Term IRI	Term label	Parent term IRI	Parent term label	Alternative term	Definition
http://purl.obolibrary.org/obo/MOD_00493	formylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated residue		A protein modification that effectively replaces a hydrogen atom with a formyl group.
http://purl.obolibrary.org/obo/MOD_01204	prompt loss of methanethiol from oxidixed methionine	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		modification from Unimod Artifact -
http://purl.obolibrary.org/obo/MOD_02116	monohydroxylated phenylalanine	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively converts an L-phenylalanine residue to a monohydroxylated phenylalanine.
http://purl.obolibrary.org/obo/MOD_02100	N2-Formyl-L-asparagine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively transforms an L-histidine residue to N2-formyl asparagine
http://purl.obolibrary.org/obo/MOD_02101	2-Amino-4,5-dioxopentanoic acid	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively transforms a histidine side chain to that of 2-Amino-4,5-dioxopentanoic acid
http://purl.obolibrary.org/obo/MOD_02102	2-hydroxy-L-phenylalanine	http://purl.obolibrary.org/obo/MOD_02099	residue modified by radical hydroxylation		A protein modification that effectively converts a L-Phenylalanine residue to 2-hydroxy-L-phenylalanine.
http://purl.obolibrary.org/obo/MOD_02104	4-hydroxy-L-phenylalanine	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively substitutes a hydroxy group at position 4 of L-phenylalanine
http://purl.obolibrary.org/obo/MOD_02105	L-2,5-dihydroxyphenylalanine (Phe)	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively converts an L-tyrosine residue to L-2',5'-dihydroxyphenylalanine.
http://purl.obolibrary.org/obo/MOD_02109	oxindolylalanine	http://purl.obolibrary.org/obo/MOD_01622	monohydroxylated tryptophan		A protein modification that effectively converts an L-tryptophan residue to a oxindolylalanine.
http://purl.obolibrary.org/obo/MOD_02110	5-hydroxy-L-proline	http://purl.obolibrary.org/obo/MOD_01024	monohydroxylated proline		A protein modification that effectively converts an L-proline residue to 5-hydroxy-L-proline
http://purl.obolibrary.org/obo/MOD_02111	(2S,4S)-5-hydroxyleucine	http://purl.obolibrary.org/obo/MOD_01411	monohydroxylated leucine		A protein modification that effectively converts an L-leucine residue to a (2S,4S)-5-hydroxyleucine.
http://purl.obolibrary.org/obo/MOD_02112	4,5-Dihydroxytryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that converts an L-tryptophan residue to 4,5-Dihydroxytryptophan.
http://purl.obolibrary.org/obo/MOD_02113	5,6-Dihydroxytryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that converts an L-tryptophan residue to 5,6-Dihydroxytryptophan.
http://purl.obolibrary.org/obo/MOD_02114	5,7-Dihydroxytryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that converts an L-tryptophan residue to 5,7-Dihydroxytryptophan.
http://purl.obolibrary.org/obo/MOD_02115	Dioxindolylalanine	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that converts an L-tryptophan residue to dioxindolylalanine.
http://purl.obolibrary.org/obo/MOD_01733	TMT6plex-127 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_02108	6-hydroxy-L-tryptophan	http://purl.obolibrary.org/obo/MOD_01622	monohydroxylated tryptophan		A protein modification that effectively converts an L-tryptophan residue to a 6-hydroxy-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_02081	alpha-amino succinylated residue	http://purl.obolibrary.org/obo/MOD_01696	alpha-amino acylated residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a succinyl group.
http://purl.obolibrary.org/obo/MOD_02082	didehydrogenated and dehydrated residue	http://purl.obolibrary.org/obo/MOD_00683	dehydrogenated residue		A protein modification that effectively removes two neutral hydrogen atoms (proton and electron) and a water moiety from a residue.
http://purl.obolibrary.org/obo/MOD_02083	4alpha-FMN modified residue	http://purl.obolibrary.org/obo/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 through the 4-alpha position of FMN.
http://purl.obolibrary.org/obo/MOD_02084	6-FMN modified residue	http://purl.obolibrary.org/obo/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 through the 6 position of FMN.
http://purl.obolibrary.org/obo/MOD_02085	8alpha-FMN modified residue	http://purl.obolibrary.org/obo/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 through the 8-alpha position of FMN.
http://purl.obolibrary.org/obo/MOD_02086	brominated phenylalanine	http://purl.obolibrary.org/obo/MOD_00754	brominated residue		A protein modification that effectively substitutes a hydrogen atom of an L-phenylalanine residue with a bromine atom.
http://purl.obolibrary.org/obo/MOD_02087	adenosine diphosphoribosyl (ADP-ribosyl) modified residue	http://purl.obolibrary.org/obo/MOD_00701	nucleotide or nucