467
T
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01548
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-115 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
X
artifact
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01549
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-116 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
Unimod:730
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
X
artifact
N-term
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01550
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-116 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
Unimod:730#N-term
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 13 (13)C 7 H 36 (14)N 5 (15)N 1 (16)O 4
432.3
432.30032
K
artifact
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01551
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-116 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
Unimod:730#K
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 16 (13)C 7 H 33 (14)N 4 (15)N 1 (16)O 5
467.27
467.26868
Y
artifact
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01552
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-116 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
Unimod:730#Y
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 13 (13)C 7 H 31 (14)N 6 (15)N 1 (16)O 4
441.26
441.26428
H
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01553
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-116 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 10 (13)C 7 H 29 (14)N 4 (15)N 1 (16)O 5
391.24
391.2374
S
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01554
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-116 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 11 (13)C 7 H 31 (14)N 4 (15)N 1 (16)O 5
405.25
405.25305
T
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01555
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-116 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
X
artifact
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01556
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-117 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
Unimod:730
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
X
artifact
N-term
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01557
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-117 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
Unimod:730#N-term
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 13 (13)C 7 H 36 (14)N 5 (15)N 1 (16)O 4
432.3
432.30032
K
artifact
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01558
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-117 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
Unimod:730#K
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 16 (13)C 7 H 33 (14)N 4 (15)N 1 (16)O 5
467.27
467.26868
Y
artifact
Unimod:730
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
MOD:01559
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-117 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
Unimod:730#Y
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
Representative mass and accurate mass for 113, 114, 116 & 117
iTRAQ8plex
iTRAQ8plex:13C(7)15N(1)
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 13 (13)C 7 H 31 (14)N 6 (15)N 1 (16)O 4
441.26
441.26428
H
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01560
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-117 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 10 (13)C 7 H 29 (14)N 4 (15)N 1 (16)O 5
391.24
391.2374
S
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01561
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-117 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
304.21
(12)C 7 (13)C 7 H 24 (14)N 3 (15)N 1 (16)O 3
304.20535
(12)C 11 (13)C 7 H 31 (14)N 4 (15)N 1 (16)O 5
405.25
405.25305
T
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01562
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-117 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
X
artifact
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01563
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-118 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
Unimod:731
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
X
artifact
N-term
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01564
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-118 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
Unimod:731#N-term
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 14 (13)C 6 H 36 (14)N 4 (15)N 2 (16)O 4
432.29
432.294
K
artifact
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01565
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-118 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
Unimod:731#K
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 17 (13)C 6 H 33 (14)N 3 (15)N 2 (16)O 5
467.26
467.26236
Y
artifact
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01566
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-118 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
Unimod:731#Y
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 14 (13)C 6 H 31 (14)N 5 (15)N 2 (16)O 4
441.26
441.25797
H
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01567
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-118 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 11 (13)C 6 H 29 (14)N 3 (15)N 2 (16)O 5
391.23
391.23108
S
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01568
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-118 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 12 (13)C 6 H 31 (14)N 3 (15)N 2 (16)O 5
405.25
405.2467
T
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01569
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-118 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
X
artifact
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01570
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-119 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
Unimod:731
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
X
artifact
N-term
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01571
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-119 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
Unimod:731#N-term
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 14 (13)C 6 H 36 (14)N 4 (15)N 2 (16)O 4
432.29
432.294
K
artifact
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01572
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-119 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
Unimod:731#K
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 17 (13)C 6 H 33 (14)N 3 (15)N 2 (16)O 5
467.26
467.26236
Y
artifact
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01573
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-119 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
Unimod:731#Y
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 14 (13)C 6 H 31 (14)N 5 (15)N 2 (16)O 4
441.26
441.25797
H
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01574
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-119 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 11 (13)C 6 H 29 (14)N 3 (15)N 2 (16)O 5
391.23
391.23108
S
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01575
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-119 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 12 (13)C 6 H 31 (14)N 3 (15)N 2 (16)O 5
405.25
405.2467
T
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01576
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-119 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
X
artifact
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01577
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-121 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
Unimod:731
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
X
artifact
N-term
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01578
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-121 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
Unimod:731#N-term
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 14 (13)C 6 H 36 (14)N 4 (15)N 2 (16)O 4
432.29
432.294
K
artifact
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01579
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-121 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
Unimod:731#K
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 17 (13)C 6 H 33 (14)N 3 (15)N 2 (16)O 5
467.26
467.26236
Y
artifact
Unimod:731
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
MOD:01580
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-121 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
Unimod:731#Y
(4-methylpiperazin-1-yl)acetyl
Accurate mass for 115, 118, 119 & 121
Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry
iTRAQ8plex:13C(6)15N(2)
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 14 (13)C 6 H 31 (14)N 5 (15)N 2 (16)O 4
441.26
441.25797
H
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01581
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-121 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 11 (13)C 6 H 29 (14)N 3 (15)N 2 (16)O 5
391.23
391.23108
S
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01582
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-121 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
304.2
(12)C 8 (13)C 6 H 24 (14)N 2 (15)N 2 (16)O 3
304.19904
(12)C 12 (13)C 6 H 31 (14)N 3 (15)N 2 (16)O 5
405.25
405.2467
T
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01583
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex-121 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
Modifications that have monoisotopic mass differences from their respective origins of 304.199039 Da.
PSI-MOD
MOD:01584
modifications with monoisotopic mass differences that are nominally equal at 304.199039 Da
Modifications that have monoisotopic mass differences from their respective origins of 304.199039 Da.
PubMed:18688235
A protein modification that effectively crosslinks an L-serine residue and a glycine residue by an ester bond to form O-glycyl-L-serine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 5 H 7 N 2 O 3
143.12
143.04567
G, S
natural
C-term
uniprot.ptm:PTM-0422
(2S)-2-amino-3-[(aminoacetyl)oxy]propanoic acid
CROSSLNK Glycyl serine ester (Gly-Ser) (interchain with S-...)
CROSSLNK Glycyl serine ester (Ser-Gly) (interchain with G-...)
O-(glycyl)-L-serine
O3-(aminoacetyl)serine
serine glycinate ester
PSI-MOD
MOD:01585
Cross-link 2.
O-glycyl-L-serine
A protein modification that effectively crosslinks an L-serine residue and a glycine residue by an ester bond to form O-glycyl-L-serine.
PubMed:17502423
RESID:AA0495
(2S)-2-amino-3-[(aminoacetyl)oxy]propanoic acid
CROSSLNK Glycyl serine ester (Gly-Ser) (interchain with S-...)
CROSSLNK Glycyl serine ester (Ser-Gly) (interchain with G-...)
O-(glycyl)-L-serine
O3-(aminoacetyl)serine
serine glycinate ester
A protein modification that effectively crosslinks an L-threonine residue and a glycine residue by an ester bond to form O-glycyl-L-threonine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 6 H 9 N 2 O 3
157.15
157.06131
G, T
natural
C-term
uniprot.ptm:PTM-0423
(2S,3R)-2-amino-3-[(aminoacetyl)oxy]butanoic acid
CROSSLNK Glycyl threonine ester (Gly-Thr) (interchain with T-...)
CROSSLNK Glycyl threonine ester (Thr-Gly) (interchain with G-...)
O-(glycyl)-L-threonine
O3-(2-aminoacetyl)threonine
threonine glycinate ester
PSI-MOD
MOD:01586
Cross-link 2.
O-glycyl-L-threonine
A protein modification that effectively crosslinks an L-threonine residue and a glycine residue by an ester bond to form O-glycyl-L-threonine.
PubMed:17502423
RESID:AA0496
(2S,3R)-2-amino-3-[(aminoacetyl)oxy]butanoic acid
CROSSLNK Glycyl threonine ester (Gly-Thr) (interchain with T-...)
CROSSLNK Glycyl threonine ester (Thr-Gly) (interchain with G-...)
O-(glycyl)-L-threonine
O3-(2-aminoacetyl)threonine
threonine glycinate ester
A protein modification that effectively converts an L-serine residue to O-(2-aminoethylphosphoryl)-L-serine.
123.05
C 2 H 6 N 1 O 3 P 1
123.00853
C 5 H 11 N 2 O 5 P 1
210.13
210.04056
S
natural
uniprot.ptm:PTM-0399
(2S)-2-amino-3-([(2-aminoethoxy)(hydroxy)phosphoryl]oxy)propanoic acid
MOD_RES O-(2-aminoethylphosphoryl)serine
O-(2-aminoethylphosphoryl)-L-serine
O3-(2-aminoethylphosphoryl)-L-serine
O3-(phosphoethanolamine)-L-serine
serine ethanolamine phosphate
serine ethanolamine phosphodiester
PSI-MOD
MOD:01587
O-(2-aminoethylphosphoryl)-L-serine
A protein modification that effectively converts an L-serine residue to O-(2-aminoethylphosphoryl)-L-serine.
PubMed:15249686
PubMed:16825186
PubMed:16949362
RESID:AA0497
(2S)-2-amino-3-([(2-aminoethoxy)(hydroxy)phosphoryl]oxy)propanoic acid
MOD_RES O-(2-aminoethylphosphoryl)serine
O-(2-aminoethylphosphoryl)-L-serine
O3-(2-aminoethylphosphoryl)-L-serine
O3-(phosphoethanolamine)-L-serine
serine ethanolamine phosphate
serine ethanolamine phosphodiester
A protein modification that effectively converts an L-serine residue to O-cholinephosphoryl-L-serine.
166.14
C 5 H 13 N 1 O 3 P 1
166.06276
1+
C 8 H 18 N 2 O 5 P 1
253.21
253.09479
S
natural
uniprot.ptm:PTM-0400
2-[([(2S)-2-amino-2-carboxyethoxy][hydroxy]phosphoryl)oxy]-N,N,N-trimethylethanaminium
2-[([(2S)-2-azanyl-2-carboxyethoxy][hydroxy]phosphoryl)oxy]-N,N,N-trimethylethanazanium
MOD_RES O-(2-cholinephosphoryl)serine
O-cholinephosphoryl-L-serine
O3-[(2-[trimethylammonio]ethyl)phosphoryl]-L-serine
O3-phosphocholine-L-serine
serine choline phosphate
serine choline phosphodiester
PSI-MOD
MOD:01588
O-cholinephosphoryl-L-serine
A protein modification that effectively converts an L-serine residue to O-cholinephosphoryl-L-serine.
PubMed:15249686
PubMed:16825186
PubMed:16949362
RESID:AA0498
2-[([(2S)-2-amino-2-carboxyethoxy][hydroxy]phosphoryl)oxy]-N,N,N-trimethylethanaminium
2-[([(2S)-2-azanyl-2-carboxyethoxy][hydroxy]phosphoryl)oxy]-N,N,N-trimethylethanazanium
MOD_RES O-(2-cholinephosphoryl)serine
O-cholinephosphoryl-L-serine
O3-[(2-[trimethylammonio]ethyl)phosphoryl]-L-serine
O3-phosphocholine-L-serine
serine choline phosphate
serine choline phosphodiester
A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine.
244.25
C 10 H 16 N 2 O 5
244.10593
C 13 H 21 N 3 O 7
331.33
331.13794
S
natural
uniprot.ptm:PTM-0547
(2S)-2-amino-3-[(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyl)oxy]propanoic acid
CARBOHYD O-linked (DADDGlc) serine
DADDGlc
O-(2,4-diacetamido-2,4-dideoxy-D-glucosyl)-L-serine
O-(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyl)-L-serine
O-[2,4-bis(acetylamino)]glucosyl-L-serine
O-seryl-beta-2,4-bis(acetylamino)glucoside
O3-(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyl)-L-serine
PSI-MOD
MOD:01589
O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine
A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine.
PubMed:15249686
PubMed:16949362
RESID:AA0499
(2S)-2-amino-3-[(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyl)oxy]propanoic acid
CARBOHYD O-linked (DADDGlc) serine
DADDGlc
O-(2,4-diacetamido-2,4-dideoxy-D-glucosyl)-L-serine
O-(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyl)-L-serine
O-[2,4-bis(acetylamino)]glucosyl-L-serine
O-seryl-beta-2,4-bis(acetylamino)glucoside
O3-(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyl)-L-serine
A protein modification that effectively converts an L-tryptophan residue to 3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan.
204.36
C 15 H 24 N 0 O 0
204.1878
C 26 H 34 N 2 O 1
390.57
390.26712
W
natural
(2S,3aR,8aS)-3a-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid
3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan
LIPID 3'-farnesyl-2',N2-cyclotryptophan
PSI-MOD
MOD:01590
3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to 3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan.
ChEBI:52950
PubMed:18323630
RESID:AA0500
(2S,3aR,8aS)-3a-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-1,2,3,3a,8,8a-hexahydropyrrolo[2,3-b]indole-2-carboxylic acid
3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan
LIPID 3'-farnesyl-2',N2-cyclotryptophan
Modifications that have monoisotopic mass differences from their respective origins of 304.205359 Da.
PSI-MOD
MOD:01591
modifications with monoisotopic mass differences that are nominally equal at 304.205359 Da
Modifications that have monoisotopic mass differences from their respective origins of 304.205359 Da.
PubMed:18688235
Modifications that have monoisotopic mass differences from their respective origins of 304.199-304.206 Da.
PSI-MOD
MOD:01592
modifications with monoisotopic mass differences that are nominally equal at 304.199-304.206 Da
Modifications that have monoisotopic mass differences from their respective origins of 304.199-304.206 Da.
PubMed:18688235
A protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex reagent derivatized residue.
4-methyl-1-methylidenepiperazin-1-ium
PSI-MOD
MOD:01593
iTRAQ8plex reporter fragment
A protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex reagent derivatized residue.
PubMed:18688235
4-methyl-1-methylidenepiperazin-1-ium
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-113 reagent derivatized residue.
1+
(12)C 6 H 13 (14)N 2
113.11
113.10732
X
artifact
4-methyl-1-methylidenepiperazin-1-ium
PSI-MOD
MOD:01594
iTRAQ8plex-113 reporter fragment
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-113 reagent derivatized residue.
PubMed:18688235
4-methyl-1-methylidenepiperazin-1-ium
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-114 reagent derivatized residue.
1+
(12)C 5 (13)C 1 H 13 (14)N 2
114.11
114.11068
X
artifact
4-methyl-1-methylidenepiperazin-1-ium
PSI-MOD
MOD:01595
iTRAQ8plex-114 reporter fragment
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-114 reagent derivatized residue.
PubMed:18688235
4-methyl-1-methylidenepiperazin-1-ium
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-115 reagent derivatized residue.
1+
(12)C 5 (13)C 1 H 13 (14)N 1 (15)N 1
115.11
115.10771
X
artifact
4-methyl-1-methylidenepiperazin-1-ium
PSI-MOD
MOD:01596
iTRAQ8plex-115 reporter fragment
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-115 reagent derivatized residue.
PubMed:18688235
4-methyl-1-methylidenepiperazin-1-ium
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-116 reagent derivatized residue.
1+
(12)C 4 (13)C 2 H 13 (14)N 1 (15)N 1
116.11
116.11107
X
artifact
4-methyl-1-methylidenepiperazin-1-ium
PSI-MOD
MOD:01597
iTRAQ8plex-116 reporter fragment
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-116 reagent derivatized residue.
PubMed:18688235
4-methyl-1-methylidenepiperazin-1-ium
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-117 reagent derivatized residue.
1+
(12)C 3 (13)C 3 H 13 (14)N 1 (15)N 1
117.11
117.114426
X
artifact
4-methyl-1-methylidenepiperazin-1-ium
PSI-MOD
MOD:01598
iTRAQ8plex-117 reporter fragment
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-117 reagent derivatized residue.
PubMed:18688235
4-methyl-1-methylidenepiperazin-1-ium
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-118 reagent derivatized residue.
1+
(12)C 3 (13)C 3 H 13 (15)N 2
118.11
118.11146
X
artifact
4-methyl-1-methylidenepiperazin-1-ium
PSI-MOD
MOD:01599
iTRAQ8plex-118 reporter fragment
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-118 reagent derivatized residue.
PubMed:18688235
4-methyl-1-methylidenepiperazin-1-ium
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-119 reagent derivatized residue.
1+
(12)C 2 (13)C 4 H 13 (15)N 2
119.11
119.114815
X
artifact
4-methyl-1-methylidenepiperazin-1-ium
PSI-MOD
MOD:01600
iTRAQ8plex-119 reporter fragment
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-119 reagent derivatized residue.
PubMed:18688235
4-methyl-1-methylidenepiperazin-1-ium
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-121 reagent derivatized residue.
1+
(13)C 6 H 13 (15)N 2
121.12
121.12152
X
artifact
4-methyl-1-methylidenepiperazin-1-ium
PSI-MOD
MOD:01601
iTRAQ8plex-121 reporter fragment
The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-121 reagent derivatized residue.
PubMed:18688235
4-methyl-1-methylidenepiperazin-1-ium
A protein modification that effectively converts an L-lysine residue, and an L-methionine residue to S-(L-lysyl)-L-methionine sulfilimine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 11 H 19 N 3 O 2 S 1
257.35
257.1198
K, M
natural
uniprot.ptm:PTM-0401
(2S)-2-amino-6-([(E)-[(3S)-3-amino-3-carboxypropyl](methyl)-lambda(4)-sulfanylidene]amino)hexanoic acid
(E)-N6-([(3S)-3-amino-3-carboxypropyl](methyl)-lambda(4)-sulfanylidene)-L-lysine
S-(L-lysyl)-L-methionine sulfilimine
S-lysyl-methionine
PSI-MOD
MOD:01602
Cross-link 2.
S-(L-lysyl)-L-methionine sulfilimine
A protein modification that effectively converts an L-lysine residue, and an L-methionine residue to S-(L-lysyl)-L-methionine sulfilimine.
PubMed:12011424
PubMed:15951440
PubMed:19729652
RESID:AA0501
(2S)-2-amino-6-([(E)-[(3S)-3-amino-3-carboxypropyl](methyl)-lambda(4)-sulfanylidene]amino)hexanoic acid
(E)-N6-([(3S)-3-amino-3-carboxypropyl](methyl)-lambda(4)-sulfanylidene)-L-lysine
S-(L-lysyl)-L-methionine sulfilimine
S-lysyl-methionine
A protein modification that effectively converts an L-lysine residue to 2x(15)N labeled L-lysine.
1.99
(14)N -2 (15)N 2
1.99407
C 6 H 12 (15)N 2 O 1
130.09
130.08904
K
artifact
Unimod:995
PSI-MOD
MOD:01603
2x(15)N labeled L-lysine
A protein modification that effectively converts an L-lysine residue to 2x(15)N labeled L-lysine.
PubMed:18688235
URL:http://www.sigmaaldrich.com/catalog/ProductDetail.do?N4=609021|ALDRICH&N5=SEARCH_CONCAT_PNO|BRAND_KEY&F=SPEC&lang=en_US0.000000E+000
A protein modification that effectively converts an L-arginine residue to 4x(15)N labeled L-arginine.
3.99
(14)N -4 (15)N 4
3.98814
C 6 H 12 (15)N 4 O 1
160.09
160.08925
R
artifact
PSI-MOD
MOD:01604
4x(15)N labeled L-arginine
A protein modification that effectively converts an L-arginine residue to 4x(15)N labeled L-arginine.
PubMed:18688235
URL:http://www.sigmaaldrich.com/catalog/ProductDetail.do?N4=600113|ALDRICH&N5=SEARCH_CONCAT_PNO|BRAND_KEY&F=SPEC&lang=en_US0.000000E+000
A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl 2-aminoadipic acid.
143.14
C 6 H 9 N 1 O 3
143.05824
C 11 H 16 N 2 O 6
272.26
272.10083
E
natural
uniprot.ptm:PTM-0406
(2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanedioic acid
5-glutamyl 2-aminoadipic acid
MOD_RES 5-glutamyl 2-aminoadipic acid
N2-(gamma-glutamyl)-2-aminoadipic acid
N2-(isoglutamyl)-2-aminoadipic acid
PSI-MOD
MOD:01605
5-glutamyl 2-aminoadipic acid
A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl 2-aminoadipic acid.
ChEBI:78503
PubMed:19620981
RESID:AA0502
(2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanedioic acid
5-glutamyl 2-aminoadipic acid
MOD_RES 5-glutamyl 2-aminoadipic acid
N2-(gamma-glutamyl)-2-aminoadipic acid
N2-(isoglutamyl)-2-aminoadipic acid
A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl 2-aminoadipic 6-phosphoric anhydride.
223.12
C 6 H 10 N 1 O 6 P 1
223.02457
C 11 H 17 N 2 O 9 P 1
352.24
352.06717
E
hypothetical
(2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)-6-oxo-6-(phosphonooxy)hexanoic acid
5-glutamyl 2-aminoadipic 6-phosphoric anhydride
PSI-MOD
MOD:01606
5-glutamyl 2-aminoadipic 6-phosphoric anhydride
A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl 2-aminoadipic 6-phosphoric anhydride.
PubMed:19620981
RESID:AA0503
(2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)-6-oxo-6-(phosphonooxy)hexanoic acid
5-glutamyl 2-aminoadipic 6-phosphoric anhydride
A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl allysine.
127.14
C 6 H 9 N 1 O 2
127.06333
C 11 H 16 N 2 O 5
256.26
256.10593
E
hypothetical
(2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)-6-oxohexanoic acid
2-(5-glutamyl)amino-6-oxohexanoic acid
5-glutamyl allysine
N2-(gamma-glutamyl)allysine
N2-(isoglutamyl)allysine
alpha-(gamma-glutamyl)allysine
PSI-MOD
MOD:01607
5-glutamyl allysine
A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl allysine.
PubMed:19620981
RESID:AA0504
(2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)-6-oxohexanoic acid
2-(5-glutamyl)amino-6-oxohexanoic acid
5-glutamyl allysine
N2-(gamma-glutamyl)allysine
N2-(isoglutamyl)allysine
alpha-(gamma-glutamyl)allysine
A protein modification that effectively converts an L-glutamic acid residue to N2-(L-isoglutamyl)-L-lysine. This is not an isopeptide cross-link.
128.18
C 6 H 12 N 2 O 1
128.09496
C 11 H 19 N 3 O 4
257.29
257.13754
E
natural
uniprot.ptm:PTM-0407
(2S)-6-amino-2-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid
5-glutamyl N2-lysine
MOD_RES 5-glutamyl N2-lysine
N2-(L-isoglutamyl)-L-lysine
N2-(gamma-glutamyl)lysine
alpha-(gamma-glutamyl)lysine
gamma-glutamyl N2-lysine
PSI-MOD
MOD:01608
N2-(L-isoglutamyl)-L-lysine
A protein modification that effectively converts an L-glutamic acid residue to N2-(L-isoglutamyl)-L-lysine. This is not an isopeptide cross-link.
PubMed:19620981
RESID:AA0505
(2S)-6-amino-2-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid
5-glutamyl N2-lysine
MOD_RES 5-glutamyl N2-lysine
N2-(L-isoglutamyl)-L-lysine
N2-(gamma-glutamyl)lysine
alpha-(gamma-glutamyl)lysine
gamma-glutamyl N2-lysine
A protein modification that effectively converts an L-tryptophan residue to 7'-hydroxy-2'-alpha-mannosyl-L-tryptophan.
178.14
C 6 H 10 N 0 O 6
178.04774
C 17 H 20 N 2 O 7
364.35
364.12704
W
natural
uniprot.ptm:PTM-0504
(2S)-2-amino-3-[7-hydroxy-2-(alpha-D-mannopyranosyl)-1H-indol-3-yl]propanoic acid
7'-hydroxy-2'-alpha-mannosyl-L-tryptophan
CARBOHYD C-linked (Man) hydroxytryptophan
PSI-MOD
MOD:01609
7'-hydroxy-2'-alpha-mannosyl-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to 7'-hydroxy-2'-alpha-mannosyl-L-tryptophan.
PubMed:19584055
RESID:AA0506
(2S)-2-amino-3-[7-hydroxy-2-(alpha-D-mannopyranosyl)-1H-indol-3-yl]propanoic acid
7'-hydroxy-2'-alpha-mannosyl-L-tryptophan
CARBOHYD C-linked (Man) hydroxytryptophan
A protein modification that effectively converts an L-threonine residue to L-threonine methyl ester.
14.03
C 1 H 2 N 0 O 0
14.01565
C 5 H 10 N 1 O 3
132.14
132.06607
T
natural
C-term
uniprot.ptm:PTM-0412
L-threonine methyl ester
MOD_RES Threonine methyl ester
methyl (2S,3R)-2-amino-3-hydroxybutanoate
methyl L-threoninate
PSI-MOD
MOD:01610
L-threonine methyl ester
A protein modification that effectively converts an L-threonine residue to L-threonine methyl ester.
PubMed:19745839
RESID:AA0507
L-threonine methyl ester
MOD_RES Threonine methyl ester
methyl (2S,3R)-2-amino-3-hydroxybutanoate
methyl L-threoninate
A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FMN.
452.32
C 17 H 17 N 4 O 9 P 1 S 0
452.0733
C 26 H 29 N 8 O 11 P 1 S 1
692.6
692.1414
C, H
natural
6-((R)-2-amino-2-carboxyethyl)sulfanyl-8alpha-[4-((S)-2-amino-2-carboxyethyl)imidazol-3-yl]-riboflavin 5'-trihydrogen phosphate
6-(S-L-cysteinyl)-8alpha-(N3'-L-histidino)-FMN
6-(S-cysteinyl)-8alpha-(N(delta)-histidyl)-FMN
6-(S-cysteinyl)-8alpha-(N(pi)-histidyl)-FMN
6-(S-cysteinyl)-8alpha-(N3'-histidyl)-FMN
6-(S-cysteinyl)-8alpha-(pros-histidyl)-FMN
BINDING FMN (covalent; via 2 links)
BINDING FMN (covalent; via 2 links, pros nitrogen)
PSI-MOD
MOD:01611
Cross-link 2.
6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FMN
A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FMN.
PubMed:17935335
RESID:AA0508
6-((R)-2-amino-2-carboxyethyl)sulfanyl-8alpha-[4-((S)-2-amino-2-carboxyethyl)imidazol-3-yl]-riboflavin 5'-trihydrogen phosphate
6-(S-L-cysteinyl)-8alpha-(N3'-L-histidino)-FMN
6-(S-cysteinyl)-8alpha-(N(delta)-histidyl)-FMN
6-(S-cysteinyl)-8alpha-(N(pi)-histidyl)-FMN
6-(S-cysteinyl)-8alpha-(N3'-histidyl)-FMN
6-(S-cysteinyl)-8alpha-(pros-histidyl)-FMN
BINDING FMN (covalent; via 2 links)
BINDING FMN (covalent; via 2 links, pros nitrogen)
A protein modification that effectively converts an L-tyrosine residue to 3'-iodo-L-tyrosine.
125.9
C 0 H -1 I 1 N 0 O 0
125.896645
C 9 H 8 I 1 N 1 O 2
289.07
288.95996
Y
natural
uniprot.ptm:PTM-0411
(2S)-2-amino-3-(4-hydroxy-3-iodophenyl)propanoic acid
3'-iodo-L-tyrosine
3-iodo-L-tyrosine
3-iodotyrosine
4-hydroxy-3-iodo-phenylalanine
MIT
MOD_RES Iodotyrosine
PSI-MOD
MOD:01612
3'-iodo-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to 3'-iodo-L-tyrosine.
ChEBI:27847
PubMed:8995307
RESID:AA0509
(2S)-2-amino-3-(4-hydroxy-3-iodophenyl)propanoic acid
3'-iodo-L-tyrosine
3-iodo-L-tyrosine
3-iodotyrosine
4-hydroxy-3-iodo-phenylalanine
MIT
MOD_RES Iodotyrosine
A protein modification that effectively converts an L-tyrosine residue to 3',5'-diiodo-L-tyrosine.
251.79
C 0 H -2 I 2 N 0 O 0
251.79329
C 9 H 7 I 2 N 1 O 2
414.97
414.85663
Y
natural
uniprot.ptm:PTM-0408
(2S)-2-amino-3-(4-hydroxy-3,5-diiodophenyl)propanoic acid
3',5'-diiodo-L-tyrosine
3,5-diiodo-L-tyrosine
3,5-diiodotyrosine
DIT
MOD_RES Diiodotyrosine
iodogorgoic acid
PSI-MOD
MOD:01613
3',5'-diiodo-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to 3',5'-diiodo-L-tyrosine.
ChEBI:15768
PubMed:8995307
RESID:AA0510
(2S)-2-amino-3-(4-hydroxy-3,5-diiodophenyl)propanoic acid
3',5'-diiodo-L-tyrosine
3,5-diiodo-L-tyrosine
3,5-diiodotyrosine
DIT
MOD_RES Diiodotyrosine
iodogorgoic acid
A protein modification that effectively converts a glycine residue to glycyl phospho-5'-adenosine.
329.21
C 10 H 12 N 5 O 6 P 1
329.05252
C 12 H 16 N 6 O 8 P 1
403.27
403.07672
G
natural
C-term
uniprot.ptm:PTM-0409
(2-aminoacetyl)oxy-([(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy)phosphinic acid
([(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl)-2-aminoethanoate
5'-adenylic-glyinate
MOD_RES Glycyl adenylate
aminoacetyl [5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl hydrogen phosphate
glycine monoanhydride with 5'-adenylic acid
glycyl 5'-adenylate
glycyl adenosine-5'-phosphate
glycyl phospho-5'-adenosine
glycyladenylate
PSI-MOD
MOD:01614
glycyl phospho-5'-adenosine
A protein modification that effectively converts a glycine residue to glycyl phospho-5'-adenosine.
PubMed:16388576
PubMed:9632726
RESID:AA0511
(2-aminoacetyl)oxy-([(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy)phosphinic acid
([(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl)-2-aminoethanoate
5'-adenylic-glyinate
MOD_RES Glycyl adenylate
aminoacetyl [5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl hydrogen phosphate
glycine monoanhydride with 5'-adenylic acid
glycyl 5'-adenylate
glycyl adenosine-5'-phosphate
glycyl phospho-5'-adenosine
glycyladenylate
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a dithioester bond to form glycyl cysteine dithioester.
14.05
C 0 H -2 N 0 O -1 S 1
13.961506
C 5 H 7 N 2 O 2 S 2
191.24
190.99489
C, G
hypothetical
C-term
uniprot.ptm:PTM-0410
(2R)-2-amino-3-[(aminoacetyl)disulfanyl]propanoic acid
2-(glycyldithio)alanine
S-glycyl cysteine persulfide
S-glycyl thiocysteine
glycyl cysteine dithioester
thioglycine cysteine disulfide
PSI-MOD
MOD:01615
Cross-link 2.
glycyl cysteine dithioester
A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a dithioester bond to form glycyl cysteine dithioester.
PubMed:11438688
PubMed:16388576
RESID:AA0512
(2R)-2-amino-3-[(aminoacetyl)disulfanyl]propanoic acid
2-(glycyldithio)alanine
S-glycyl cysteine persulfide
S-glycyl thiocysteine
glycyl cysteine dithioester
thioglycine cysteine disulfide
A protein modification that effectively cross-links two L-cysteine residues and adds three sulfur atoms to form trithiocystine.
94.16
C 0 H -2 N 0 O 0 S 3
93.900566
C 6 H 8 N 2 O 2 S 5
300.44
299.91895
C, C
natural
uniprot.ptm:PTM-0417
(2R,2'R)-3,3'-pentasulfane-1,5-diylbis(2-aminopropanoic acid)
3,3'-pentathiobisalanine
bis(2-amino-2-carboxyethyl)pentasulfide
trithiocystine
PSI-MOD
MOD:01616
Cross-link 2.
trithiocystine
A protein modification that effectively cross-links two L-cysteine residues and adds three sulfur atoms to form trithiocystine.
PubMed:19438211
RESID:AA0513
(2R,2'R)-3,3'-pentasulfane-1,5-diylbis(2-aminopropanoic acid)
3,3'-pentathiobisalanine
bis(2-amino-2-carboxyethyl)pentasulfide
trithiocystine
A protein modification that effectively converts an L-threonine residue to O-(6-phosphomannosyl)-L-threonine.
242.12
C 6 H 11 N 0 O 8 P 1
242.01915
C 10 H 18 N 1 O 10 P 1
343.22
343.06683
T
natural
uniprot.ptm:PTM-0596
(2S,3R)-2-amino-3-[6-phosphonooxy-alpha-D-mannopyranosyloxy]butanoic acid
CARBOHYD O-linked (Man6P) threonine
O-(6-phosphomannosyl)-L-threonine
O3-(6-phosphomannosyl)threonine
PSI-MOD
MOD:01617
O-(6-phosphomannosyl)-L-threonine
A protein modification that effectively converts an L-threonine residue to O-(6-phosphomannosyl)-L-threonine.
PubMed:20044576
RESID:AA0514
(2S,3R)-2-amino-3-[6-phosphonooxy-alpha-D-mannopyranosyloxy]butanoic acid
CARBOHYD O-linked (Man6P) threonine
O-(6-phosphomannosyl)-L-threonine
O3-(6-phosphomannosyl)threonine
A protein modification that effectively converts an L-alaine residue and an L-asparagine residue to L-alanyl-L-isoaspartyl cyclopeptide.
-17.03
C 0 H -3 N -1 O 0
-17.026548
C 7 H 9 N 2 O 3
169.16
169.06131
A, N
natural
N-term
uniprot.ptm:PTM-0418
(2S,5S)-2-methyl-3,7-dioxo-1,4-diazepane-5-carboxylic acid
1,4.2-anhydro(L-alanyl-L-aspartic acid)
CROSSLNK Alanine isoaspartyl cyclopeptide (Ala-Asn)
L-alanyl-L-isoaspartyl cyclopeptide
PSI-MOD
MOD:01618
Cross-link 2.
L-alanyl-L-isoaspartyl cyclopeptide
A protein modification that effectively converts an L-alaine residue and an L-asparagine residue to L-alanyl-L-isoaspartyl cyclopeptide.
PubMed:19928958
PubMed:3207697
RESID:AA0515
(2S,5S)-2-methyl-3,7-dioxo-1,4-diazepane-5-carboxylic acid
1,4.2-anhydro(L-alanyl-L-aspartic acid)
CROSSLNK Alanine isoaspartyl cyclopeptide (Ala-Asn)
L-alanyl-L-isoaspartyl cyclopeptide
A protein modification that crosslinks two cysteine residues by formation of a chain of two or more bonded sulfur atoms.
PSI-MOD
MOD:01619
multisulfide crosslinked residues
A protein modification that crosslinks two cysteine residues by formation of a chain of two or more bonded sulfur atoms.
PubMed:18688235
A protein modification that crosslinks two cysteine residues by formation of a chain of three or more bonded sulfur atoms.
PSI-MOD
MOD:01620
polysulfide crosslinked residues
A protein modification that crosslinks two cysteine residues by formation of a chain of three or more bonded sulfur atoms.
PubMed:18688235
A protein modification that crosslinks two or more amino acid residues by forming an adduct with a compound containing a flavin group.
PSI-MOD
MOD:01621
flavin crosslinked residues
A protein modification that crosslinks two or more amino acid residues by forming an adduct with a compound containing a flavin group.
PubMed:18688235
A protein modification that effectively converts an L-tryptophan residue to one of several monohydroxylated tryptophan residues, including 3-hydroxy-L-tryptophan and 7'-hydroxy-L-tryptophan.
16.0
C 0 H 0 N 0 O 1
15.994915
C 11 H 10 N 2 O 2
202.21
202.07423
W
natural
Unimod:35
oxyw
PSI-MOD
Oxidation
MOD:01622
monohydroxylated tryptophan
A protein modification that effectively converts an L-tryptophan residue to one of several monohydroxylated tryptophan residues, including 3-hydroxy-L-tryptophan and 7'-hydroxy-L-tryptophan.
OMSSA:90
Unimod:35#W
oxyw
Oxidation
A protein modification that effectively converts a glycine residue to a C-terminal 1-thioglycine.
16.06
C 0 H 0 N 0 O -1 S 1
15.977156
C 2 H 3 N 1 S 1
73.11
72.99862
G
natural
C-term
PSI-MOD
MOD:01623
1-thioglycine (C-terminal)
A protein modification that effectively converts a glycine residue to a C-terminal 1-thioglycine.
PubMed:11463785
PubMed:19145231
PubMed:9367957
RESID:AA0265#var
A protein modification that crosslinks an asparagine and the following glycine residue with the formation of (2-aminosuccinimidyl)acetic acid and the release of ammonia.
-17.03
C 0 H -3 N -1 O 0
-17.026548
C 6 H 6 N 2 O 3
154.13
154.03784
G, N
hypothetical
uniprot.ptm:PTM-0450
(2-aminosuccinimidyl)acetic acid
(3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid
CROSSLNK (2-aminosuccinimidyl)acetic acid (Asn-Gly)
N-(2-aminosuccinyl)glycine
[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]acetic acid
anhydroaspartyl glycine
aspartimide glycine
PSI-MOD
MOD:01624
Cross-link 2.
(2-aminosuccinimidyl)acetic acid (Asn)
A protein modification that crosslinks an asparagine and the following glycine residue with the formation of (2-aminosuccinimidyl)acetic acid and the release of ammonia.
PubMed:10801322
PubMed:2015294
RESID:AA0441#ASN
(2-aminosuccinimidyl)acetic acid
(3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid
CROSSLNK (2-aminosuccinimidyl)acetic acid (Asn-Gly)
N-(2-aminosuccinyl)glycine
[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]acetic acid
anhydroaspartyl glycine
aspartimide glycine
A protein modification that effectively converts a glycine residue to 1-thioglycine.
16.06
C 0 H 0 N 0 O -1 S 1
15.977156
G
natural
1-thioglycine
2-amino-1-sulfanylethanone
MOD_RES 1-thioglycine
S(O)Gly
aminoethanethioic acid
aminothioacetic acid
PSI-MOD
Carboxy->Thiocarboxy
thiocarboxylic acid
MOD:01625
This modification occurs naturally in two forms. At an interior peptide location (MOD:00270) it exists as aminoethanethionic acid, or aminoethanethioic O-acid. At the C-terminal (MOD:01623) it exists as aminoethanethiolic acid, or aminoethanethioic S-acid [JSG].
1-thioglycine
A protein modification that effectively converts a glycine residue to 1-thioglycine.
PubMed:11463785
PubMed:9367957
RESID:AA0265
1-thioglycine
2-amino-1-sulfanylethanone
MOD_RES 1-thioglycine
S(O)Gly
aminoethanethioic acid
aminothioacetic acid
Carboxy->Thiocarboxy
thiocarboxylic acid
A protein modification that forms L-cystine by forming a disulfide bond that either cross-links two peptidyl L-cysteine residues, or modifies a peptidyl cysteine with a free cysteine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
natural
(2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid)
3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid)
3,3'-dithiobis(2-aminopropanoic acid)
3,3'-dithiobisalanine
3,3'-dithiodialanine
Cys2
Cystine ((Cys)2)
L-cystine
beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide
beta,beta'-dithiodialanine
bis(alpha-aminopropionic acid)-beta-disulfide
bis(beta-amino-beta-carboxyethyl)disulfide
dicysteine
PSI-MOD
2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid
MOD:01626
This modification occurs naturally in two forms. It exists as a disulfide cross-link of two cysteine residues (MOD:00034), or as a disulfide cross-link of a cysteine residues and a free cysteine (MOD:00765).
L-cystine
A protein modification that forms L-cystine by forming a disulfide bond that either cross-links two peptidyl L-cysteine residues, or modifies a peptidyl cysteine with a free cysteine.
ChEBI:16283
PubMed:1988019
PubMed:2001356
PubMed:2076469
PubMed:3083866
PubMed:366603
PubMed:7918467
PubMed:8344916
RESID:AA0025
(2R,2'R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid)
3,3'-disulfane-1,2-diylbis(2-azanylpropanoic acid)
3,3'-dithiobis(2-aminopropanoic acid)
3,3'-dithiobisalanine
3,3'-dithiodialanine
Cys2
Cystine ((Cys)2)
L-cystine
beta,beta'-diamino-beta,beta'-dicarboxydiethyldisulfide
beta,beta'-dithiodialanine
bis(alpha-aminopropionic acid)-beta-disulfide
bis(beta-amino-beta-carboxyethyl)disulfide
dicysteine
2-amino-3-(2-amino-2-carboxy-ethyl)disulfanyl-propanoic acid
A protein modification that forms L-cysteinyl-L-selenocysteine either by the natural process of cross-linking an L-cysteine residue and an L-selenocysteine residue, or by the hypothetical process of substituting a selenium for a sulfur atom in cystine.
C 6 H 8 N 2 O 2 S 1 Se 1
251.17
251.94717
C, X
natural
PSI-MOD
MOD:01627
Cross-link 2.
L-cysteinyl-L-selenocysteine
A protein modification that forms L-cysteinyl-L-selenocysteine either by the natural process of cross-linking an L-cysteine residue and an L-selenocysteine residue, or by the hypothetical process of substituting a selenium for a sulfur atom in cystine.
PubMed:12911312
PubMed:18688235
A protein modification that forms (2-aminosuccinimidyl)acetic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following glycine residue.
C 6 H 6 N 2 O 3
154.13
154.03784
G, X
hypothetical
PSI-MOD
MOD:01628
Cross-link 2; this cross-link is formed by the condensation of an aspartic acid residue or an asparagine residue with the alpha-amido of the following residue.
(2-aminosuccinimidyl)acetic acid
A protein modification that forms (2-aminosuccinimidyl)acetic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following glycine residue.
PubMed:10801322
PubMed:18688235
A protein modification that forms cyclo[(prolylserin)-O-yl] cysteinate by the natural process of cross-linking an L-cysteine residue an L-proline residue, and an L-serine residue, or by effectively modifying a cysteine residue.
C 11 H 16 N 3 O 4 S 1
286.33
286.08615
X
natural
C-term
(3,6-dioxopyrrolo[4,5-a]piperazin-2-yl)methyl cysteinate
MOD_RES Cyclo[(prolylserin)-O-yl] cysteinate
[(3S,8aS)-1,4-dioxooctahydropyrrolo[1,2-a]pyrazin-3-yl]methyl (2R)-2-amino-3-sulfanylpropanoate
cyclo[(prolylserin)-O-yl] cysteinate
PSI-MOD
MOD:01629
cyclo[(prolylserin)-O-yl] cysteinate
A protein modification that forms cyclo[(prolylserin)-O-yl] cysteinate by the natural process of cross-linking an L-cysteine residue an L-proline residue, and an L-serine residue, or by effectively modifying a cysteine residue.
PubMed:7961166
RESID:AA0489
(3,6-dioxopyrrolo[4,5-a]piperazin-2-yl)methyl cysteinate
MOD_RES Cyclo[(prolylserin)-O-yl] cysteinate
[(3S,8aS)-1,4-dioxooctahydropyrrolo[1,2-a]pyrazin-3-yl]methyl (2R)-2-amino-3-sulfanylpropanoate
cyclo[(prolylserin)-O-yl] cysteinate
A protein modification that effectively crosslinks either an L-glutamine residue or an L-glutamic acid residue with an L-lysine residue by an isopeptide bond to form N6-(L-isoglutamyl)-L-lysine .
C 11 H 17 N 3 O 3
239.27
239.12698
K, X
natural
uniprot.ptm:PTM-0397
(2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid
2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid
5-glutamyl N6-lysine
N alpha -(gamma-Glutamyl)-lysine
N(epsilon)-(gamma-glutamyl)lysine
N6-(L-isoglutamyl)-L-lysine
PSI-MOD
MOD:01630
Cross-link 2.
N6-(L-isoglutamyl)-L-lysine
A protein modification that effectively crosslinks either an L-glutamine residue or an L-glutamic acid residue with an L-lysine residue by an isopeptide bond to form N6-(L-isoglutamyl)-L-lysine .
ChEBI:21863
DeltaMass:0
PubMed:2461365
PubMed:5637041
PubMed:5656070
PubMed:8598899
RESID:AA0124
(2S)-2-amino-6-([(4S)-4-amino-4-carboxybutanoyl]amino)hexanoic acid
2-azanyl-6-([4-azanyl-4-carboxybutanoyl]azanyl)hexanoic acid
5-glutamyl N6-lysine
N alpha -(gamma-Glutamyl)-lysine
N(epsilon)-(gamma-glutamyl)lysine
N6-(L-isoglutamyl)-L-lysine
A protein modification that effectively removes or replaces an L-alanine.
-71.08
C -3 H -5 N -1 O -1
-71.03712
A
natural
PSI-MOD
MOD:01631
This represents the loss or replacement of an L-alanine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-alanine removal
A protein modification that effectively removes or replaces an L-alanine.
PubMed:18688235
A protein modification that effectively removes or replaces an L-arginine.
-156.19
C -6 H -12 N -4 O -1
-156.1011
R
natural
PSI-MOD
MOD:01632
This represents the loss or replacement of an L-arginine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-arginine removal
A protein modification that effectively removes or replaces an L-arginine.
PubMed:18688235
A protein modification that effectively removes or replaces an L-asparagine.
-114.1
C -4 H -6 N -2 O -2
-114.04293
N
natural
PSI-MOD
MOD:01633
This represents the loss or replacement of an L-asparagine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-asparagine removal
A protein modification that effectively removes or replaces an L-asparagine.
PubMed:18688235
A protein modification that effectively removes or replaces an L-aspartic acid.
-115.09
C -4 H -5 N -1 O -3
-115.02694
D
natural
PSI-MOD
MOD:01634
This represents the loss or replacement of an L-aspartic acid residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-aspartic acid removal
A protein modification that effectively removes or replaces an L-aspartic acid.
PubMed:18688235
A protein modification that effectively removes or replaces an L-cysteine.
-103.14
C -3 H -5 N -1 O -1 S -1
-103.009186
C
natural
PSI-MOD
MOD:01635
This represents the loss or replacement of an L-cysteine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-cysteine removal
A protein modification that effectively removes or replaces an L-cysteine.
PubMed:18688235
A protein modification that effectively removes or replaces an L-glutamic acid.
-129.12
C -5 H -7 N -1 O -3
-129.04259
E
natural
PSI-MOD
MOD:01636
This represents the loss or replacement of an L-glutamic acid residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-glutamic acid removal
A protein modification that effectively removes or replaces an L-glutamic acid.
PubMed:18688235
A protein modification that effectively removes or replaces an L-glutamine.
-128.13
C -5 H -8 N -2 O -2
-128.05858
Q
natural
PSI-MOD
MOD:01637
This represents the loss or replacement of an L-glutamine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-glutamine removal
A protein modification that effectively removes or replaces an L-glutamine.
PubMed:18688235
A protein modification that effectively removes or replaces a glycine.
-57.05
C -2 H -3 N -1 O -1
-57.021465
G
natural
PSI-MOD
MOD:01638
This represents the loss or replacement of an glycine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
glycine removal
A protein modification that effectively removes or replaces a glycine.
PubMed:18688235
A protein modification that effectively removes or replaces an L-histidine.
-137.14
C -6 H -7 N -3 O -1
-137.05891
H
natural
PSI-MOD
MOD:01639
This represents the loss or replacement of an L-histidine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-histidine removal
A protein modification that effectively removes or replaces an L-histidine.
PubMed:18688235
A protein modification that effectively removes or replaces an L-isoleucine.
-113.16
C -6 H -11 N -1 O -1
-113.08406
I
natural
PSI-MOD
MOD:01640
This represents the loss or replacement of an L-isoleucine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-isoleucine removal
A protein modification that effectively removes or replaces an L-isoleucine.
PubMed:18688235
A protein modification that effectively removes or replaces an L-leucine.
-113.16
C -6 H -11 N -1 O -1
-113.08406
L
natural
PSI-MOD
MOD:01641
This represents the loss or replacement of an L-leucine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-leucine removal
A protein modification that effectively removes or replaces an L-leucine.
PubMed:18688235
A protein modification that effectively removes or replaces an L-lysine.
-128.18
C -6 H -12 N -2 O -1
-128.09496
K
natural
PSI-MOD
MOD:01642
This represents the loss or replacement of an L-lysine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-lysine removal
A protein modification that effectively removes or replaces an L-lysine.
PubMed:18688235
A protein modification that effectively removes or replaces an L-methionine.
-131.19
C -5 H -9 N -1 O -1 S -1
-131.04048
M
natural
Unimod:765
ntermmcleave
PSI-MOD
Met-loss
MOD:01643
This represents the loss or replacement of an L-methionine residue in a polypeptide, including initiator methionine removal in eukaryotes. It may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution [JSG].
L-methionine removal
A protein modification that effectively removes or replaces an L-methionine.
OMSSA:9
PubMed:3327521
Unimod:765
ntermmcleave
Met-loss
A protein modification that effectively removes or replaces an L-phenylalanine.
-147.18
C -9 H -9 N -1 O -1
-147.06842
F
natural
PSI-MOD
MOD:01644
This represents the loss or replacement of an L-phenylalanine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-phenylalanine removal
A protein modification that effectively removes or replaces an L-phenylalanine.
PubMed:18688235
A protein modification that effectively removes or replaces an L-proline.
-97.12
C -5 H -7 N -1 O -1
-97.052765
P
natural
PSI-MOD
MOD:01645
This represents the loss or replacement of an L-proline residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-proline removal
A protein modification that effectively removes or replaces an L-proline.
PubMed:18688235
A protein modification that effectively removes or replaces an L-serine.
-87.08
C -3 H -5 N -1 O -2
-87.03203
S
natural
PSI-MOD
MOD:01646
This represents the loss or replacement of an L-serine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-serine removal
A protein modification that effectively removes or replaces an L-serine.
PubMed:18688235
A protein modification that effectively removes or replaces an L-threonine.
-101.1
C -4 H -7 N -1 O -2
-101.047676
T
natural
PSI-MOD
MOD:01647
This represents the loss or replacement of an L-threonine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-threonine removal
A protein modification that effectively removes or replaces an L-threonine.
PubMed:18688235
A protein modification that effectively removes or replaces an L-tryptophan.
-186.21
C -11 H -10 N -2 O -1
-186.07932
W
natural
PSI-MOD
MOD:01648
This represents the loss or replacement of an L-tryptophan residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-tryptophan removal
A protein modification that effectively removes or replaces an L-tryptophan.
PubMed:18688235
A protein modification that effectively removes or replaces an L-tyrosine.
-163.18
C -9 H -9 N -1 O -2
-163.06332
Y
natural
PSI-MOD
MOD:01649
This represents the loss or replacement of an L-tyrosine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-tyrosine removal
A protein modification that effectively removes or replaces an L-tyrosine.
PubMed:18688235
A protein modification that effectively removes or replaces an L-valine.
-99.13
C -5 H -9 N -1 O -1
-99.06841
V
natural
PSI-MOD
MOD:01650
This represents the loss or replacement of an L-valine residue in a polypeptide, and may be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
L-valine removal
A protein modification that effectively removes or replaces an L-valine.
PubMed:18688235
A protein modification that effectively removes a natural, standard, encoded residue.
X
natural
PSI-MOD
MOD:01651
This represents the loss of an encoded residue in a polypeptide.
natural, standard, encoded residue removal
A protein modification that effectively removes a natural, standard, encoded residue.
PubMed:18688235
A protein modification that is produced by formation of an adduct with a sulfonyl halide compound used as a reagent.
X
artifact
PSI-MOD
MOD:01652
These reagents typically react with N6-amino group of lysine residues and a free alpha-amino group of a peptide.
sulfonyl halide reagent derivatized residue
A protein modification that is produced by formation of an adduct with a sulfonyl halide compound used as a reagent.
PubMed:18688235
A protein modification that is produced by formation of an adduct with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride.
233.29
C 12 H 11 N 1 O 2 S 1
233.05106
X
artifact
Unimod:139
Dansyl (Dns)
DansylRes
PSI-MOD
5-dimethylaminonaphthalene-1-sulfonyl
Dansyl
MOD:01653
dansyl chloride derivatized residue
A protein modification that is produced by formation of an adduct with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride.
DeltaMass:0
Unimod:139
Dansyl (Dns)
DansylRes
5-dimethylaminonaphthalene-1-sulfonyl
Dansyl
A protein modification that is produced by reaction with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride, to form N6-Dansyl-lysine.
233.29
C 12 H 11 N 1 O 2 S 1
233.05106
C 18 H 23 N 3 O 3 S 1
361.46
361.14603
K
artifact
Unimod:139
N6DansylLys
PSI-MOD
5-dimethylaminonaphthalene-1-sulfonyl
Dansyl
MOD:01654
N6-Dansyl derivatized lysine
A protein modification that is produced by reaction with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride, to form N6-Dansyl-lysine.
Unimod:139#K
N6DansylLys
5-dimethylaminonaphthalene-1-sulfonyl
Dansyl
A protein modification that is produced by reaction with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride, to form an alpha-amino-Dansyl-derivatized residue.
233.29
C 12 H 11 N 1 O 2 S 1
233.05106
X
artifact
Unimod:139
N2DansylRes
PSI-MOD
5-dimethylaminonaphthalene-1-sulfonyl
Dansyl
MOD:01655
alpha-amino-Dansyl derivatized residue
A protein modification that is produced by reaction with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride, to form an alpha-amino-Dansyl-derivatized residue.
Unimod:139#N-term
N2DansylRes
5-dimethylaminonaphthalene-1-sulfonyl
Dansyl
A protein modification that is produced by formation of an adduct with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, Dabsyl chloride.
287.34
C 14 H 13 N 3 O 2 S 1
287.07285
X
artifact
4-([4-(dimethylamino)phenyl]diazenyl)benzenesulfonyl
DabsylRes
PSI-MOD
MOD:01656
Dabsyl chloride derivatized residue
A protein modification that is produced by formation of an adduct with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, Dabsyl chloride.
PubMed:18688235
4-([4-(dimethylamino)phenyl]diazenyl)benzenesulfonyl
DabsylRes
A protein modification that is produced by reaction with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, dabsyl chloride, to form N6-Dabsyl-lysine.
287.34
C 14 H 13 N 3 O 2 S 1
287.07285
C 20 H 25 N 5 O 3 S 1
415.51
415.16782
K
artifact
N6-[4-([4-(dimethylamino)phenyl]diazenyl)benzenesulfonyl]lysine
N6DabsylLys
PSI-MOD
MOD:01657
N6-Dabsyl derivatized lysine
A protein modification that is produced by reaction with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, dabsyl chloride, to form N6-Dabsyl-lysine.
PubMed:18688235
N6-[4-([4-(dimethylamino)phenyl]diazenyl)benzenesulfonyl]lysine
N6DabsylLys
A protein modification that is produced by reaction with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, dabsyl chloride, to form an alpha-amino-Dabsyl-derivatized residue.
287.34
C 14 H 13 N 3 O 2 S 1
287.07285
X
artifact
N-term
N2DabsylRes
PSI-MOD
MOD:01658
alpha-amino-Dabsyl derivatized residue
A protein modification that is produced by reaction with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, dabsyl chloride, to form an alpha-amino-Dabsyl-derivatized residue.
PubMed:18688235
N2DabsylRes
A protein modification that is produced by formation of an adduct with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A.
484.5
C 22 H 16 N 2 O 7 S 2
484.0399
X
artifact
1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
1-amino-9,10-dioxo-4-{[3-(vinylsulfonyl)phenyl]amino}-9,10-dihydroanthracene-2-sulfonic acid
Uniblue A
UniblueARes
PSI-MOD
MOD:01659
This reagent has a reactive sulfonyl vinyl and typically reacts with the free thiol group of cysteine residues.
Uniblue A derivatized residue
A protein modification that is produced by formation of an adduct with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A.
PubMed:18688235
1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
1-amino-9,10-dioxo-4-{[3-(vinylsulfonyl)phenyl]amino}-9,10-dihydroanthracene-2-sulfonic acid
Uniblue A
UniblueARes
A protein modification that is produced by reaction with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A, to form Uniblue A cysteine adduct.
484.5
C 22 H 16 N 2 O 7 S 2
484.0399
C 25 H 21 N 3 O 8 S 3
587.64
587.0491
C
artifact
1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
1-amino-9,10-dioxo-4-{[3-(vinylsulfonyl)phenyl]amino}-9,10-dihydroanthracene-2-sulfonate
SUniblueACys
Uniblue A
PSI-MOD
MOD:01660
Uniblue A derivatized cysteine
A protein modification that is produced by reaction with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A, to form Uniblue A cysteine adduct.
PubMed:18688235
1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
1-amino-9,10-dioxo-4-{[3-(vinylsulfonyl)phenyl]amino}-9,10-dihydroanthracene-2-sulfonate
SUniblueACys
Uniblue A
A protein modification that effectively converts an L-tyrosine residue to pyruvic acid.
-93.13
C -6 H -7 N -1 O 0
-93.057846
C 3 H 3 O 2
71.06
71.013306
Y
natural
N-term
uniprot.ptm:PTM-0662
2-oxopropanoic acid
MOD_RES Pyruvic acid (Tyr)
pyruvic acid
PSI-MOD
MOD:01661
pyruvic acid (Tyr)
A protein modification that effectively converts an L-tyrosine residue to pyruvic acid.
PubMed:10085076
PubMed:3042771
PubMed:500639
PubMed:8464063
RESID:AA0127#TYR
2-oxopropanoic acid
MOD_RES Pyruvic acid (Tyr)
pyruvic acid
A protein modification that effectively converts an L-glutamine residue to N5-(ADP-ribosyl)-L-glutamine.
541.3
C 15 H 21 N 5 O 13 P 2
541.0611
C 20 H 29 N 7 O 15 P 2
669.43
669.1197
Q
natural
(S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-5-oxopentanoic acid
N5-(ADP-ribosyl)-L-glutamine
N5-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-glutamine
N5-alpha-D-ribofuranosyl-L-glutamine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
PSI-MOD
MOD:01662
N5-(ADP-ribosyl)-L-glutamine
A protein modification that effectively converts an L-glutamine residue to N5-(ADP-ribosyl)-L-glutamine.
PubMed:20185726
RESID:AA0518
(S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-5-oxopentanoic acid
N5-(ADP-ribosyl)-L-glutamine
N5-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-glutamine
N5-alpha-D-ribofuranosyl-L-glutamine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
A protein modification that effectively converts an L-threonine residue to O-(ADP-ribosyl)-L-threonine.
541.3
C 15 H 21 N 5 O 13 P 2
541.0611
C 19 H 28 N 6 O 15 P 2
642.41
642.10876
T
natural
(S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-butanoic acid
O-(ADP-ribosyl)-L-threonine
O3-(ADP-ribosyl)-L-threonine
O3-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-threonine
O3-alpha-D-ribofuranosyl-L-threonine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
PSI-MOD
MOD:01663
O-(ADP-ribosyl)-L-threonine
A protein modification that effectively converts an L-threonine residue to O-(ADP-ribosyl)-L-threonine.
PubMed:20185726
RESID:AA0519
(S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-butanoic acid
O-(ADP-ribosyl)-L-threonine
O3-(ADP-ribosyl)-L-threonine
O3-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-threonine
O3-alpha-D-ribofuranosyl-L-threonine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)
A protein modification that effectively converts an L-tryptophan residue to a 7'-hydroxy-L-tryptophan.
16.0
C 0 H 0 N 0 O 1
15.994915
C 11 H 10 N 2 O 2
202.21
202.07423
W
natural
uniprot.ptm:PTM-0427
(2S)-2-amino-3-(7-hydroxy-1H-indol-3-yl)propanoic acid
7'-hydroxy-L-tryptophan
7-hydroxy-L-tryptophan
PSI-MOD
MOD:01664
7'-hydroxy-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to a 7'-hydroxy-L-tryptophan.
PubMed:20223990
RESID:AA0520
(2S)-2-amino-3-(7-hydroxy-1H-indol-3-yl)propanoic acid
7'-hydroxy-L-tryptophan
7-hydroxy-L-tryptophan
A protein modification that effectively crosslinks an N-terminal L-valine residue and a strand of DNA at the C-1 of a ribose, freeing the nucleotide base and forming N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-valine.
V
hypothetical
N-term
(2S)-2-[(3R,4R)-3,4-dihydroxy-5-(phosphonooxy)pentylidene]amino-3-methylbutanoic acid
ACT_SITE Schiff-base intermediate with DNA; via amino nitrogen
DNA glycosylase valine Schiff base intermediate
N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-valine
PSI-MOD
MOD:01665
N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-valine
A protein modification that effectively crosslinks an N-terminal L-valine residue and a strand of DNA at the C-1 of a ribose, freeing the nucleotide base and forming N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-valine.
PubMed:20185759
RESID:AA0521
(2S)-2-[(3R,4R)-3,4-dihydroxy-5-(phosphonooxy)pentylidene]amino-3-methylbutanoic acid
ACT_SITE Schiff-base intermediate with DNA; via amino nitrogen
DNA glycosylase valine Schiff base intermediate
N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-valine
A protein modification that is produced by formation of an adduct with epicocconone.
410.42
C 23 H 22 O 7
410.13657
X
artifact
(6S,9aS)-6-(hydroxymethyl)-3-[(1Z,4E,6E,8E)-1-hydroxy-3-oxodeca-1,4,6,8-tetraen-1-yl]-9a-methyl-5,6-dihydro-2H-furo[3,2-g]isochromene-2,9(9aH)-dione
Deep Purple
LavaPurple
Lightning Fast
PSI-MOD
MOD:01666
epicocconone derivatized residue
A protein modification that is produced by formation of an adduct with epicocconone.
PubMed:18688235
(6S,9aS)-6-(hydroxymethyl)-3-[(1Z,4E,6E,8E)-1-hydroxy-3-oxodeca-1,4,6,8-tetraen-1-yl]-9a-methyl-5,6-dihydro-2H-furo[3,2-g]isochromene-2,9(9aH)-dione
Deep Purple
LavaPurple
Lightning Fast
A protein modification that is produced by formation of an adduct with epicocconone.
410.42
C 23 H 22 O 7
410.13657
C 29 H 34 N 2 O 8
538.6
538.2315
K
artifact
(6Z,7aS)-3-[(1Z,4E,6E,8E)-1-hydroxy-3-oxodeca-1,4,6,8-tetraen-1-yl]-7a-methyl-6-[([(1S)-1-amino-1-carboxylpentyl]amino)methylidene]-5-[(2S)-2,3-dihydroxypropyl]-1-benzofuran-2,7(6H,7aH)-dione
DeepPurple
LavaPurple
Lightning Fast
PSI-MOD
MOD:01667
N6-epicoccononyl lysine adduct
A protein modification that is produced by formation of an adduct with epicocconone.
PubMed:18688235
(6Z,7aS)-3-[(1Z,4E,6E,8E)-1-hydroxy-3-oxodeca-1,4,6,8-tetraen-1-yl]-7a-methyl-6-[([(1S)-1-amino-1-carboxylpentyl]amino)methylidene]-5-[(2S)-2,3-dihydroxypropyl]-1-benzofuran-2,7(6H,7aH)-dione
DeepPurple
LavaPurple
Lightning Fast
A protein modification that effectively converts an L-aspartic acid residue to O4-(8alpha-FAD)-L-aspartate.
783.54
C 27 H 31 N 9 O 15 P 2
783.1415
C 31 H 36 N 10 O 18 P 2
898.63
898.16846
D
natural
(2S)-2-amino-4-oxo-4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxybutanoic acid
8alpha-[(4-aspartyl)oxy]FAD
O4-(8alpha-FAD)-L-aspartate
PSI-MOD
MOD:01668
O4-(8alpha-FAD)-L-aspartate
A protein modification that effectively converts an L-aspartic acid residue to O4-(8alpha-FAD)-L-aspartate.
PubMed:20080101
RESID:AA0522
(2S)-2-amino-4-oxo-4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxybutanoic acid
8alpha-[(4-aspartyl)oxy]FAD
O4-(8alpha-FAD)-L-aspartate
A protein modification that effectively converts an L-arginine residue to N(omega),N(omega),N'(omega)-trimethyl-L-arginine.
42.08
C 3 H 6 N 0 O 0
42.04695
C 9 H 18 N 4 O 1
198.27
198.14806
R
hypothetical
Unimod:37
(2S)-2-amino-5-([(dimethylamino)(methylamino)methylidene]amino)pentanoic acid
(2S)-2-amino-5-([(dimethylamino)(methylimino)methyl]amino)pentanoic acid
2-[(4S)-4-amino-5-oxopentyl]-1,1,3-trimethylguanidine
N(G)-trimethylarginine
N5-[(dimethylamino)(imino)methyl]ornithine
NoNoNo'Me3Arg
omega-N,omega-N,omega-N'-trimethyl-L-arginine
trimethylationr
PSI-MOD
Trimethyl
tri-Methylation
MOD:01669
trimethyl-L-arginine
A protein modification that effectively converts an L-arginine residue to N(omega),N(omega),N'(omega)-trimethyl-L-arginine.
OMSSA:117
PubMed:11704273
PubMed:602668
RESID:AA0523
Unimod:37#R
(2S)-2-amino-5-([(dimethylamino)(methylamino)methylidene]amino)pentanoic acid
(2S)-2-amino-5-([(dimethylamino)(methylimino)methyl]amino)pentanoic acid
2-[(4S)-4-amino-5-oxopentyl]-1,1,3-trimethylguanidine
N(G)-trimethylarginine
N5-[(dimethylamino)(imino)methyl]ornithine
NoNoNo'Me3Arg
omega-N,omega-N,omega-N'-trimethyl-L-arginine
trimethylationr
Trimethyl
tri-Methylation
A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine.
34.44
C 0 Cl 1 H -1 N 0 O 0
33.96103
C 6 Cl 1 H 11 N 2 O 1
162.62
162.05598
K
hypothetical
(2S)-2-amino-6-(chloroamino)hexanoic acid
N(zeta)-chlorolysine
N6-chloro-L-lysine
N6ClLys
epsilon-chlorolysine
lysine chloramine
PSI-MOD
MOD:01670
N6-chloro-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine.
PubMed:16091367
PubMed:16195462
PubMed:17260957
RESID:AA0524
(2S)-2-amino-6-(chloroamino)hexanoic acid
N(zeta)-chlorolysine
N6-chloro-L-lysine
N6ClLys
epsilon-chlorolysine
lysine chloramine
A protein modification that effectively converts an L-threonine residue to O-(L-isoaspartyl)-L-threonine, using free L-asparagine and releasing ammonia.
115.09
C 4 H 5 N 1 O 3
115.02694
C 8 H 12 N 2 O 5
216.19
216.07462
T
natural
(2S)-2-amino-4-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-4-oxobutanoic acid
(2S,3R)-2-amino-3-([(4S)-3-amino-3-carboxypropanoyl]oxy)propanoic acid
ACT_SITE O-isoaspartyl threonine intermediate
O(beta)-(beta-aspartyl)threonine
O-(L-isoaspartyl)-L-threonine
O3-(isoaspartyl)-threonine
PSI-MOD
MOD:01671
This is a threonine active intermediate and not an ester cross-link of peptides [JSG].
O-(L-isoaspartyl)-L-threonine (active site intermediate)
A protein modification that effectively converts an L-threonine residue to O-(L-isoaspartyl)-L-threonine, using free L-asparagine and releasing ammonia.
PubMed:8706862
RESID:AA0525#THR
(2S)-2-amino-4-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-4-oxobutanoic acid
(2S,3R)-2-amino-3-([(4S)-3-amino-3-carboxypropanoyl]oxy)propanoic acid
ACT_SITE O-isoaspartyl threonine intermediate
O(beta)-(beta-aspartyl)threonine
O-(L-isoaspartyl)-L-threonine
O3-(isoaspartyl)-threonine
A protein modification that effectively substitutes a hydrogen atom of an L-lysine residue with a halogen atom.
K
PSI-MOD
MOD:01672
halogenated lysine
A protein modification that effectively substitutes a hydrogen atom of an L-lysine residue with a halogen atom.
PubMed:18688235
A protein modification that effectively replaces a hydrogen atom with an N-acetylaminohexose group through a glycosidic bond.
203.19
C 8 H 13 N 1 O 5
203.07938
X
Unimod:43
HexNAcRes
PSI-MOD
HexNAc
N-Acetylhexosamine
MOD:01673
N-acetylaminohexosylated residue
A protein modification that effectively replaces a hydrogen atom with an N-acetylaminohexose group through a glycosidic bond.
Unimod:43
HexNAcRes
HexNAc
N-Acetylhexosamine
A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminohexosyl)-L-asparagine.
203.19
C 8 H 13 N 1 O 5
203.07938
C 12 H 19 N 3 O 7
317.3
317.1223
N
natural
Unimod:43
(S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-hexopyranosyl)amino-4-oxobutanoic acid
HexNAcAsn
N4-(2-acetamido-2-deoxy-beta-D-hexopyranosyl)-L-asparagine
N4-(2-acetylamino-2-deoxy-beta-D-hexopyranosyl)-L-asparagine
N4-(N-acetylhexosaminyl)asparagine
N4-asparagine-beta-N-acetylhexosaminide
N4-glycosyl-L-asparagine
N4-glycosylasparagine
N4HexNAcAsn
hexNAcN
PSI-MOD
HexNAc
N-Acetylhexosamine
MOD:01674
N4-(N-acetylamino)hexosyl-L-asparagine
A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminohexosyl)-L-asparagine.
OMSSA:182
Unimod:43#N
(S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-hexopyranosyl)amino-4-oxobutanoic acid
HexNAcAsn
N4-(2-acetamido-2-deoxy-beta-D-hexopyranosyl)-L-asparagine
N4-(2-acetylamino-2-deoxy-beta-D-hexopyranosyl)-L-asparagine
N4-(N-acetylhexosaminyl)asparagine
N4-asparagine-beta-N-acetylhexosaminide
N4-glycosyl-L-asparagine
N4-glycosylasparagine
N4HexNAcAsn
hexNAcN
HexNAc
N-Acetylhexosamine
A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminohexosyl)-L-serine.
203.19
C 8 H 13 N 1 O 5
203.07938
C 11 H 18 N 2 O 7
290.27
290.1114
S
natural
Unimod:43
(S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-hexopyranosyloxy)propanoic acid
O-(2-acetylamino-2-deoxy-beta-D-hexopyranosyl)-L-serine
O-(N-acetylhexosaminyl)serine
O-glycosylserine
O-seryl-beta-N-acetylhexosaminide
O3-(2-acetamido-2-deoxy-beta-D-hexopyranosyl)-L-serine
OHexNAcSer
hexNAcS
PSI-MOD
HexNAc
N-Acetylhexosamine
MOD:01675
O-(N-acetylamino)hexosyl-L-serine
A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminohexosyl)-L-serine.
OMSSA:184
Unimod:43#S
(S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-hexopyranosyloxy)propanoic acid
O-(2-acetylamino-2-deoxy-beta-D-hexopyranosyl)-L-serine
O-(N-acetylhexosaminyl)serine
O-glycosylserine
O-seryl-beta-N-acetylhexosaminide
O3-(2-acetamido-2-deoxy-beta-D-hexopyranosyl)-L-serine
OHexNAcSer
hexNAcS
HexNAc
N-Acetylhexosamine
A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminohexosyl)-L-threonine.
203.19
C 8 H 13 N 1 O 5
203.07938
C 12 H 20 N 2 O 7
304.3
304.12704
T
natural
Unimod:43
(2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxyhexopyranosyloxy)butanoic acid
O-(N-acetylhexcosaminyl)-L-threonine
O-glycosylthreonine
O3-(N-acetylhexosaminyl)threonine
OHexNAcThr
hexNAcT
PSI-MOD
HexNAc
N-Acetylhexosamine
MOD:01676
O-(N-acetylamino)hexosyl-L-threonine
A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminohexosyl)-L-threonine.
OMSSA:185
Unimod:43#T
(2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxyhexopyranosyloxy)butanoic acid
O-(N-acetylhexcosaminyl)-L-threonine
O-glycosylthreonine
O3-(N-acetylhexosaminyl)threonine
OHexNAcThr
hexNAcT
HexNAc
N-Acetylhexosamine
A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)hexosyl-L-hydroxyproline.
219.19
C 8 H 13 N 1 O 6
219.07428
C 13 H 20 N 2 O 7
316.31
316.12704
P
natural
(2S,4R)-4-[2-acetamido-2-deoxy-alpha-D-hexopyranosyloxy]pyrrolidine-2-carboxylic acid
4-(N-acetylhexosaminyloxy)proline
4-[(2-N-acetylamino)-alpha-D-hexopyranosyl]oxyproline
O4-glycosyl-hydroxyproline
O4HexNAcHyPro
alpha-2-(N-acetylamino)hexopyranosyl-4-hydroxyproline
PSI-MOD
HexNAc
MOD:01677
secondary to RESID:AA0030
O4-(N-acetylamino)hexosyl-L-hydroxyproline
A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)hexosyl-L-hydroxyproline.
PubMed:18688235
(2S,4R)-4-[2-acetamido-2-deoxy-alpha-D-hexopyranosyloxy]pyrrolidine-2-carboxylic acid
4-(N-acetylhexosaminyloxy)proline
4-[(2-N-acetylamino)-alpha-D-hexopyranosyl]oxyproline
O4-glycosyl-hydroxyproline
O4HexNAcHyPro
alpha-2-(N-acetylamino)hexopyranosyl-4-hydroxyproline
HexNAc
A protein modification that effectively coverts L-lysine to N6-carbamoyl-L-lysine.
43.02
C 1 H 1 N 1 O 1
43.005814
C 7 H 13 N 3 O 2
171.2
171.10078
K
artifact
Unimod:5
uniprot.ptm:PTM-0675
2-amino-6-ureido-hexanoic acid
MOD_RES N6-carbamoyllysine
N6-(aminocarbonyl)-L-lysine
N6CbmLys
carbamylk
homocitrulline
PSI-MOD
Carbamyl
Carbamylation
MOD:01678
This modification can be produced by hydrogen cyanate, either as a reagent or as released by urea degradation in solution [JSG].
N6-carbamoyl-L-lysine
A protein modification that effectively coverts L-lysine to N6-carbamoyl-L-lysine.
ChEBI:144369
DeltaMass:56
OMSSA:31
PubMed:10978403
PubMed:12203680
Unimod:5#K
2-amino-6-ureido-hexanoic acid
MOD_RES N6-carbamoyllysine
N6-(aminocarbonyl)-L-lysine
N6CbmLys
carbamylk
homocitrulline
Carbamyl
Carbamylation
A protein modification that effectively replaces a residue alpha amino or imino hydrogen with a carbamoyl group.
43.02
C 1 H 1 N 1 O 1
43.005814
X
artifact
N-term
Unimod:5
N2CbmRes
ntermcarbamyl
PSI-MOD
Carbamyl
Carbamylation
MOD:01679
This modification can be produced by hydrogen cyanate, either as a reagent or as released by urea degradation. This modification effectively blocks Edman degradation, and because it can dehydrate to a cyanate group and react with another peptide N-terminal, it can effectively block two peptide molecules [JSG].
alpha-aminocarbamoylated residue
A protein modification that effectively replaces a residue alpha amino or imino hydrogen with a carbamoyl group.
DeltaMass:56
OMSSA:32
PubMed:10978403
PubMed:12203680
Unimod:5#N-term
N2CbmRes
ntermcarbamyl
Carbamyl
Carbamylation
A protein modification that effectively replaces one residue alpha amino or imino hydrogen with one methyl group.
14.03
C 1 H 2 N 0 O 0
14.01565
X
natural
N-term
Unimod:34
N2Me1Res
ntermmethyl
ntermpepmethyl
PSI-MOD
Methyl
Methylation
MOD:01680
Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence [JSG].
alpha-amino monomethylated residue
A protein modification that effectively replaces one residue alpha amino or imino hydrogen with one methyl group.
OMSSA:11
OMSSA:76
Unimod:34#N-term
N2Me1Res
ntermmethyl
ntermpepmethyl
Methyl
Methylation
A protein modification that effectively replaces one hydrogen atom of an L-aspartic acid residue with one methyl group.
14.03
C 1 H 2 N 0 O 0
14.01565
C 5 H 7 N 1 O 3
129.12
129.04259
D
artifact
Unimod:34
Me1Asp
methyld
PSI-MOD
Methyl
Methylation
MOD:01681
monomethylated L-aspartic acid
A protein modification that effectively replaces one hydrogen atom of an L-aspartic acid residue with one methyl group.
OMSSA:16
Unimod:34#D
Me1Asp
methyld
Methyl
Methylation
A protein modification that effectively replaces one hydrogen atom of an L-cysteine residue with one methyl group.
14.03
C 1 H 2 N 0 O 0
14.01565
C 4 H 7 N 1 O 1 S 1
117.17
117.02483
C
natural
Unimod:34
Me1Cys
methylc
PSI-MOD
Methyl
Methylation
MOD:01682
monomethylated L-cysteine
A protein modification that effectively replaces one hydrogen atom of an L-cysteine residue with one methyl group.
OMSSA:73
Unimod:34#C
Me1Cys
methylc
Methyl
Methylation
A protein modification that effectively replaces one hydrogen atom of an L-lysine residue with one methyl group.
14.03
C 1 H 2 N 0 O 0
14.01565
C 7 H 15 N 2 O 2
159.21
159.11336
K
natural
Me1Lys
methylk
PSI-MOD
Methyl
Methylation
MOD:01683
monomethylated L-lysine
A protein modification that effectively replaces one hydrogen atom of an L-lysine residue with one methyl group.
OMSSA:0
Me1Lys
methylk
Methyl
Methylation
A protein modification that effectively converts an L-cysteine residue to a palmitoylated-L-cysteine, such as N-palmitoyl-L-cysteine or S-palmitoyl-L-cysteine.
238.41
C 16 H 30 N 0 O 1 S 0
238.22966
C 19 H 35 N 1 O 2 S 1
341.55
341.23886
C
natural
Unimod:47
Hexadecanoylated L-cysteine
PamCys
palmitoylationc
PSI-MOD
Palmitoyl
Palmitoylation
MOD:01684
palmitoylated-L-cysteine
A protein modification that effectively converts an L-cysteine residue to a palmitoylated-L-cysteine, such as N-palmitoyl-L-cysteine or S-palmitoyl-L-cysteine.
OMSSA:92
Unimod:47
Hexadecanoylated L-cysteine
PamCys
palmitoylationc
Palmitoyl
Palmitoylation
A protein modification that effectively replaces a residue alpha-amino group with a alpha-palmitoylamino group.
238.41
C 16 H 30 N 0 O 1 S 0
238.22966
X
natural
N-term
Unimod:47
N2PamRes
PSI-MOD
Palmitoyl
Palmitoylation
MOD:01685
alpha-amino palmitoylated residue
A protein modification that effectively replaces a residue alpha-amino group with a alpha-palmitoylamino group.
Unimod:47#N-term
N2PamRes
Palmitoyl
Palmitoylation
A protein modification that effectively replaces two alpha amino hydrogen atoms with two methyl group.
28.05
C 2 H 4
28.0313
X
N-term
Unimod:36
N2Me2Res
ntermpepdimethyl
PSI-MOD
Dimethyl
di-Methylation
MOD:01686
For alpha-amino acids, both N-alpha-monomethylation and complete N-alpha protonation and trimethylation have been observed, but incomplete dimethylation has not been reported as a natural process. For N-terminal proline residues, dimethylation can only be effectively accomplished with a protonated imino group, whereas this process accounts only for dimethylation and not protonation. See MOD:00889.
alpha-amino dimethylated residue
A protein modification that effectively replaces two alpha amino hydrogen atoms with two methyl group.
OMSSA:38
Unimod:36#N-term
N2Me2Res
ntermpepdimethyl
Dimethyl
di-Methylation
A protein modification that effectively replaces an alpha-aminium group with a trimethylaminium group.
42.08
C 3 H 6 N 0 O 0
42.046402
1+
X
natural
N-term
Unimod:37
N2Me3Res
ntermtrimethyl
PSI-MOD
Trimethyl
tri-Methylation
MOD:01687
For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative N2Me3+Res process (MOD:01698) accounts for both protonation and trimethylation.
alpha-amino trimethylated residue
A protein modification that effectively replaces an alpha-aminium group with a trimethylaminium group.
OMSSA:12
Unimod:37#N-term
N2Me3Res
ntermtrimethyl
Trimethyl
tri-Methylation
A protein modification that effectively converts an L-asparagine residue to one of the diastereomeric 3-hydroxy-L-asparagine residues.
16.0
C 0 H 0 N 0 O 1
15.994915
C 4 H 6 N 2 O 3
130.1
130.03784
N
natural
Unimod:35
3HyAsn
hydroxylationn
monohydroxylated asparagine
PSI-MOD
Oxidation
MOD:01688
3-hydroxy-L-asparagine
A protein modification that effectively converts an L-asparagine residue to one of the diastereomeric 3-hydroxy-L-asparagine residues.
OMSSA:61
Unimod:35#N
3HyAsn
hydroxylationn
monohydroxylated asparagine
Oxidation
A protein modification that effectively converts a carboxyl-terminal residue to an alpha-carboxyl (1-carboxyl) methyl ester.
14.03
C 1 H 2 N 0 O 0 S 0
14.01565
X
natural
C-term
Unimod:34
C1OMeRes
ctermpepmeester
ctermpepmethyl
PSI-MOD
Methyl
MOD:01689
alpha-carboxyl methylated residue
A protein modification that effectively converts a carboxyl-terminal residue to an alpha-carboxyl (1-carboxyl) methyl ester.
OMSSA:18
OMSSA:68
Unimod:34#C-term
C1OMeRes
ctermpepmeester
ctermpepmethyl
Methyl
Methyl
A protein modification that effectively converts an L-cysteine residue to N-[(12R)-12-hydroxymyristoyl]-L-cysteine.
226.36
C 14 H 26 N 0 O 2 S 0
226.19328
C 17 H 32 N 1 O 3 S 1
330.51
330.2103
C
natural
N-term
uniprot.ptm:PTM-0419
2-[(12R)-12-hydroxytetradecanoyl]amino-3-sulfanylpropanoic acid
LIPID N-[(12R)-12-hydroxymyristoyl]cysteine
N-[(12R)-12-hydroxymyristoyl]-L-cysteine
N-[(12R)-12-hydroxytetradecanoyl]cysteine
PSI-MOD
MOD:01690
N-[(12R)-12-hydroxymyristoyl]-L-cysteine
A protein modification that effectively converts an L-cysteine residue to N-[(12R)-12-hydroxymyristoyl]-L-cysteine.
RESID:AA0516
2-[(12R)-12-hydroxytetradecanoyl]amino-3-sulfanylpropanoic acid
LIPID N-[(12R)-12-hydroxymyristoyl]cysteine
N-[(12R)-12-hydroxymyristoyl]-L-cysteine
N-[(12R)-12-hydroxytetradecanoyl]cysteine
A protein modification that effectively converts an L-cysteine residue to N-(12-ketomyristoyl)-L-cysteine.
224.34
C 14 H 24 N 0 O 2 S 0
224.17763
C 17 H 30 N 1 O 3 S 1
328.49
328.19464
C
natural
N-term
uniprot.ptm:PTM-0420
2-(12-oxotetradecanoyl)amino-3-sulfanylpropanoic acid
LIPID N-(12-oxomyristoyl)cysteine
N-(12-ketomyristoyl)-L-cysteine
N-(12-oxotetradecanoyl)cysteine
PSI-MOD
MOD:01691
N-(12-ketomyristoyl)-L-cysteine
A protein modification that effectively converts an L-cysteine residue to N-(12-ketomyristoyl)-L-cysteine.
PubMed:19053188
RESID:AA0517
2-(12-oxotetradecanoyl)amino-3-sulfanylpropanoic acid
LIPID N-(12-oxomyristoyl)cysteine
N-(12-ketomyristoyl)-L-cysteine
N-(12-oxotetradecanoyl)cysteine
A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl semialdehyde.
-16.0
C 0 H 0 N 0 O -1
-15.994915
C 5 H 7 N 1 O 2
113.12
113.047676
E
artifact
gamma-glutamyl semialdehyde
glutamyl 5-semialdehyde
glutamyl aldehyde
PSI-MOD
Deoxy
MOD:01692
glutamyl semialdehyde (Glu)
A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl semialdehyde.
PubMed:18688235
PubMed:743268
gamma-glutamyl semialdehyde
glutamyl 5-semialdehyde
glutamyl aldehyde
Deoxy
A protein modification that effectively replaces a residue alpha amino or imino hydrogen with a (pyrid-3-yl)acetyl group.
119.12
C 7 H 5 N 1 O 1
119.03712
X
artifact
N-term
Unimod:25
ntermpeppyridyl
PSI-MOD
Pyridylacetyl
pyridylacetyl
MOD:01693
Produced by reaction with N-[(pyrid-3-yl)acetyl]oxy-succinimide [JSG].
alpha-amino pyridylacetylated residue
A protein modification that effectively replaces a residue alpha amino or imino hydrogen with a (pyrid-3-yl)acetyl group.
OMSSA:107
PubMed:9276974
Unimod:25#N-term
ntermpeppyridyl
Pyridylacetyl
pyridylacetyl
A protein modification that effectively results from forming an adduct between an L-cysteine residue and the bioluminescent compound didehydrocoelenterazine to form S-(coelenterazin-3a-yl)-L-cysteine.
421.46
C 26 H 19 N 3 O 3 S 0
421.14264
C 29 H 24 N 4 O 4 S 1
524.6
524.15186
C
natural
uniprot.ptm:PTM-0428
(2R)-2-amino-3-([(4-hydroxyphenyl)(8-benzyl-3-oxo-6-[4-hydroxyphenyl]-3,7-dihydroimidazo[1,2-a]pyrazin-2-yl)methyl]sulfanyl)propanoic acid
MOD_RES S-(coelenterazin-3a-yl)cysteine
S-(coelenterazin-3a-yl)-L-cysteine
dehydrocoelenterazine cysteine adduct
symplectin chromophore
PSI-MOD
MOD:01694
S-(coelenterazin-3a-yl)-L-cysteine
A protein modification that effectively results from forming an adduct between an L-cysteine residue and the bioluminescent compound didehydrocoelenterazine to form S-(coelenterazin-3a-yl)-L-cysteine.
ChEBI:2311
PubMed:18997450
RESID:AA0526
(2R)-2-amino-3-([(4-hydroxyphenyl)(8-benzyl-3-oxo-6-[4-hydroxyphenyl]-3,7-dihydroimidazo[1,2-a]pyrazin-2-yl)methyl]sulfanyl)propanoic acid
MOD_RES S-(coelenterazin-3a-yl)cysteine
S-(coelenterazin-3a-yl)-L-cysteine
dehydrocoelenterazine cysteine adduct
symplectin chromophore
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an 3-(carboxamidomethylthio)propanoyl group.
145.18
C 5 H 7 N 1 O 2 S 1
145.01974
X
artifact
N-term
Unimod:293
PSI-MOD
3-(carbamidomethylthio)propanoyl
CAMthiopropanoyl
MOD:01695
alpha-amino 3-(carboxamidomethylthio)propanoylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an 3-(carboxamidomethylthio)propanoyl group.
PubMed:15121203
Unimod:293#N-term
3-(carbamidomethylthio)propanoyl
CAMthiopropanoyl
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group.
X
natural
N-term
PSI-MOD
MOD:01696
alpha-amino acylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group.
PubMed:18688235
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an 4-(2-aminoethyl)benzenesulfonyl group.
183.23
C 8 H 9 N 1 O 2 S 1
183.0354
X
artifact
N-term
Unimod:276
PSI-MOD
AEBS
Aminoethylbenzenesulfonylation
MOD:01697
See the comment for MOD:00596 [JSG].
alpha-amino 4-(2-aminoethyl)benzenesulfonylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an 4-(2-aminoethyl)benzenesulfonyl group.
DeltaMass:235
PubMed:8597590
Unimod:276#N-term
AEBS
Aminoethylbenzenesulfonylation
A protein modification that effectively replaces an amino group with a trimethylaminium group.
43.09
C 3 H 7 N 0 O 0 S 0
43.054226
1+
X
natural
N-term
N2Me3+Res
PSI-MOD
Trimethyl
tri-Methylation
MOD:01698
alpha-amino trimethylated protonated-residue
A protein modification that effectively replaces an amino group with a trimethylaminium group.
PubMed:18688235
N2Me3+Res
Trimethyl
tri-Methylation
A protein modification that effectively adds a hydrogen cation, a proton, forming a cationic residue.
1.01
C 0 H 1 N 0 O 0
1.007276
1+
X
natural
H+NRes
PSI-MOD
MOD:01699
protonated residue
A protein modification that effectively adds a hydrogen cation, a proton, forming a cationic residue.
PubMed:18688235
H+NRes
A protein modification that effectively adds a proton to a residue alpha-amnino or alpha-imino group forming an alpha-aminium or alpha-iminium group, respectively.
1.01
C 0 H 1 N 0 O 0
1.007276
1+
X
natural
N-term
N2H+NRes
PSI-MOD
MOD:01700
alpha-amino protonated residue
A protein modification that effectively adds a proton to a residue alpha-amnino or alpha-imino group forming an alpha-aminium or alpha-iminium group, respectively.
PubMed:18688235
N2H+NRes
A protein modification that effectively removes a hydrogen cation, a proton, forming an anionic residue.
-1.01
C 0 H -1 N 0 O 0
-1.007276
1-
X
natural
H-NRes
PSI-MOD
MOD:01701
deprotonated residue
A protein modification that effectively removes a hydrogen cation, a proton, forming an anionic residue.
PubMed:18688235
H-NRes
A protein modification that effectively removes a proton from a residue 1-carboxyl group (referred to as the alpha-carboxyl), forming a carboxylate anion.
-1.01
C 0 H -1 N 0 O 0
-1.007276
1-
X
natural
C-term
C1H-NRes
PSI-MOD
MOD:01702
alpha-carboxyl deprotonated residue
A protein modification that effectively removes a proton from a residue 1-carboxyl group (referred to as the alpha-carboxyl), forming a carboxylate anion.
PubMed:18688235
C1H-NRes
A protein modification that effectively converts a source amino acid residue to dehydrobutyrine.
C 4 H 5 N 1 O 1
83.09
83.03712
X
Dehydroamino butyric acid
beta-elim-t
dHAbu
dehydro
phospholosst
PSI-MOD
Dehydrated
Dehydration
MOD:01703
dehydrobutyrine
A protein modification that effectively converts a source amino acid residue to dehydrobutyrine.
PubMed:18688235
Dehydroamino butyric acid
beta-elim-t
dHAbu
dehydro
phospholosst
Dehydrated
Dehydrated
Dehydration
A protein modification that effectively converts an L-methionine residue to dehydrobutyrine, by neutral loss of methyl sulfide.
-48.1
C -1 H -4 N 0 O 0 S -1
-48.003372
C 4 H 5 N 1 O 1
83.09
83.03712
M
artifact
dHAbu(Met)
PSI-MOD
MOD:01704
It is expected that this neutral loss will produce a mix of (E)- and (Z)-isomers [JSG].
dehydrobutyrine (Met)
A protein modification that effectively converts an L-methionine residue to dehydrobutyrine, by neutral loss of methyl sulfide.
PubMed:18688235
dHAbu(Met)
A protein modification that effectively replaces a residue hydrogen with an isotope tagged reagent acyl group.
X
artifact
PSI-MOD
MOD:01705
isotope tagged reagent acylated residue
A protein modification that effectively replaces a residue hydrogen with an isotope tagged reagent acyl group.
PubMed:18688235
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an isotope tagged reagent acyl group.
X
artifact
PSI-MOD
MOD:01706
isotope tagged reagent N-acylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an isotope tagged reagent acyl group.
PubMed:18688235
A protein modification that effectively replaces a residue hydroxyl group with an isotope tagged reagent acyloxy group.
X
artifact
PSI-MOD
MOD:01707
isotope tagged reagent O-acylated residue
A protein modification that effectively replaces a residue hydroxyl group with an isotope tagged reagent acyloxy group.
PubMed:18688235
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an isotope tagged reagent acyl group.
X
artifact
N-term
PSI-MOD
MOD:01708
isotope tagged reagent alpha-amino acylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an isotope tagged reagent acyl group.
PubMed:18688235
A protein modification that effectively replaces a residue amino- or imino-hydrogen with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups.
X
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01709
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex reporter+balance reagent N-acylated residue
A protein modification that effectively replaces a residue amino- or imino-hydrogen with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces a residue amino- or imino-hydrogen with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups.
X
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01710
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex reporter+balance reagent N-acylated residue
A protein modification that effectively replaces a residue amino- or imino-hydrogen with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups.
X
artifact
N-term
Unimod:214
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01711
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups.
Unimod:214#N-term
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups.
X
artifact
N-term
Unimod:214
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01712
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance groups.
Unimod:214#N-term
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces a residue hydroxyl with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance acyloxy groups.
X
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01713
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ4plex reporter+balance reagent O-acylated residue
A protein modification that effectively replaces a residue hydroxyl with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance acyloxy groups.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces a residue hydroxyl with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance acyloxy groups.
X
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
MOD:01714
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
iTRAQ8plex reporter+balance reagent O-acylated residue
A protein modification that effectively replaces a residue hydroxyl with one of the Applied Biosystems iTRAQ8plex reagent reporter+balance acyloxy groups.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
A protein modification that effectively replaces a hydrogen atom of a residue with a Proteome Sciences TMT6plex reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
X
artifact
Unimod:214
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01715
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with a Proteome Sciences TMT6plex reporter+balance group.
Unimod:214
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-126 reagent acylated residue.
2,6-dimethyl-1-methylidenepiperidinium
cysTMT6plex reporter fragment
PSI-MOD
MOD:01716
TMT6plex reporter fragment
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-126 reagent acylated residue.
PubMed:18688235
2,6-dimethyl-1-methylidenepiperidinium
cysTMT6plex reporter fragment
A protein modification that effectively replaces a residue amino- or imino-hydrogen with a Proteome Sciences TMT6plex reporter+balance group.
X
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01717
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex reporter+balance reagent N-acylated residue
A protein modification that effectively replaces a residue amino- or imino-hydrogen with a Proteome Sciences TMT6plex reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a Proteome Sciences TMT6plex reporter+balance group.
X
artifact
N-term
Unimod:214
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01718
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a Proteome Sciences TMT6plex reporter+balance group.
Unimod:214#N-term
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a residue hydroxyl with one of the Proteome Sciences TMT6plex reagent reporter+balance acyloxy groups.
X
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01719
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex reporter+balance reagent O-acylated residue
A protein modification that effectively replaces a residue hydroxyl with one of the Proteome Sciences TMT6plex reagent reporter+balance acyloxy groups.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
X
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01720
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-126 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-126 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
X
artifact
N-term
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01721
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-126 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-126 reporter+balance group.
Unimod:737#N-term
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 14 (13)C 4 H 32 (14)N 3 (15)N 1 O 3
357.26
357.2579
K
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01722
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-126 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
Unimod:737#K
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 17 (13)C 4 H 29 (14)N 2 (15)N 1 O 4
392.23
392.22626
Y
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01723
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-126 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
Unimod:737#Y
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 14 (13)C 4 H 27 (14)N 4 (15)N 1 O 3
366.22
366.22183
H
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01724
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-126 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 11 (13)C 4 H 25 (14)N 2 (15)N 1 O 4
316.19
316.19495
S
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01725
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-126 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 12 (13)C 4 H 27 (14)N 2 (15)N 1 O 4
330.21
330.2106
T
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01726
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-126 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-126 reagent acylated residue.
1+
(12)C 8 H 16 (14)N 1
126.13
126.12772
X
artifact
2,6-dimethyl-1-methylidenepiperidinium
cysTMT6plex-126 reporter fragment
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01727
TMT6plex-126 reporter fragment
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-126 reagent acylated residue.
PubMed:18688235
2,6-dimethyl-1-methylidenepiperidinium
cysTMT6plex-126 reporter fragment
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
X
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01728
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-127 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-127 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
X
artifact
N-term
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01729
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-127 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-127 reporter+balance group.
Unimod:737#N-term
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 14 (13)C 4 H 32 (14)N 3 (15)N 1 O 3
357.26
357.2579
K
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01730
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-127 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
Unimod:737#K
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16
229.16293
Y
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01731
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-127 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
Unimod:737#Y
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 14 (13)C 4 H 27 (14)N 4 (15)N 1 O 3
366.22
366.22183
H
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01732
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-127 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 11 (13)C 4 H 25 (14)N 2 (15)N 1 O 4
316.19
316.19495
S
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01733
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-127 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 12 (13)C 4 H 27 (14)N 2 (15)N 1 O 4
330.21
330.2106
T
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01734
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-127 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-127 reagent acylated residue.
1+
(12)C 7 (13)C 1 H 16 (14)N 1
127.13
127.13108
X
artifact
2,6-dimethyl-1-methylidenepiperidinium
cysTMT6plex-127 reporter fragment
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01735
TMT6plex-127 reporter fragment
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-127 reagent acylated residue.
PubMed:18688235
2,6-dimethyl-1-methylidenepiperidinium
cysTMT6plex-127 reporter fragment
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
X
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01736
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-128 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-128 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
X
artifact
N-term
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01737
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-128 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-128 reporter+balance group.
Unimod:737#N-term
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 14 (13)C 4 H 32 (14)N 3 (15)N 1 O 3
357.26
357.2579
K
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01738
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-128 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
Unimod:737#K
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 17 (13)C 4 H 29 (14)N 2 (15)N 1 O 4
392.23
392.22626
Y
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01739
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-128 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
Unimod:737#Y
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 14 (13)C 4 H 27 (14)N 4 (15)N 1 O 3
366.22
366.22183
H
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01740
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-128 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 11 (13)C 4 H 25 (14)N 2 (15)N 1 O 4
316.19
316.19495
S
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01741
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-128 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 12 (13)C 4 H 27 (14)N 2 (15)N 1 O 4
330.21
330.2106
T
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01742
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-128 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-128 reagent acylated residue.
1+
(12)C 6 (13)C 2 H 16 (14)N 1
128.13
128.13443
X
artifact
2,6-dimethyl-1-methylidenepiperidinium
cysTMT6plex-128 reporter fragment
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01743
TMT6plex-128 reporter fragment
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-128 reagent acylated residue.
PubMed:18688235
2,6-dimethyl-1-methylidenepiperidinium
cysTMT6plex-128 reporter fragment
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
X
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01744
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-129 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-129 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
X
artifact
N-term
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01745
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-129 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-129 reporter+balance group.
Unimod:737#N-term
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 14 (13)C 4 H 32 (14)N 3 (15)N 1 O 3
357.26
357.2579
K
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01746
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-129 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
Unimod:737#K
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 17 (13)C 4 H 29 (14)N 2 (15)N 1 O 4
392.23
392.22626
Y
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01747
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-129 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
Unimod:737#Y
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 14 (13)C 4 H 27 (14)N 4 (15)N 1 O 3
366.22
366.22183
H
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01748
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-129 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 11 (13)C 4 H 25 (14)N 2 (15)N 1 O 4
316.19
316.19495
S
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01749
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-129 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 12 (13)C 4 H 27 (14)N 2 (15)N 1 O 4
330.21
330.2106
T
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01750
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-129 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-129 reagent acylated residue.
1+
(12)C 5 (13)C 3 H 16 (14)N 1
129.14
129.13779
X
artifact
2,6-dimethyl-1-methylidenepiperidinium
cysTMT6plex-129 reporter fragment
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01751
TMT6plex-129 reporter fragment
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-129 reagent acylated residue.
PubMed:18688235
2,6-dimethyl-1-methylidenepiperidinium
cysTMT6plex-129 reporter fragment
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
X
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01752
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-130 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-130 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
X
artifact
N-term
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01753
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-130 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-130 reporter+balance group.
Unimod:737#N-term
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 14 (13)C 4 H 32 (14)N 3 (15)N 1 O 3
357.26
357.2579
K
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01754
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-130 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
Unimod:737#K
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 17 (13)C 4 H 29 (14)N 2 (15)N 1 O 4
392.23
392.22626
Y
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01755
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-130 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
Unimod:737#Y
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 14 (13)C 4 H 27 (14)N 4 (15)N 1 O 3
366.22
366.22183
H
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01756
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-130 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 11 (13)C 4 H 25 (14)N 2 (15)N 1 O 4
316.19
316.19495
S
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01757
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-130 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 12 (13)C 4 H 27 (14)N 2 (15)N 1 O 4
330.21
330.2106
T
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01758
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-130 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-130 reagent acylated residue.
1+
(12)C 4 (13)C 4 H 16 (14)N 1
130.14
130.14114
X
artifact
2,6-dimethyl-1-methylidenepiperidinium
cysTMT6plex-130 reporter fragment
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01759
TMT6plex-130 reporter fragment
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-130 reagent acylated residue.
PubMed:18688235
2,6-dimethyl-1-methylidenepiperidinium
cysTMT6plex-130 reporter fragment
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
X
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
cysTMT6plex-131 reporter fragment
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01760
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-131 reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
cysTMT6plex-131 reporter fragment
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-131 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
X
artifact
N-term
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01761
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-131 reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-131 reporter+balance group.
Unimod:737#N-term
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 14 (13)C 4 H 32 (14)N 3 (15)N 1 O 3
357.26
357.2579
K
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01762
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-131 reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
Unimod:737#K
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 17 (13)C 4 H 29 (14)N 2 (15)N 1 O 4
392.23
392.22626
Y
artifact
Unimod:737
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01763
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-131 reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
Unimod:737#Y
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 14 (13)C 4 H 27 (14)N 4 (15)N 1 O 3
366.22
366.22183
H
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01764
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-131 reporter+balance reagent N'-acylated histidine
A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 11 (13)C 4 H 25 (14)N 2 (15)N 1 O 4
316.19
316.19495
S
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01765
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-131 reporter+balance reagent O3-acylated serine
A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
229.16
(12)C 8 (13)C 4 H 20 (14)N 1 (15)N 1 O 2
229.16293
(12)C 12 (13)C 4 H 27 (14)N 2 (15)N 1 O 4
330.21
330.2106
T
artifact
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01766
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
TMT6plex-131 reporter+balance reagent O3-acylated threonine
A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
PubMed:18688235
3-[(2,6-dimethylpiperidin-1-yl)acetyl]amino)propanoyl
Sixplex Tandem Mass Tag(TM)
TMT6plex
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-131 reagent acylated residue.
1+
(12)C 4 (13)C 4 H 16 (15)N 1
131.14
131.13818
X
artifact
2,6-dimethyl-1-methylidenepiperidinium
PSI-MOD
Sixplex Tandem Mass Tag(TM)
TMT6plex
MOD:01767
TMT6plex-131 reporter fragment
The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-131 reagent acylated residue.
PubMed:18688235
2,6-dimethyl-1-methylidenepiperidinium
Sixplex Tandem Mass Tag(TM)
TMT6plex
A protein modification that effectively replaces a residue hydroxyl group with a palmitoleyloxy group.
236.4
C 16 H 28 N 0 O 1
236.21402
X
natural
PSI-MOD
MOD:01768
O-palmitoleylated residue
A protein modification that effectively replaces a residue hydroxyl group with a palmitoleyloxy group.
PubMed:18688235
A protein modification that effectively converts an L-threonine residue to O-palmitoleyl-L-threonine.
236.4
C 16 H 28 N 0 O 1
236.21402
C 20 H 35 N 1 O 3
337.5
337.2617
T
natural
Unimod:431
(2S,3R)-2-amino-3-((Z)-9-hexadecenoyloxy)butanoic acid
L-threonine cis-9-hexadecenoate ester
O-palmitoleylated L-threonine
O3-palmitoleyl-threonine
mod188
PSI-MOD
Palmitoleyl
palmitoleyl
MOD:01769
O-palmitoleyl-L-threonine
A protein modification that effectively converts an L-threonine residue to O-palmitoleyl-L-threonine.
OMSSA:188
PubMed:6642431
PubMed:8413602
RESID:AA0079#var
Unimod:431#T
(2S,3R)-2-amino-3-((Z)-9-hexadecenoyloxy)butanoic acid
L-threonine cis-9-hexadecenoate ester
O-palmitoleylated L-threonine
O3-palmitoleyl-threonine
mod188
Palmitoleyl
palmitoleyl
A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine amide.
254.44
C 16 H 32 N 1 O 1
254.24838
C 20 H 39 N 2 O 3
355.54
355.29608
T
natural
C-term
(2S,3R)-2-amino-3-(hexadecanoyloxy)butanamide
OPamThrN
PSI-MOD
MOD:01770
O-palmitoyl-L-threonine amide
A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine amide.
PubMed:8413602
RESID:AA0079#var
RESID:AA0097#var
(2S,3R)-2-amino-3-(hexadecanoyloxy)butanamide
OPamThrN
The farnesyl cation protein modification reporter fragment produced by fragmentation of some farnesyl modified residues.
1+
C 15 H 25
205.36
205.19508
X
natural
(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ylium
Farn+
farnesyl cation
PSI-MOD
MOD:01771
farnesyl reporter fragment
The farnesyl cation protein modification reporter fragment produced by fragmentation of some farnesyl modified residues.
PubMed:15609361
PubMed:18688235
(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ylium
Farn+
farnesyl cation
The palmityl cation protein modification reporter fragment produced by fragmentation of some palmitoyl modified residues.
1+
C 16 H 31 O 1
239.42
239.23694
X
natural
Pam+
PSI-MOD
palmityl cation
MOD:01772
palmityl reporter fragment
The palmityl cation protein modification reporter fragment produced by fragmentation of some palmitoyl modified residues.
PubMed:18688235
PubMed:8413602
Pam+
palmityl cation
Covalent modification of a trimethyllysine residue with secondary loss of a neutral trimethylamine molecular fragment.
-59.11
C -3 H -9 N -1 O 0
-59.074047
1+
C 6 H 10 N 1 O 1
112.15
112.07569
MOD:00083
artifact
dMe3N6Me3+Lys
PSI-MOD
MOD:01773
N6,N6,N6-trimethyl-L-lysine with neutral loss of trimethylamine
Covalent modification of a trimethyllysine residue with secondary loss of a neutral trimethylamine molecular fragment.
PubMed:17205979
PubMed:18688235
dMe3N6Me3+Lys
A protein modification that effectively converts an L-lysine residue to N6-octanoyl-L-lysine.
126.2
C 8 H 14 N 0 O 1
126.10446
C 14 H 26 N 2 O 2
254.37
254.19943
K
natural
(2S)-2-amino-6-(octanoylamino)hexanoic acid
N(zeta)-octanoyllysine
N6-(1-oxooctyl)-L-lysine
N6-octanoyl-L-lysine
epsilon-octanoyllysine
PSI-MOD
MOD:01774
N6-octanoyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-octanoyl-L-lysine.
PubMed:12591875
PubMed:2215217
RESID:AA0527
(2S)-2-amino-6-(octanoylamino)hexanoic acid
N(zeta)-octanoyllysine
N6-(1-oxooctyl)-L-lysine
N6-octanoyl-L-lysine
epsilon-octanoyllysine
A protein modification that effectively converts an L-glutamine residue to 5-glutamyl serotonin.
159.19
C 10 H 9 N 1 O 1
159.06842
C 15 H 17 N 3 O 3
287.32
287.12698
Q
natural
(2S)-2-amino-5-([2-(5-hydroxy-1H-indol-3-yl)ethyl]amino)-5-oxopentanoic acid
5-glutamyl serotonin
N2-(gamma-glutamyl)-5-hydoxytryptamine
N5-[2-(5-hydroxy-3-indolyl)ethyl]glutamine
PSI-MOD
MOD:01775
5-glutamyl serotonin
A protein modification that effectively converts an L-glutamine residue to 5-glutamyl serotonin.
PubMed:11805836
PubMed:14697203
RESID:AA0528
(2S)-2-amino-5-([2-(5-hydroxy-1H-indol-3-yl)ethyl]amino)-5-oxopentanoic acid
5-glutamyl serotonin
N2-(gamma-glutamyl)-5-hydoxytryptamine
N5-[2-(5-hydroxy-3-indolyl)ethyl]glutamine
A protein modification that effectively converts an L-cysteine residue to S-methylthiocarbonylaminoethylcysteine.
117.17
C 4 H 7 N 1 O 1 S 1
117.02483
C 7 H 12 N 2 O 2 S 2
220.31
220.03403
C
artifact
(2R)-2-amino-3-([2-([(methylsulfanyl)carbonyl]amino)ethyl]sulfanyl)propanoic acid
L-cysteine N-(methylthiocarbonyl)aziridine adduct
MTCTK
N6-methylthiocarbonyl-4-thialysine
S-[2-([(methylthio)carbonyl]amino)ethyl]-L-cysteine
PSI-MOD
MOD:01776
This modified residue is a chemical analog of N6-acetyl-L-lysine produced from L-cysteine by methylthiocarbonylaziridine (MTCA, S-methyl aziridine-1-carbothioate).
S-methylthiocarbonylaminoethylcysteine (Cys)
A protein modification that effectively converts an L-cysteine residue to S-methylthiocarbonylaminoethylcysteine.
PubMed:18688235
PubMed:20608637
(2R)-2-amino-3-([2-([(methylsulfanyl)carbonyl]amino)ethyl]sulfanyl)propanoic acid
L-cysteine N-(methylthiocarbonyl)aziridine adduct
MTCTK
N6-methylthiocarbonyl-4-thialysine
S-[2-([(methylthio)carbonyl]amino)ethyl]-L-cysteine
A protein modification that effectively converts a C-terminal glycine residue to S-(glycyl)-L-cysteine by forming a thioester bond with a free L-cysteine.
103.14
C 3 H 5 N 1 O 1 S 1
103.009186
C 5 H 9 N 2 O 3 S 1
177.2
177.03339
G
natural
C-term
(2R)-2-amino-3-[(aminoacetyl)sulfanyl]propanoic acid
1-(cystein-S-yl)-glycinate
MOD_RES CysO-cysteine adduct
S-(2-amino-1-oxoethyl)cysteine
S-(glycyl)-L-cysteine
glycine cysteine thioester
PSI-MOD
MOD:01777
This is not the cross-linking of two peptides, but the modification of a C-terminal glycine by formation of an thioester bond with a free cysteine. For the cross-linking of two peptide see MOD:00211 [JSG].
S-(glycyl)-L-cysteine (Gly)
A protein modification that effectively converts a C-terminal glycine residue to S-(glycyl)-L-cysteine by forming a thioester bond with a free L-cysteine.
ChEBI:22050
PubMed:17726030
PubMed:18359941
PubMed:18771296
PubMed:18799456
PubMed:18842002
PubMed:3306404
RESID:AA0206
(2R)-2-amino-3-[(aminoacetyl)sulfanyl]propanoic acid
1-(cystein-S-yl)-glycinate
MOD_RES CysO-cysteine adduct
S-(2-amino-1-oxoethyl)cysteine
S-(glycyl)-L-cysteine
glycine cysteine thioester
A protein modification that effectively converts a C-terminal glycine residue to N-(glycyl)-L-cysteine by forming a peptide bond with a free L-cysteine.
103.14
C 3 H 5 N 1 O 1 S 1
103.009186
C 5 H 9 N 2 O 3 S 1
177.2
177.03339
G
hypothetical
C-term
uniprot.ptm:PTM-0433
(2R)-2-[(aminoacetyl)amino]-3-sulfanylpropanoic acid
MOD_RES CysO-cysteine adduct
N-(2-amino-1-oxoethyl)cysteine
N-(glycyl)-L-cysteine
PSI-MOD
MOD:01778
N-(glycyl)-L-cysteine
A protein modification that effectively converts a C-terminal glycine residue to N-(glycyl)-L-cysteine by forming a peptide bond with a free L-cysteine.
PubMed:18771296
PubMed:18799456
PubMed:18842002
RESID:AA0529
(2R)-2-[(aminoacetyl)amino]-3-sulfanylpropanoic acid
MOD_RES CysO-cysteine adduct
N-(2-amino-1-oxoethyl)cysteine
N-(glycyl)-L-cysteine
A protein modification that effectively converts an L-lysine residue to N6-(L-lysyl)-L-lysine by formation of an isopeptide bond between the carboxyl group of a free lysine and the N6-amino group of the peptidyl L-lysine.
128.18
C 6 H 12 N 2 O 1
128.09496
C 12 H 24 N 4 O 2
256.35
256.1899
K
natural
(2S)-2-amino-6-([(2S)-2,6-diaminohexanoyl]amino)hexanoic acid
N6-(L-lysyl)-L-lysine
N6-(alpha-lysyl)-lysine
PSI-MOD
MOD:01779
This is not the cross-linking of two peptides, but the modification of a peptidyl lysine by formation of an isopeptide bond with a free lysine [JSG].
N6-(L-lysyl)-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-(L-lysyl)-L-lysine by formation of an isopeptide bond between the carboxyl group of a free lysine and the N6-amino group of the peptidyl L-lysine.
PubMed:18201202
PubMed:20729861
RESID:AA0530
(2S)-2-amino-6-([(2S)-2,6-diaminohexanoyl]amino)hexanoic acid
N6-(L-lysyl)-L-lysine
N6-(alpha-lysyl)-lysine
A protein modification that effectively converts an L-lysine residue to N6-(beta-lysyl)-L-5-hydroxylysine by formation of an isopeptide bond between the carboxyl group of a free beta-lysine and the N6-amino group of a peptidyl L-lysine.
144.17
C 6 H 12 N 2 O 2
144.08987
C 12 H 24 N 4 O 3
272.35
272.18484
K
hypothetical
uniprot.ptm:PTM-0474
(2S)-2-amino-6-([(3R)-3,6-diaminohexanoyl]amino)-5-hydroxyhexanoic acid
5-hydroxy-N6-(beta-lysyl)-L-lysine
5-hydroxy-N6-[(3R)-beta-lysyl]lysine
EF-P lysine derivative
MOD_RES N6-(3,6-diaminohexanoyl)-5-hydroxylysine
N6-[(3R)-3,6-diaminohexanoyl]-L-5-hydroxylysine
lysyl spermidine derivative [misidentification]
PSI-MOD
MOD:01780
N6-(beta-lysyl)-L-5-hydroxylysine
A protein modification that effectively converts an L-lysine residue to N6-(beta-lysyl)-L-5-hydroxylysine by formation of an isopeptide bond between the carboxyl group of a free beta-lysine and the N6-amino group of a peptidyl L-lysine.
PubMed:18201202
PubMed:20729861
RESID:AA0531
(2S)-2-amino-6-([(3R)-3,6-diaminohexanoyl]amino)-5-hydroxyhexanoic acid
5-hydroxy-N6-(beta-lysyl)-L-lysine
5-hydroxy-N6-[(3R)-beta-lysyl]lysine
EF-P lysine derivative
MOD_RES N6-(3,6-diaminohexanoyl)-5-hydroxylysine
N6-[(3R)-3,6-diaminohexanoyl]-L-5-hydroxylysine
lysyl spermidine derivative [misidentification]
A protein modification that effectively converts an L-lysine residue to N6-butanoyl-L-lysine.
70.09
C 4 H 6 N 0 O 1
70.04186
C 10 H 18 N 2 O 2
198.27
198.13683
K
hypothetical
Unimod:1289
uniprot.ptm:PTM-0637
(2S)-2-amino-6-(butanoylamino)hexanoic acid
(2S)-2-azanyl-6-(butanoylamino)hexanoic acid
2-amino-6-butyrylaminocaproic acid
MOD_RES N6-butyryllysine
N(zeta)-butanoyllysine
N6-(1-oxobutyl)-L-lysine
N6-butanoyl-L-lysine
N6-butyryllysine
epsilon-butanoyl-L-lysine
epsilon-butyryl-L-lysine
PSI-MOD
MOD:01781
The binding of histone peptides with butanoylated lysine to nuclear bromodomain proteins is non-specific and weaker than binding to the corresponding acetylated lysine peptides [JSG].
N6-butanoyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-butanoyl-L-lysine.
PubMed:17267393
PubMed:20715035
RESID:AA0532
Unimod:1289
(2S)-2-amino-6-(butanoylamino)hexanoic acid
(2S)-2-azanyl-6-(butanoylamino)hexanoic acid
2-amino-6-butyrylaminocaproic acid
MOD_RES N6-butyryllysine
N(zeta)-butanoyllysine
N6-(1-oxobutyl)-L-lysine
N6-butanoyl-L-lysine
N6-butyryllysine
epsilon-butanoyl-L-lysine
epsilon-butyryl-L-lysine
A protein modification that effectively converts an L-serine residue to N-methyl-L-serine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 4 H 7 N 1 O 2
101.1
101.047676
S
natural
uniprot.ptm:PTM-0432
(2S)-3-hydroxy-2-(methylamino)propanoic acid
MOD_RES N-methylserine
N-methyl-L-serine
N-methylserine
PSI-MOD
MOD:01782
N-methyl-L-serine
A protein modification that effectively converts an L-serine residue to N-methyl-L-serine.
PubMed:20668449
RESID:AA0533
(2S)-3-hydroxy-2-(methylamino)propanoic acid
MOD_RES N-methylserine
N-methyl-L-serine
N-methylserine
A protein modification that effectively converts an L-serine residue to N,N-dimethyl-L-serine.
28.05
C 2 H 4 N 0 O 0
28.0313
C 5 H 10 N 1 O 2
116.14
116.07115
S
natural
N-term
uniprot.ptm:PTM-0431
(2S)-2-(dimethylamino)propanoic acid
MOD_RES N,N-dimethylserine
N,N-dimethyl-L-serine
N,N-dimethylserine
PSI-MOD
MOD:01783
N,N-dimethyl-L-serine
A protein modification that effectively converts an L-serine residue to N,N-dimethyl-L-serine.
PubMed:20668449
RESID:AA0534
(2S)-2-(dimethylamino)propanoic acid
MOD_RES N,N-dimethylserine
N,N-dimethyl-L-serine
N,N-dimethylserine
A protein modification that effectively converts an L-serine residue to N,N,N-trimethyl-L-serine.
43.09
C 3 H 7 N 0 O 0
43.054226
1+
C 6 H 13 N 1 O 2
131.17
131.09409
S
natural
N-term
uniprot.ptm:PTM-0430
(1S)-1-carboxy-2-hydroxy-N,N,N-trimethylethanaminium
(1S)-1-carboxy-2-hydroxy-N,N,N-trimethylethanazanium
(2S)-2-trimethylammonio-3-hydroxypropanoic acid
MOD_RES N,N,N-trimethylserine
N,N,N-trimethyl-L-serine
N,N,N-trimethylserine cation
N,N,N-trimethylserinium
PSI-MOD
MOD:01784
N,N,N-trimethyl-L-serine
A protein modification that effectively converts an L-serine residue to N,N,N-trimethyl-L-serine.
PubMed:20668449
PubMed:3979397
RESID:AA0535
(1S)-1-carboxy-2-hydroxy-N,N,N-trimethylethanaminium
(1S)-1-carboxy-2-hydroxy-N,N,N-trimethylethanazanium
(2S)-2-trimethylammonio-3-hydroxypropanoic acid
MOD_RES N,N,N-trimethylserine
N,N,N-trimethyl-L-serine
N,N,N-trimethylserine cation
N,N,N-trimethylserinium
A protein modification that effectively converts an L-threonine residue to O-(L-isoglutamyl)-L-threonine, using free L-glutamine and releasing ammonia.
129.12
C 5 H 7 N 1 O 3
129.04259
C 9 H 14 N 2 O 5
230.22
230.09027
T
hypothetical
(2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid
(2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid
5-(threon-O3-yl)glutamate
O(beta)-(gamma-glutamyl)threonine
O-(L-isoglutamyl)-L-threonine
O3-(isoglutamyl)threonine
PSI-MOD
MOD:01785
This is not an ester cross-link of peptides [JSG].
O-(L-isoglutamyl)-L-threonine (active site intermediate)
A protein modification that effectively converts an L-threonine residue to O-(L-isoglutamyl)-L-threonine, using free L-glutamine and releasing ammonia.
PubMed:8706862
RESID:AA0536#THR
(2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid
(2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid
5-(threon-O3-yl)glutamate
O(beta)-(gamma-glutamyl)threonine
O-(L-isoglutamyl)-L-threonine
O3-(isoglutamyl)threonine
A protein modification that effectively converts an L-tyrosine residue to 3'-nitro-L-tyrosine.
45.0
C 0 H -1 N 1 O 2
44.985077
C 9 H 8 N 2 O 4
208.17
208.0484
Y
natural
uniprot.ptm:PTM-0434
(2S)-2-amino-3-(4-hydroxy-3-nitrophenyl)propanoic acid
3'-nitro-L-tyrosine
3-nitro-L-tyrosine
3-nitrotyrosine
MOD_RES 3'-Nitrotyrosine
m-nitrotyrosine
meta-nitrotyrosine
PSI-MOD
MOD:01786
3'-nitro-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to 3'-nitro-L-tyrosine.
ChEBI:44454
PubMed:16944230
PubMed:5339594
RESID:AA0537
(2S)-2-amino-3-(4-hydroxy-3-nitrophenyl)propanoic acid
3'-nitro-L-tyrosine
3-nitro-L-tyrosine
3-nitrotyrosine
MOD_RES 3'-Nitrotyrosine
m-nitrotyrosine
meta-nitrotyrosine
A protein modification that effectively cross-links two L-tyrosine residues through their 5' positions by amine nitrogen to form 5'-(L-tyros-5'-yl)amino-L-tyrosine.
13.0
C 0 H -1 N 1 O 0
12.995249
C 18 H 17 N 3 O 4
339.35
339.12192
Y, Y
hypothetical
uniprot.ptm:PTM-0320
(2S,2'S)-3,3'-[iminobis(4-hydroxybenzene-3,1-diyl)]bis(2-aminopropanoic acid)
5'-(L-tyros-5'-yl)amino-L-tyrosine
5'-[(tyros-5'-yl)amino]tyrosine
5'-tyrosyl-5'-aminotyrosine
CROSSLNK 5'-tyrosyl-5'-aminotyrosine (Tyr-Tyr) (interchain)
bis(LTQ) linkage
PSI-MOD
MOD:01787
Cross-link 2.
5'-(L-tyros-5'-yl)amino-L-tyrosine
A protein modification that effectively cross-links two L-tyrosine residues through their 5' positions by amine nitrogen to form 5'-(L-tyros-5'-yl)amino-L-tyrosine.
PubMed:18781570
RESID:AA0459
(2S,2'S)-3,3'-[iminobis(4-hydroxybenzene-3,1-diyl)]bis(2-aminopropanoic acid)
5'-(L-tyros-5'-yl)amino-L-tyrosine
5'-[(tyros-5'-yl)amino]tyrosine
5'-tyrosyl-5'-aminotyrosine
CROSSLNK 5'-tyrosyl-5'-aminotyrosine (Tyr-Tyr) (interchain)
bis(LTQ) linkage
A protein modification that effectively converts an N-terminal L-histidine residue to histidine immonium ion.
-27.0
C -1 H 1 N 0 O -1
-26.987638
1+
C 5 H 8 N 3 O 0
110.14
110.07127
H
artifact
2-(1H-imidazolyl)ethaniminium
PSI-MOD
MOD:01788
This fragment corresponds to the first ion in an a+ series.
histidine immonium ion
A protein modification that effectively converts an N-terminal L-histidine residue to histidine immonium ion.
PubMed:17074506
PubMed:18688235
2-(1H-imidazolyl)ethaniminium
A protein modification that effectively converts an N-terminal L-phenylalanine residue to phenylalanine immonium ion.
-27.0
C -1 H 1 N 0 O -1
-26.987638
1+
C 8 H 10 N 1 O 0
120.17
120.08077
F
artifact
2-phenylethaniminium
PSI-MOD
MOD:01789
This fragment corresponds to the first ion in an a+ series.
phenylalanine immonium ion
A protein modification that effectively converts an N-terminal L-phenylalanine residue to phenylalanine immonium ion.
PubMed:17074506
PubMed:18688235
2-phenylethaniminium
A protein modification that effectively converts an an N-terminal L-tyrosine residue to tyrosine immonium ion.
-27.0
C -1 H 1 N 0 O -1
-26.987638
1+
C 8 H 10 N 1 O 1
136.17
136.07568
Y
artifact
2-(4-hydroxyphenyl)ethaniminium
PSI-MOD
MOD:01790
This fragment corresponds to the first ion in an a+ series.
tyrosine immonium ion
A protein modification that effectively converts an an N-terminal L-tyrosine residue to tyrosine immonium ion.
PubMed:17074506
PubMed:18688235
2-(4-hydroxyphenyl)ethaniminium
A protein modification that effectively converts an N-terminal phosphohistidine residue to phosphohistidine immonium ion.
-27.0
C -1 H 1 N 0 O -1
-26.987638
1+
C 5 H 9 N 3 O 3 P 1
190.12
190.0376
MOD:00890
artifact
2-(1H-imidazolyl)ethaniminium
PSI-MOD
MOD:01791
This fragment corresponds to the first ion in an a+ series.
phosphohistidine immonium ion
A protein modification that effectively converts an N-terminal phosphohistidine residue to phosphohistidine immonium ion.
PubMed:17690871
PubMed:18688235
PubMed:20847263
2-(1H-imidazolyl)ethaniminium
A protein modification that effectively converts an N-terminal O4'-phospho-L-tyrosine residue to tyrosine immonium ion.
-27.0
C -1 H 1 N 0 O -1
-26.987638
1+
C 8 H 11 N 1 O 4 P 1
216.15
216.04202
MOD:00048
artifact
2-(4-phosphonoxyphenyl)ethaniminium
PSI-MOD
MOD:01792
This fragment corresponds to the first ion in an a+ series.
phosphotyrosine immonium ion
A protein modification that effectively converts an N-terminal O4'-phospho-L-tyrosine residue to tyrosine immonium ion.
PubMed:17690871
PubMed:18688235
2-(4-phosphonoxyphenyl)ethaniminium
A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine sulfoxide.
73.05
C 2 H 3 N 1 O 2
73.01638
C 5 H 8 N 2 O 3 S 1
176.19
176.02556
C
artifact
CamCO
S-carbamoylmethyl-L-cysteine sulfoxide
PSI-MOD
MOD:01793
S-carboxamidomethyl-L-cysteine sulfoxide
A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine sulfoxide.
PubMed:11212008
PubMed:17689096
PubMed:18306178
PubMed:18688235
CamCO
S-carbamoylmethyl-L-cysteine sulfoxide
A protein modification that effectively replaces the methyl group of a residue containing common isotopes with a 1x(13)C,3x(2)H labeled monomethylated residue.
18.04
(13)C 1 (1)H -1 (2)H 3
18.037834
X
artifact
PSI-MOD
Methyl:2H(3)13C(1)
MOD:01794
1x(13)C,3x(2)H labeled monomethylated residue
A protein modification that effectively replaces the methyl group of a residue containing common isotopes with a 1x(13)C,3x(2)H labeled monomethylated residue.
PubMed:18688235
Methyl:2H(3)13C(1)
A protein modification that effectively converts an L-methionine residue containing common isotopes to 1x(13)C,3x(2)H C(6)-labeled L-methionine.
4.02
(12)C -1 (13)C 1 (1)H -3 (2)H 3
4.022185
(12)C 4 (13)C 1 (1)H 6 (2)H 3 N 1 O 1 S 1
135.06
135.06267
M
artifact
PSI-MOD
Methyl:2H(3)13C(1)
MOD:01795
1x(13)C,3x(2)H C(6)-labeled L-methionine
A protein modification that effectively converts an L-methionine residue containing common isotopes to 1x(13)C,3x(2)H C(6)-labeled L-methionine.
PubMed:15782174
PubMed:18688235
Methyl:2H(3)13C(1)
A protein modification that effectively converts an L-methionine residue containing common isotopes to 1x(13)C,3x(2)H C(6)-labeled L-methionine sulfoxide.
20.02
(12)C -1 (13)C 1 (1)H -3 (2)H 3 O 1
20.0171
(12)C 4 (13)C 1 (1)H 6 (2)H 3 N 1 O 2 S 1
151.06
151.05759
M
artifact
PSI-MOD
MOD:01796
1x(13)C,3x(2)H C(6)-labeled L-methionine sulfoxide
A protein modification that effectively converts an L-methionine residue containing common isotopes to 1x(13)C,3x(2)H C(6)-labeled L-methionine sulfoxide.
PubMed:15782174
PubMed:18688235
A protein modification that effectively converts an N-terminal 1'-phosphohistidine residue to 1'-phosphohistidine immonium ion.
-27.0
C -1 H 1 N 0 O -1
-26.987638
1+
C 5 H 9 N 3 O 3 P 1
190.12
190.0376
MOD:00044
artifact
2-((1-phosphono-1H-imidazol-4-yl)ethaniminium
Ntau-phosphorylated L-histidine
PSI-MOD
MOD:01797
This fragment corresponds to the first ion in an a+ series.
1'-phosphohistidine immonium ion
A protein modification that effectively converts an N-terminal 1'-phosphohistidine residue to 1'-phosphohistidine immonium ion.
PubMed:17690871
PubMed:18688235
PubMed:20847263
2-((1-phosphono-1H-imidazol-4-yl)ethaniminium
Ntau-phosphorylated L-histidine
A protein modification that effectively converts an N-terminal 3'-phosphohistidine residue to 3'-phosphohistidine immonium ion.
-27.0
C -1 H 1 N 0 O -1
-26.987638
1+
C 5 H 9 N 3 O 3 P 1
190.12
190.0376
MOD:00045
artifact
2-(1-phosphono-1H-imidazol-5-yl)ethaniminium
Npi-phosphorylated L-histidine
PSI-MOD
MOD:01798
This fragment corresponds to the first ion in an a+ series.
3'-phosphohistidine immonium ion
A protein modification that effectively converts an N-terminal 3'-phosphohistidine residue to 3'-phosphohistidine immonium ion.
PubMed:18688235
2-(1-phosphono-1H-imidazol-5-yl)ethaniminium
Npi-phosphorylated L-histidine
A protein modification that effectively converts an L-alanine residue to a methylated serine, such as N-methylserine, N,N-dimethylserine, or N,N,N-trimethylserine.
S
MeSer
PSI-MOD
MOD:01799
methylated serine
A protein modification that effectively converts an L-alanine residue to a methylated serine, such as N-methylserine, N,N-dimethylserine, or N,N,N-trimethylserine.
PubMed:18688235
MeSer
A protein modification that effectively replaces an L-serine alpha amino hydrogen with a methyl group.
S
natural
N-term
PSI-MOD
MOD:01800
N-methylated serine
A protein modification that effectively replaces an L-serine alpha amino hydrogen with a methyl group.
PubMed:18688235
A protein modification that effectively converts an L-serine residue to an L-serinium (protonated L-serine).
1.01
C 0 H 1 N 0 O 0
1.007276
1+
C 3 H 7 N 1 O 2
89.09
89.04713
S
natural
N-term
PSI-MOD
MOD:01801
protonated L-serine (L-serinium) residue
A protein modification that effectively converts an L-serine residue to an L-serinium (protonated L-serine).
PubMed:18688235
A protein modification that effectively converts an L-serinium (protonated L-serine) residue to an N,N,N-trimethyl-L-serine.
42.08
C 3 H 6 N 0 O 0
42.046402
1+
C 6 H 13 N 1 O 2
131.17
131.09409
MOD:01801
natural
N-term
N2Me3Ala
PSI-MOD
MOD:01802
For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative N2Me3+Ser process (MOD:00071) accounts for both protonation and trimethylation.
N,N,N-trimethyl-L-serine (from L-serinium)
A protein modification that effectively converts an L-serinium (protonated L-serine) residue to an N,N,N-trimethyl-L-serine.
PubMed:18688235
N2Me3Ala
A protein modification that effectively converts an L-threonine residue to a methylated threonine, such as O-methyl-L-threonine or L-threonine methyl ester.
T
natural
OMeThr
PSI-MOD
MOD:01803
O-methylated threonine
A protein modification that effectively converts an L-threonine residue to a methylated threonine, such as O-methyl-L-threonine or L-threonine methyl ester.
PubMed:18688235
OMeThr
A protein modification that effectively results from forming an adduct with a glycosylphosphate through a phosphodiester bond.
PSI-MOD
MOD:01804
glycosylphosphorylated residue
A protein modification that effectively results from forming an adduct with a glycosylphosphate through a phosphodiester bond.
PubMed:18688235
A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)-glycine and the release of water.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 6 H 7 N 2 O 3
155.13
155.04567
D, G
natural
N-term
uniprot.ptm:PTM-0490
(2S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid
2-amino-N4-(carboxymethyl)-butanediamic acid
CROSSLNK Isoaspartyl glycine isopeptide (Asp-Gly)
CROSSLNK Isoaspartyl glycine isopeptide (Gly-Asp)
N-(L-isoaspartyl)-glycine
N-beta-aspartylglycine
N4-(carboxymethyl)-asparagine
isoaspartyl glycine
PSI-MOD
MOD:01805
Cross-link 2.
N-(L-isoaspartyl)-glycine (Asp)
A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)-glycine and the release of water.
ChEBI:21479
PubMed:1826288
PubMed:18671394
RESID:AA0126
(2S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid
2-amino-N4-(carboxymethyl)-butanediamic acid
CROSSLNK Isoaspartyl glycine isopeptide (Asp-Gly)
CROSSLNK Isoaspartyl glycine isopeptide (Gly-Asp)
N-(L-isoaspartyl)-glycine
N-beta-aspartylglycine
N4-(carboxymethyl)-asparagine
isoaspartyl glycine
A protein modification that effectively converts an L-leucine residue to N,N-dimethyl-L-leucine.
28.05
C 2 H 4 N 0 O 0
28.0313
C 8 H 16 N 1 O 1
142.22
142.12318
L
hypothetical
N-term
uniprot.ptm:PTM-0435
(2S)-2-(dimethylamino)-4-methylpentanoic acid
2-(dimethylamino)-4-methylvaleric acid
2-(dimethylazanyl)-4-methylpentanoic acid
MOD_RES N,N-dimethylleucine
N,N-dimethyl-L-leucine
N,N-dimethylleucine
PSI-MOD
MOD:01806
N,N-dimethyl-L-leucine
A protein modification that effectively converts an L-leucine residue to N,N-dimethyl-L-leucine.
PubMed:19522542
RESID:AA0538
(2S)-2-(dimethylamino)-4-methylpentanoic acid
2-(dimethylamino)-4-methylvaleric acid
2-(dimethylazanyl)-4-methylpentanoic acid
MOD_RES N,N-dimethylleucine
N,N-dimethyl-L-leucine
N,N-dimethylleucine
A protein modification that effectively converts an L-glutamic acid residue to N-formyl-L-glutamic acid.
28.01
C 1 H 0 N 0 O 1
27.994915
C 6 H 8 N 1 O 4
158.13
158.04533
E
artifact
N-term
(2S)-2-(formylamino)pentanedioic acid
2-(formylazanyl)pentanedioic acid
2-formamidopentanedioic acid
2-formylaminopentanedioic acid
N-formyl-L-glutamic acid
PSI-MOD
MOD:01807
N-formyl-L-glutamic acid
A protein modification that effectively converts an L-glutamic acid residue to N-formyl-L-glutamic acid.
PubMed:18001127
RESID:AA0539
(2S)-2-(formylamino)pentanedioic acid
2-(formylazanyl)pentanedioic acid
2-formamidopentanedioic acid
2-formylaminopentanedioic acid
N-formyl-L-glutamic acid
A protein modification that effectively replaces an L-leucine alpha amino hydrogen with a methyl group.
L
MeLeu
PSI-MOD
MOD:01808
N-methylated leucine
A protein modification that effectively replaces an L-leucine alpha amino hydrogen with a methyl group.
PubMed:18688235
MeLeu
A protein modification that effectively converts a residue containing common isotopes to a 5x(13)C,1x(15)N labeled residue.
6.01
(12)C -5 (13)C 5 (14)N -1 (15)N 1
6.013809
X
artifact
Unimod:268
PSI-MOD
13C(5) 15N(1) Silac label
Label:13C(5)15N(1)
MOD:01809
5x(13)C,1x(15)N labeled residue
A protein modification that effectively converts a residue containing common isotopes to a 5x(13)C,1x(15)N labeled residue.
PubMed:12771378
Unimod:268
13C(5) 15N(1) Silac label
Label:13C(5)15N(1)
A protein modification that effectively converts an L-proline residue to 5x(13)C,1x(15)N labeled L-proline.
6.01
(12)C -5 (13)C 5 (14)N -1 (15)N 1
6.013809
(13)C 5 H 7 (15)N 1 O 1
103.07
103.066574
P
artifact
Unimod:268
PSI-MOD
13C(5) 15N(1) Silac label
Label:13C(5)15N(1)
MOD:01810
5x(13)C,1x(15)N labeled L-proline
A protein modification that effectively converts an L-proline residue to 5x(13)C,1x(15)N labeled L-proline.
PubMed:12771378
Unimod:268#P
13C(5) 15N(1) Silac label
Label:13C(5)15N(1)
A protein modification that effectively converts an L-methionine residue to 5x(13)C,1x(15)N labeled L-methionine.
6.01
(12)C -5 (13)C 5 (14)N -1 (15)N 1
6.013809
(13)C 5 H 9 (15)N 1 O 1 S 1
137.05
137.05429
M
artifact
Unimod:268
PSI-MOD
13C(5) 15N(1) Silac label
Label:13C(5)15N(1)
MOD:01811
5x(13)C,1x(15)N labeled L-methionine
A protein modification that effectively converts an L-methionine residue to 5x(13)C,1x(15)N labeled L-methionine.
PubMed:12771378
Unimod:268#M
13C(5) 15N(1) Silac label
Label:13C(5)15N(1)
A protein modification that effectively converts an L-methionine residue to 5x(13)C,1x(15)N labeled L-methionine sulfoxide.
6.01
(12)C -5 (13)C 5 (14)N -1 (15)N 1
6.013809
(13)C 5 H 9 (15)N 1 O 2 S 1
153.05
153.04921
M
artifact
Unimod:268
PSI-MOD
13C(5) 15N(1) Silac label
Label:13C(5)15N(1)
MOD:01812
5x(13)C,1x(15)N labeled L-methionine sulfoxide
A protein modification that effectively converts an L-methionine residue to 5x(13)C,1x(15)N labeled L-methionine sulfoxide.
PubMed:12771378
Unimod:268#M
13C(5) 15N(1) Silac label
Label:13C(5)15N(1)
A protein modification that effectively substitutes a morpholine-2-acetyl group for a hydrogen atom.
127.14
C 6 H 9 N 1 O 2
127.06333
X
artifact
Unimod:29
N-succinimidylmorpholine-2-acetate derivative
PSI-MOD
N-Succinimidyl-2-morpholine acetate
SMA
MOD:01813
The Unimod name "N-Succinimidyl-3-morpholine acetate" appears to have been a typographical error [JSG].
morpholine-2-acetylated residue
A protein modification that effectively substitutes a morpholine-2-acetyl group for a hydrogen atom.
PubMed:10446193
Unimod:29
N-succinimidylmorpholine-2-acetate derivative
N-Succinimidyl-2-morpholine acetate
SMA
A protein modification that effectively cross-links a cysteine and two serine residues to form L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid.
-54.07
C 0 H -8 N -1 O -2 S 0
-54.055504
C 9 H 7 N 2 O 3 S 1
223.23
223.01773
C, S, S
natural
uniprot.ptm:PTM-0454
6-[(1R)-1-amino-2-sulfanylethyl]-3-hydroxypyridine-2,5-dicarboxylic acid
6-[1-azanyl-2-sulfanylethyl]-3-hydroxypyridine-2,5-dicarboxylic acid
L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid
PSI-MOD
CROSSLNK 3-hydroxypyridine-2,5-dicarboxylic acid (Ser-Cys)
MOD:01814
Cross-link 3.
L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid
A protein modification that effectively cross-links a cysteine and two serine residues to form L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid.
PubMed:18406324
PubMed:19678698
PubMed:893891
RESID:AA0540
6-[(1R)-1-amino-2-sulfanylethyl]-3-hydroxypyridine-2,5-dicarboxylic acid
6-[1-azanyl-2-sulfanylethyl]-3-hydroxypyridine-2,5-dicarboxylic acid
L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid
CROSSLNK 3-hydroxypyridine-2,5-dicarboxylic acid (Ser-Cys)
A protein modification that effectively crosslinks an L-cysteine residue and an L-glutamic acid residue to form L-glutamate thiazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 8 H 8 N 2 O 3 S 1
212.22
212.02556
C, E
natural
uniprot.ptm:PTM-0456
2-[(1S)-1-amino-3-carboxypropyl]-1,3-thiazole-4-carboxylic acid
2-[-1-azanyl-3-carboxypropyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Glu-Cys)
L-glutamate thiazole-4-carboxylic acid
PSI-MOD
MOD:01815
Cross-link 2.
L-glutamate thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-glutamic acid residue to form L-glutamate thiazole-4-carboxylic acid.
PubMed:18406324
PubMed:19678698
PubMed:893891
RESID:AA0541
2-[(1S)-1-amino-3-carboxypropyl]-1,3-thiazole-4-carboxylic acid
2-[-1-azanyl-3-carboxypropyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Glu-Cys)
L-glutamate thiazole-4-carboxylic acid
A protein modification that effectively converts an L-tryptophan residue to a 2'-hydroxy-L-tryptophan.
16.0
C 0 H 0 N 0 O 1
15.994915
C 11 H 10 N 2 O 2
202.21
202.07423
W
artifact
(2S)-2-amino-3-(2-hydroxy-1H-indol-3-yl)propanoic acid
2'-hydroxy-L-tryptophan
2-azanyl-3-(2-hydroxy-1H-indol-3-yl)propanoic acid
2-hydroxy-L-tryptophan
2-hydroxy-tryptophan
PSI-MOD
MOD:01816
2'-hydroxy-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to a 2'-hydroxy-L-tryptophan.
PubMed:11714714
RESID:AA0542
(2S)-2-amino-3-(2-hydroxy-1H-indol-3-yl)propanoic acid
2'-hydroxy-L-tryptophan
2-azanyl-3-(2-hydroxy-1H-indol-3-yl)propanoic acid
2-hydroxy-L-tryptophan
2-hydroxy-tryptophan
A protein modification that effectively converts an L-tryptophan residue to a 2'-oxo-L-tryptophan.
16.0
C 0 H 0 N 0 O 1
15.994915
C 11 H 10 N 2 O 2
202.21
202.07423
W
artifact
(2S)-2-amino-3-[(3S)-2-oxo-2,3-dihydro-1H-indol-3-yl]propanoic acid
2'-oxo-L-tryptophan
2-azanyl-3-[(3S)-2-oxo-2,3-dihydro-1H-indol-3-yl]propanoic acid
2-oxo-L-tryptophan
2-oxotryptophan
PSI-MOD
MOD:01817
2'-oxo-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to a 2'-oxo-L-tryptophan.
PubMed:9461080
RESID:AA0543
(2S)-2-amino-3-[(3S)-2-oxo-2,3-dihydro-1H-indol-3-yl]propanoic acid
2'-oxo-L-tryptophan
2-azanyl-3-[(3S)-2-oxo-2,3-dihydro-1H-indol-3-yl]propanoic acid
2-oxo-L-tryptophan
2-oxotryptophan
A protein modification that effectively cross-links two tryptophan residues to form 1'-(L-tryptophan-3'-yl)-L-tryptophan.
-2.02
C 0 H -2 N 0 O 0
-2.01565
C 22 H 18 N 4 O 2
370.41
370.14297
W, W
natural
uniprot.ptm:PTM-0544
(2S,2'S)-3,3'-(3'H-1,3'-biindole-3,3'-diyl)bis(2-aminopropanoic acid)
1-(L-tryptophan-3-yl)-L-tryptophan
2-amino-3-[2-[2-amino-3-(2-carboxyethyl)-1H-indol-4-yl]-1H-indol-3-yl]propanoic acid
3-[(2S)-2-amino-2-carboxyethyl]-3-(3-[(2S)-2-amino-2-carboxyethyl]-1H-indol-2-yl)-1H-indole
3-[2-azanyl-2-carboxyethyl]-3-(3-[2-azanyl-2-carboxyethyl]-1H-indol-2-yl)-1H-indole
ditryptophan
PSI-MOD
MOD:01818
Cross-link 2.
1'-(L-tryptophan-3'-yl)-L-tryptophan
A protein modification that effectively cross-links two tryptophan residues to form 1'-(L-tryptophan-3'-yl)-L-tryptophan.
PubMed:20600836
RESID:AA0544
(2S,2'S)-3,3'-(3'H-1,3'-biindole-3,3'-diyl)bis(2-aminopropanoic acid)
1-(L-tryptophan-3-yl)-L-tryptophan
2-amino-3-[2-[2-amino-3-(2-carboxyethyl)-1H-indol-4-yl]-1H-indol-3-yl]propanoic acid
3-[(2S)-2-amino-2-carboxyethyl]-3-(3-[(2S)-2-amino-2-carboxyethyl]-1H-indol-2-yl)-1H-indole
3-[2-azanyl-2-carboxyethyl]-3-(3-[2-azanyl-2-carboxyethyl]-1H-indol-2-yl)-1H-indole
ditryptophan
A protein modification that effectively converts an L-lysine residue to N6-succinyl-L-lysine.
100.07
C 4 H 4 N 0 O 3
100.016045
C 10 H 16 N 2 O 4
228.25
228.11101
K
natural
uniprot.ptm:PTM-0438
(2S)-2-amino-6-[(3-carboxypropanoyl)amino]hexanoic acid
2-azanyl-6-[(3-carboxypropanoyl)azanyl]hexanoic acid
4-[[(5S)-5-amino-6-hydroxy-6-oxohexyl]amino]-4-oxobutanoate
MOD_RES N6-succinyllysine
N(epsilon)-(succinyl)lysine
N6-succinyl-L-lysine
succinyllysine
PSI-MOD
MOD:01819
N6-succinyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-succinyl-L-lysine.
PubMed:16582421
PubMed:21151122
RESID:AA0545
(2S)-2-amino-6-[(3-carboxypropanoyl)amino]hexanoic acid
2-azanyl-6-[(3-carboxypropanoyl)azanyl]hexanoic acid
4-[[(5S)-5-amino-6-hydroxy-6-oxohexyl]amino]-4-oxobutanoate
MOD_RES N6-succinyllysine
N(epsilon)-(succinyl)lysine
N6-succinyl-L-lysine
succinyllysine
A protein modification that effectively replaces a cysteine sulhydryl hydrogen with an isotope tagged sulfhydryl reagent group.
C
artifact
PSI-MOD
MOD:01820
isotope tagged sufhydryl reagent modified cysteine
A protein modification that effectively replaces a cysteine sulhydryl hydrogen with an isotope tagged sulfhydryl reagent group.
PubMed:18688235
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex reporter+balance group.
C
artifact
Unimod:985
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
PSI-MOD
cysTMT6plex
cysteine-reactive Sixplex Tandem Mass Tag(TM)
MOD:01821
The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
cysTMT6plex reporter+balance reagent cysteine disulfide
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex reporter+balance group.
URL:http://www.piercenet.com/files/2162220.pdf
Unimod:985
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
cysTMT6plex
cysteine-reactive Sixplex Tandem Mass Tag(TM)
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-zero reporter+balance group.
299.17
(12)C 14 H 25 (14)N 3 O 2 S 1
299.16675
(12)C 17 H 32 (14)N 4 O 4 S 2
420.19
420.1865
C
artifact
Unimod:984
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
PSI-MOD
Native cysteine-reactive Tandem Mass Tag(TM)
cysTMT
MOD:01822
The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
cysTMT6plex-zero reporter+balance reagent cysteine disulfide
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-zero reporter+balance group.
URL:http://www.piercenet.com/files/2162220.pdf
Unimod:984
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
Native cysteine-reactive Tandem Mass Tag(TM)
cysTMT
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-126 reporter+balance group.
304.18
(12)C 10 (13)C 4 H 25 (14)N 2 (15)N 1 O 2 S 1
304.17722
(12)C 13 (13)C 4 H 32 (14)N 3 (15)N 1 O 4 S 2
425.2
425.19696
C
artifact
Unimod:985
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
PSI-MOD
cysTMT6plex
cysteine-reactive Sixplex Tandem Mass Tag(TM)
MOD:01823
The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
cysTMT6plex-126 reporter+balance reagent cysteine disulfide
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-126 reporter+balance group.
PubMed:18688235
URL:http://www.piercenet.com/files/2162220.pdf
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
cysTMT6plex
cysteine-reactive Sixplex Tandem Mass Tag(TM)
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-127 reporter+balance group.
304.18
(12)C 10 (13)C 4 H 25 (14)N 2 (15)N 1 O 2 S 1
304.17722
(12)C 13 (13)C 4 H 32 (14)N 3 (15)N 1 O 4 S 2
425.2
425.19696
C
artifact
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
PSI-MOD
cysTMT6plex
cysteine-reactive Sixplex Tandem Mass Tag(TM)
MOD:01824
The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
cysTMT6plex-127 reporter+balance reagent cysteine disulfide
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-127 reporter+balance group.
PubMed:18688235
URL:http://www.piercenet.com/files/2162220.pdf
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
cysTMT6plex
cysteine-reactive Sixplex Tandem Mass Tag(TM)
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-128 reporter+balance group.
304.18
(12)C 10 (13)C 4 H 25 (14)N 2 (15)N 1 O 2 S 1
304.17722
(12)C 13 (13)C 4 H 32 (14)N 3 (15)N 1 O 4 S 2
425.2
425.19696
C
artifact
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
PSI-MOD
cysTMT6plex
cysteine-reactive Sixplex Tandem Mass Tag(TM)
MOD:01825
The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
cysTMT6plex-128 reporter+balance reagent cysteine disulfide
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-128 reporter+balance group.
PubMed:18688235
URL:http://www.piercenet.com/files/2162220.pdf
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
cysTMT6plex
cysteine-reactive Sixplex Tandem Mass Tag(TM)
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-129 reporter+balance group.
304.18
(12)C 10 (13)C 4 H 25 (14)N 2 (15)N 1 O 2 S 1
304.17722
(12)C 13 (13)C 4 H 32 (14)N 3 (15)N 1 O 4 S 2
425.2
425.19696
C
artifact
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
PSI-MOD
cysTMT6plex
cysteine-reactive Sixplex Tandem Mass Tag(TM)
MOD:01826
The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
cysTMT6plex-129 reporter+balance reagent cysteine disulfide
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-129 reporter+balance group.
PubMed:18688235
URL:http://www.piercenet.com/files/2162220.pdf
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
cysTMT6plex
cysteine-reactive Sixplex Tandem Mass Tag(TM)
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-130 reporter+balance group.
304.18
(12)C 10 (13)C 4 H 25 (14)N 2 (15)N 1 O 2 S 1
304.17722
(12)C 13 (13)C 4 H 32 (14)N 3 (15)N 1 O 4 S 2
425.2
425.19696
C
artifact
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
PSI-MOD
cysTMT6plex
cysteine-reactive Sixplex Tandem Mass Tag(TM)
MOD:01827
The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
cysTMT6plex-130 reporter+balance reagent cysteine disulfide
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-130 reporter+balance group.
PubMed:18688235
URL:http://www.piercenet.com/files/2162220.pdf
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
cysTMT6plex
cysteine-reactive Sixplex Tandem Mass Tag(TM)
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-131 reporter+balance group.
304.18
(12)C 10 (13)C 4 H 25 (14)N 2 (15)N 1 O 2 S 1
304.17722
(12)C 13 (13)C 4 H 32 (14)N 3 (15)N 1 O 4 S 2
425.2
425.19696
C
artifact
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
PSI-MOD
cysTMT6plex
cysteine-reactive Sixplex Tandem Mass Tag(TM)
MOD:01828
The reagent consists of a reporter group, a balance group and a protein sulfhydryl reactive pyridine disulfanyl group. The reporter group, an isotopically labeled 1,2,6-trimethylpiperidine, is connected to a 3-(carbonylamino)propanoyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
cysTMT6plex-131 reporter+balance reagent cysteine disulfide
A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-131 reporter+balance group.
PubMed:18688235
URL:http://www.piercenet.com/files/2162220.pdf
S-(2-{3-[2-(2,6-dimethylpiperidin-1-yl)acetamido]propanamido}ethyl)sulfanyl
cysTMT6plex
cysteine-reactive Sixplex Tandem Mass Tag(TM)
A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine sulfoxide.
58.04
C 2 H 2 N 0 O 2 S 0
58.005478
C 5 H 7 N 1 O 3 S 1
161.18
161.01466
C
artifact
CmCO
PSI-MOD
MOD:01829
S-carboxymethyl-L-cysteine sulfoxide
A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine sulfoxide.
PubMed:17689096
PubMed:18688235
CmCO
A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine sulfone.
74.03
C 2 H 2 N 0 O 3 S 0
74.0004
C 5 H 7 N 1 O 4 S 1
177.17
177.00958
C
artifact
CmCO2
PSI-MOD
MOD:01830
S-carboxymethyl-L-cysteine sulfone
A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine sulfone.
PubMed:18688235
CmCO2
A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine sulfone.
89.05
C 2 H 3 N 1 O 3
89.01129
C 5 H 8 N 2 O 4 S 1
192.19
192.02048
C
artifact
CamCO2
S-carbamoylmethyl-L-cysteine sulfone
PSI-MOD
MOD:01831
S-carboxamidomethyl-L-cysteine sulfone
A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine sulfone.
PubMed:18688235
CamCO2
S-carbamoylmethyl-L-cysteine sulfone
A protein modification that effectively converts a residue containing common isotopes to a 5x(13)C-labeled residue.
5.02
(12)C -5 (13)C 5
5.016774
X
artifact
Unimod:772
PSI-MOD
13C(5) Silac label
Label:13C(5)
MOD:01832
5x(13)C-labeled residue
A protein modification that effectively converts a residue containing common isotopes to a 5x(13)C-labeled residue.
PubMed:12771378
Unimod:772
13C(5) Silac label
Label:13C(5)
A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine.
5.02
(12)C -5 (13)C 5 H 0 N 0 O 0 S 0
5.016774
(13)C 5 H 9 N 1 O 1 S 1
136.06
136.05727
M
artifact
PSI-MOD
MOD:01833
5x(13)C-labeled L-methionine
A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine.
PubMed:18688235
url:
A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine sulfoxide.
5.02
(12)C -5 (13)C 5 H 0 N 0 O 0 S 0
5.016774
(13)C 5 H 9 N 1 O 2 S 1
152.05
152.05217
MOD:00719
artifact
PSI-MOD
MOD:01834
5x(13)C-labeled L-methionine sulfoxide
A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine sulfoxide.
PubMed:18688235
A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine sulfone.
5.02
(12)C -5 (13)C 5 H 0 N 0 O 0 S 0
5.016774
(13)C 5 H 9 N 1 O 3 S 1
168.05
168.04709
MOD:00256
artifact
PSI-MOD
MOD:01835
5x(13)C-labeled L-methionine sulfone
A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine sulfone.
PubMed:18688235
A protein modification that effectively converts an L-lysine residue to N6-[([1-(6-nitro-2H-1,3-benzodioxol-5-yl)ethoxy]carbonyl]lysine.
237.17
C 10 H 7 N 1 O 6
237.02734
C 16 H 19 N 3 O 7
365.34
365.1223
K
artifact
(2S)-2-amino-6-[([1-(6-nitro-1,3-benzodioxol-5-yl)ethoxy]carbonyl)amino]hexanoic acid
[(alpha-methyl-6-nitro-piperonyloxy)carbonyl]lysine
PSI-MOD
MOD:01836
N6-[([1-(6-nitro-2H-1,3-benzodioxol-5-yl)ethoxy]carbonyl]lysine
A protein modification that effectively converts an L-lysine residue to N6-[([1-(6-nitro-2H-1,3-benzodioxol-5-yl)ethoxy]carbonyl]lysine.
PubMed:18688235
PubMed:20218600
PubMed:21271704
(2S)-2-amino-6-[([1-(6-nitro-1,3-benzodioxol-5-yl)ethoxy]carbonyl)amino]hexanoic acid
[(alpha-methyl-6-nitro-piperonyloxy)carbonyl]lysine
A protein modification that effectively cross-links two L-cysteine residues with a thioether bond to form L-lanthionine.
-34.08
C 0 H -2 N 0 O 0 S -1
-33.98772
C 6 H 8 N 2 O 2 S 1
172.2
172.03065
C, C
hypothetical
(2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid)
(R)-S-(2-amino-2-carboxyethyl)-L-cysteine
(R,R)-2,6-diamino-4-thiaheptanedioic acid
(R,R)-3,3'-thiobis-(2-aminopropanoic acid)
(R,R)-bis(2-amino-2-carboxyethyl)sulfide
2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid
3,3'-thiobis-L-alanine
L-lanthionine
PSI-MOD
MOD:01837
Cross-link 2.
L-lanthionine (Cys-Cys)
A protein modification that effectively cross-links two L-cysteine residues with a thioether bond to form L-lanthionine.
ChEBI:21347
PubMed:20805503
PubMed:6007887
RESID:AA0110#CYS2
(2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid)
(R)-S-(2-amino-2-carboxyethyl)-L-cysteine
(R,R)-2,6-diamino-4-thiaheptanedioic acid
(R,R)-3,3'-thiobis-(2-aminopropanoic acid)
(R,R)-bis(2-amino-2-carboxyethyl)sulfide
2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid
3,3'-thiobis-L-alanine
L-lanthionine
A protein modification that effectively converts an L-lysine residue to L-lysinoalanine.
87.08
C 3 H 5 N 1 O 2
87.03203
C 9 H 17 N 3 O 3
215.25
215.12698
K
natural
uniprot.ptm:PTM-0439
(2R,9S)-lysinoalanine
(2S)-2-amino-6-([(2R)-2-amino-2-carboxyethyl]amino)hexanoic acid
L-lysinoalanine
LAL
MOD_RES Lysino-D-alanine (Lys)
N-epsilon-(2-amino-2-carboxyethyl)-L-lysine
N6-(2-amino-2-carboxyethyl)-L-lysine
alaninolysine
lysino-D-alanine
PSI-MOD
MOD:01838
This entry is for the modification of peptidyl lysine by a free serine. For the crosslink of peptidyl serine and peptidyl lysine see MOD:00132.
L-lysinoalanine (Lys)
A protein modification that effectively converts an L-lysine residue to L-lysinoalanine.
PubMed:19155267
PubMed:2544544
RESID:AA0123#LYS
(2R,9S)-lysinoalanine
(2S)-2-amino-6-([(2R)-2-amino-2-carboxyethyl]amino)hexanoic acid
L-lysinoalanine
LAL
MOD_RES Lysino-D-alanine (Lys)
N-epsilon-(2-amino-2-carboxyethyl)-L-lysine
N6-(2-amino-2-carboxyethyl)-L-lysine
alaninolysine
lysino-D-alanine
A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 6 H 8 N 2 O 2 S 1
172.2
172.03065
C, X
artifact
PSI-MOD
MOD:01839
Cross-link 2. For the natural form of the lanthionine cross-link see MOD:00120 meso-lanthionine [JSG].
L-lanthionine
A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine.
PubMed:18688235
A protein modification that effectively converts an L-isoleucine residue to L-allo-isoleucine.
0.0
C 0 H 0 N 0 O 0
0.0
C 6 H 11 N 1 O 1
113.16
113.08406
I
natural
uniprot.ptm:PTM-0442
(2S,3R)-2-amino-3-methylpentanoic acid
2-azanyl-3-methylpentanoic acid
3-methyl-norvaline
L-allo-isoleucine
L-threo-isoleucine
MOD_RES L-allo-isoleucine
allo-L-isoleucine
alpha-amino-beta-methylvaleric acid
PSI-MOD
MOD:01840
L-allo-isoleucine
A protein modification that effectively converts an L-isoleucine residue to L-allo-isoleucine.
ChEBI:43433
PubMed:20805503
RESID:AA0546
(2S,3R)-2-amino-3-methylpentanoic acid
2-azanyl-3-methylpentanoic acid
3-methyl-norvaline
L-allo-isoleucine
L-threo-isoleucine
MOD_RES L-allo-isoleucine
allo-L-isoleucine
alpha-amino-beta-methylvaleric acid
A protein modification that effectively cross-links either two or an L-cysteine residue and an L-serine residue by a thioether bond to form a lanthionine, either D- or L- or meso-lanthionine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 6 H 8 N 2 O 2 S 1
172.2
172.03065
C, X
artifact
2,6-diamino-4-thiaheptanedioic acid
2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid
3,3'-thiobis-(2-aminopropanoic acid)
3,3'-thiobis-L-alanine
S-(2-amino-2-carboxyethyl)-L-cysteine
bis(2-amino-2-carboxyethyl)sulfanediyl
bis(2-amino-2-carboxyethyl)sulfide
PSI-MOD
MOD:01841
Cross-link 2. [JSG].
lanthionine
A protein modification that effectively cross-links either two or an L-cysteine residue and an L-serine residue by a thioether bond to form a lanthionine, either D- or L- or meso-lanthionine.
PubMed:18688235
2,6-diamino-4-thiaheptanedioic acid
2-amino-3-(2-amino-2-carboxyethyl)sulfanylpropanoic acid
3,3'-thiobis-(2-aminopropanoic acid)
3,3'-thiobis-L-alanine
S-(2-amino-2-carboxyethyl)-L-cysteine
bis(2-amino-2-carboxyethyl)sulfanediyl
bis(2-amino-2-carboxyethyl)sulfide
A protein modification that effectively converts two L-cysteine residues to S-(2-aminovinyl)-L-cysteine.
-80.1
C -1 H -4 N 0 O -2 S -1
-79.9932
C 5 H 7 N 2 O 1 S 1
143.18
143.02791
C, C
natural
C-term
uniprot.ptm:PTM-0443
(2R)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid
(R,Z)-S-(2-aminovinyl)cysteine
S-(2-aminovinyl)-L-cysteine
PSI-MOD
MOD:01842
Cross-link 2.
S-(2-aminovinyl)-L-cysteine
A protein modification that effectively converts two L-cysteine residues to S-(2-aminovinyl)-L-cysteine.
PubMed:20805503
RESID:AA0548
(2R)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid
(R,Z)-S-(2-aminovinyl)cysteine
S-(2-aminovinyl)-L-cysteine
A protein modification that effectively converts an L-tryptophan residue to 5'-chloro-L-tryptophan.
34.44
C 0 Cl 1 H -1 N 0 O 0
33.96103
C 11 Cl 1 H 9 N 2 O 1
220.66
220.04034
W
natural
uniprot.ptm:PTM-0444
(2S)-2-amino-3-(5-chloro-1H-indol-3-yl)propanoic acid
5'-chloro-L-tryptophan
MOD_RES 5'-chlorotryptophan
PSI-MOD
MOD:01843
5'-chloro-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to 5'-chloro-L-tryptophan.
PubMed:18215770
RESID:AA0549
(2S)-2-amino-3-(5-chloro-1H-indol-3-yl)propanoic acid
5'-chloro-L-tryptophan
MOD_RES 5'-chlorotryptophan
A protein modification that effectively converts an L-cysteine residue and an L-leucine residue to 2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid.
-5.06
C 0 H -7 N -1 O 1 S 0
-5.062935
C 9 H 10 N 1 O 3 S 1
212.24
212.03813
C, L
natural
N-term
uniprot.ptm:PTM-0448
(4Z)-4-[hydroxy(sulfanyl)methylidene]-2-(3-methylbutanoyl)-1,3-oxazol-5(4H)-one [tautomer]
2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid
5-hydroxy-2-(3-methylbutanoyl)-1,3-oxazole-4-carbothioic O-acid
MOD_RES 2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid (Leu-Cys)
PSI-MOD
MOD:01844
Cross-link 2.
2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid
A protein modification that effectively converts an L-cysteine residue and an L-leucine residue to 2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid.
PubMed:15361623
PubMed:18729522
PubMed:20961038
PubMed:21254756
RESID:AA0550
(4Z)-4-[hydroxy(sulfanyl)methylidene]-2-(3-methylbutanoyl)-1,3-oxazol-5(4H)-one [tautomer]
2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid
5-hydroxy-2-(3-methylbutanoyl)-1,3-oxazole-4-carbothioic O-acid
MOD_RES 2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid (Leu-Cys)
A protein modification that effectively converts an L-cysteine residue and an L-proline residue to L-proline 5-hydroxyoxazole-4-carbothionic acid.
-4.03
C 0 H -4 N 0 O 0 S 0
-4.0313
C 8 H 8 N 2 O 2 S 1
196.22
196.03065
C, P
natural
uniprot.ptm:PTM-0449
(4Z)-4-[hydroxy(sulfanyl)methylidene]-2-[(2S)-pyrrolidin-2-yl]-1,3-oxazol-5(4H)-one [tautomer]
5-hydroxy-2-[(2S)-pyrrolidin-2-yl]-1,3-oxazole-4-carbothioic O-acid
CROSSLNK Proline 5-hydroxy-oxazole-4-carbothionic acid (Pro-Cys)
L-proline 5-hydroxy-oxazole-4-carbothionic acid
PSI-MOD
MOD:01845
Cross-link 2.
L-proline 5-hydroxyoxazole-4-carbothionic acid
A protein modification that effectively converts an L-cysteine residue and an L-proline residue to L-proline 5-hydroxyoxazole-4-carbothionic acid.
PubMed:15361623
PubMed:18729522
PubMed:20961038
PubMed:21254756
RESID:AA0551
(4Z)-4-[hydroxy(sulfanyl)methylidene]-2-[(2S)-pyrrolidin-2-yl]-1,3-oxazol-5(4H)-one [tautomer]
5-hydroxy-2-[(2S)-pyrrolidin-2-yl]-1,3-oxazole-4-carbothioic O-acid
CROSSLNK Proline 5-hydroxy-oxazole-4-carbothionic acid (Pro-Cys)
L-proline 5-hydroxy-oxazole-4-carbothionic acid
A protein modification that effectively converts two L-cysteine residues, and a copper atom to the methanobactin OB3b copper complex.
85.46
C 0 Cu 1 H -10 N 0 O 2 S 0
84.84118
C 6 Cu 1 H 0 N 2 O 4 S 2
291.74
290.85956
C, C
natural
N-term
METAL copper [Cu-methanobactin OB3b complex]
bis[4-(hydroxy[sulfanyl-kappaS]methylidene)-1,3-oxazol-5(4H)-onato-kappaN]copper
methanobactin OB3b copper complex
PSI-MOD
MOD:01846
Cross-link 2.
methanobactin OB3b copper complex
A protein modification that effectively converts two L-cysteine residues, and a copper atom to the methanobactin OB3b copper complex.
PubMed:15361623
PubMed:18729522
PubMed:20961038
PubMed:21254756
RESID:AA0552
METAL copper [Cu-methanobactin OB3b complex]
bis[4-(hydroxy[sulfanyl-kappaS]methylidene)-1,3-oxazol-5(4H)-onato-kappaN]copper
methanobactin OB3b copper complex
A protein modification that effectively converts an L-cysteine residue to L-cysteine sulfinyl phosphate.
111.98
C 0 H 1 N 0 O 5 P 1 S 0
111.95616
C 3 H 6 N 1 O 6 P 1 S 1
215.12
214.96535
C
hypothetical
(2R)-2-amino-3-[(phosphonooxy)sulfinyl]propanoic acid
L-cysteine sulfinyl phosphate
cysteine sulfinic phosphoryl ester
PSI-MOD
MOD:01847
L-cysteine sulfinyl phosphate
A protein modification that effectively converts an L-cysteine residue to L-cysteine sulfinyl phosphate.
PubMed:16565085
RESID:AA0557
(2R)-2-amino-3-[(phosphonooxy)sulfinyl]propanoic acid
L-cysteine sulfinyl phosphate
cysteine sulfinic phosphoryl ester
A protein modification that effectively converts an L-cysteine residue to S-(spermidinoglutathion-S-yl)-L-cysteine.
432.54
C 17 H 32 N 6 O 5 S 1
432.21548
C 20 H 37 N 7 O 6 S 2
535.68
535.2247
C
natural
(2R)-2-amino-3-([(2R)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)-2-([2-([3-([4-aminobutyl]amino)propyl]carbamoyl)methyl]carbamoyl)ethyl]disulfanyl)propanoic acid
L-gamma-glutamyl-[S-(L-cystein-S-yl)]-L-cysteinyl-N-{3-[(4-aminobutyl)amino]propyl}glycinamide
S-(spermidinoglutathion-S-yl)-L-cysteine
cysteine glutathionylspermidine disulfide
PSI-MOD
MOD:01848
S-(spermidinoglutathion-S-yl)-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-(spermidinoglutathion-S-yl)-L-cysteine.
ChEBI:16613
PubMed:20530482
RESID:AA0558
(2R)-2-amino-3-([(2R)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)-2-([2-([3-([4-aminobutyl]amino)propyl]carbamoyl)methyl]carbamoyl)ethyl]disulfanyl)propanoic acid
L-gamma-glutamyl-[S-(L-cystein-S-yl)]-L-cysteinyl-N-{3-[(4-aminobutyl)amino]propyl}glycinamide
S-(spermidinoglutathion-S-yl)-L-cysteine
cysteine glutathionylspermidine disulfide
A protein modification that effectively cross-links two L-cysteine residues by a thioether bond to form S-(2-aminovinyl)-D-cysteine.
-80.1
C -1 H -4 N 0 O -2 S -1
-79.9932
C 5 H 7 N 2 O 1 S 1
143.18
143.02791
C, C
natural
C-term
uniprot.ptm:PTM-0446
(2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid
(S,Z)-S-(2-aminovinyl)cysteine
CROSSLNK S-(2-aminovinyl)-D-cysteine (Cys-Cys)
S-(2-aminovinyl)-D-cysteine
PSI-MOD
MOD:01849
Cross-link 2.
S-(2-aminovinyl)-D-cysteine (Cys-Cys)
A protein modification that effectively cross-links two L-cysteine residues by a thioether bond to form S-(2-aminovinyl)-D-cysteine.
PubMed:20805503
RESID:AA0204#CYS2
(2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid
(S,Z)-S-(2-aminovinyl)cysteine
CROSSLNK S-(2-aminovinyl)-D-cysteine (Cys-Cys)
S-(2-aminovinyl)-D-cysteine
A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-D-cysteine.
C 5 H 7 N 2 O 1 S 1
143.18
143.02791
C, X
natural
C-term
(2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid
(S,Z)-S-(2-aminovinyl)cysteine
S-(2-aminovinyl)-D-cysteine
PSI-MOD
MOD:01850
Cross-link 2.
S-(2-aminovinyl)-D-cysteine
A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-D-cysteine.
RESID:AA0204
(2S)-2-amino-3-([(Z)-2-aminoethenyl]sulfanyl)propanoic acid
(S,Z)-S-(2-aminovinyl)cysteine
S-(2-aminovinyl)-D-cysteine
A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-cysteine.
C 5 H 7 N 2 O 1 S 1
143.18
143.02791
C, X
natural
C-term
2-amino-3-([2-aminoethenyl]sulfanyl)propanoic acid
PSI-MOD
MOD:01851
Cross-link 2.
S-(2-aminovinyl)-cysteine
A protein modification that effectively cross-links either two L-cysteine residues, or an L-cysteine residue and an L-serine residue by a thioether bond to form S-(2-aminovinyl)-cysteine.
PubMed:18688235
2-amino-3-([2-aminoethenyl]sulfanyl)propanoic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to release hydrogen sulfide and form 2-amino-6-(2-amino-2-carboxyethylamino)hexanoic acid.
-34.08
C 0 H -2 N 0 O 0 S -1
-33.98772
C 9 H 15 N 3 O 2
197.24
197.11642
C, K
hypothetical
Lysinoalanine (from Cysteine)
PSI-MOD
MOD:01852
Cross-link 2. This entry is for a crosslink of peptidyl cysteine and peptidyl lysine. For the modification of peptidyl lysine by a free serine see MOD:01838. From DeltaMass: Average Mass: -34 with no citation or formula. [JSG]
L-lysinoalanine (Lys-Cys)
A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to release hydrogen sulfide and form 2-amino-6-(2-amino-2-carboxyethylamino)hexanoic acid.
DeltaMass:0
Lysinoalanine (from Cysteine)
A protein modification that effectively converts an L-lysine residue to L-lysinoalanine either by forming a cross-link with peptidyl-cysteine or peptidyl-serine, or by condensation with free serine.
K
natural
PSI-MOD
MOD:01853
L-lysinoalanine
A protein modification that effectively converts an L-lysine residue to L-lysinoalanine either by forming a cross-link with peptidyl-cysteine or peptidyl-serine, or by condensation with free serine.
PubMed:18688235
A protein modification that effectively adds one oxygen atom to a sulfur atom of a residue without removing hydrogen atoms.
PSI-MOD
MOD:01854
sulfur monooxygenated residue
A protein modification that effectively adds one oxygen atom to a sulfur atom of a residue without removing hydrogen atoms.
PubMed:18688235
A protein modification that effectively adds two oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms.
PSI-MOD
MOD:01855
sulfur dioxygenated residue
A protein modification that effectively adds two oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms.
PubMed:18688235
A protein modification that crosslinks two residues by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 1,3-oxazole-4-carbothionic acid.
PSI-MOD
MOD:01856
oxazole/oxazoline ring crosslinked residues (Cys)
A protein modification that crosslinks two residues by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 1,3-oxazole-4-carbothionic acid.
PubMed:18688235
A protein modification that effectively cross-links an L-cysteine residue and an L-methionine residue by a thioether bond to form 2-(L-cystein-S-yl)-methionine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 8 H 12 N 2 O 2 S 2
232.32
232.03403
C, M
natural
uniprot.ptm:PTM-0495
(2R)-2-amino-2-([2-amino-2-carboxyethyl]sulfanyl)-4-(methylsulfanyl)butanoic acid
2-(L-cystein-S-yl)-methionine
CROSSLNK 2-(S-cysteinyl)-methionine (Cys-Met)
PSI-MOD
MOD:01857
Cross-link 2. The chirality around the methionine alpha-carbon has not been determined.
2-(L-cystein-S-yl)-methionine
A protein modification that effectively cross-links an L-cysteine residue and an L-methionine residue by a thioether bond to form 2-(L-cystein-S-yl)-methionine.
PubMed:20805502
RESID:AA0559
(2R)-2-amino-2-([2-amino-2-carboxyethyl]sulfanyl)-4-(methylsulfanyl)butanoic acid
2-(L-cystein-S-yl)-methionine
CROSSLNK 2-(S-cysteinyl)-methionine (Cys-Met)
A protein modification that effectively converts an L-cysteine residue to S-(N-acetylamino)glucosyl-L-cysteine.
203.19
C 8 H 13 N 1 O 5 S 0
203.07938
C 11 H 18 N 2 O 6 S 1
306.33
306.08856
C
natural
uniprot.ptm:PTM-0628
(2R)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosylsulfanyl)propanoic acid
CARBOHYD S-linked (GlcNAc) cysteine
S-(N-acetylamino)glucosyl-L-cysteine
S-[(N-acetylamino)glycosyl]cysteine
S-[beta-D-(N-acetylamino)glucopyranosyl]cysteine
PSI-MOD
MOD:01858
S-(N-acetylamino)glucosyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-(N-acetylamino)glucosyl-L-cysteine.
ChEBI:61631
PubMed:21251913
PubMed:21395300
RESID:AA0560
(2R)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosylsulfanyl)propanoic acid
CARBOHYD S-linked (GlcNAc) cysteine
S-(N-acetylamino)glucosyl-L-cysteine
S-[(N-acetylamino)glycosyl]cysteine
S-[beta-D-(N-acetylamino)glucopyranosyl]cysteine
A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form 4-amino-3-isothiazolidinone-L-phenylalanine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 12 H 12 N 2 O 2 S 1
248.3
248.06195
C, F
hypothetical
uniprot.ptm:PTM-0451
(2S)-2-[(4R)-4-amino-3-oxo-1,2-thiazolidin-2-yl]-3-phenylpropanoic acid
2-(4-amino-3-oxo-isothiazolidin-2-yl)-3-phenylpropanoic acid
4-amino-3-isothiazolidinone-L-phenylalanine
CROSSLNK N,N-(cysteine-1,S-diyl)phenylalanine (Cys-Phe)
N,N-(L-cysteine-1,S-diyl)-L-phenylalanine
cysteinyl phenylalanine sulfenamide
phenylalanine-cysteine sulfenyl amide cross-link
phenylalanine-cysteine sulphenyl amide cross-link
PSI-MOD
MOD:01859
Cross-link 2.
4-amino-3-isothiazolidinone-L-phenylalanine
A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form 4-amino-3-isothiazolidinone-L-phenylalanine.
PubMed:17502599
RESID:AA0562
(2S)-2-[(4R)-4-amino-3-oxo-1,2-thiazolidin-2-yl]-3-phenylpropanoic acid
2-(4-amino-3-oxo-isothiazolidin-2-yl)-3-phenylpropanoic acid
4-amino-3-isothiazolidinone-L-phenylalanine
CROSSLNK N,N-(cysteine-1,S-diyl)phenylalanine (Cys-Phe)
N,N-(L-cysteine-1,S-diyl)-L-phenylalanine
cysteinyl phenylalanine sulfenamide
phenylalanine-cysteine sulfenyl amide cross-link
phenylalanine-cysteine sulphenyl amide cross-link
A protein modification that effectively converts an L-cysteine residue to L-cysteine bacillithiol disulfide.
396.37
C 13 H 20 N 2 O 10 S 1
396.08386
C 16 H 25 N 3 O 11 S 2
499.51
499.09305
C
natural
uniprot.ptm:PTM-0452
(2S)-(2-[S-(L-cystein-S-yl)-L-cysteinyl]amino-2-deoxy-alpha-D-glucopyranosyloxy)-butanedioic acid
BSH
L-cysteine bacillithiol disulfide
MOD_RES S-bacillithiol cysteine disulfide
PSI-MOD
MOD:01860
L-cysteine bacillithiol disulfide
A protein modification that effectively converts an L-cysteine residue to L-cysteine bacillithiol disulfide.
ChEBI:61338
PubMed:19578333
RESID:AA0563
(2S)-(2-[S-(L-cystein-S-yl)-L-cysteinyl]amino-2-deoxy-alpha-D-glucopyranosyloxy)-butanedioic acid
BSH
L-cysteine bacillithiol disulfide
MOD_RES S-bacillithiol cysteine disulfide
A protein modification that crosslinks two residues by condensation of a cysteine thiol with the amido nitrogen of the following residue to form an isothiazolidinone ring.
PSI-MOD
MOD:01861
The isothiazolidinone ring is usually formed by the reaction of a cysteine sulfenic acid with the amido nitrogen releasing water.
isothiazolidinone ring crosslinked residues
A protein modification that crosslinks two residues by condensation of a cysteine thiol with the amido nitrogen of the following residue to form an isothiazolidinone ring.
PubMed:18688235
A protein modification that effectively replaces the hydrogen atom of a cysteine sulfanyl group with a substituted sulfanyl group, forming a disulfide bond that does not cross-link two encoded peptide chains.
C
S-thiolation
PSI-MOD
MOD:01862
disulfide conjugated residue
A protein modification that effectively replaces the hydrogen atom of a cysteine sulfanyl group with a substituted sulfanyl group, forming a disulfide bond that does not cross-link two encoded peptide chains.
PubMed:18688235
S-thiolation
A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems mTRAQ reagent reporter+balance groups.
X
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems mTRAQ(TM) reagent
MOD:01863
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
mTRAQ reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems mTRAQ reagent reporter+balance groups.
PubMed:18688235
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems mTRAQ(TM) reagent
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems mTRAQ light reporter+balance group.
140.09
(12)C 7 H 12 (14)N 2 (16)O 1
140.09496
X
artifact
Unimod:888
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
Applied Biosystems mTRAQ(TM) reagent
mTRAQ heavy
MOD:01864
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
mTRAQ light reporter+balance reagent acylated residue
A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems mTRAQ light reporter+balance group.
Unimod:888
(4-methylpiperazin-1-yl)acetyl
Applied Biosystems mTRAQ(TM) reagent
mTRAQ heavy
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems mTRAQ light reporter+balance group.
140.09
(12)C 7 H 12 (14)N 2 (16)O 1
140.09496
X
artifact
N-term
Unimod:888
(4-methylpiperazin-1-yl)acetyl
mTRAQ light on nterm
PSI-MOD
Applied Biosystems mTRAQ(TM) reagent
mTRAQ light
MOD:01865
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
mTRAQ light reporter+balance reagent acylated N-terminal
A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems mTRAQ light reporter+balance group.
OMSSA:208
Unimod:888#N-term
(4-methylpiperazin-1-yl)acetyl
mTRAQ light on nterm
Applied Biosystems mTRAQ(TM) reagent
mTRAQ light
A protein modification that effectively replaces the N6-amino hydrogen atom of a lysine residue with the Applied Biosystems mTRAQ light reporter+balance group.
140.09
(12)C 7 H 12 (14)N 2 (16)O 1
140.09496
(12)C 13 H 24 N 2 (14)N 2 O 1 (16)O 1
268.19
268.1899
K
artifact
Unimod:888
(4-methylpiperazin-1-yl)acetyl
mTRAQ light on K
PSI-MOD
Applied Biosystems mTRAQ(TM) reagent
mTRAQ light
MOD:01866
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
mTRAQ light reporter+balance reagent N6-acylated lysine
A protein modification that effectively replaces the N6-amino hydrogen atom of a lysine residue with the Applied Biosystems mTRAQ light reporter+balance group.
OMSSA:209
Unimod:888#K
(4-methylpiperazin-1-yl)acetyl
mTRAQ light on K
Applied Biosystems mTRAQ(TM) reagent
mTRAQ light
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems mTRAQ light reporter+balance group.
140.09
(12)C 7 H 12 (14)N 2 (16)O 1
140.09496
(12)C 16 H 21 (14)N 3 O 2 (16)O 1
303.16
303.1583
Y
artifact
Unimod:888
(4-methylpiperazin-1-yl)acetyl
mTRAQ light on Y
PSI-MOD
Applied Biosystems mTRAQ(TM) reagent
mTRAQ light
MOD:01867
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification.
mTRAQ light reporter+balance reagent O4'-acylated tyrosine
A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems mTRAQ light reporter+balance group.
OMSSA:210
Unimod:888#Y
(4-methylpiperazin-1-yl)acetyl
mTRAQ light on Y
Applied Biosystems mTRAQ(TM) reagent
mTRAQ light
Modifications that have monoisotopic mass differences from their respective origins of 140.094963 Da.
PSI-MOD
MOD:01868
modifications with monoisotopic mass differences that are nominally equal at 140.094963 Da
Modifications that have monoisotopic mass differences from their respective origins of 140.094963 Da.
PubMed:18688235
The protein modification reporter fragment produced by an Applied Biosystems mTRAQ light reagent derivatized residue.
1+
(12)C 6 H 13 (14)N 2
113.11
113.10732
X
artifact
4-methyl-1-methylidenepiperazin-1-ium
PSI-MOD
MOD:01869
mTRAQ light reporter fragment
The protein modification reporter fragment produced by an Applied Biosystems mTRAQ light reagent derivatized residue.
PubMed:18688235
4-methyl-1-methylidenepiperazin-1-ium
A protein modification reporter fragment produced by an Applied Biosystems mTRAQ reagent derivatized residue.
PSI-MOD
MOD:01870
mTRAQ reporter fragment
A protein modification reporter fragment produced by an Applied Biosystems mTRAQ reagent derivatized residue.
PubMed:18688235
A protein modification that effectively cyclizes an S-carboxamidomethyl-L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid with the loss of ammonia.
-17.03
C 0 H -3 N -1 O 0 S 0
-17.026548
C 5 H 6 N 1 O 2 S 1
144.17
144.01192
MOD:01060
artifact
N-term
Unimod:26
(R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid
5-oxothiomorpholine-3-carboxylic acid
Otc
PSI-MOD
Pyro-carbamidomethyl
S-carbamoylmethylcysteine cyclization (N-terminus)
MOD:01871
cyclized N-terminal S-carboxamidomethyl-L-cysteine
A protein modification that effectively cyclizes an S-carboxamidomethyl-L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid with the loss of ammonia.
DeltaMass:336
PubMed:12643538
Unimod:26
(R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid
5-oxothiomorpholine-3-carboxylic acid
Otc
Pyro-carbamidomethyl
S-carbamoylmethylcysteine cyclization (N-terminus)
A protein modification that effectively cyclizes an S-carboxymethyl-L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid with the loss of water.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 5 H 6 N 1 O 2 S 1
144.17
144.01192
MOD:01061
artifact
N-term
Unimod:26
(R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid
5-oxothiomorpholine-3-carboxylic acid
Otc
PSI-MOD
Pyro-carbamidomethyl
S-carbamoylmethylcysteine cyclization (N-terminus)
MOD:01872
Contrary to the impression given in Unimod entry 26, the cyclization of N-terminal S-carboxymethyl-L-cysteine is not reported in PubMed:1263538. The cyclization would be expected to proceed under strongly acidic conditions [JSG].
cyclized N-terminal S-carboxymethyl-L-cysteine
A protein modification that effectively cyclizes an S-carboxymethyl-L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid with the loss of water.
PubMed:12643538
Unimod:26
(R)-5-oxoperhydro-1,4-thiazine-3-carboxylic acid
5-oxothiomorpholine-3-carboxylic acid
Otc
Pyro-carbamidomethyl
S-carbamoylmethylcysteine cyclization (N-terminus)
A protein modification that effectively converts an L-alanine residue to N-carboxy-L-alanine.
44.01
C 1 H 0 N 0 O 2
43.98983
C 4 H 6 N 1 O 3
116.1
116.03477
A
natural
N-term
(S)-2-carboxyamino-propanoic acid
2-carbamic-propanoic acid
N-carboxymethionine
PSI-MOD
MOD:01873
This metastable modification can be formed by a protein N-terminal in solutions with a high concentration of dissolved carbon dioxide [JSG].
N-carboxy-L-alanine
A protein modification that effectively converts an L-alanine residue to N-carboxy-L-alanine.
PubMed:18688235
PubMed:4593770
PubMed:4647257
PubMed:8312270
(S)-2-carboxyamino-propanoic acid
2-carbamic-propanoic acid
N-carboxymethionine
A protein modification that effectively converts an L-alanine residue to N-carboxy-L-valine.
44.01
C 1 H 0 N 0 O 2
43.98983
C 6 H 10 N 1 O 3
144.15
144.06607
V
natural
N-term
(S)-2-carboxyamino-propanoic acid
2-carbamic-propanoic acid
N-carboxymethionine
PSI-MOD
MOD:01874
This metastable modification can be formed by a protein N-terminal in solutions with a high concentration of dissolved carbon dioxide [JSG].
N-carboxy-L-valine
A protein modification that effectively converts an L-alanine residue to N-carboxy-L-valine.
PubMed:18688235
PubMed:4593770
PubMed:4647257
PubMed:8312270
(S)-2-carboxyamino-propanoic acid
2-carbamic-propanoic acid
N-carboxymethionine
A protein modification that effectively replaces an N6-amino hydrogen atom of L-lysine with an acyl group.
K
natural
N6AcylLys
PSI-MOD
MOD:01875
N6-acylated L-lysine
A protein modification that effectively replaces an N6-amino hydrogen atom of L-lysine with an acyl group.
PubMed:18688235
N6AcylLys
OBSOLETE because identical to MOD:00457
MOD:00457
100.02
(12)C 4 (1)H 4 O 3
100.016045
X
artifact
N-term
PSI-MOD
MOD:01876
4x(1)H,4x(12)C-labeled alpha-amino succinylated residue
true
OBSOLETE because identical to MOD:00457
PubMed:18688235
A protein modification that effectively converts an L-cysteine residue and an L-arginine residue to 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid.
-6.05
C 0 H -6 N 0 O 0 S 0
-6.04695
C 9 H 12 N 5 O 2 S 1
254.29
254.07117
C, R
natural
N-term
uniprot.ptm:PTM-0457
(4Z)-2-(4-guanidinobutanoyl)-5-oxo-4-(sulfanylmethylidene)-4,5-dihydro-1H-imidazole
2-(4-guanidinobutanoyl)-5-hydroxy-1H-imidazole-4-carbothioic O-acid
2-(4-guanidinobutanoyl)-5-hydroxy-4-thioformyl-1H-imidazole [tautomer]
2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid
CROSSLNK 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid (Arg-Cys)
PSI-MOD
MOD:01877
Cross-link 2.
2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid
A protein modification that effectively converts an L-cysteine residue and an L-arginine residue to 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid.
PubMed:20961038
RESID:AA0553
(4Z)-2-(4-guanidinobutanoyl)-5-oxo-4-(sulfanylmethylidene)-4,5-dihydro-1H-imidazole
2-(4-guanidinobutanoyl)-5-hydroxy-1H-imidazole-4-carbothioic O-acid
2-(4-guanidinobutanoyl)-5-hydroxy-4-thioformyl-1H-imidazole [tautomer]
2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid
CROSSLNK 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid (Arg-Cys)
A protein modification that effectively converts an L-cysteine residue and an L-threonine residue to L-threonine 5-hydroxyoxazole-4-carbothionic acid.
-4.03
C 0 H -4 N 0 O 0 S 0
-4.0313
C 7 H 8 N 2 O 3 S 1
200.21
200.02556
C, T
natural
uniprot.ptm:PTM-0458
(4Z)-2-[(1S,2R)-1-amino-2-hydroxypropyl]-4-(sulfanylmethylidene)-1,3-oxazol-5(4H)-one [tautomer]
2-[(1S,2R)-1-amino-2-hydroxypropyl]-5-hydroxy-1,3-oxazole-4-carbothioic O-acid
CROSSLNK Threonine 5-hydroxy-oxazole-4-carbonthionic acid (Thr-Cys)
L-threonine 5-hydroxy-oxazole-4-carbonthionic acid
PSI-MOD
MOD:01878
Cross-link 2.
L-threonine 5-hydroxyoxazole-4-carbonthionic acid
A protein modification that effectively converts an L-cysteine residue and an L-threonine residue to L-threonine 5-hydroxyoxazole-4-carbothionic acid.
PubMed:20961038
RESID:AA0554
(4Z)-2-[(1S,2R)-1-amino-2-hydroxypropyl]-4-(sulfanylmethylidene)-1,3-oxazol-5(4H)-one [tautomer]
2-[(1S,2R)-1-amino-2-hydroxypropyl]-5-hydroxy-1,3-oxazole-4-carbothioic O-acid
CROSSLNK Threonine 5-hydroxy-oxazole-4-carbonthionic acid (Thr-Cys)
L-threonine 5-hydroxy-oxazole-4-carbonthionic acid
A protein modification that effectively converts two L-cysteine residues, an L-arginine residue, an L-threonine residue and a copper atom to the methanobactin SB2 copper complex.
84.48
C 0 Cu 1 H -9 N 1 O 1 S 0
83.85716
C 6 Cu 1 H 1 N 3 O 3 S 2
290.76
289.87552
C, C, R, T
natural
N-term
METAL copper [Cu-methanobactin SB2 complex]
[5-(hydroxy[sulfanyl-kappaS]methylene)-3,5-dihydro-4H-imidazol-4-onato-kappaN1][4-(hydroxy[sulfanyl-kappaS]methylene)-1,3-oxazol-5(4H)-onato-kappaN]copper
methanobactin SB2 copper complex
PSI-MOD
MOD:01879
Cross-link 2.
methanobactin SB2 copper complex
A protein modification that effectively converts two L-cysteine residues, an L-arginine residue, an L-threonine residue and a copper atom to the methanobactin SB2 copper complex.
PubMed:20961038
RESID:AA0555
METAL copper [Cu-methanobactin SB2 complex]
[5-(hydroxy[sulfanyl-kappaS]methylene)-3,5-dihydro-4H-imidazol-4-onato-kappaN1][4-(hydroxy[sulfanyl-kappaS]methylene)-1,3-oxazol-5(4H)-onato-kappaN]copper
methanobactin SB2 copper complex
modification from RESID
71.12
C 4 H 9 N 1 O 0
71.0735
C 10 H 21 N 3 O 1
199.3
199.16846
K
natural
uniprot.ptm:PTM-0684
(2S)-2-amino-6-[(4-aminobutyl)amino]hexanoic acid
L-deoxyhypusine
MOD_RES Deoxyhypusine
N6-(4-aminobutyl)lysine
deoxyhypusine
PSI-MOD
MOD:01880
L-deoxyhypusine
modification from RESID
ChEBI:50038
PubMed:16452303
RESID:AA0564
(2S)-2-amino-6-[(4-aminobutyl)amino]hexanoic acid
L-deoxyhypusine
MOD_RES Deoxyhypusine
N6-(4-aminobutyl)lysine
deoxyhypusine
A protein modification that effectively crosslinks an L-phenylalanine residue and an L-valine residue by a free radical process effectively releasing a hydrogen molecule and forming 3-(L-phenylalan-2'-yl)-L-valine.
-2.02
C 0 H -2 N 0 O 0
-2.01565
C 14 H 16 N 2 O 2
244.29
244.12119
F, V
natural
(2S)-2-amino-4-(2-[(2S)-2-amino-2-carboxyethyl]phenyl)-3-methylbutanoic acid
3-(L-phenylalan-2'-yl)-L-valine
symerythrin valine-phenylalanine cross-link
PSI-MOD
MOD:01881
Cross-link 2.
3-(L-phenylalan-2'-yl)-L-valine
A protein modification that effectively crosslinks an L-phenylalanine residue and an L-valine residue by a free radical process effectively releasing a hydrogen molecule and forming 3-(L-phenylalan-2'-yl)-L-valine.
PubMed:21596985
RESID:AA0565
(2S)-2-amino-4-(2-[(2S)-2-amino-2-carboxyethyl]phenyl)-3-methylbutanoic acid
3-(L-phenylalan-2'-yl)-L-valine
symerythrin valine-phenylalanine cross-link
A protein modification that effectively crosslinks the carbonyl of an amino acid residue at position n with the alpha amino of a glycine residue at position n+2 to form a 5-imidazolinone ring.
PSI-MOD
MOD:01882
5-imidazolinone ring crosslinked residues (Gly)
A protein modification that effectively crosslinks the carbonyl of an amino acid residue at position n with the alpha amino of a glycine residue at position n+2 to form a 5-imidazolinone ring.
PubMed:18688235
A protein modification that crosslinks two residues by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 5-imidazolinone ring.
PSI-MOD
MOD:01883
5-imidazolinone ring crosslinked residues (Cys)
A protein modification that crosslinks two residues by rearrangement and condensation of a cysteine with the carbonyl of the preceding residue to form a 5-imidazolinone ring.
PubMed:18688235
A protein modification that effectively replaces a hydrogen atom with a 4-aminobutyl group, usually derived from spermidine.
X
PSI-MOD
MOD:01884
4-aminobutylated residue
A protein modification that effectively replaces a hydrogen atom with a 4-aminobutyl group, usually derived from spermidine.
PubMed:18688235
A protein modification that effectively replaces a hydrogen atom with a biotinyl group.
226.29
C 10 H 14 N 2 O 2 S 1
226.0776
X
natural
5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl
Biotinylation
BtnRes
PSI-MOD
MOD:01885
biotinylated residue
A protein modification that effectively replaces a hydrogen atom with a biotinyl group.
PubMed:18688235
5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl
Biotinylation
BtnRes
A protein modification that effectively replaces a hydrogen atom with an sulfanyl or substituted sulfanyl group.
X
PSI-MOD
MOD:01886
thiolated residue
A protein modification that effectively replaces a hydrogen atom with an sulfanyl or substituted sulfanyl group.
PubMed:18688235
A protein modification that is produced by reaction with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A, to form Uniblue A lysine adduct.
484.5
C 22 H 16 N 2 O 7 S 2
484.0399
C 28 H 28 N 4 O 8 S 2
612.67
612.1348
K
artifact
1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
1-amino-9,10-dioxo-4-{[3-(vinylsulfonyl)phenyl]amino}-9,10-dihydroanthracene-2-sulfonate
N6UniblueALys
Uniblue A
PSI-MOD
MOD:01887
Uniblue A derivatized lysine
A protein modification that is produced by reaction with 1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate, Uniblue A, to form Uniblue A lysine adduct.
PubMed:18688235
1-amino-4-{[3-(ethenylsulfonyl)phenyl]amino}-9,10-dioxo-9,10-dihydroanthracene-2-sulfonate
1-amino-9,10-dioxo-4-{[3-(vinylsulfonyl)phenyl]amino}-9,10-dihydroanthracene-2-sulfonate
N6UniblueALys
Uniblue A
A protein modification that effectively removes two neutral hydrogen atoms (proton and electron) from a residue.
-2.02
C 0 H -2 N 0 O 0
-2.01565
X
Unimod:401
2dHRes
PSI-MOD
MOD:01888
didehydrogenated residue
A protein modification that effectively removes two neutral hydrogen atoms (proton and electron) from a residue.
Unimod:401
2dHRes
A protein modification that effectively converts an L-cysteine residue to S-(2-succinyl)-L-cysteine, by addition of either fumaric acid or maleic acid.
116.07
C 4 H 4 N 0 O 4 S 0
116.010956
C 7 H 9 N 1 O 5 S 1
219.21
219.02014
C
natural
Unimod:957
uniprot.ptm:PTM-0674
(2R)-2-amino-3-([(1R)-1,2-dicarboxyethyl]sulfanyl)propanoic acid
(2R)-2-{[(2R)-2-amino-2-carboxyethyl]sulfanyl}butanedioic acid
2-((2-amino-2-carboxyethyl)thio)butanedioic acid
2-amino-3-(1,2-dicarboxyethylthio)propanoic acid
MOD_RES S-(2-succinyl)cysteine
S-(1,2-dicarboxyethyl)cysteine
S-(2-succinyl)-L-cysteine
S-(2-succinyl)cysteine
S-[(2R)-2-succinyl]-L-cysteine
PSI-MOD
MOD:01889
S-(2-succinyl)-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-(2-succinyl)-L-cysteine, by addition of either fumaric acid or maleic acid.
PubMed:16624247
PubMed:18448829
PubMed:20677745
RESID:AA0561
Unimod:957
(2R)-2-amino-3-([(1R)-1,2-dicarboxyethyl]sulfanyl)propanoic acid
(2R)-2-{[(2R)-2-amino-2-carboxyethyl]sulfanyl}butanedioic acid
2-((2-amino-2-carboxyethyl)thio)butanedioic acid
2-amino-3-(1,2-dicarboxyethylthio)propanoic acid
MOD_RES S-(2-succinyl)cysteine
S-(1,2-dicarboxyethyl)cysteine
S-(2-succinyl)-L-cysteine
S-(2-succinyl)cysteine
S-[(2R)-2-succinyl]-L-cysteine
A protein modification that effectively crosslinks an N-formyl-L-methionine residue and an L-histidine residue to form N-[(L-histidin-1'-yl)methyl]-L-methionine.
-16.0
C 0 H 0 N 0 O -1 S 0
-15.994915
C 12 H 17 N 4 O 2 S 1
281.35
281.1072
H, MOD:00030
hypothetical
N-term
(2S)-2-([(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)methyl]amino)-4-(methylsulfanyl)butanoic acid
N-[(L-histidin-1'-yl)methyl]-L-methionine
PSI-MOD
MOD:01890
Cross-link 2.
N-[(L-histidin-1'-yl)methyl]-L-methionine (fMet)
A protein modification that effectively crosslinks an N-formyl-L-methionine residue and an L-histidine residue to form N-[(L-histidin-1'-yl)methyl]-L-methionine.
PubMed:19622680
RESID:AA0566#FMET
(2S)-2-([(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)methyl]amino)-4-(methylsulfanyl)butanoic acid
N-[(L-histidin-1'-yl)methyl]-L-methionine
A protein modification that effectively crosslinks an L-methionine residue and an L-histidine residue to form N-[(L-histidin-1'-yl)methyl]-L-methionine.
12.01
C 1 H 0 N 0 O 0 S 0
12.0
C 12 H 17 N 4 O 2 S 1
281.35
281.1072
H, M
hypothetical
N-term
(2S)-2-([(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)methyl]amino)-4-(methylsulfanyl)butanoic acid
N-[(L-histidin-1'-yl)methyl]-L-methionine
PSI-MOD
MOD:01891
Cross-link 2.
N-[(L-histidin-1'-yl)methyl]-L-methionine (Met)
A protein modification that effectively crosslinks an L-methionine residue and an L-histidine residue to form N-[(L-histidin-1'-yl)methyl]-L-methionine.
PubMed:19622680
RESID:AA0566#MET
(2S)-2-([(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)methyl]amino)-4-(methylsulfanyl)butanoic acid
N-[(L-histidin-1'-yl)methyl]-L-methionine
A protein modification that effectively converts an L-lysine residue to N6-crotonyl-L-lysine.
68.07
C 4 H 4 N 0 O 1
68.026215
C 10 H 16 N 2 O 2
196.25
196.12119
K
hypothetical
uniprot.ptm:PTM-0475
(2S)-2-amino-6-[(2E)-but-2-enamido]hexanoic acid
(2S)-2-amino-6-[(2E)-but-2-enoylamino]hexanoic acid
(2S)-2-azanyl-6-[(2E)-but-2-enoylazanyl]hexanoic acid
MOD_RES N6-crotonyl-L-lysine
N(epsilon)-crotonyllysine
N6-(E)-crotonyllysine
N6-[(2E)-2-butenoyl]-L-lysine
N6-crotonyl-L-lysine
N6-crotonyllysine
N6-trans-crotonyllysine
PSI-MOD
MOD:01892
N6-crotonyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-crotonyl-L-lysine.
PubMed:21925322
RESID:AA0567
(2S)-2-amino-6-[(2E)-but-2-enamido]hexanoic acid
(2S)-2-amino-6-[(2E)-but-2-enoylamino]hexanoic acid
(2S)-2-azanyl-6-[(2E)-but-2-enoylazanyl]hexanoic acid
MOD_RES N6-crotonyl-L-lysine
N(epsilon)-crotonyllysine
N6-(E)-crotonyllysine
N6-[(2E)-2-butenoyl]-L-lysine
N6-crotonyl-L-lysine
N6-crotonyllysine
N6-trans-crotonyllysine
A protein modification that effectively converts an L-lysine residue to N6-malonyl-L-lysine.
86.05
C 3 H 2 N 0 O 3
86.0004
C 9 H 14 N 2 O 4
214.22
214.09535
K
hypothetical
uniprot.ptm:PTM-0467
(2S)-2-amino-6-[(carboxyacetyl)amino]hexanoic acid
2-azanyl-6-[(carboxyacetyl)azanyl]hexanoic acid
MOD_RES N6-malonyllysine
N(epsilon)-(malonyl)lysine
N6-(carboxyacetyl)lysine
N6-malonyl-L-lysine
N6-malonyllysine
malonyllysine
PSI-MOD
MOD:01893
N6-malonyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-malonyl-L-lysine.
PubMed:21908771
PubMed:8349414
RESID:AA0568
(2S)-2-amino-6-[(carboxyacetyl)amino]hexanoic acid
2-azanyl-6-[(carboxyacetyl)azanyl]hexanoic acid
MOD_RES N6-malonyllysine
N(epsilon)-(malonyl)lysine
N6-(carboxyacetyl)lysine
N6-malonyl-L-lysine
N6-malonyllysine
malonyllysine
A protein modification that effectively replaces a hydrogen atom with an propanoyl group.
56.06
C 3 H 4 O 1
56.026215
X
artifact
Unimod:58
PSI-MOD
Propionate labeling reagent light form (N-term & K)
Propionyl
MOD:01894
propanoylated residue
A protein modification that effectively replaces a hydrogen atom with an propanoyl group.
PubMed:11857757
PubMed:11999733
PubMed:12175151
Unimod:58
Propionate labeling reagent light form (N-term & K)
Propionyl
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(12)C-labeled propanoyl group.
56.03
(12)C 3 H 4 O 1
56.026215
X
artifact
Unimod:58
PSI-MOD
Propionate labeling reagent light form (N-term & K)
Propionyl
MOD:01895
alpha-amino 3x(12)C-labeled propanoylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(12)C-labeled propanoyl group.
PubMed:11857757
PubMed:11999733
PubMed:12175151
Unimod:58#N-term
Propionate labeling reagent light form (N-term & K)
Propionyl
A protein modification produced by trifluoroacetic acid forming an adduct, either a salt or a hydrogen bonded carboxylic acid dimer, with an amino acid residue.
114.02
C 2 F 3 H 1 O 2
113.99287
X
artifact
TFA
PSI-MOD
MOD:01896
Trifluoroacetic acid has been observed to form adducts in both negative and positive mode analysis (Mark Collins, private communication) [JSG].
trifluoroacetic acid adduct
A protein modification produced by trifluoroacetic acid forming an adduct, either a salt or a hydrogen bonded carboxylic acid dimer, with an amino acid residue.
PubMed:18688235
TFA
A protein modification that effectively converts an L-isoleucine residue to 5-hydroxy-3-methyl-L-proline.
13.98
C 0 H -2 N 0 O 1
13.979265
C 6 H 9 N 1 O 2
127.14
127.06333
I
natural
uniprot.ptm:PTM-0466
(2S,3S,5Xi)-5-hydroxy-3-methylpyrrolidine-2-carboxylic acid
5-hydroxy-3-methyl-L-proline
5-hydroxy-3-methylproline
5Hy3MePro(Ile)
MOD_RES 5-hydroxy-3-methylproline (Ile)
beta-methyl-delta-hydroxyproline
PSI-MOD
MOD:01897
5-hydroxy-3-methyl-L-proline (Ile)
A protein modification that effectively converts an L-isoleucine residue to 5-hydroxy-3-methyl-L-proline.
PubMed:21788474
PubMed:7592021
PubMed:8557573
RESID:AA0473
(2S,3S,5Xi)-5-hydroxy-3-methylpyrrolidine-2-carboxylic acid
5-hydroxy-3-methyl-L-proline
5-hydroxy-3-methylproline
5Hy3MePro(Ile)
MOD_RES 5-hydroxy-3-methylproline (Ile)
beta-methyl-delta-hydroxyproline
modification from RESID
28.05
C 2 H 4 N 0 O 0
28.0313
C 8 H 17 N 4 O 1
185.25
185.14024
R
natural
N-term
uniprot.ptm:PTM-0459
(2S)-5-[(diaminomethylidene)amino]-2-(dimethylamino)pentanoic acid
(2S)-5-carbamimidamido-2-(dimethylamino)pentanoic acid [tautomer]
MOD_RES N2,N2-dimethylarginine
N(alpha),N(alpha)-dimethylarginine
N2,N2-dimethyl-L-arginine
N2,N2-dimethylarginine
PSI-MOD
MOD:01898
N2,N2-dimethyl-L-arginine
modification from RESID
PubMed:21568297
PubMed:21950656
RESID:AA0569
(2S)-5-[(diaminomethylidene)amino]-2-(dimethylamino)pentanoic acid
(2S)-5-carbamimidamido-2-(dimethylamino)pentanoic acid [tautomer]
MOD_RES N2,N2-dimethylarginine
N(alpha),N(alpha)-dimethylarginine
N2,N2-dimethyl-L-arginine
N2,N2-dimethylarginine
A protein modification that effectively crosslinks an L-arginine residue and an L-cysteine residue to form arginine thiazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 9 H 13 N 5 O 1 S 1
239.3
239.08408
C, R
natural
uniprot.ptm:PTM-0460
2-[(1S)-1-amino-4-([diaminomethylidene]amino)butyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Arg-Cys)
L-arginine thiazole-4-carboxylic acid
PSI-MOD
MOD:01899
Cross-link 2.
L-arginine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-arginine residue and an L-cysteine residue to form arginine thiazole-4-carboxylic acid.
PubMed:21568297
PubMed:21950656
RESID:AA0570
2-[(1S)-1-amino-4-([diaminomethylidene]amino)butyl]-1,3-thiazole-4-carboxylic acid
CROSSLNK Thiazole-4-carboxylic acid (Arg-Cys)
L-arginine thiazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-cysteine 5-methyloxazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1 S 0
-20.026215
C 7 H 8 N 2 O 2 S 1
184.21
184.03065
C, T
natural
uniprot.ptm:PTM-0461
2-[(1R)-1-amino-2-sulfanylethyl]-5-methyl-1,3-oxazole-4-carboxylic acid
2-[(1R)-1-azanyl-2-sulfanylethyl]-5-methyl-1,3-oxazole-4-carboxylic acid
CROSSLNK 5-methyloxazole-4-carboxylic acid (Cys-Thr)
L-cysteine 5-methyloxazole-4-carboxylic acid
PSI-MOD
MOD:01900
Cross-link 2.
L-cysteine 5-methyloxazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-cysteine 5-methyloxazole-4-carboxylic acid.
PubMed:21568297
PubMed:21950656
RESID:AA0571
2-[(1R)-1-amino-2-sulfanylethyl]-5-methyl-1,3-oxazole-4-carboxylic acid
2-[(1R)-1-azanyl-2-sulfanylethyl]-5-methyl-1,3-oxazole-4-carboxylic acid
CROSSLNK 5-methyloxazole-4-carboxylic acid (Cys-Thr)
L-cysteine 5-methyloxazole-4-carboxylic acid
A protein modification that effectively crosslinks two L-threonine residues to form L-threonine 5-methyloxazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1
-20.026215
C 8 H 10 N 2 O 3
182.18
182.06914
T, T
natural
uniprot.ptm:PTM-0462
2-[(1S,2R)-1-amino-2-hydroxypropyl]-5-methyl-1,3-oxazole-4-carboxylic acid
2-[(1S,2R)-1-azanyl-2-hydroxypropyl]-5-methyl-1,3-oxazole-4-carboxylic acid
CROSSLNK 5-methyloxazole-4-carboxylic acid (Thr-Thr)
L-threonine 5-methyloxazole-4-carboxylic acid
PSI-MOD
MOD:01901
Cross-link 2.
L-threonine 5-methyloxazole-4-carboxylic acid
A protein modification that effectively crosslinks two L-threonine residues to form L-threonine 5-methyloxazole-4-carboxylic acid.
PubMed:21568297
PubMed:21950656
RESID:AA0572
2-[(1S,2R)-1-amino-2-hydroxypropyl]-5-methyl-1,3-oxazole-4-carboxylic acid
2-[(1S,2R)-1-azanyl-2-hydroxypropyl]-5-methyl-1,3-oxazole-4-carboxylic acid
CROSSLNK 5-methyloxazole-4-carboxylic acid (Thr-Thr)
L-threonine 5-methyloxazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-isoleucine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1
-20.026215
C 9 H 12 N 2 O 2
180.21
180.08987
I, S
natural
uniprot.ptm:PTM-0463
2-[(1S,2S)-1-amino-2-methylbutyl]-1,3-oxazole-4-carboxylic acid
2-[(1S,2S)-1-azanyl-2-methylbutyl]-1,3-oxazole-4-carboxylic acid
CROSSLNK Oxazole-4-carboxylic acid (Ile-Ser)
L-isoleucine oxazole-4-carboxylic acid
PSI-MOD
MOD:01902
Cross-link 2.
L-isoleucine oxazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-isoleucine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid.
PubMed:21568297
PubMed:21950656
RESID:AA0573
2-[(1S,2S)-1-amino-2-methylbutyl]-1,3-oxazole-4-carboxylic acid
2-[(1S,2S)-1-azanyl-2-methylbutyl]-1,3-oxazole-4-carboxylic acid
CROSSLNK Oxazole-4-carboxylic acid (Ile-Ser)
L-isoleucine oxazole-4-carboxylic acid
A protein modification that effectively crosslinks two L-serine residues to form serine oxazole-4-carboxylic acid.
-20.03
C 0 H -4 N 0 O -1
-20.026215
C 6 H 6 N 2 O 3
154.13
154.03784
S, S
natural
uniprot.ptm:PTM-0464
2-[(1S)-1-amino-2-hydroxyethyl]-1,3-oxazole-4-carboxylic acid
2-[(1S)-1-azanyl-2-hydroxyethyl]-1,3-oxazole-4-carboxylic acid
CROSSLNK Oxazole-4-carboxylic acid (Ser-Ser)
L-serine oxazole-4-carboxylic acid
PSI-MOD
MOD:01903
Cross-link 2.
L-serine oxazole-4-carboxylic acid
A protein modification that effectively crosslinks two L-serine residues to form serine oxazole-4-carboxylic acid.
PubMed:21568297
PubMed:21950656
RESID:AA0574
2-[(1S)-1-amino-2-hydroxyethyl]-1,3-oxazole-4-carboxylic acid
2-[(1S)-1-azanyl-2-hydroxyethyl]-1,3-oxazole-4-carboxylic acid
CROSSLNK Oxazole-4-carboxylic acid (Ser-Ser)
L-serine oxazole-4-carboxylic acid
A protein modification that effectively crosslinks an L-serine residue and an L-threonine residue to form L-serine 5-methyloxazoline-4-carboxylic acid.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 7 H 10 N 2 O 3
170.17
170.06914
S, T
natural
uniprot.ptm:PTM-0465
2-[(1S)-1-amino-2-hydroxyethyl]-5-methyl-1,3-oxazoline-4-carboxylic acid
2-[(1S)-1-amino-2-hydroxyethyl]-5-methyl-4,5-dihydro-1,3-oxazole-4-carboxylic acid
2-[(1S)-1-azanyl-2-hydroxyethyl]-5-methyl-4,5-dihydro-1,3-oxazole-4-carboxylic acid
CROSSLNK 5-methyloxazoline-4-carboxylic acid (Ser-Thr)
L-serine 5-methyloxazoline-4-carboxylic acid
PSI-MOD
MOD:01904
Cross-link 2.
L-serine 5-methyloxazoline-4-carboxylic acid
A protein modification that effectively crosslinks an L-serine residue and an L-threonine residue to form L-serine 5-methyloxazoline-4-carboxylic acid.
PubMed:21568297
PubMed:21950656
RESID:AA0575
2-[(1S)-1-amino-2-hydroxyethyl]-5-methyl-1,3-oxazoline-4-carboxylic acid
2-[(1S)-1-amino-2-hydroxyethyl]-5-methyl-4,5-dihydro-1,3-oxazole-4-carboxylic acid
2-[(1S)-1-azanyl-2-hydroxyethyl]-5-methyl-4,5-dihydro-1,3-oxazole-4-carboxylic acid
CROSSLNK 5-methyloxazoline-4-carboxylic acid (Ser-Thr)
L-serine 5-methyloxazoline-4-carboxylic acid
A protein modification that effectively converts a source amino acid residue to 5-hydroxy-3-methyl-L-proline.
C 6 H 9 N 1 O 2
127.14
127.06333
X
natural
(2S,3S,5Xi)-5-hydroxy-3-methylpyrrolidine-2-carboxylic acid
5-hydroxy-3-methyl-L-proline
5-hydroxy-3-methylproline
5Hy3MePro
MOD_RES 5-hydroxy-3-methylproline (Ile)
beta-methyl-delta-hydroxyproline
PSI-MOD
MOD:01905
5-hydroxy-3-methyl-L-proline
A protein modification that effectively converts a source amino acid residue to 5-hydroxy-3-methyl-L-proline.
PubMed:7592021
PubMed:8557573
RESID:AA0473
(2S,3S,5Xi)-5-hydroxy-3-methylpyrrolidine-2-carboxylic acid
5-hydroxy-3-methyl-L-proline
5-hydroxy-3-methylproline
5Hy3MePro
MOD_RES 5-hydroxy-3-methylproline (Ile)
beta-methyl-delta-hydroxyproline
A protein modification that effectively converts an L-methionine residue to dehydromethionine.
-1.01
C 0 H -1 N 0 O 0 S 0
-1.008374
1+
C 5 H 9 N 1 O 1 S 1
131.19
131.03993
M
artifact
N-term
(3S)-3-carboxy-1-methylisothiazolidin-1-ium
L-dehydromethionine
PSI-MOD
MOD:01906
dehydromethionine
A protein modification that effectively converts an L-methionine residue to dehydromethionine.
PubMed:18688235
PubMed:19775156
(3S)-3-carboxy-1-methylisothiazolidin-1-ium
L-dehydromethionine
A protein modification that effectively converts an L-methioninium (protonated L-methionine) residue to dehydromethionine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.016199
1+
C 5 H 9 N 1 O 1 S 1
131.19
131.03993
MOD:001464
artifact
N-term
(3S)-3-carboxy-1-methylisothiazolidin-1-ium
L-dehydromethionine
PSI-MOD
MOD:01907
This process accounts only for cyclizaation and not protonation. The alternative process (MOD:01906) accounts for both protonation and cyclization.
dehydromethionine (from L-methioninium)
A protein modification that effectively converts an L-methioninium (protonated L-methionine) residue to dehydromethionine.
PubMed:18688235
PubMed:19775156
(3S)-3-carboxy-1-methylisothiazolidin-1-ium
L-dehydromethionine
A protein modification that effectively converts a residue to the 4-sulfophenyl isothiocyanate adduct, alpha-amino-[(4-sulfophenyl)carbamothioyl] residue.
215.24
C 7 H 5 N 1 O 3 S 2
214.97108
X
artifact
Unimod:261
alpha-amino-[(4-sulfophenyl)carbamothioyl] residue
PSI-MOD
4-sulfophenyl isothiocyanate
SPITC
MOD:01908
4-sulfophenyl isothiocyanate alpha-amino derivatized residue
A protein modification that effectively converts a residue to the 4-sulfophenyl isothiocyanate adduct, alpha-amino-[(4-sulfophenyl)carbamothioyl] residue.
PubMed:14689565
PubMed:14745769
PubMed:15549660
PubMed:16526082
Unimod:261#N-term
alpha-amino-[(4-sulfophenyl)carbamothioyl] residue
4-sulfophenyl isothiocyanate
SPITC
A protein modification that effectively converts a residue to the 6x(13)C labeled 4-sulfophenyl isothiocyanate adduct, alpha-amino-[(4-sulfophenyl)carbamothioyl] residue.
220.99
(12)C 1 (13)C 6 H 5 N 1 O 3 S 2
220.99121
X
artifact
Unimod:464
PSI-MOD
4-sulfophenyl isothiocyanate (Heavy C13)
SPITC:13C(6)
MOD:01909
6x(13)C labeled 4-sulfophenyl isothiocyanate alpha-amino derivatized residue
A protein modification that effectively converts a residue to the 6x(13)C labeled 4-sulfophenyl isothiocyanate adduct, alpha-amino-[(4-sulfophenyl)carbamothioyl] residue.
PubMed:11467524
PubMed:16526082
Unimod:464#N-term
4-sulfophenyl isothiocyanate (Heavy C13)
SPITC:13C(6)
A protein modification that effectively substitutes one hydrogen atom of a residue with one fluorine atom.
17.99
C 0 F 1 H -1 N 0 O 0
17.990578
X
artifact
Unimod:127
F1Res
PSI-MOD
MOD:01910
monofluorinated residue
A protein modification that effectively substitutes one hydrogen atom of a residue with one fluorine atom.
Unimod:127
F1Res
A protein modification that effectively substitutes one hydrogen atom of a residue with one chlorine atom.
34.44
C 0 Cl 1 H -1 N 0 O 0
33.96103
X
artifact
Unimod:936
Cl1Res
PSI-MOD
MOD:01911
monochlorinated residue
A protein modification that effectively substitutes one hydrogen atom of a residue with one chlorine atom.
Unimod:936
Cl1Res
A protein modification that effectively substitutes one hydrogen atom of a residue with one bromine atom.
78.9
Br 1 C 0 H -1 N 0 O 0
77.910515
X
artifact
Unimod:340
Br1Res
PSI-MOD
MOD:01912
monobrominated residue
A protein modification that effectively substitutes one hydrogen atom of a residue with one bromine atom.
Unimod:340
Br1Res
A protein modification that effectively substitutes one hydrogen atom of an L-tryptophan residue with one chlorine atom.
34.44
C 0 Cl 1 H -1 N 0 O 0
33.96103
C 11 Cl 1 H 9 N 2 O 1
220.66
220.04034
W
artifact
Cl1Trp
PSI-MOD
MOD:01913
monochlorinated L-tryptophan
A protein modification that effectively substitutes one hydrogen atom of an L-tryptophan residue with one chlorine atom.
PubMed:18688235
Cl1Trp
A protein modification that effectively converts a 5-hydroxy-L-lysine residue to O5-galactosyl-L-hydroxylysine.
162.14
C 6 H 10 O 5
162.05283
C 16 H 22 N 2 O 7
354.36
354.1427
MOD:00037
natural
Unimod:907
uniprot.ptm:PTM-0556
CARBOHYD O-linked (Gal) hydroxylysine
OGal5HyLys
PSI-MOD
Galactosyl hydroxylysine
MOD:01914
Secondary to RESID:AA0028. This intermediate is rarely observed [JSG].
O5-galactosyl-L-hydroxylysine
A protein modification that effectively converts a 5-hydroxy-L-lysine residue to O5-galactosyl-L-hydroxylysine.
PMID:743239
PubMed:17516569
Unimod:907
CARBOHYD O-linked (Gal) hydroxylysine
OGal5HyLys
Galactosyl hydroxylysine
A protein modification that effectively converts an L-alanine residue to N-formyl-L-alanine.
28.01
C 1 H 0 N 0 O 1
27.994915
C 4 H 6 N 1 O 2
100.1
100.039856
A
hypothetical
N-term
(2S)-2-(formylamino)propanoic acid
2-formamidopropanoic acid
2-formamidopropionic acid
N-formyl-L-alanine
PSI-MOD
MOD:01915
N-formyl-L-alanine
A protein modification that effectively converts an L-alanine residue to N-formyl-L-alanine.
PubMed:9334739
RESID:AA0576
(2S)-2-(formylamino)propanoic acid
2-formamidopropanoic acid
2-formamidopropionic acid
N-formyl-L-alanine
A protein modification that effectively converts an L-tyrosine residue to O4'-(N-acetylamino)galactosyl-L-tyrosine.
203.19
C 8 H 13 N 1 O 5
203.07938
C 17 H 22 N 2 O 7
366.37
366.1427
Y
natural
uniprot.ptm:PTM-0570
(2S)-2-amino-3-(D-2-acetamido-2-deoxygalactopyranosyloxy)phenylpropanoic acid
CARBOHYD O-linked (GalNAc) tyrosine
O4'-(N-acetylamino)galactosyl-L-tyrosine
O4'-(N-acetylgalactosaminyl)tyrosine
O4'-glycosyl-L-tyrosine
mucin type O-glycosyltyrosine
PSI-MOD
MOD:01916
O4'-(N-acetylamino)galactosyl-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to O4'-(N-acetylamino)galactosyl-L-tyrosine.
PubMed:21712440
PubMed:21983924
RESID:AA0577
(2S)-2-amino-3-(D-2-acetamido-2-deoxygalactopyranosyloxy)phenylpropanoic acid
CARBOHYD O-linked (GalNAc) tyrosine
O4'-(N-acetylamino)galactosyl-L-tyrosine
O4'-(N-acetylgalactosaminyl)tyrosine
O4'-glycosyl-L-tyrosine
mucin type O-glycosyltyrosine
A protein modification that effectively crosslinks an L-aspartic acid residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine and the release of water.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 10 H 15 N 3 O 3
225.25
225.11134
D, K
natural
uniprot.ptm:PTM-0486
(2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid
CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn)
N(epsilon)-(beta-aspartyl)lysine
N6-(L-isoaspartyl)-L-lysine
XLNK-4Asp-N6Lys(Asp)
beta-(N6-lysyl)aspartyl acid
isoaspartyl N6-lysine
PSI-MOD
MOD:01917
Cross-link 2.
N6-(L-isoaspartyl)-L-lysine (Asp)
A protein modification that effectively crosslinks an L-aspartic acid residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine and the release of water.
ChEBI:21862
PubMed:11000116
PubMed:15044436
PubMed:18063798
PubMed:6503713
RESID:AA0294#ASP
(2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid
CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn)
N(epsilon)-(beta-aspartyl)lysine
N6-(L-isoaspartyl)-L-lysine
XLNK-4Asp-N6Lys(Asp)
beta-(N6-lysyl)aspartyl acid
isoaspartyl N6-lysine
A protein modification that effectively converts an L-lysine residue to (2S,5S)-5-hydroxylysine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 6 H 12 N 2 O 2
144.17
144.08987
K
natural
uniprot.ptm:PTM-0472
(2S,5S)-2,6-diamino-5-hydroxyhexanoic acid
(2S,5S)-5-hydroxylysine
2,6-bisazanyl-5-hydroxyhexanoic acid
2,6-diamino-2,3,4,6-tetradeoxyhexonic acid
L-allo-delta-hydroxylysine
L-threo-delta-hydroxylysine
MOD_RES (5S)-5-hydroxylysine
alpha,epsilon-diamino-delta-hydroxycaproic acid
PSI-MOD
MOD:01918
(2S,5S)-5-hydroxylysine
A protein modification that effectively converts an L-lysine residue to (2S,5S)-5-hydroxylysine.
PubMed:19574390
PubMed:22238144
RESID:AA0578
(2S,5S)-2,6-diamino-5-hydroxyhexanoic acid
(2S,5S)-5-hydroxylysine
2,6-bisazanyl-5-hydroxyhexanoic acid
2,6-diamino-2,3,4,6-tetradeoxyhexonic acid
L-allo-delta-hydroxylysine
L-threo-delta-hydroxylysine
MOD_RES (5S)-5-hydroxylysine
alpha,epsilon-diamino-delta-hydroxycaproic acid
A protein modification that effectively converts an L-aspartic acid residue to (2S,3S)-3-hydroxyaspartic acid.
16.0
C 0 H 0 N 0 O 1
15.994915
C 4 H 5 N 1 O 4
131.09
131.02185
D
natural
uniprot.ptm:PTM-0473
(2S,3S)-2-amino-3-hydroxybutanedioic acid
(2S,3S)-3-hydroxyaspartic acid
(3S)-3-hydroxy-L-aspartic acid
2-amino-3-hydroxysuccinic acid
2-azanyl-3-hydroxybutanedioic acid
3-hydroxyaspartic acid
L-threo-3-hydroxyaspartic acid
L-threo-beta-hydroxyaspartic acid
MOD_RES (3S)-3-hydroxyaspartate
PSI-MOD
MOD:01919
(2S,3S)-3-hydroxyaspartic acid
A protein modification that effectively converts an L-aspartic acid residue to (2S,3S)-3-hydroxyaspartic acid.
ChEBI:10696
ChEBI:138111
PubMed:21177872
RESID:AA0579
(2S,3S)-2-amino-3-hydroxybutanedioic acid
(2S,3S)-3-hydroxyaspartic acid
(3S)-3-hydroxy-L-aspartic acid
2-amino-3-hydroxysuccinic acid
2-azanyl-3-hydroxybutanedioic acid
3-hydroxyaspartic acid
L-threo-3-hydroxyaspartic acid
L-threo-beta-hydroxyaspartic acid
MOD_RES (3S)-3-hydroxyaspartate
A protein modification that effectively converts an L-histidine residue to 3-hydroxy-L-histidine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 6 H 7 N 3 O 2
153.14
153.05383
H
natural
uniprot.ptm:PTM-0477
(2S)-2-amino-3-hydroxy-3-(1H-imidazol-4-yl)propanoic acid
3-hydroxy-L-histidine
MOD_RES (3S)-3-hydroxyhistidine
PSI-MOD
MOD:01920
3-hydroxy-L-histidine
A protein modification that effectively converts an L-histidine residue to 3-hydroxy-L-histidine.
ChEBI:138021
PubMed:21251231
RESID:AA0580
(2S)-2-amino-3-hydroxy-3-(1H-imidazol-4-yl)propanoic acid
3-hydroxy-L-histidine
MOD_RES (3S)-3-hydroxyhistidine
A protein modification that effectively converts an L-aspartic acid residue to D-aspartic acid.
0.0
C 0 H 0 N 0 O 0
0.0
C 4 H 5 N 1 O 3
115.09
115.02694
D
artifactual
(2R)-2-aminobutanedioic acid
2-azanylbutanedioic acid
D-aspartic acid
aminosuccinic acid
PSI-MOD
MOD:01921
D-aspartic acid (Asp)
A protein modification that effectively converts an L-aspartic acid residue to D-aspartic acid.
ChEBI:48094
PubMed:9384562
RESID:AA0190#ASP
(2R)-2-aminobutanedioic acid
2-azanylbutanedioic acid
D-aspartic acid
aminosuccinic acid
A protein modification that effectively converts an L-serine residue to 3-methoxydehydroalanine.
12.01
C 1 H 0 N 0 O 0
12.0
C 4 H 5 N 1 O 2
99.09
99.03203
S
natural
2-amino-3-methoxyprop-2-enoic acid
3-methoxydehydroalanine
3-methoxydidehydroalanine
PSI-MOD
MOD:01922
3-methoxydehydroalanine
A protein modification that effectively converts an L-serine residue to 3-methoxydehydroalanine.
PubMed:19745839
RESID:AA0582
2-amino-3-methoxyprop-2-enoic acid
3-methoxydehydroalanine
3-methoxydidehydroalanine
A protein modification that effectively crosslinks an L-aspartic acid residue and an L-lysine residue by an isopeptide bond to form N6-(L-aspartyl)-L-lysine and the release of water.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 10 H 16 N 3 O 4
242.26
242.11407
D, K
natural
C-term
(2S)-2-amino-6-([(2S)-2-amino-3-carboxypropanoyl]amino)hexanoic acid
N(epsilon)-(alpha-aspartyl)lysine
N6-(L-aspartyl)-L-lysine
XLNK-4Asp-N6Lys(Asp)
alpha-(N6-lysyl)aspartyl acid
aspartyl N6-lysine
PSI-MOD
MOD:01923
Cross-link 2.
N6-(L-aspartyl)-L-lysine
A protein modification that effectively crosslinks an L-aspartic acid residue and an L-lysine residue by an isopeptide bond to form N6-(L-aspartyl)-L-lysine and the release of water.
PubMed:15044436
RESID:AA0583
(2S)-2-amino-6-([(2S)-2-amino-3-carboxypropanoyl]amino)hexanoic acid
N(epsilon)-(alpha-aspartyl)lysine
N6-(L-aspartyl)-L-lysine
XLNK-4Asp-N6Lys(Asp)
alpha-(N6-lysyl)aspartyl acid
aspartyl N6-lysine
A protein modification that effectively converts an L-cysteine residue to S-octanoyl-L-cysteine.
126.2
C 8 H 14 N 0 O 1 S 0
126.10446
C 11 H 19 N 1 O 2 S 1
229.34
229.11365
C
natural
(2S)-2-amino-3-(octanoylsulfanyl)propanoic acid
2-amino-3-(octanoylthio)propanoic acid
ACT_SITE Acyl-thioester intermediate
S-octanoyl-L-cysteine
cysteine octanoate thioester
PSI-MOD
MOD:01924
S-octanoyl-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-octanoyl-L-cysteine.
PubMed:12591875
PubMed:16342964
RESID:AA0584
(2S)-2-amino-3-(octanoylsulfanyl)propanoic acid
2-amino-3-(octanoylthio)propanoic acid
ACT_SITE Acyl-thioester intermediate
S-octanoyl-L-cysteine
cysteine octanoate thioester
A protein modification that effectively converts an L-lysine residue to (2S,5R)-5-hydroxylysine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 6 H 12 N 2 O 2
144.17
144.08987
K
natural
uniprot.ptm:PTM-0471
(2S,5R)-2,6-diamino-5-hydroxyhexanoic acid
(2S,5R)-5-hydroxylysine
2,6-bisazanyl-5-hydroxyhexanoic acid
2,6-diamino-2,3,4,6-tetradeoxyhexonic acid
5-hydroxylated L-lysine
5HyLys
L-erythro-delta-hydroxylysine
MOD_RES (2S,5R)-5-hydroxylysine
alpha,epsilon-diamino-delta-hydroxycaproic acid
PSI-MOD
MOD:01925
(2S,5R)-5-hydroxylysine
A protein modification that effectively converts an L-lysine residue to (2S,5R)-5-hydroxylysine.
ChEBI:18040
PubMed:13375629
PubMed:15504407
PubMed:16101297
PubMed:2857489
RESID:AA0028
(2S,5R)-2,6-diamino-5-hydroxyhexanoic acid
(2S,5R)-5-hydroxylysine
2,6-bisazanyl-5-hydroxyhexanoic acid
2,6-diamino-2,3,4,6-tetradeoxyhexonic acid
5-hydroxylated L-lysine
5HyLys
L-erythro-delta-hydroxylysine
MOD_RES (2S,5R)-5-hydroxylysine
alpha,epsilon-diamino-delta-hydroxycaproic acid
A protein modification that effectively converts an L-aspartic acid residue to one of the diastereomeric 3-hydroxy-L-aspartic acid residues.
16.0
C 0 H 0 N 0 O 1
15.994915
C 4 H 5 N 1 O 4
131.09
131.02185
D
natural
Unimod:35
(2S)-2-amino-3-hydroxybutanedioic acid
(2S)-3-hydroxyaspartic acid
3HyAsp
erythro-beta-hydroxylated L-aspartic acid
hydroxylationd
monohydroxylated aspartic acid
PSI-MOD
Oxidation
MOD:01926
3-hydroxy-L-aspartic acid
A protein modification that effectively converts an L-aspartic acid residue to one of the diastereomeric 3-hydroxy-L-aspartic acid residues.
OMSSA:59
Unimod:35#D
(2S)-2-amino-3-hydroxybutanedioic acid
(2S)-3-hydroxyaspartic acid
3HyAsp
erythro-beta-hydroxylated L-aspartic acid
hydroxylationd
monohydroxylated aspartic acid
Oxidation
A protein modification that effectively converts an L-tyrosine residue to O4'-glycosyltyrosine.
Y
natural
OGlycoTyr
PSI-MOD
MOD:01927
O-glycosyl-L-tyrosine
A protein modification that effectively converts an L-tyrosine residue to O4'-glycosyltyrosine.
PubMed:18688235
OGlycoTyr
A protein modification that effectively crosslinks either an L-asparagine residue or an L-aspartic acid residue with a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)glycine.
C 6 H 7 N 2 O 3
155.13
155.04567
G
natural
N-term
(2S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid
2-amino-N4-(carboxymethyl)-butanediamic acid
N-(L-isoaspartyl)-glycine
N-beta-aspartylglycine
N4-(carboxymethyl)-asparagine
XLNK-4Asp-NGly
isoaspartyl glycine
PSI-MOD
MOD:01928
Cross-link 2.
N-(L-isoaspartyl)-glycine
A protein modification that effectively crosslinks either an L-asparagine residue or an L-aspartic acid residue with a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)glycine.
ChEBI:21479
PubMed:1826288
RESID:AA0126
(2S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid
2-amino-N4-(carboxymethyl)-butanediamic acid
N-(L-isoaspartyl)-glycine
N-beta-aspartylglycine
N4-(carboxymethyl)-asparagine
XLNK-4Asp-NGly
isoaspartyl glycine
A protein modification that effectively crosslinks an either an L-asparagine residue or an L-aspartic acid residue with an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine.
C 10 H 15 N 3 O 3
225.25
225.11134
K
natural
(2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid
CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn)
N(epsilon)-(beta-aspartyl)lysine
N-(beta-Aspartyl)-Lysine (Crosslink)
N6-(L-isoaspartyl)-L-lysine
XLNK-4Asp-N6Lys
beta-(N6-lysyl)aspartyl acid
isoaspartyl N6-lysine
PSI-MOD
MOD:01929
Cross-link 2.
N6-(L-isoaspartyl)-L-lysine
A protein modification that effectively crosslinks an either an L-asparagine residue or an L-aspartic acid residue with an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine.
ChEBI:21862
DeltaMass:0
PubMed:11000116
PubMed:6503713
RESID:AA0294
(2S)-2-amino-6-([(3S)-3-amino-3-carboxypropanoyl]amino)hexanoic acid
CROSSLNK Isoaspartyl lysine isopeptide (Lys-Asn)
N(epsilon)-(beta-aspartyl)lysine
N-(beta-Aspartyl)-Lysine (Crosslink)
N6-(L-isoaspartyl)-L-lysine
XLNK-4Asp-N6Lys
beta-(N6-lysyl)aspartyl acid
isoaspartyl N6-lysine
A protein modification that effectively converts an L-asparagine residue to D-aspartic acid.
0.98
C 0 H -1 N -1 O 1
0.984016
C 4 H 5 N 1 O 3
115.09
115.02694
N
artifactual
(2R)-2-aminobutanedioic acid
2-azanylbutanedioic acid
D-aspartic acid
aminosuccinic acid
PSI-MOD
MOD:01930
D-aspartic acid (Asn)
A protein modification that effectively converts an L-asparagine residue to D-aspartic acid.
ChEBI:48094
PubMed:9384562
RESID:AA0190#ASN
(2R)-2-aminobutanedioic acid
2-azanylbutanedioic acid
D-aspartic acid
aminosuccinic acid
A protein modification that effectively converts an L-lysine residue to N6-phospho-L-lysine.
79.98
C 0 H 1 N 0 O 3 P 1
79.96633
C 6 H 13 N 2 O 4 P 1
208.15
208.0613
K
hypothetical
(2S)-2-amino-6-(phosphonoamino)hexanoic acid
(2S)-2-azanyl-6-(phosphonoamino)hexanoic acid
6-phospholysine
N(6)-phosphonolysine
N(epsilon)-phospholysine
N(epsilon)-phosphonolysine
N(epsilon)-phosphonyllysine
N(epsilon)-phosphoryllysine
N6-phospho-L-lysine
PSI-MOD
MOD:01931
N6-phospho-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-phospho-L-lysine.
PubMed:20144148
RESID:AA0585
(2S)-2-amino-6-(phosphonoamino)hexanoic acid
(2S)-2-azanyl-6-(phosphonoamino)hexanoic acid
6-phospholysine
N(6)-phosphonolysine
N(epsilon)-phospholysine
N(epsilon)-phosphonolysine
N(epsilon)-phosphonyllysine
N(epsilon)-phosphoryllysine
N6-phospho-L-lysine
A protein modification that effectively cross-links two lysine residues with a carbon-nitrogen bond to form L-lysinonorleucine..
-17.03
C 0 H -3 N -1 O 0
-17.026548
C 12 H 21 N 3 O 2
239.32
239.16338
K, K
natural
(2S)-2-amino-6-([(5S)-5-amino-5-carboxypentyl]amino)hexanoic acid
(2S,2'S)-6,6'-iminobis(2-aminohexanoic acid)
6-(N6-L-lysino)-L-norleucine
L-lysinonorleucine
N6-[(5S)-5-amino-5-carboxypentyl]-L-lysine
lysinonorleucine
lysinorleucine [misspelling]
lysylnorleucine
PSI-MOD
MOD:01932
Cross-link 2.
L-lysinonorleucine
A protein modification that effectively cross-links two lysine residues with a carbon-nitrogen bond to form L-lysinonorleucine..
PubMed:5117030
PubMed:5817620
PubMed:5879466
PubMed:6030254
RESID:AA0586
(2S)-2-amino-6-([(5S)-5-amino-5-carboxypentyl]amino)hexanoic acid
(2S,2'S)-6,6'-iminobis(2-aminohexanoic acid)
6-(N6-L-lysino)-L-norleucine
L-lysinonorleucine
N6-[(5S)-5-amino-5-carboxypentyl]-L-lysine
lysinonorleucine
lysinorleucine [misspelling]
lysylnorleucine
A protein modification that effectively cross-links four L-lysine residues to form desmosine.
-58.15
C 0 H -16 N -3 O 0
-58.13497
1+
C 24 H 32 N 5 O 4
454.55
454.24487
K, K, K, K
natural
4-[(4S)-4-amino-4-carboxybutyl]-1-[(5S)-5-amino-5-carboxypentyl]-3,5-bis[(3S)-3-amino-3-carboxypropyl]pyridinium
6-[4-(4-amino-4-carboxybutyl)-3,5-bis(3-amino-3-carboxypropyl)pyridinio]norleucine
desmosine
PSI-MOD
MOD:01933
Cross-link 4.
desmosine
A protein modification that effectively cross-links four L-lysine residues to form desmosine.
ChEBI:37629
PubMed:13941623
PubMed:14109938
PubMed:14109939
PubMed:5839176
RESID:AA0587
4-[(4S)-4-amino-4-carboxybutyl]-1-[(5S)-5-amino-5-carboxypentyl]-3,5-bis[(3S)-3-amino-3-carboxypropyl]pyridinium
6-[4-(4-amino-4-carboxybutyl)-3,5-bis(3-amino-3-carboxypropyl)pyridinio]norleucine
desmosine
A protein modification that effectively cross-links four L-lysine residues to form isodesmosine.
-58.15
C 0 H -16 N -3 O 0
-58.13497
1+
C 24 H 32 N 5 O 4
454.55
454.24487
K, K, K, K
natural
2-[(4S)-4-amino-4-carboxybutyl]-1-[(5S)-5-amino-5-carboxypentyl]-3,5-bis[(3S)-3-amino-3-carboxypropyl]pyridinium
6-[2-(4-amino-4-carboxybutyl)-3,5-bis(3-amino-3-carboxypropyl)pyridinio]norleucine
isodesmosine
PSI-MOD
MOD:01934
Cross-link 4.
isodesmosine
A protein modification that effectively cross-links four L-lysine residues to form isodesmosine.
ChEBI:37629
PubMed:13941623
PubMed:14109938
PubMed:14109939
PubMed:5839176
RESID:AA0588
2-[(4S)-4-amino-4-carboxybutyl]-1-[(5S)-5-amino-5-carboxypentyl]-3,5-bis[(3S)-3-amino-3-carboxypropyl]pyridinium
6-[2-(4-amino-4-carboxybutyl)-3,5-bis(3-amino-3-carboxypropyl)pyridinio]norleucine
isodesmosine
modification from RESID
178.14
C 6 H 10 N 0 O 6
178.04774
C 12 H 22 N 2 O 7
306.32
306.1427
K
natural
uniprot.ptm:PTM-0572
(D-glucopyranosyl)oxy-L-lysine
CARBOHYD O-linked (Glc) hydroxylysine
O-glucosyl-L-hydroxylysine
PSI-MOD
MOD:01935
O-glucosyl-L-hydroxylysine
modification from RESID
PubMed:22045808
RESID:AA0589
(D-glucopyranosyl)oxy-L-lysine
CARBOHYD O-linked (Glc) hydroxylysine
O-glucosyl-L-hydroxylysine
A protein modification that effectively converts an L-lysine residue to N6-oleoyl-L-lysine.
264.45
C 18 H 32 N 0 O 1
264.24533
C 24 H 44 N 2 O 2
392.63
392.34027
K
natural
(2S)-2-amino-6-([(9Z)-octadec-9-enoyl]amino)hexanoic acid
N6-[(9Z)-1-oxo-9-octadecenyl]lysine
N6-oleoyl-L-lysine
PSI-MOD
MOD:01936
N6-oleoyl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-oleoyl-L-lysine.
PubMed:20942504
RESID:AA0590
(2S)-2-amino-6-([(9Z)-octadec-9-enoyl]amino)hexanoic acid
N6-[(9Z)-1-oxo-9-octadecenyl]lysine
N6-oleoyl-L-lysine
A protein modification that effectively converts an L-methionine residue to N-palmitoyl-L-methionine.
238.41
C 16 H 30 N 0 O 1 S 0
238.22966
C 21 H 40 N 1 O 2 S 1
370.62
370.27798
M
natural
N-term
(2S)-2-(hexadecanoylamino)-4-(methylsulfanyl)butanoic acid
2-(hexadecanamido)-4-(methylsulfanyl)butanoic acid
LIPID N-palmitoyl methionine
N-(1-oxohexadecyl)methionine
N-palmitoyl-L-methionine
PSI-MOD
MOD:01937
N-palmitoyl-L-methionine
A protein modification that effectively converts an L-methionine residue to N-palmitoyl-L-methionine.
PubMed:20942504
RESID:AA0591
(2S)-2-(hexadecanoylamino)-4-(methylsulfanyl)butanoic acid
2-(hexadecanamido)-4-(methylsulfanyl)butanoic acid
LIPID N-palmitoyl methionine
N-(1-oxohexadecyl)methionine
N-palmitoyl-L-methionine
A protein modification that crosslinks an asparagine and the following cysteine residue with the formation of (2-aminosuccinimidyl)-3-sulfanylpropanoic acid and the release of ammonia.
-17.03
C 0 H -3 N -1 O 0 S 0
-17.026548
C 7 H 8 N 2 O 3 S 1
200.21
200.02556
C, N
natural
(2R)-2-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-3-sulfanylpropanoic acid
2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid
aspartimide cysteine
PSI-MOD
MOD:01938
Cross-link 2.
2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid (Asn)
A protein modification that crosslinks an asparagine and the following cysteine residue with the formation of (2-aminosuccinimidyl)-3-sulfanylpropanoic acid and the release of ammonia.
RESID:AA0592#ASN
(2R)-2-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-3-sulfanylpropanoic acid
2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid
aspartimide cysteine
A protein modification that crosslinks an aspartic acid and the following cysteine residue with the formation of (2-aminosuccinimidyl)-3-sulfanylpropanoic acid and the loss of a water molecule.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 7 H 8 N 2 O 3 S 1
200.21
200.02556
C, D
natural
(2R)-2-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-3-sulfanylpropanoic acid
2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid
aspartimide cysteine
PSI-MOD
MOD:01939
Cross-link 2.
2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid (Asp)
A protein modification that crosslinks an aspartic acid and the following cysteine residue with the formation of (2-aminosuccinimidyl)-3-sulfanylpropanoic acid and the loss of a water molecule.
RESID:AA0592#ASP
(2R)-2-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-3-sulfanylpropanoic acid
2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid
aspartimide cysteine
A protein modification that crosslinks an asparagine and the following glutamic acid residue with the formation of (2-aminosuccinimidyl)pentanedioic acid and the release of ammonia.
-17.03
C 0 H -3 N -1 O 0
-17.026548
C 9 H 10 N 2 O 5
226.19
226.05898
E, N
natural
(4S)-4-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-5-oxopentanoic acid
2-(2-aminosuccinimidyl)pentanedioic acid
aspartimide glutamic acid
PSI-MOD
MOD:01940
Cross-link 2.
2-(2-aminosuccinimidyl)pentanedioic acid (Asn)
A protein modification that crosslinks an asparagine and the following glutamic acid residue with the formation of (2-aminosuccinimidyl)pentanedioic acid and the release of ammonia.
RESID:AA0593#ASN
(4S)-4-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-5-oxopentanoic acid
2-(2-aminosuccinimidyl)pentanedioic acid
aspartimide glutamic acid
A protein modification that crosslinks an aspartic acid and the following glycine residue with the formation of (2-aminosuccinimidyl)pentanedioic acid and the loss of a water molecule.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 9 H 10 N 2 O 5
226.19
226.05898
D, E
natural
(4S)-4-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-5-oxopentanoic acid
2-(2-aminosuccinimidyl)pentanedioic acid
aspartimide glutamic acid
PSI-MOD
MOD:01941
Cross-link 2.
2-(2-aminosuccinimidyl)pentanedioic acid (Asp)
A protein modification that crosslinks an aspartic acid and the following glycine residue with the formation of (2-aminosuccinimidyl)pentanedioic acid and the loss of a water molecule.
RESID:AA0593#ASP
(4S)-4-[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]-5-oxopentanoic acid
2-(2-aminosuccinimidyl)pentanedioic acid
aspartimide glutamic acid
A protein modification that effectively converts a source amino acid residue to D-aspartic acid.
C 4 H 5 N 1 O 3
115.09
115.02694
X
artifactual
(2R)-2-aminobutanedioic acid
2-azanylbutanedioic acid
D-aspartic acid
aminosuccinic acid
PSI-MOD
MOD:01942
D-aspartic acid
A protein modification that effectively converts a source amino acid residue to D-aspartic acid.
ChEBI:48094
PubMed:9384562
RESID:AA0190
(2R)-2-aminobutanedioic acid
2-azanylbutanedioic acid
D-aspartic acid
aminosuccinic acid
A protein modification that crosslinks two adjacent residues by formation of a pyrrolidione ring.
PSI-MOD
MOD:01943
pyrrolidione ring crosslinked residues
A protein modification that crosslinks two adjacent residues by formation of a pyrrolidione ring.
PubMed:18688235
A protein modification that forms (2-aminosuccinimidyl)acetic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following residue.
X
hypothetical
PSI-MOD
MOD:01944
Cross-link 2; this cross-link is formed by the condensation of an aspartic acid residue or an asparagine residue with the alpha-amido of the following residue.
2-aminosuccinimide ring crosslinked residues
A protein modification that forms (2-aminosuccinimidyl)acetic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following residue.
PubMed:18688235
A protein modification that forms (2-aminosuccinimidyl)-3-sulfanylpropanoic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following cysteine residue.
C 6 H 6 N 2 O 3
154.13
154.03784
C, X
hypothetical
PSI-MOD
MOD:01945
Cross-link 2; this cross-link is formed by the condensation of an aspartic acid residue or an asparagine residue with the alpha-amido of the following residue.
2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid
A protein modification that forms (2-aminosuccinimidyl)-3-sulfanylpropanoic acid by crosslinking either an aspartic acid residue or an asparagine residue with the following cysteine residue.
PubMed:18688235
A protein modification that forms (2-aminosuccinimidyl)pentanedioicacid by crosslinking either an aspartic acid residue or an asparagine residue with the following glutamic acid
residue.
C 6 H 6 N 2 O 3
154.13
154.03784
E, X
hypothetical
PSI-MOD
MOD:01946
Cross-link 2; this cross-link is formed by the condensation of an aspartic acid residue or an asparagine residue with the alpha-amido of the following residue.
2-(2-aminosuccinimidyl)pentanedioic acid
A protein modification that forms (2-aminosuccinimidyl)pentanedioicacid by crosslinking either an aspartic acid residue or an asparagine residue with the following glutamic acid
residue.
PubMed:18688235
A protein modification that effectively cross-links an L-threonine residue and an L-aspartic acid residue with an ester bond to form O-(L-isoaspartyl)-L-threonine.
-18.02
C 0 H -2 N 0 O -1
-18.010565
C 8 H 10 N 2 O 4
198.18
198.06406
D, T
natural
(2S)-2-amino-4-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-4-oxobutanoic acid
(2S,3R)-2-amino-3-([(4S)-3-amino-3-carboxypropanoyl]oxy)propanoic acid
CROSSLNK isoaspartyl threonine ester (Thr-Asp)
O(beta)-(beta-aspartyl)threonine
O-(L-isoaspartyl)-L-threonine
O3-(isoaspartyl)-threonine
PSI-MOD
MOD:01947
Cross-link 2.
O-(L-isoaspartyl)-L-threonine (cross-link)
A protein modification that effectively cross-links an L-threonine residue and an L-aspartic acid residue with an ester bond to form O-(L-isoaspartyl)-L-threonine.
PubMed:17157318
PubMed:8706862
RESID:AA0525#TDX
(2S)-2-amino-4-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-4-oxobutanoic acid
(2S,3R)-2-amino-3-([(4S)-3-amino-3-carboxypropanoyl]oxy)propanoic acid
CROSSLNK isoaspartyl threonine ester (Thr-Asp)
O(beta)-(beta-aspartyl)threonine
O-(L-isoaspartyl)-L-threonine
O3-(isoaspartyl)-threonine
A protein modification that effectively cross-links an L-cysteine residue and two L-serine residues by a thioether bond and a carbon-carbon bond to form labionin.
-36.03
C 0 H -4 N 0 O -2 S 0
-36.02113
C 9 H 11 N 3 O 3 S 1
241.26
241.05211
C, S, S
natural
(2S,4S)-2,4-diamino-2-[([(2R)-2-amino-2-carboxyethyl]sulfanyl)methyl]pentanedioic acid
(2S,4S,8R)-2,4,8-triamino-4-carboxy-6-thianonanedioic acid
(2S,4S,8R)-labionin
labionin
PSI-MOD
MOD:01948
Cross-link 3.
labionin
A protein modification that effectively cross-links an L-cysteine residue and two L-serine residues by a thioether bond and a carbon-carbon bond to form labionin.
PubMed:20082397
RESID:AA0594
(2S,4S)-2,4-diamino-2-[([(2R)-2-amino-2-carboxyethyl]sulfanyl)methyl]pentanedioic acid
(2S,4S,8R)-2,4,8-triamino-4-carboxy-6-thianonanedioic acid
(2S,4S,8R)-labionin
labionin
A protein modification that effectively cross-links a phenylalanine and two tyrosine residues to form coelenterazine.
-50.06
C -1 H -6 N 0 O -2
-50.036777
C 26 H 21 N 3 O 3
423.47
423.1583
F, Y, Y
hypothetical
N-term
8-benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one
Oplophorus luciferin
coelenterazine
PSI-MOD
MOD:01949
Cross-link 3.
coelenterazine
A protein modification that effectively cross-links a phenylalanine and two tyrosine residues to form coelenterazine.
ChEBI:2311
PubMed:10830969
PubMed:11572972
PubMed:19833098
RESID:AA0595
8-benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one
Oplophorus luciferin
coelenterazine
A protein modification that effectively converts an L-glutamine residue to L-isoglutamyl histamine.
94.12
C 5 H 6 N 2 O 0
94.0531
C 10 H 14 N 4 O 2
222.25
222.11168
Q
natural
uniprot.ptm:PTM-0488
(2S)-2-amino-5-([2-(1H-imidazol-5-yl)ethyl]amino)-5-oxopentanoic acid
(gamma-glutamyl)histamine
L-isoglutamyl histamine
PSI-MOD
MOD:01950
L-isoglutamyl histamine
A protein modification that effectively converts an L-glutamine residue to L-isoglutamyl histamine.
PubMed:23022564
RESID:AA0596
(2S)-2-amino-5-([2-(1H-imidazol-5-yl)ethyl]amino)-5-oxopentanoic acid
(gamma-glutamyl)histamine
L-isoglutamyl histamine
A protein modification that effectively crosslinks an L-glutamine residue and an L-serine residue by an ester bond and releasing ammonia to form O-(L-isoglutamyl)-L-serine.
-17.03
C 0 H -3 N -1 O 0
-17.026548
C 8 H 10 N 2 O 4
198.18
198.06406
Q, S
natural
(2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid
O(beta)-(gamma-glutamyl)serine
O-(L-isoglutamyl)-L-serine
O3-(isoglutamyl)-serine
PSI-MOD
MOD:01951
Cross-link 2.
O-(L-isoglutamyl)-L-serine (Gln-Ser)
A protein modification that effectively crosslinks an L-glutamine residue and an L-serine residue by an ester bond and releasing ammonia to form O-(L-isoglutamyl)-L-serine.
PubMed:17051152
RESID:AA0597#QSX
(2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid
O(beta)-(gamma-glutamyl)serine
O-(L-isoglutamyl)-L-serine
O3-(isoglutamyl)-serine
A protein modification that effectively cross-links an L-threonine residue and an L-glutamine residue with an ester bond releasing ammonia to form O-(L-isoglutamyl)-L-threonine.
-17.03
C 0 H -3 N -1 O 0
-17.026548
C 9 H 12 N 2 O 4
212.2
212.07971
Q, T
natural
(2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid
(2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid
5-(threon-O3-yl)glutamate
O(beta)-(gamma-glutamyl)threonine
O-(L-isoglutamyl)-L-threonine
O3-(isoglutamyl)threonine
PSI-MOD
MOD:01952
Cross-link 2.
O-(L-isoglutamyl)-L-threonine (Gln-Thr)
A protein modification that effectively cross-links an L-threonine residue and an L-glutamine residue with an ester bond releasing ammonia to form O-(L-isoglutamyl)-L-threonine.
PubMed:17051152
RESID:AA0536#TQX
(2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid
(2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid
5-(threon-O3-yl)glutamate
O(beta)-(gamma-glutamyl)threonine
O-(L-isoglutamyl)-L-threonine
O3-(isoglutamyl)threonine
A protein modification that effectively converts four L-cysteine residues and a four-iron cluster to tetrakis-L-cysteinyl tetrairon octanitrosyl.
459.4
C 0 Fe 4 H -4 N 8 O 8 S 0
459.69235
C 12 Fe 4 H 16 N 12 O 12 S 4
871.95
871.7291
C, C, C, C
hypothetical
PSI-MOD
MOD:01953
Cross-link 4.
tetrakis-L-cysteinyl tetrairon octanitrosyl
A protein modification that effectively converts four L-cysteine residues and a four-iron cluster to tetrakis-L-cysteinyl tetrairon octanitrosyl.
PubMed:21182249
RESID:AA0599
A protein modification that effectively converts an L-selenocysteine residue to dehydroalanine.
-80.99
C 0 H -2 N 0 O 0 Se -1
-81.932175
C 3 H 3 N 1 O 1
69.06
69.02146
U
natural
2,3-didehydroalanine
2-aminoacrylic acid
2-aminopropenoic acid
4-methylidene-imidazole-5-one (MIO) active site
Dha
anhydroserine
dehydroalanine
PSI-MOD
MOD:01954
dehydroalanine (Sec)
A protein modification that effectively converts an L-selenocysteine residue to dehydroalanine.
ChEBI:17123
PubMed:10220322
PubMed:12781460
PubMed:1547888
PubMed:1815586
PubMed:20805503
PubMed:21420488
PubMed:22031445
PubMed:2914619
PubMed:7947813
PubMed:8239649
RESID:AA0181
2,3-didehydroalanine
2-aminoacrylic acid
2-aminopropenoic acid
4-methylidene-imidazole-5-one (MIO) active site
Dha
anhydroserine
dehydroalanine
modification from RESID
333.78
C 0 Ca 1 H -6 Mn 4 N 0 O 5
333.6424
C 32 Ca 1 H 38 Mn 4 N 9 O 23
1176.53
1175.9229
A, D, D, E, E, E, H
natural
C-term
4Mn-Ca-5O cluster
L-alaninato bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese pentoxide
mu2-alaninato-1kappaO(1),3kappaO(1')-mu2-aspartato-1kappaO(4),5kappaO(4')-mu2-aspartato-2kappaO(4),3kappaO(4')-mu2-glutamato-3kappaO(5),4kappaO(5')-mu2-glutamato-4kappaO(5),5kappaO(5')-mu-glutamato-2kappaO(5)-mu-histidino-2kappaN(tau)-mu4-oxido-1:2:4:5kappa(4)O-tri-mu3-oxido-1:2:3kappa(3)O;1:3:4kappa(3)O;2:3:4kappa(3)O;mu-oxido-4:5kappa(2)O-calciumtetramanganese
photosystem II catalytic cluster
PSI-MOD
MOD:01955
Cross-link 7.
L-alaninato bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese pentoxide
modification from RESID
PubMed:21499260
RESID:AA0600
4Mn-Ca-5O cluster
L-alaninato bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese pentoxide
mu2-alaninato-1kappaO(1),3kappaO(1')-mu2-aspartato-1kappaO(4),5kappaO(4')-mu2-aspartato-2kappaO(4),3kappaO(4')-mu2-glutamato-3kappaO(5),4kappaO(5')-mu2-glutamato-4kappaO(5),5kappaO(5')-mu-glutamato-2kappaO(5)-mu-histidino-2kappaN(tau)-mu4-oxido-1:2:4:5kappa(4)O-tri-mu3-oxido-1:2:3kappa(3)O;1:3:4kappa(3)O;2:3:4kappa(3)O;mu-oxido-4:5kappa(2)O-calciumtetramanganese
photosystem II catalytic cluster
A protein modification that effectively converts an L-arginine residue to (3R)-3-hydroxy-L-arginine.
16.0
C 0 H 0 N 0 O 1
15.994915
C 6 H 12 N 4 O 2
172.19
172.09602
R
natural
uniprot.ptm:PTM-0476
(2S,3R)-2-amino-5-[(diaminomethylidene)amino]-3-hydroxypentanoic acid
(3R)-3-hydroxy-L-arginine
2-amino-5-(carbamimidamido)-3-hydroxypentanoic acid [tautomer]
2-amino-5-[(aminoiminomethyl)amino]-3-hydroxypentanoic acid [tautomer]
2-amino-5-guanidino-3-hydroxypentanoic acid
C(beta)-hydroxyarginine
MOD_RES (3R)-3-hydroxyarginine
beta-hydroxyarginine
PSI-MOD
MOD:01956
(3R)-3-hydroxy-L-arginine
A protein modification that effectively converts an L-arginine residue to (3R)-3-hydroxy-L-arginine.
PubMed:10094780
PubMed:23103944
PubMed:786730
RESID:AA0601
(2S,3R)-2-amino-5-[(diaminomethylidene)amino]-3-hydroxypentanoic acid
(3R)-3-hydroxy-L-arginine
2-amino-5-(carbamimidamido)-3-hydroxypentanoic acid [tautomer]
2-amino-5-[(aminoiminomethyl)amino]-3-hydroxypentanoic acid [tautomer]
2-amino-5-guanidino-3-hydroxypentanoic acid
C(beta)-hydroxyarginine
MOD_RES (3R)-3-hydroxyarginine
beta-hydroxyarginine
A protein modification that effectively converts an L-proline residue to 2-hydroxyproline.
16.0
C 0 H 0 N 0 O 1
15.994915
C 5 H 7 N 1 O 2
113.12
113.047676
P
hypothetical
uniprot.ptm:PTM-0668
(2R)-2-hydroxypyrrolidine-2-carboxylic acid
2-hydroxyproline
2-oxidanylpyrrolidine-2-carboxylic acid
MOD_RES 2-hydroxyproline
alpha-hydroxyproline
PSI-MOD
MOD:01957
2-hydroxyproline
A protein modification that effectively converts an L-proline residue to 2-hydroxyproline.
ChEBI:141809
PubMed:23385463
RESID:AA0602
(2R)-2-hydroxypyrrolidine-2-carboxylic acid
2-hydroxyproline
2-oxidanylpyrrolidine-2-carboxylic acid
MOD_RES 2-hydroxyproline
alpha-hydroxyproline
A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to bis-L-cysteinyl bisglutathion-S-yl diiron disulfide.
786.42
C 20 Fe 2 H 30 N 6 O 12 S 4
785.9503
C 26 Fe 2 H 40 N 8 O 14 S 6
992.7
991.9687
C, C
natural
bis-L-cysteinyl bisglutathion-S-yl diiron disulfide
di-mu-sulfido-bis(cysteinato)-1kappaS,2kappaS-bis(glutathionato)-1kappaS,2kappaS-diiron
mitochondrial glutaredoxin 2 dimer iron-sulfur cluster
plant glutaredoxin C1 dimer iron-sulfur cluster
PSI-MOD
MOD:01958
Cross-link 2.
bis-L-cysteinyl bisglutathion-S-yl diiron disulfide
A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to bis-L-cysteinyl bisglutathion-S-yl diiron disulfide.
PubMed:17121859
RESID:AA0603
bis-L-cysteinyl bisglutathion-S-yl diiron disulfide
di-mu-sulfido-bis(cysteinato)-1kappaS,2kappaS-bis(glutathionato)-1kappaS,2kappaS-diiron
mitochondrial glutaredoxin 2 dimer iron-sulfur cluster
plant glutaredoxin C1 dimer iron-sulfur cluster
A protein modification that effectively converts three L-cysteine residues, an L-glutamic acid and a four-iron four-sulfur cluster to tris-L-cysteinyl L-glutamato tetrairon tetrasulfide.
347.59
C 0 Fe 4 H -4 N 0 O 0 S 4
347.59674
C 14 Fe 4 H 18 N 4 O 6 S 7
786.12
785.6669
C, C, C, E
natural
tris-L-cysteinyl L-glutamato tetrairon tetrasulfide
tris-mu3-sulfido-tris(cysteinato)-1kappaS,2kappaS,3kappaS-glutamato-4kappaO(5),4kappaO(5')-tetrairon
PSI-MOD
MOD:01959
Cross-link 4.
tris-L-cysteinyl L-glutamato tetrairon tetrasulfide
A protein modification that effectively converts three L-cysteine residues, an L-glutamic acid and a four-iron four-sulfur cluster to tris-L-cysteinyl L-glutamato tetrairon tetrasulfide.
PubMed:21167158
RESID:AA0604
tris-L-cysteinyl L-glutamato tetrairon tetrasulfide
tris-mu3-sulfido-tris(cysteinato)-1kappaS,2kappaS,3kappaS-glutamato-4kappaO(5),4kappaO(5')-tetrairon
A protein modification that effectively converts three L-cysteine residues, an L-glutamine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-glutamin-O6-yl tetrairon tetrasulfide.
347.59
C 0 Fe 4 H -4 N 0 O 0 S 4
347.59674
C 14 Fe 4 H 19 N 5 O 5 S 7
785.14
784.68286
C, C, C, Q
natural
METAL Iron-sulfur (4Fe-4S)
tris-L-cysteinyl L-glutamin-O6-yl tetrairon tetrasulfide
tris-mu3-sulfido-tris(cysteinato)-1kappaS,2kappaS,3kappaS-glutaminato-4kappaN(5)-tetrairon
PSI-MOD
MOD:01960
Cross-link 4.
tris-L-cysteinyl L-glutamin-O6-yl tetrairon tetrasulfide
A protein modification that effectively converts three L-cysteine residues, an L-glutamine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-glutamin-O6-yl tetrairon tetrasulfide.
PubMed:11796730
RESID:AA0605
METAL Iron-sulfur (4Fe-4S)
tris-L-cysteinyl L-glutamin-O6-yl tetrairon tetrasulfide
tris-mu3-sulfido-tris(cysteinato)-1kappaS,2kappaS,3kappaS-glutaminato-4kappaN(5)-tetrairon
OBSOLETE because redundant and identical to MOD:01785. Remap to MOD:01785.
MOD:01785
129.12
C 5 H 7 N 1 O 3
129.04259
C 9 H 14 N 2 O 5
230.22
230.09027
T
natural
(2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid
(2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid
5-(threon-O3-yl)glutamate
O(beta)-(gamma-glutamyl)threonine
O-(L-isoglutamyl)-L-threonine
O3-(isoglutamyl)threonine
PSI-MOD
MOD:01961
O-(L-isoglutamyl)-L-threonine (THR)
true
OBSOLETE because redundant and identical to MOD:01785. Remap to MOD:01785.
PubMed:16618936
PubMed:17051152
PubMed:17687277
PubMed:18555071
RESID:AA0536#THR
(2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid
(2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid
5-(threon-O3-yl)glutamate
O(beta)-(gamma-glutamyl)threonine
O-(L-isoglutamyl)-L-threonine
O3-(isoglutamyl)threonine
A protein modification that effectively converts an L-asparagine residue to N4-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-asparagine.
228.25
C 10 H 16 N 2 O 4
228.11101
C 14 H 22 N 4 O 6
342.35
342.15393
N
natural
uniprot.ptm:PTM-0506
(2S)-2-amino-4-[(2,4-diacetylamino-2,4,6-trideoxy-beta-D-glucopyranosyl)amino]-4-oxobutanoic acid
CARBOHYD N-linked (DATDGlc) asparagine
DABA
DATDH
DiNAcBac
N4-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-asparagine
N4-[2,4-bis(acetylamino)-2,4,6-trideoxy-beta-D-glucopyranosyl]-L-asparagine
N4-[N,N-diacetylbacillosaminyl]asparagine
N4-[N2,N4-diacetylbacillosaminyl]asparagine
PSI-MOD
MOD:01962
N4-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-asparagine
A protein modification that effectively converts an L-asparagine residue to N4-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-asparagine.
PubMed:12186869
PubMed:19236052
RESID:AA0606
(2S)-2-amino-4-[(2,4-diacetylamino-2,4,6-trideoxy-beta-D-glucopyranosyl)amino]-4-oxobutanoic acid
CARBOHYD N-linked (DATDGlc) asparagine
DABA
DATDH
DiNAcBac
N4-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-asparagine
N4-[2,4-bis(acetylamino)-2,4,6-trideoxy-beta-D-glucopyranosyl]-L-asparagine
N4-[N,N-diacetylbacillosaminyl]asparagine
N4-[N2,N4-diacetylbacillosaminyl]asparagine
A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-serine.
228.25
C 10 H 16 N 2 O 4
228.11101
C 13 H 21 N 3 O 6
315.33
315.14304
S
natural
uniprot.ptm:PTM-0548
(2S)-2-amino-4-[(2,4-diacetamido-2,4,6-trideoxy-beta-D-glucopyranosyl)oxy]propanoic acid
CARBOHYD O-linked (DATDGlc) serine
DABA
DATDH
DiNAcBac
O-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-serine
O-[2,4-bis(acetylamino)-2,4,6-trideoxy-beta-D-glucopyranosyl]-L-serine
O-[N,N-diacetylbacillosaminyl]serine
O-[N2,N4-diacetylbacillosaminyl]serine
PSI-MOD
MOD:01963
O-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-serine
A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-serine.
PubMed:23030644
RESID:AA0607
(2S)-2-amino-4-[(2,4-diacetamido-2,4,6-trideoxy-beta-D-glucopyranosyl)oxy]propanoic acid
CARBOHYD O-linked (DATDGlc) serine
DABA
DATDH
DiNAcBac
O-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-serine
O-[2,4-bis(acetylamino)-2,4,6-trideoxy-beta-D-glucopyranosyl]-L-serine
O-[N,N-diacetylbacillosaminyl]serine
O-[N2,N4-diacetylbacillosaminyl]serine
A protein modification that effectively converts an L-serine residue to O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucosyl)-L-serine.
274.27
C 11 H 18 N 2 O 6
274.1165
C 14 H 23 N 3 O 8
361.35
361.14853
S
natural
uniprot.ptm:PTM-0549
(2S)-2-amino-3-[(2-acetamido-4-glycerylamino-2,4,6-trideoxy-D-glucopyranosyl)oxy]propanoic acid
CARBOHYD O-linked (GATDGlc) serine
GATDH
O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucopyranosyl)-L-serine
O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucosyl)-L-serine
O-(N2-acetyl-N4-glycerylbacillosaminyl)-L-serine
PSI-MOD
MOD:01964
O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucosyl)-L-serine
A protein modification that effectively converts an L-serine residue to O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucosyl)-L-serine.
PubMed:17804791
RESID:AA0608
(2S)-2-amino-3-[(2-acetamido-4-glycerylamino-2,4,6-trideoxy-D-glucopyranosyl)oxy]propanoic acid
CARBOHYD O-linked (GATDGlc) serine
GATDH
O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucopyranosyl)-L-serine
O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucosyl)-L-serine
O-(N2-acetyl-N4-glycerylbacillosaminyl)-L-serine
A protein modification that effectively converts an L-lysine residue to 2xC(13),3x(2)H labeled N6-acetyl-L-lysine.
47.04
(13)C 2 (1)H -1 (2)H 3 O 1
47.036106
(12)C 6 (13)C 2 (1)H 11 (2)H 3 N 2 O 2
175.13
175.13107
K
artifact
Acetate labeling reagent (K) (heavy form, +5amu)
COFRADIC heavy acetyl 13C2 2H3
PSI-MOD
MOD:01965
2xC(13),3x(2)H labeled N6-acetyl-L-lysine
A protein modification that effectively converts an L-lysine residue to 2xC(13),3x(2)H labeled N6-acetyl-L-lysine.
PubMed:18688235
Acetate labeling reagent (K) (heavy form, +5amu)
COFRADIC heavy acetyl 13C2 2H3
OBSOLETE because redundant and identical to MOD:00720. Remap to MOD:00720.
MOD:00720
16.0
C 0 H 0 N 0 O 1 S 0
15.994915
C 5 H 9 N 1 O 2 S 1
147.19
147.0354
M
natural
(2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid
L-methionine (R)-S-oxide
L-methionine (R)-sulfoxide
MOD_RES Methionine (R)-sulfoxide
PSI-MOD
MOD:01966
L-methionine (R)-sulfoxide
true
OBSOLETE because redundant and identical to MOD:00720. Remap to MOD:00720.
ChEBI:45764
PubMed:21406390
PubMed:22116028
PubMed:23911929
RESID:AA0581
(2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid
L-methionine (R)-S-oxide
L-methionine (R)-sulfoxide
MOD_RES Methionine (R)-sulfoxide
A protein modification that effectively converts an L-arginine residue to omega-N-(N-acetylamino)glucosyl-L-arginine.
203.19
C 8 H 13 N 1 O 5
203.07938
C 14 H 25 N 5 O 6
359.38
359.18048
R
natural
uniprot.ptm:PTM-0518
(2S)-2-amino-5-[(amino[(2-N-acetylamino-2-deoxy-D-glucopyranosyl)amino]methylidene)amino]pentanoic acid
CARBOHYD N-linked (GlcNAc) arginine
N(omega)-(2-N-acetylaminoglucosyl)arginine
N(omega)-(2-acetamido-2-deoxy-D-glucopyranosyl)-L-arginine
N(omega)-(2-acetylamino-2-deoxy-D-glucopyranosyl)-L-arginine
NG-(2-N-acetylaminoglucosyl)arginine
NG-(2-acetamido-2-deoxy-D-glucopyranosyl)-L-arginine
NG-(2-acetylamino-2-deoxy-D-glucopyranosyl)-L-arginine
omega-N-(2-N-acetylaminoglucosyl)arginine
omega-N-(2-acetamido-2-deoxy-D-glucopyranosyl)-L-arginine
omega-N-(2-acetylamino-2-deoxy-D-glucopyranosyl)-L-arginine
omega-N-(N-acetylamino)glucosyl-L-arginine
PSI-MOD
MOD:01967
omega-N-(N-acetylamino)glucosyl-L-arginine
A protein modification that effectively converts an L-arginine residue to omega-N-(N-acetylamino)glucosyl-L-arginine.
PubMed:23955153
RESID:AA0609
(2S)-2-amino-5-[(amino[(2-N-acetylamino-2-deoxy-D-glucopyranosyl)amino]methylidene)amino]pentanoic acid
CARBOHYD N-linked (GlcNAc) arginine
N(omega)-(2-N-acetylaminoglucosyl)arginine
N(omega)-(2-acetamido-2-deoxy-D-glucopyranosyl)-L-arginine
N(omega)-(2-acetylamino-2-deoxy-D-glucopyranosyl)-L-arginine
NG-(2-N-acetylaminoglucosyl)arginine
NG-(2-acetamido-2-deoxy-D-glucopyranosyl)-L-arginine
NG-(2-acetylamino-2-deoxy-D-glucopyranosyl)-L-arginine
omega-N-(2-N-acetylaminoglucosyl)arginine
omega-N-(2-acetamido-2-deoxy-D-glucopyranosyl)-L-arginine
omega-N-(2-acetylamino-2-deoxy-D-glucopyranosyl)-L-arginine
omega-N-(N-acetylamino)glucosyl-L-arginine
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2R,3R,2'R)-3-methyllanthionine.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 7 H 10 N 2 O 2 S 1
186.23
186.0463
C, T
natural
(2R,3R)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanoic acid
(2R,3R,2'R)-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid
(2R,3R,2'R)-3-methyllanthionine
(2R,3R,6R)-2,6-diamino-3-methyl-4-thiaheptanedioic acid
(2R,3R,6R)-3-methyllanthionine
2-azanyl-3-[(2-azanyl-2-carboxyethyl)sulfanyl]butanoic acid
3-methyl-L,L-lanthionine
cysteine-3-L-butyrine thioether
PSI-MOD
MOD:01968
Cross-link 2.
(2R,3R,2'R)-3-methyllanthionine
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form (2R,3R,2'R)-3-methyllanthionine.
PubMed:23314913
RESID:AA0610
(2R,3R)-2-amino-3-([(2R)-2-amino-2-carboxyethyl]sulfanyl)butanoic acid
(2R,3R,2'R)-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid
(2R,3R,2'R)-3-methyllanthionine
(2R,3R,6R)-2,6-diamino-3-methyl-4-thiaheptanedioic acid
(2R,3R,6R)-3-methyllanthionine
2-azanyl-3-[(2-azanyl-2-carboxyethyl)sulfanyl]butanoic acid
3-methyl-L,L-lanthionine
cysteine-3-L-butyrine thioether
A protein modification that effectively converts an L-cysteine residue to S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine.
289.31
C 10 H 15 N 3 O 5 S 1
289.07324
C 13 H 20 N 4 O 6 S 2
392.44
392.08243
C
natural
(2S)-2-amino-5-([(2R)-1-([2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-2-oxoethyl]amino)-1-oxo-3-sulfanylpropan-2-yl]amino)-5-oxopentanoic acid
ACT_SITE S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine intermediate
S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine
S-(glutathion-1-yl)-L-cysteine
PSI-MOD
MOD:01969
S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine
A protein modification that effectively converts an L-cysteine residue to S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine.
PubMed:9398217
RESID:AA0611
(2S)-2-amino-5-([(2R)-1-([2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-2-oxoethyl]amino)-1-oxo-3-sulfanylpropan-2-yl]amino)-5-oxopentanoic acid
ACT_SITE S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine intermediate
S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine
S-(glutathion-1-yl)-L-cysteine
A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl glutamic acid, forming an isopeptide bond with a free glutamic acid.
129.12
C 5 H 7 N 1 O 3
129.04259
C 10 H 14 N 2 O 6
258.23
258.08517
E
natural
Unimod:450
uniprot.ptm:PTM-0479
(2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)pentanedioic acid
(2S)-2-[(4S)-4-amino-4-carboxybutanamido]pentanedioic acid
2-([4-azanyl-4-carboxybutanoyl]azanyl)pentanedioic acid
5-glutamyl glutamic acid
MOD_RES 5-glutamyl glutamate
N alpha -(gamma-Glutamyl)-Glu
N-(gamma-L-glutamyl)-L-glutamic acid
gamma-glutamylglutamate
isoglutamyl glutamic acid
isoglutamyl monoglutamic acid
PSI-MOD
Glu
monoglutamyl
MOD:01970
5-glutamyl glutamic acid
A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl glutamic acid, forming an isopeptide bond with a free glutamic acid.
PubMed:10747868
PubMed:15525938
PubMed:1680872
PubMed:23434852
RESID:AA0612
Unimod:450
(2S)-2-([(4S)-4-amino-4-carboxybutanoyl]amino)pentanedioic acid
(2S)-2-[(4S)-4-amino-4-carboxybutanamido]pentanedioic acid
2-([4-azanyl-4-carboxybutanoyl]azanyl)pentanedioic acid
5-glutamyl glutamic acid
MOD_RES 5-glutamyl glutamate
N alpha -(gamma-Glutamyl)-Glu
N-(gamma-L-glutamyl)-L-glutamic acid
gamma-glutamylglutamate
isoglutamyl glutamic acid
isoglutamyl monoglutamic acid
Glu
monoglutamyl
A protein modification that effectively converts an L-glutamic acid residue to N2-ornithine.
114.15
C 5 H 10 N 2 O 1
114.079315
C 10 H 17 N 3 O 4
243.26
243.1219
E
hypothetical
uniprot.ptm:PTM-0478
(2S)-5-amino-2-([(4S)-4-amino-4-carboxybutanoyl]amino)pentanoic acid
(2S)-5-amino-2-[(4S)-4-amino-4-carboxybutanamido]pentanoic acid
4-amino-5-[(4-amino-1-carboxy-butyl)amino]-5-ketovaleric acid
4-amino-5-[(4-amino-1-carboxy-butyl)amino]-5-oxopentanoic acid
5-glutamyl N2-ornithine
MOD_RES 5-glutamyl N2-ornithine
N2-(L-isoglutamyl)-L-ornithine
N2-(gamma-glutamyl)ornithine
gamma-glutamylornithine
PSI-MOD
MOD:01971
5-glutamyl N2-ornithine
A protein modification that effectively converts an L-glutamic acid residue to N2-ornithine.
ChEBI:136763
PubMed:23434852
RESID:AA0613
(2S)-5-amino-2-([(4S)-4-amino-4-carboxybutanoyl]amino)pentanoic acid
(2S)-5-amino-2-[(4S)-4-amino-4-carboxybutanamido]pentanoic acid
4-amino-5-[(4-amino-1-carboxy-butyl)amino]-5-ketovaleric acid
4-amino-5-[(4-amino-1-carboxy-butyl)amino]-5-oxopentanoic acid
5-glutamyl N2-ornithine
MOD_RES 5-glutamyl N2-ornithine
N2-(L-isoglutamyl)-L-ornithine
N2-(gamma-glutamyl)ornithine
gamma-glutamylornithine
A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl coenzyme A thioester.
749.52
C 21 H 34 N 7 O 15 P 3 S 1
749.1046
C 26 H 41 N 8 O 18 P 3 S 1
878.63
878.1472
E
natural
(2S)-2-amino-5-(2-[([3-([(2R)-2-hydroxy-3,3-dimethyl-4-([3'-phospho-adenosyl-5'-diphosphoryl]-oxy)-butanoyl]-amino)-propanoyl]-amino)-ethyl]-sulfanyl)-5-oxopentanoic acid
(2S)-2-amino-5-([2-(3-[(2R)-2-hydroxy-3,3-dimethyl-4-([3'-phospho-adenosyl-5'-diphosphoryl]-oxy)-butanamido]-propanamido)-ethyl]-sulfanyl)-5-oxopentanoic acid
5-glutamyl 4-[(3'-phospho-adenosyl-5'-diphosphoryl)oxy]pantetheine thioester
5-glutamyl coenzyme A thioester
5-glutamyl coenzyme A thioester intermediate
PSI-MOD
MOD:01972
5-glutamyl coenzyme A thioester
A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl coenzyme A thioester.
PubMed:16253988
PubMed:20977214
PubMed:7915164
RESID:AA0614
(2S)-2-amino-5-(2-[([3-([(2R)-2-hydroxy-3,3-dimethyl-4-([3'-phospho-adenosyl-5'-diphosphoryl]-oxy)-butanoyl]-amino)-propanoyl]-amino)-ethyl]-sulfanyl)-5-oxopentanoic acid
(2S)-2-amino-5-([2-(3-[(2R)-2-hydroxy-3,3-dimethyl-4-([3'-phospho-adenosyl-5'-diphosphoryl]-oxy)-butanamido]-propanamido)-ethyl]-sulfanyl)-5-oxopentanoic acid
5-glutamyl 4-[(3'-phospho-adenosyl-5'-diphosphoryl)oxy]pantetheine thioester
5-glutamyl coenzyme A thioester
5-glutamyl coenzyme A thioester intermediate
A protein modification that effectively converts an L-lysine residue to N6-(3-phosphoglyceryl)-L-lysine.
168.04
C 3 H 5 N 0 O 6 P 1
167.98238
C 9 H 17 N 2 O 7 P 1
296.22
296.07733
K
natural
(2S)-2-amino-6-([(2R)-2-hydroxy-3-(phosphonooxy)propanoyl]amino)hexanoic acid
(2S)-2-amino-6-[(2R)-2-hydroxy-3-(phosphonooxy)propanamido]hexanoic acid
3-phosphoglyceryl-lysine
N6-(3-phosphoglyceryl)-L-lysine
PSI-MOD
MOD:01973
N6-(3-phosphoglyceryl)-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-(3-phosphoglyceryl)-L-lysine.
PubMed:23908237
RESID:AA0615
(2S)-2-amino-6-([(2R)-2-hydroxy-3-(phosphonooxy)propanoyl]amino)hexanoic acid
(2S)-2-amino-6-[(2R)-2-hydroxy-3-(phosphonooxy)propanamido]hexanoic acid
3-phosphoglyceryl-lysine
N6-(3-phosphoglyceryl)-L-lysine
A protein modification that effectively converts an L-methionine residue to S-methyl-L-methionine.
15.03
C 1 H 3 N 0 O 0 S 0
15.022927
1+
C 6 H 12 N 1 O 1 S 1
146.23
146.06342
M
natural
uniprot.ptm:PTM-0636
(2S)-2-amino-4-(dimethylsulfonio)butanoate
(3S)-(3-amino-3-carboxypropyl)dimethylsulfanium
S-methyl-L-methionine
S-methylmethionine
S-methylmethioninium
[(3S)-3-amino-3-carboxypropyl](dimethyl)sulfonium
vitamin U
PSI-MOD
MOD:01974
S-methyl-L-methionine
A protein modification that effectively converts an L-methionine residue to S-methyl-L-methionine.
ChEBI:17728
PubMed:23532849
RESID:AA0616
(2S)-2-amino-4-(dimethylsulfonio)butanoate
(3S)-(3-amino-3-carboxypropyl)dimethylsulfanium
S-methyl-L-methionine
S-methylmethionine
S-methylmethioninium
[(3S)-3-amino-3-carboxypropyl](dimethyl)sulfonium
vitamin U
A protein modification that effectively converts an L-cysteine residue to S-(poly-3-hydroxybutyrate)-L-cysteine.
C
natural
uniprot.ptm:PTM-0641
(alpha)-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-(omega)-[(3R)-3-hydroxybutanoyl]-poly([(3R)-3-methyl-1-oxopropane-1,3-diyl]oxy)
MOD_RES S-poly(beta-hydroxybutyryl)lysine
S-poly(3-hydroxybutanoate)cysteine
S-poly(3-hydroxybutanoic acid)cysteine
S-poly(3-hydroxybutyrate)-L-cysteine
S-poly(3-hydroxybutyrate)cysteine
S-poly(3-hydroxybutyric acid)cysteine
S-poly(beta-hydroxybutyrate)cysteine
S-poly[(R)-3-hydroxybutyrate]cysteine
PSI-MOD
MOD:01975
S-poly(3-hydroxybutyrate)-L-cysteine
A protein modification that effectively converts an L-cysteine residue to S-(poly-3-hydroxybutyrate)-L-cysteine.
PubMed:19711985
PubMed:9888824
RESID:AA0617
(alpha)-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-(omega)-[(3R)-3-hydroxybutanoyl]-poly([(3R)-3-methyl-1-oxopropane-1,3-diyl]oxy)
MOD_RES S-poly(beta-hydroxybutyryl)lysine
S-poly(3-hydroxybutanoate)cysteine
S-poly(3-hydroxybutanoic acid)cysteine
S-poly(3-hydroxybutyrate)-L-cysteine
S-poly(3-hydroxybutyrate)cysteine
S-poly(3-hydroxybutyric acid)cysteine
S-poly(beta-hydroxybutyrate)cysteine
S-poly[(R)-3-hydroxybutyrate]cysteine
A protein modification that effectively converts an L-serine residue to O3-(poly-3-hydroxybutyrate)-L-serine.
S
natural
uniprot.ptm:PTM-0640
(2S)-2-amino-3-[([(3R)-3-hydroxybutanoyl]oxy)-poly([(3R)-3-methyl-1-oxopropane-1,3-diyl]oxy)]propanoic acid
MOD_RES O3-poly(beta-hydroxybutyryl)lysine
O3-(poly-3-hydroxybutyrate)-L-serine
O3-poly(3-hydroxybutanoate)serine
O3-poly(3-hydroxybutanoic acid)serine
O3-poly(3-hydroxybutyrate)serine
O3-poly(3-hydroxybutyric acid)serine
O3-poly(beta-hydroxybutyrate)serine
O3-poly[(R)-3-hydroxybutyrate]serine
PSI-MOD
MOD:01976
O3-(poly-3-hydroxybutyrate)-L-serine
A protein modification that effectively converts an L-serine residue to O3-(poly-3-hydroxybutyrate)-L-serine.
PubMed:17659252
PubMed:20004640
RESID:AA0618
(2S)-2-amino-3-[([(3R)-3-hydroxybutanoyl]oxy)-poly([(3R)-3-methyl-1-oxopropane-1,3-diyl]oxy)]propanoic acid
MOD_RES O3-poly(beta-hydroxybutyryl)lysine
O3-(poly-3-hydroxybutyrate)-L-serine
O3-poly(3-hydroxybutanoate)serine
O3-poly(3-hydroxybutanoic acid)serine
O3-poly(3-hydroxybutyrate)serine
O3-poly(3-hydroxybutyric acid)serine
O3-poly(beta-hydroxybutyrate)serine
O3-poly[(R)-3-hydroxybutyrate]serine
A protein modification that effectively crosslinks either an L-glutamine residue or an L-glutamic acid residue with an L-serine residue by an ester bond to form O-(L-isoglutamyl)-L-serine.
C 8 H 10 N 2 O 4
198.18
198.06406
S, X
natural
(2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid
O(beta)-(gamma-glutamyl)serine
O-(L-isoglutamyl)-L-serine
O3-(isoglutamyl)-serine
PSI-MOD
MOD:01977
Cross-link 2.
O-(L-isoglutamyl)-L-serine
A protein modification that effectively crosslinks either an L-glutamine residue or an L-glutamic acid residue with an L-serine residue by an ester bond to form O-(L-isoglutamyl)-L-serine.
PubMed:17051152
RESID:AA0597
(2S)-2-amino-5-[(2S)-2-amino-2-carboxyethoxy]-5-oxopentanoic acid
O(beta)-(gamma-glutamyl)serine
O-(L-isoglutamyl)-L-serine
O3-(isoglutamyl)-serine
A protein modification that effectively converts an L-threonine residue to O-(L-isoaspartyl)-L-threonine, using either free L-asparagine and releasing ammonia or using a peptidyl L-aspartic acid residue and releasing water.
C 8 H 12 N 2 O 5
216.19
216.07462
T, X
natural
(2S)-2-amino-4-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-4-oxobutanoic acid
(2S,3R)-2-amino-3-([(4S)-3-amino-3-carboxypropanoyl]oxy)propanoic acid
O(beta)-(beta-aspartyl)threonine
O-(L-isoaspartyl)-L-threonine
O3-(isoaspartyl)-threonine
PSI-MOD
MOD:01978
This is a threonine active intermediate and not an ester cross-link of peptides [JSG].
O-(L-isoaspartyl)-L-threonine
A protein modification that effectively converts an L-threonine residue to O-(L-isoaspartyl)-L-threonine, using either free L-asparagine and releasing ammonia or using a peptidyl L-aspartic acid residue and releasing water.
PubMed:8706862
RESID:AA0525
(2S)-2-amino-4-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-4-oxobutanoic acid
(2S,3R)-2-amino-3-([(4S)-3-amino-3-carboxypropanoyl]oxy)propanoic acid
O(beta)-(beta-aspartyl)threonine
O-(L-isoaspartyl)-L-threonine
O3-(isoaspartyl)-threonine
A protein modification that effectively converts an L-threonine residue to O-(L-isoglutamyl)-L-threonine, using free L-glutamine and releasing ammonia, or using a peptidyl L-glutamine and releasing ammonia.
C 9 H 14 N 2 O 5
230.22
230.09027
T, X
hypothetical
(2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid
(2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid
5-(threon-O3-yl)glutamate
O(beta)-(gamma-glutamyl)threonine
O-(L-isoglutamyl)-L-threonine
O3-(isoglutamyl)threonine
PSI-MOD
MOD:01979
This is not an ester cross-link of peptides [JSG].
O-(L-isoglutamyl)-L-threonine
A protein modification that effectively converts an L-threonine residue to O-(L-isoglutamyl)-L-threonine, using free L-glutamine and releasing ammonia, or using a peptidyl L-glutamine and releasing ammonia.
PubMed:8706862
RESID:AA0536
(2S)-2-amino-5-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-5-oxopentanoic acid
(2S,3R)-2-amino-3-([(4S)-4-amino-4-carboxybutanoyl]oxy)-propanoic acid
5-(threon-O3-yl)glutamate
O(beta)-(gamma-glutamyl)threonine
O-(L-isoglutamyl)-L-threonine
O3-(isoglutamyl)threonine
A protein modification that effectively converts an L-arginine residue to N4-glycosyl-arginine.
R
natural
Unimod:41
(2S)-2-amino-5-(beta-D-glucopyranosyl[imino(methylamino)methyl]amino)pentanoic acid
NG-beta-D-glucosylarginine
omega-N-(beta-D-glucosyl)-L-arginine
omega-N-glucosyl-L-arginine
omega-N-glycosyl-L-arginine
PSI-MOD
Hex
Hexose
MOD:01980
omega-N-glycosyl-L-arginine
A protein modification that effectively converts an L-arginine residue to N4-glycosyl-arginine.
PubMed:15279557
PubMed:8521968
PubMed:9536051
RESID:AA0327
Unimod:41#R
(2S)-2-amino-5-(beta-D-glucopyranosyl[imino(methylamino)methyl]amino)pentanoic acid
NG-beta-D-glucosylarginine
omega-N-(beta-D-glucosyl)-L-arginine
omega-N-glucosyl-L-arginine
omega-N-glycosyl-L-arginine
Hex
Hexose
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 3-methyllanthionine with unresolved stereospecificity.
-18.02
C 0 H -2 N 0 O -1 S 0
-18.010565
C 7 H 10 N 2 O 2 S 1
186.23
186.0463
C, T
natural
2,6-diamino-3-methyl-4-thiaheptanedioic acid
2-amino-3-([2-amino-2-carboxyethyl]sulfanyl)butanoic acid
2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid
2-azanyl-3-[(2-azanyl-2-carboxyethyl)sulfanyl]butanoic acid
3-methyllanthionine
cysteine-3-L-butyrine thioether
PSI-MOD
MOD:01981
Cross-link 2.
3-methyllanthionine
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 3-methyllanthionine with unresolved stereospecificity.
PubMed:18688235
2,6-diamino-3-methyl-4-thiaheptanedioic acid
2-amino-3-([2-amino-2-carboxyethyl]sulfanyl)butanoic acid
2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid
2-azanyl-3-[(2-azanyl-2-carboxyethyl)sulfanyl]butanoic acid
3-methyllanthionine
cysteine-3-L-butyrine thioether
modification from RESID
43.09
C 3 H 7 N 0 O 0
43.054775
1+
C 5 H 11 N 1 O 1
101.15
101.08406
G
natural
N-term
uniprot.ptm:PTM-0485
(trimethylammonio)ethanoic acid
1-carboxy-N,N,N-trimethylmethanazanium
2-trimethylammonioacetate
MOD_RES N,N,N-trimethylglycine
N,N,N-trimethylglycine cation
N,N,N-trimethylglycinium
N2Me3+Gly
betaine
carboxy-N,N,N-trimethylmethanaminium
carboxymethyl-trimethylazanium
glycine betaine
PSI-MOD
MOD:01982
N,N,N-trimethylglycine
modification from RESID
ChEBI:17750
PubMed:23818633
PubMed:23978223
RESID:AA0619
(trimethylammonio)ethanoic acid
1-carboxy-N,N,N-trimethylmethanazanium
2-trimethylammonioacetate
MOD_RES N,N,N-trimethylglycine
N,N,N-trimethylglycine cation
N,N,N-trimethylglycinium
N2Me3+Gly
betaine
carboxy-N,N,N-trimethylmethanaminium
carboxymethyl-trimethylazanium
glycine betaine
A protein modification that effectively converts a glycine residue to N,N-dimethyllglycine.
28.05
C 2 H 4 N 0 O 0
28.0313
C 4 H 8 N 1 O 1
86.11
86.06059
G
natural
N-term
uniprot.ptm:PTM-0484
(dimethylamino)ethanoic acid
1-carboxy-N,N-dimethylaminomethane
2-(dimethylamino)acetic acid
MOD_RES N,N-dimethylglycine
vitamin B16
PSI-MOD
MOD:01983
N,N-dimethylglycine
A protein modification that effectively converts a glycine residue to N,N-dimethyllglycine.
ChEBI:17724
PubMed:23818633
PubMed:23978223
RESID:AA0620
(dimethylamino)ethanoic acid
1-carboxy-N,N-dimethylaminomethane
2-(dimethylamino)acetic acid
MOD_RES N,N-dimethylglycine
vitamin B16
A protein modification that effectively cross-links an L-cysteine residue and an L-alanine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-alanine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 6 H 8 N 2 O 2 S 1
172.2
172.03065
A, C
natural
(2R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid
(2R,5R)-2,5-diamino-5-methyl-4-thiahexanedioic acid
alpha-(L-cystein-S-yl)-L-alanine
PSI-MOD
MOD:01984
Cross-link 2.
2-(L-cystein-S-yl)-L-alanine
A protein modification that effectively cross-links an L-cysteine residue and an L-alanine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-alanine.
PubMed:21526839
RESID:AA0621
(2R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid
(2R,5R)-2,5-diamino-5-methyl-4-thiahexanedioic acid
alpha-(L-cystein-S-yl)-L-alanine
A protein modification that effectively cross-links an L-cysteine residue and an L-asparagine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-asparagine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 7 H 9 N 3 O 3 S 1
215.23
215.03647
C, N
natural
(2S)-2,4-diamino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-4-oxobutanoic acid
alpha-(L-cystein-S-yl)-D-asparagine
PSI-MOD
MOD:01985
Cross-link 2.
2-(L-cystein-S-yl)-D-asparagine
A protein modification that effectively cross-links an L-cysteine residue and an L-asparagine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-asparagine.
PubMed:21786372
RESID:AA0622
(2S)-2,4-diamino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-4-oxobutanoic acid
alpha-(L-cystein-S-yl)-D-asparagine
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-serine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 6 H 8 N 2 O 3 S 1
188.2
188.02556
C, S
natural
(2R)-2-amino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-hydroxypropanoic acid
(2R,5R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiahexanoic acid
PSI-MOD
MOD:01986
Cross-link 2.
2-(L-cystein-S-yl)-L-serine
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-serine.
PubMed:21526839
RESID:AA0623
(2R)-2-amino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-hydroxypropanoic acid
(2R,5R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiahexanoic acid
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-serine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 6 H 8 N 2 O 3 S 1
188.2
188.02556
C, S
natural
(2R,5S)-2,5-diamino-5-carboxy-6-hydroxy-4-thiahexanoic acid
(2S)-2-amino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-hydroxypropanoic acid
PSI-MOD
MOD:01987
Cross-link 2.
2-(L-cystein-S-yl)-D-serine
A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-serine.
PubMed:21786372
RESID:AA0624
(2R,5S)-2,5-diamino-5-carboxy-6-hydroxy-4-thiahexanoic acid
(2S)-2-amino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-hydroxypropanoic acid
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-threonine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 7 H 10 N 2 O 3 S 1
202.23
202.04121
C, T
natural
(2R,3R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid
(2R,5R,6R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiaheptanoic acid
alpha-(L-cystein-S-yl)-L-threonine
PSI-MOD
MOD:01988
Cross-link 2.
2-(L-cystein-S-yl)-L-threonine
A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-threonine.
PubMed:21526839
RESID:AA0625
(2R,3R)-2-amino-2-[(2R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid
(2R,5R,6R)-2,5-diamino-5-carboxy-6-hydroxy-4-thiaheptanoic acid
alpha-(L-cystein-S-yl)-L-threonine
A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-tyrosine.
-2.02
C 0 H -2 N 0 O 0 S 0
-2.01565
C 12 H 12 N 2 O 3 S 1
264.3
264.05685
C, Y
natural
(2R,5S)-2,5-diamino-5-carboxyl-6-(hydroxyphenyl)-4-thiahexanoic acid
(2S)-2-amino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-(4-hydroxyphenyl)propanoic acid
alpha-(L-cystein-S-yl)-D-tyrosine
PSI-MOD
MOD:01989
Cross-link 2.
2-(L-cystein-S-yl)-D-tyrosine
A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-tyrosine.
PubMed:21526839
RESID:AA0626
(2R,5S)-2,5-diamino-5-carboxyl-6-(hydroxyphenyl)-4-thiahexanoic acid
(2S)-2-amino-2-([(2R)-2-amino-2-carboxyethyl]sulfanyl)-3-(4-hydroxyphenyl)propanoic acid
alpha-(L-cystein-S-yl)-D-tyrosine
A protein modification that effectively converts a glycine residue to a glycinium (protonated glycine).
1.01
C 0 H 1 N 0 O 0
1.007276
1+
C 2 H 5 N 1 O 1
59.07
59.036564
G
natural
N-term
PSI-MOD
MOD:01990
protonated glycine (glycinium) residue
A protein modification that effectively converts a glycine residue to a glycinium (protonated glycine).
ChEBI:64723
PubMed:18688235
A protein modification that effectively converts a glycinium (protonated glycine) residue to an N,N,N-trimethylglycine.
42.08
C 3 H 6 N 0 O 0
42.046402
1+
C 5 H 11 N 1 O 1
101.15
101.08351
MOD:01990
natural
N-term
N2Me3Gly
PSI-MOD
MOD:01991
For amino acids residues, amine trimethylation can effectively only be accomplished with an aminium, protonated primary amino, group. This process accounts only for trimethylation and not protonation. The alternative N2Me3+Gly process (MOD:01982) accounts for both protonation and trimethylation.
N,N,N-trimethylglycine (from glycinium)
A protein modification that effectively converts a glycinium (protonated glycine) residue to an N,N,N-trimethylglycine.
ChEBI:17750
PubMed:23818633
PubMed:23978223
RESID:AA0619
N2Me3Gly
A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and the alpha-carbon of another amino acid residue.
PSI-MOD
MOD:01992
alpha-carbon thioether crosslinked residues
A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and the alpha-carbon of another amino acid residue.
PubMed:18688235
A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and the beta-carbon of another amino acid residue.
PSI-MOD
MOD:01993
These are typical lanthionine-like crosslinks.
beta-carbon thioether crosslinked residues
A protein modification that crosslinks two residues by formation of a thioether bond between a cysteine thiol and the beta-carbon of another amino acid residue.
PubMed:18688235
A protein modification that effectively converts an L-tryptophan residue to N1'-formyl-L-tryptophan.
28.01
C 1 H 0 N 0 O 1
27.994915
C 12 H 10 N 2 O 2
214.22
214.07423
W
hypothetical
N1'FoTrp
PSI-MOD
MOD:01994
This modifications has not been reported as commonly encountered [JSG].
N1'-formyl-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to N1'-formyl-L-tryptophan.
PubMed:18688235
N1'FoTrp
A protein modification that effectively converts an L-tryptophan residue to N2-formyl-L-tryptophan.
28.01
C 1 H 0 N 0 O 1
27.994915
C 12 H 11 N 2 O 2
215.23
215.08205
W
hypothetical
N-term
N2FoTrp
PSI-MOD
MOD:01995
This modifications has not been reported as commonly encountered [JSG].
N2-formyl-L-tryptophan
A protein modification that effectively converts an L-tryptophan residue to N2-formyl-L-tryptophan.
PubMed:18688235
N2FoTrp
A protein modification that effectively replaces a hydrogen atom with an butanoyl group.
70.09
C 4 H 6 O 1
70.04186
X
ButRes
butyrylation
PSI-MOD
Butyryl
MOD:01996
Amino hydrogens are replaced to produce amides; hydroxyl hydrogens are replaced to produce esters; and hydrosulfanyl (thiol) hydrogens are replaced to produce sulfanyl esters (thiol esters).
butanoylated residue
A protein modification that effectively replaces a hydrogen atom with an butanoyl group.
PubMed:18688235
ButRes
butyrylation
Butyryl
A protein modification that effectively replaces a residue amino or imino hydrogen with a butanoyl group.
70.09
C 4 H 6 N 0 O 1
70.04186
X
N-butanoyl
N-butanoylation
N-butyryl
N-butyrylation
NButRes
PSI-MOD
MOD:01997
N-butanoylated residue
A protein modification that effectively replaces a residue amino or imino hydrogen with a butanoyl group.
PubMed:18688235
N-butanoyl
N-butanoylation
N-butyryl
N-butyrylation
NButRes
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a butanoyl group.
70.09
C 4 H 6 N 0 O 1
70.04186
X
artifact
N-term
N2ButRes
PSI-MOD
MOD:01998
alpha-amino butanoylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a butanoyl group.
PubMed:18688235
N2ButRes
A protein modification that effectively converts an L-lysine residue to N6-retinylidene-(11-cis)-L-lysine.
266.43
C 20 H 26 N 0 O 0
266.20346
C 26 H 38 N 2 O 1
394.6
394.2984
K
natural
(2S)-2-amino-6-[(2E,4Z,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid
PSI-MOD
MOD:01999
N6-(11-cis)-retinylidene-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-retinylidene-(11-cis)-L-lysine.
PubMed:18688235
(2S)-2-amino-6-[(2E,4Z,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid
A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine (unspecified geometric isomer).
266.43
C 20 H 26 N 0 O 0
266.20346
C 26 H 38 N 2 O 1
394.6
394.2984
K
natural
(2S)-2-amino-6-[3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid
PSI-MOD
MOD:02000
N6-retinylidene-L-lysine (unspecified geometric isomer)
A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine (unspecified geometric isomer).
PubMed:18688235
(2S)-2-amino-6-[3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid
A protein modification that effectively replaces a hydrogen atom with a stearoyl group.
266.47
C 18 H 34 O 1
266.26096
X
natural
PSI-MOD
MOD:02001
stearoylated residue
A protein modification that effectively replaces a residue sulfanyl group with a palmitoleylsulfanyl group.
236.4
C 16 H 28 N 0 O 1
236.21402
X
natural
PSI-MOD
MOD:02002
S-palmitoleylated residue
A protein modification that effectively replaces an O3-hydroxy hydrogen atom of L-serine with an acyl group.
S
natural
PSI-MOD
MOD:02003
O3-acylated L-serine
A protein modification that effectively replaces an O3-hydroxy hydrogen atom of L-threonine with an acyl group.
T
natural
PSI-MOD
MOD:02004
O3-acylated L-threonine
A protein modification that effectively replaces an sulfanyl hydrogen atom of L-cysteine with an acyl group.
C
natural
PSI-MOD
MOD:02005
S-acylated L-cysteine
A protein modification that effectively replaces a residue sulfanyl group with a stearoylsulfanyl group.
266.47
C 18 H 34 O 1
266.26096
X
natural
PSI-MOD
MOD:02006
S-stearoylated residue
A protein modification that effectively converts an L-lysine residue to N6-palmitoleyl-L-lysine.
236.4
C 16 H 28 N 0 O 1
236.21402
C 22 H 40 N 2 O 2
364.58
364.309
K
natural
PSI-MOD
MOD:02007
N6-palmitoleyl-L-lysine
A protein modification that effectively replaces a residue amino group with a palmitoleylamino group.
236.4
C 16 H 28 N 0 O 1
236.21402
X
natural
PSI-MOD
MOD:02008
N-palmitoleylated residue
A protein modification that effectively converts an L-lysine residue to N6-stearoyl-L-lysine.
266.47
C 18 H 34 O 1
266.26096
C 24 H 46 N 2 O 2
394.65
394.35593
K
natural
PSI-MOD
MOD:02009
N6-stearoyl-L-lysine
A protein modification that effectively replaces a residue amino group with a stearoylamino group.
266.47
C 18 H 34 O 1
266.26096
X
natural
PSI-MOD
MOD:02010
N-stearoylated residue
A protein modification that effectively replaces a residue amino group with a oleoylamino group.
264.45
C 18 H 32 N 0 O 1
264.24533
X
natural
PSI-MOD
MOD:02011
N-oleoylated residue
A protein modification that effectively replaces a hydrogen atom with a oleoyl group.
264.45
C 18 H 32 N 0 O 1
264.24533
X
natural
PSI-MOD
MOD:02012
oleoylated residue
A protein modification that effectively converts an L-lysine residue to N6-linoloyl-L-lysine.
262.45
C 18 H 30 N 0 O 1
262.22968
C 24 H 42 N 2 O 2
390.63
390.32462
K
natural
PSI-MOD
MOD:02013
N6-linoloyl-L-lysine
A protein modification that effectively replaces a residue amino group with a linoloylamino group.
262.45
C 18 H 30 N 0 O 1
262.22968
X
natural
PSI-MOD
MOD:02014
N-linoloylated residue
A protein modification that effectively replaces a hydrogen atom with a linoloyl group.
262.45
C 18 H 30 N 0 O 1
262.22968
X
natural
PSI-MOD
MOD:02015
linoloylated residue
A protein modification that effectively converts an L-lysine residue to N6-arachidonoyl-L-lysine.
286.49
C 20 H 30 N 0 O 1
286.22968
C 26 H 42 N 2 O 2
414.67
414.32462
K
natural
PSI-MOD
MOD:02016
N6-arachidonoyl-L-lysine
A protein modification that effectively replaces a residue amino group with an arachidonoylamino group.
286.49
C 20 H 30 N 0 O 1
286.22968
X
natural
PSI-MOD
MOD:02017
N-arachidonoylated residue
A protein modification that effectively replaces a hydrogen atom with an arachidonoyl group.
286.49
C 20 H 30 N 0 O 1
286.22968
X
natural
PSI-MOD
MOD:02018
arachidonoylated residue
A protein modification that effectively converts an L-lysine residue to N6-timnodonoyl-L-lysine.
284.48
C 20 H 28 N 0 O 1
284.21402
C 26 H 40 N 2 O 2
412.66
412.309
K
natural
PSI-MOD
MOD:02019
N6-timnodonoyl-L-lysine
A protein modification that effectively replaces a residue amino group with a timnodonoylamino group.
284.48
C 20 H 28 N 0 O 1
284.21402
X
natural
PSI-MOD
MOD:02020
N-timnodonoylated residue
A protein modification that effectively replaces a hydrogen atom with a timnodonoyl group.
284.48
C 20 H 28 N 0 O 1
284.21402
X
natural
PSI-MOD
MOD:02021
timnodonoylated residue
A protein modification that effectively converts an L-lysine residue to N6-cervonoyl-L-lysine.
310.53
C 22 H 30 N 0 O 1
310.22968
C 28 H 42 N 2 O 2
438.71
438.32462
K
natural
PSI-MOD
MOD:02022
N6-cervonoyl-L-lysine
A protein modification that effectively replaces a residue amino group with a cervonoylamino group.
310.53
C 22 H 30 N 0 O 1
310.22968
X
natural
PSI-MOD
MOD:02023
N-cervonoylated residue
A protein modification that effectively replaces a hydrogen atom with a cervonoyl group.
310.53
C 22 H 30 N 0 O 1
310.22968
X
natural
PSI-MOD
MOD:02024
cervonoylated residue
A protein modification that effectively converts the alpha amino group of a glutamine residue to glutaminyl glutamic acid by forming an isopeptide bond with the side chain carboxyl group of a free glutamic acid.
128.13
C 5 H 8 N 2 O 2
128.05858
C 10 H 15 N 3 O 5
257.24
257.10117
E
natural
PSI-MOD
MOD:02025
5-glutaminyl glutamic acid
A protein modification that effectively converts the alpha amino group of a glutamine residue to glutaminyl glutamic acid by forming an isopeptide bond with the side chain carboxyl group of a free glutamic acid.
PubMed:28801462
A protein modification that effectively cross-links an L-cysteinyl-L-glycine dipeptide and an L-cysteine residue by a disulfide bond to form S-(cysteinyl-glycyl)-L-cysteine.
176.17
C 5 H 8 N 2 O 3 S 1
176.02556
C 8 H 13 N 3 O 4 S 2
279.33
279.03476
C
natural
PSI-MOD
MOD:02026
Glutamyl-transpeptidase cleaves glutathione into cysteinylglycine (Cys-Gly) and a Glu residue. [PubMed:28537416]
S-(cysteinyl-glycyl)-L-cysteine
A protein modification that effectively cross-links an L-cysteinyl-L-glycine dipeptide and an L-cysteine residue by a disulfide bond to form S-(cysteinyl-glycyl)-L-cysteine.
PubMed:20594348
PubMed:27936627
PubMed:29627744
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a URM1 protein.
K
natural
PSI-MOD
MOD:02027
urmylated lysine
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a URM1 protein.
PubMed:10713047
PubMed:21209336
A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups.
144.1
144.10242
X
artifact
(4-methylpiperazin-1-yl)acetyl
PSI-MOD
iTRAQ
MOD:02028
The reagent consists of a reporter group, a balance group and a protein reactive N-oxysuccinimide group. The reporter group, an isotopically labeled 1,4-dimethylpiperazine, is connected to a carbonyl balance group that is isotopically labeled to produce a nominally isobaric combined modification. Four versions of chemically identical iTRAQ4plex moyeties, but with different isotope distribution. This modification is calculated as the average of the four species. It has no isotopic distribution reality, the exact mass does not correspond to any real isotopic distribution.
iTRAQ4plex reporter+balance reagent acylated residue, average mass modification
A protein modification that effectively replaces a hydrogen atom of a residue with one of the Applied Biosystems iTRAQ4plex reagent reporter+balance groups.
Unimod:214
(4-methylpiperazin-1-yl)acetyl
iTRAQ
A protein modification that effectively specifies the boundary conformation of two adjacent source amino acid residues, the second (C-term side) being a L-proline, where the carbonyl group of the amide bond of the N-side of the L-proline is positioned such that the organodiyl group is in the cis orientation (omega=0)
0.0
C 0 H 0 N 0 O 0
0.0
X, P
natural
PSI-MOD
MOD:02029
cis-peptidyl-L-proline
A protein modification that effectively specifies the boundary conformation of two adjacent source amino acid residues, the second (C-term side) being a L-proline, where the carbonyl group of the amide bond of the N-side of the L-proline is positioned such that the organodiyl group is in the cis orientation (omega=0)
ChEBI:83833
PubMed:15311922
PubMed:15735342
PubMed:24116866
PubMed:5485910
A protein modification that effectively specifies the boundary conformation of two adjacent source amino acid residues, the second (C-term side) being a L-proline, where the carbonyl group of the amide bond of the N-side of the L-proline is positioned such that the organodiyl group is in the trans orientation (omega=180)
0.0
C 0 H 0 N 0 O 0
0.0
X, P
natural
PSI-MOD
MOD:02030
trans-peptidyl-L-proline
A protein modification that effectively specifies the boundary conformation of two adjacent source amino acid residues, the second (C-term side) being a L-proline, where the carbonyl group of the amide bond of the N-side of the L-proline is positioned such that the organodiyl group is in the trans orientation (omega=180)
ChEBI:83834
PubMed:15311922
PubMed:15735342
PubMed:24116866
PubMed:5485910
modification from Unimod N-linked glycosylation, dHex Hex(4) HexNAc(5)
1810.68
C 70 H 115 N 5 O 49
1809.666
C 74 H 121 N 7 O 51
1924.78
1923.709
N
natural
GNO:G03382KH
Unimod:1519
PSI-MOD
dHex Hex(4) HexNAc(5)
MOD:02031
dHex1Hex4HexNAc5 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, dHex Hex(4) HexNAc(5)
PubMed:33135055
Unimod:1519
dHex Hex(4) HexNAc(5)
modification from Unimod N-linked glycosylation, dHex(2) Hex(4) HexNAc(5)
1956.82
C 76 H 125 N 5 O 53
1955.724
C 80 H 131 N 7 O 55
2070.92
2069.7668
N
natural
GNO:G70418MS
Unimod:1785
PSI-MOD
dHex(2) Hex(4) HexNAc(5)
MOD:02032
dHex2Hex4HexNAc5 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, dHex(2) Hex(4) HexNAc(5)
PubMed:33135055
Unimod:1785
dHex(2) Hex(4) HexNAc(5)
modification from Unimod N-linked glycosylation, dHex Hex(5) HexNAc(3)
1566.43
C 60 H 99 N 3 O 44
1565.5602
C 64 H 105 N 5 O 46
1680.53
1679.603
N
natural
GNO:G82119TF
Unimod:1484
PSI-MOD
dHex Hex(5) HexNAc(3)
MOD:02033
dHex1Hex5HexNAc3 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, dHex Hex(5) HexNAc(3)
PubMed:33135055
Unimod:1484
dHex Hex(5) HexNAc(3)
modification from Unimod N-linked glycosylation, dHex Hex(3) HexNAc(6)
1851.73
C 72 H 118 N 6 O 49
1850.6926
C 76 H 124 N 8 O 51
1965.83
1964.7356
N
natural
GNO:G50757KG
Unimod:1781
PSI-MOD
dHex Hex(3) HexNAc(6)
MOD:02034
dHex1Hex3HexNAc6 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, dHex Hex(3) HexNAc(6)
PubMed:33135055
Unimod:1781
dHex Hex(3) HexNAc(6)
modification from Unimod N-linked glycosylation, dHex Hex(6) HexNAc(3)
1728.57
C 66 H 109 N 3 O 49
1727.6129
C 70 H 115 N 5 O 51
1842.67
1841.6559
N
natural
GNO:G84820NF
Unimod:1509
PSI-MOD
dHex Hex(6) HexNAc(3)
MOD:02035
dHex1Hex6HexNAc3 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, dHex Hex(6) HexNAc(3)
PubMed:33135055
Unimod:1509
dHex Hex(6) HexNAc(3)
modification from Unimod N-linked glycosylation, Hex(9)HexNAc(2)
1865.66
C 70 H 116 N 2 O 55
1864.6342
C 74 H 122 N 4 O 57
1979.76
1978.6771
N
natural
GNO:G70101JE
Unimod:1531
PSI-MOD
M9/Man9
MOD:02036
Hex9HexNAc2 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, Hex(9)HexNAc(2)
PubMed:33135055
Unimod:1531
M9/Man9
modification from Unimod N-linked glycosylation, Hex(7) HexNAc(2)
1541.38
C 58 H 96 N 2 O 45
1540.5286
C 62 H 102 N 4 O 47
1655.48
1654.5714
N
natural
GNO:G05724UK
Unimod:1480
PSI-MOD
M7/Man7
MOD:02037
Hex7HexNAc2 N4-glycosylated asparagine
modification from Unimod N-linked glycosylation, Hex(7) HexNAc(2)
PubMed:33135055
Unimod:1480
M7/Man7
A protein modification that effectively replaces one hydrogen atom of an L-histidine residue with one methyl group.
14.03
C 1 H 2 N 0 O 0
14.01565
C 7 H 9 N 3 O 1
151.17
151.07455
H
natural
Unimod:34
uniprot.ptm:PTM-0176
MOD_RES Methylhistidine
Me1His
methylh
PSI-MOD
Methyl
MOD:02038
monomethylated L-histidine
A protein modification that effectively replaces one hydrogen atom of an L-histidine residue with one methyl group.
DeltaMass:215
OMSSA:77
Unimod:34#H
MOD_RES Methylhistidine
Me1His
methylh
Methyl
A protein modification that effectively replaces a hydrogen group with a amino group
X
AmRes
PSI-MOD
MOD:02039
aminated residue
AmRes
A protein modification that contains an L-alanine residue crosslinked to one or more amino acid residues.
A
XlnkAla
PSI-MOD
MOD:02040
crosslinked L-alanine residue
A protein modification that contains an L-alanine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkAla
A protein modification that contains an L-arginine residue crosslinked to one or more amino acid residues.
R
XlnkArg
PSI-MOD
MOD:02041
crosslinked L-arginine residue
A protein modification that contains an L-arginine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkArg
A protein modification that contains an L-asparagine residue crosslinked to one or more amino acid residues.
N
XlnkAsn
PSI-MOD
MOD:02042
crosslinked L-asparagine residue
A protein modification that contains an L-asparagine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkAsn
A protein modification that contains an L-aspartic acid residue crosslinked to one or more amino acid residues.
D
XlnkAsp
PSI-MOD
MOD:02043
crosslinked L-aspartic acid residue
A protein modification that contains an L-aspartic acid residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkAsp
A protein modification that contains an L-cysteine residue crosslinked to one or more amino acid residues.
C
XlnkCys
PSI-MOD
MOD:02044
crosslinked L-cysteine residue
A protein modification that contains an L-cysteine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkCys
A protein modification that contains an L-glutamic acid residue crosslinked to one or more amino acid residues.
E
XlnkGlu
PSI-MOD
MOD:02045
crosslinked L-glutamic acid residue
A protein modification that contains an L-glutamic acid residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkGlu
A protein modification that contains an L-glutamine residue crosslinked to one or more amino acid residues.
Q
XlnkGln
PSI-MOD
MOD:02046
crosslinked L-glutamine residue
A protein modification that contains an L-glutamine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkGln
A protein modification that contains a glycine residue crosslinked to one or more amino acid residues.
G
XlnkGly
PSI-MOD
MOD:02047
crosslinked glycine residue
A protein modification that contains a glycine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkGly
A protein modification that contains an L-histidine residue crosslinked to one or more amino acid residues.
H
XlnkHis
PSI-MOD
MOD:02048
crosslinked L-histidine residue
A protein modification that contains an L-histidine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkHis
A protein modification that contains an L-isoleucine residue crosslinked to one or more amino acid residues.
I
XlnkIle
PSI-MOD
MOD:02049
crosslinked L-isoleucine residue
A protein modification that contains an L-isoleucine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkIle
A protein modification that contains an L-leucine residue crosslinked to one or more amino acid residues.
L
XlnkLeu
PSI-MOD
MOD:02050
crosslinked L-leucine residue
A protein modification that contains an L-leucine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkLeu
A protein modification that contains an L-lysine residue crosslinked to one or more amino acid residues.
K
XlnkLys
PSI-MOD
MOD:02051
crosslinked L-lysine residue
A protein modification that contains an L-lysine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkLys
A protein modification that contains an L-methionine residue crosslinked to one or more amino acid residues.
M
XlnkMet
PSI-MOD
MOD:02052
crosslinked L-methionine residue
A protein modification that contains an L-methionine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkMet
A protein modification that contains an L-phenylalanine residue crosslinked to one or more amino acid residues.
F
XlnkPhe
PSI-MOD
MOD:02053
crosslinked L-phenylalanine residue
A protein modification that contains an L-phenylalanine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkPhe
A protein modification that contains an L-proline residue crosslinked to one or more amino acid residues.
P
XlnkPro
PSI-MOD
MOD:02054
crosslinked L-proline residue
A protein modification that contains an L-proline residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkPro
A protein modification that contains an L-serine residue crosslinked to one or more amino acid residues.
S
XlnkSer
PSI-MOD
MOD:02055
crosslinked L-serine residue
A protein modification that contains an L-serine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkSer
A protein modification that contains an L-threonine residue crosslinked to one or more amino acid residues.
T
XlnkThr
PSI-MOD
MOD:02056
crosslinked L-threonine residue
A protein modification that contains an L-threonine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkThr
A protein modification that contains an L-tryptophan residue crosslinked to one or more amino acid residues.
W
XlnkTrp
PSI-MOD
MOD:02057
crosslinked L-tryptophan residue
A protein modification that contains an L-tryptophan residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkTrp
A protein modification that contains an L-tyrosine residue crosslinked to one or more amino acid residues.
Y
XlnkTyr
PSI-MOD
MOD:02058
crosslinked L-tyrosine residue
A protein modification that contains an L-tyrosine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkTyr
A protein modification that contains an L-valine residue crosslinked to one or more amino acid residues.
V
XlnkVal
PSI-MOD
MOD:02059
crosslinked L-valine residue
A protein modification that contains an L-valine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkVal
A protein modification that contains an D-asparagine residue crosslinked to one or more amino acid residues.
MOD:00203
XlnkDAsn
PSI-MOD
MOD:02060
crosslinked D-asparagine residue
A protein modification that contains an D-asparagine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkDAsn
A protein modification that contains an L-selenocysteine residue crosslinked to one or more amino acid residues.
U
PSI-MOD
MOD:02061
crosslinked L-selenocysteine residue
A protein modification that contains an L-selenocysteine residue crosslinked to one or more amino acid residues.
PubMed:18688235
A protein modification that contains an N-formyl-L-methionine residue crosslinked to one or more amino acid residues.
MOD:00030
PSI-MOD
MOD:02062
crosslinked N-formyl-L-methionine residue
A protein modification that contains an N-formyl-L-methionine residue crosslinked to one or more amino acid residues.
PubMed:18688235
A protein modification that contains an D-phenylalanine residue crosslinked to one or more amino acid residues.
F
XlnkDPhe
PSI-MOD
MOD:02063
crosslinked D-phenylalanine residue
A protein modification that contains an D-phenylalanine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkDPhe
A protein modification that contains an D-serine residue crosslinked to one or more amino acid residues.
S
XlnkDSer
PSI-MOD
MOD:02064
crosslinked D-serine residue
A protein modification that contains an D-serine residue crosslinked to one or more amino acid residues.
PubMed:18688235
XlnkDSer
A protein modification that contains an L-alanine residue coordinated to one or more metal atoms or metal clusters.
A
PSI-MOD
MOD:02065
metal or metal cluster coordinated L-alanine residue
A protein modification that contains an L-alanine residue coordinated to one or more metal atoms or metal clusters.
PubMed:18688235
A protein modification that contains an L-aspartic acid residue coordinated to one or more metal atoms or metal clusters.
D
PSI-MOD
MOD:02066
metal or metal cluster coordinated L-aspartic acid residue
A protein modification that contains an L-aspartic acid residue coordinated to one or more metal atoms or metal clusters.
PubMed:18688235
A protein modification that contains an L-cysteine residue coordinated to one or more metal atoms or metal clusters.
C
PSI-MOD
MOD:02067
metal or metal cluster coordinated L-cysteine residue
A protein modification that contains an L-cysteine residue coordinated to one or more metal atoms or metal clusters.
PubMed:18688235
A protein modification that contains an L-glutamic acid residue coordinated to one or more metal atoms or metal clusters.
E
PSI-MOD
MOD:02068
metal or metal cluster coordinated L-glutamic acid residue
A protein modification that contains an L-glutamic acid residue coordinated to one or more metal atoms or metal clusters.
PubMed:18688235
A protein modification that contains an L-glutamine residue coordinated to one or more metal atoms or metal clusters.
Q
PSI-MOD
MOD:02069
metal or metal cluster coordinated L-glutamine residue
A protein modification that contains an L-glutamine residue coordinated to one or more metal atoms or metal clusters.
PubMed:18688235
A protein modification that contains an L-histidine residue coordinated to one or more metal atoms or metal clusters.
H
PSI-MOD
MOD:02070
metal or metal cluster coordinated L-histidine residue
A protein modification that contains an L-histidine residue coordinated to one or more metal atoms or metal clusters.
PubMed:18688235
A protein modification that contains an L-methionine residue coordinated to one or more metal atoms or metal clusters.
M
PSI-MOD
MOD:02071
metal or metal cluster coordinated L-methionine residue
A protein modification that contains an L-methionine residue coordinated to one or more metal atoms or metal clusters.
PubMed:18688235
A protein modification that contains an L-serine residue coordinated to one or more metal atoms or metal clusters.
S
PSI-MOD
MOD:02072
metal or metal cluster coordinated L-serine residue
A protein modification that contains an L-serine residue coordinated to one or more metal atoms or metal clusters.
PubMed:18688235
A protein modification that contains an L-selenocysteine residue coordinated to one or more metal atoms or metal clusters.
U
PSI-MOD
MOD:02073
metal or metal cluster coordinated L-selenocysteine residue
A protein modification that contains an L-selenocysteine residue coordinated to one or more metal atoms or metal clusters.
PubMed:18688235
A protein modification that contains an L-lysine residue coordinated to one or more metal atoms or metal clusters.
K
PSI-MOD
MOD:02074
metal or metal cluster coordinated L-lysine residue
A protein modification that contains an L-lysine residue coordinated to one or more metal atoms or metal clusters.
PubMed:18688235
A protein modification that contains an L-tyrosine residue coordinated to one or more metal atoms or metal clusters.
Y
PSI-MOD
MOD:02075
metal or metal cluster coordinated L-tyrosine residue
A protein modification that contains an L-tyrosine residue coordinated to one or more metal atoms or metal clusters.
PubMed:18688235
A protein modification that contains an L-arginine residue coordinated to one or more metal atoms or metal clusters.
R
PSI-MOD
MOD:02076
metal or metal cluster coordinated L-arginine residue
A protein modification that contains an L-arginine residue coordinated to one or more metal atoms or metal clusters.
PubMed:18688235
A protein modification that effectively replaces a hydrogen atom with an nitrosyl (NO) group.
29.0
C 0 H -1 N 1 O 1 S 0
28.990164
X
natural
Unimod:275
PSI-MOD
Nitrosyl
MOD:02077
nitrosylated residue
A protein modification that effectively replaces a hydrogen atom with an nitrosyl (NO) group.
PubMed:10442087
PubMed:11562475
PubMed:15688001
PubMed:8626764
PubMed:8637569
Unimod:275
Nitrosyl
A protein modification that effectively replaces one or more hydrogen atoms with one or more acetyl groups.
X
artifact
AcRes
PSI-MOD
Acetyl
MOD:02078
acetylated residue
A protein modification that effectively replaces one or more hydrogen atoms with one or more acetyl groups.
PubMed:11857757
PubMed:11999733
PubMed:12175151
PubMed:14730666
PubMed:15350136
AcRes
Acetyl
A protein modification that effectively replaces one hydrogen atom with one acetyl group.
84.07
C 4 H 4 N 0 O 2
84.021126
X
artifact
Ac2Res
PSI-MOD
Diacetyl
MOD:02079
Amino hydrogens are replaced to produce amides; hydroxyl hydrogens are replaced to produce esters; and hydrosulfanyl (thiol) hydrogens are replaced to produce sulfanyl esters (thiol esters). From DeltaMass: Average Mass: 42
diacetylated residue
A protein modification that effectively replaces one hydrogen atom with one acetyl group.
PubMed:11857757
PubMed:11999733
PubMed:12175151
PubMed:14730666
PubMed:15350136
Unimod:1
Ac2Res
Diacetyl
A protein modification that effectively converts an L-serine residue to either N-acetyl-L-serine, O-acetyl-L-serine, or N,O-diacetyl-L-serine.
84.07
C 4 H 4 N 0 O 2
84.021126
C 7 H 10 N 1 O 4
172.16
172.06099
S
natural
Ac2Ser
PSI-MOD
MOD:02080
diacetylated L-serine
A protein modification that effectively converts an L-serine residue to either N-acetyl-L-serine, O-acetyl-L-serine, or N,O-diacetyl-L-serine.
PubMed:18688235
Ac2Ser
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a succinyl group.
100.07
C 4 H 4 O 3
100.016045
X
natural
N-term
Unimod:64
PSI-MOD
Succinyl
MOD:02081
alpha-amino succinylated residue
A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a succinyl group.
PubMed:11857757
PubMed:12175151
Unimod:64#N-term
Succinyl
A protein modification that effectively removes two neutral hydrogen atoms (proton and electron) and a water moiety from a residue.
-20.03
C 0 H -4 N 0 O -1
-20.026215
X
2dHdH2ORes
PSI-MOD
MOD:02082
didehydrogenated and dehydrated residue
A protein modification that effectively removes two neutral hydrogen atoms (proton and electron) and a water moiety from a residue.
Unimod:401
2dHdH2ORes
A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through the 4-alpha position of FMN.
456.35
C 17 H 21 N 4 O 9 P 1
456.1046
X
natural
4aFMNRes
PSI-MOD
MOD:02083
4alpha-FMN modified residue
A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through the 4-alpha position of FMN.
PubMed:18688235
4aFMNRes
A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through the 6 position of FMN.
454.33
C 17 H 19 N 4 O 9 P 1
454.08896
X
natural
6-FMNRes
PSI-MOD
MOD:02084
6-FMN modified residue
A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through the 6 position of FMN.
PubMed:18688235
6-FMNRes
A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through the 8-alpha position of FMN.
454.33
C 17 H 19 N 4 O 9 P 1
454.08896
X
natural
8a-FMNRes
PSI-MOD
MOD:02085
8alpha-FMN modified residue
A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group through the 8-alpha position of FMN.
PubMed:18688235
8a-FMNRes
A protein modification that effectively substitutes a hydrogen atom of an L-phenylalanine residue with a bromine atom.
F
BrPhe
PSI-MOD
MOD:02086
brominated phenylalanine
A protein modification that effectively substitutes a hydrogen atom of an L-phenylalanine residue with a bromine atom.
PubMed:18688235
BrPhe
A protein modification that effectively results from forming an adduct with one or more ADP-ribose moieties or to modified residues through formation of a glycosidic bond.
X
natural
ADPRibRes
PSI-MOD
MOD:02087
adenosine diphosphoribosyl (ADP-ribosyl) modified residue
A protein modification that effectively results from forming an adduct with one or more ADP-ribose moieties or to modified residues through formation of a glycosidic bond.
DeltaMass:0
ADPRibRes
A protein modification that effectively replaces a natural, standard, encoded residue.
X
natural
PSI-MOD
MOD:02088
This represents the replacement of an encoded residue in a polypeptide, and must be combined with the formula or mass of another entry that is the replacement residue to represent a mutation or substitution.
natural, standard, encoded residue substitution
A protein modification that effectively replaces a natural, standard, encoded residue.
PubMed:18688235
A protein modification that effectively crosslinks an L-serine residue and 5'-phosphouridine through a phosphodiester bond to form O-(phospho-5'-uridine)-L-serine.
306.17
C 9 H 11 N 2 O 8 P 1
306.0253
C 12 H 16 N 3 O 9 P 1
377.24
377.0624
S
natural
Unimod:417
uniprot.ptm:PTM-0501
MOD_RES O-UMP-serine
OUMPSer
PSI-MOD
PhosphoUridine
MOD:02089
O-(phospho-5'-uridine)-L-serine
A protein modification that effectively crosslinks an L-serine residue and 5'-phosphouridine through a phosphodiester bond to form O-(phospho-5'-uridine)-L-serine.
ChEBI:156051
DeltaMass:0
PubMed:22504181
Unimod:417#S
MOD_RES O-UMP-serine
OUMPSer
PhosphoUridine
A protein modification that effectively modifies an L-threonine residue with 5'-phosphouridine through a phosphodiester bond to form O-(phospho-5'-uridine)-L-threonine.
306.17
C 9 H 11 N 2 O 8 P 1
306.0253
C 13 H 18 N 3 O 9 P 1
391.27
391.07806
T
natural
Unimod:417
uniprot.ptm:PTM-0502
MOD_RES O-UMP-threonine
OUMPThr
PSI-MOD
PhosphoUridine
MOD:02090
O-(phospho-5'-uridine)-L-threonine
A protein modification that effectively modifies an L-threonine residue with 5'-phosphouridine through a phosphodiester bond to form O-(phospho-5'-uridine)-L-threonine.
ChEBI:156052
DeltaMass:0
PubMed:22504181
Unimod:417#T
MOD_RES O-UMP-threonine
OUMPThr
PhosphoUridine
A protein modification that effectively modifies an L-serine residue with 5'-phosphoadenosine through a phosphodiester bond to form O-(phospho-5'-adenosine)-L-serine.
329.21
C 10 H 12 N 5 O 6 P 1
329.05252
C 13 H 17 N 6 O 8 P 1
416.28
416.08456
S
natural
Unimod:405
uniprot.ptm:PTM-0651
MOD_RES O-AMP-serine
PSI-MOD
Phosphoadenosine
MOD:02091
O-(phospho-5'-adenosine)-L-serine
A protein modification that effectively modifies an L-serine residue with 5'-phosphoadenosine through a phosphodiester bond to form O-(phospho-5'-adenosine)-L-serine.
PubMed:21472612
Unimod:405#S
MOD_RES O-AMP-serine
Phosphoadenosine
A protein modification that effectively converts an L-cysteine residue to form S-methylbutanedioic acid-L-cysteine by alkylation with itaconate through a thioether bond.
130.1
C 5 H 6 N 0 O 4 P 0 S 0
130.02661
C 8 H 11 N 1 O 5 P 0 S 1
233.24
233.0358
C
natural
uniprot.ptm:PTM-0676
MOD_RES S-(2,3-dicarboxypropyl)cysteine
PSI-MOD
MOD:02092
S-methylbutanedioic acid-L-cysteine
A protein modification that effectively converts an L-cysteine residue to form S-methylbutanedioic acid-L-cysteine by alkylation with itaconate through a thioether bond.
PubMed:29590092
MOD_RES S-(2,3-dicarboxypropyl)cysteine
A protein modification that effectively converts an L-lysine residue to N6-(2-hydroxyisobutanoyl)-L-lysine.
86.09
C 4 H 6 N 0 O 2
86.03678
C 10 H 18 N 2 O 3
214.27
214.13174
K
natural
Unimod:1849
uniprot.ptm:PTM-0638
MOD_RES N6-(2-hydroxyisobutyryl)lysine
PSI-MOD
MOD:02093
N6-(2-hydroxyisobutanoyl)-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-(2-hydroxyisobutanoyl)-L-lysine.
ChEBI:144968
PubMed:24681537
PubMed:29775581
Unimod:1849
MOD_RES N6-(2-hydroxyisobutyryl)lysine
A protein modification that effectively converts an L-lysine residue to N6-((3R)-3-hydroxybutanoyl)-L-lysine.
86.09
C 4 H 6 N 0 O 2
86.03678
C 10 H 18 N 2 O 3
214.27
214.13174
K
natural
uniprot.ptm:PTM-0499
MOD_RES N6-(beta-hydroxybutyryl)lysine
PSI-MOD
MOD:02094
N6-((3R)-3-hydroxybutanoyl)-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-((3R)-3-hydroxybutanoyl)-L-lysine.
ChEBI:149490
PubMed:27105115
MOD_RES N6-(beta-hydroxybutyryl)lysine
A protein modification that effectively converts an L-lysine residue to N6-glutaryl-L-lysine.
114.1
C 5 H 6 N 0 O 3
114.03169
C 11 H 18 N 2 O 4
242.28
242.12666
K
natural
uniprot.ptm:PTM-0487
MOD_RES N6-glutaryllysine
PSI-MOD
MOD:02095
N6-glutaryl-L-lysine
A protein modification that effectively converts an L-lysine residue to N6-glutaryl-L-lysine.
ChEBI:87828
PubMed:24703693
MOD_RES N6-glutaryllysine
A protein modification that effectively converts a D-asparagine residue to N4-methyl-D-asparagine.
14.03
C 1 H 2 N 0 O 0
14.01565
C 5 H 8 N 2 O 2
128.13
128.05858
N
natural
uniprot.ptm:PTM-0691
MOD_RES N4-methyl-D-asparagine
N4-methylated D-asparagine
PSI-MOD
MOD:02096
N4-methyl-D-asparagine
A protein modification that effectively converts a D-asparagine residue to N4-methyl-D-asparagine.
ChEBI:149514
PubMed:22983711
MOD_RES N4-methyl-D-asparagine
N4-methylated D-asparagine
A protein modification that modifies a D-asparagine residue.
ModDAsn
PSI-MOD
MOD:02097
modified D-asparagine residue
A protein modification that modifies a D-asparagine residue.
PubMed:18688235
ModDAsn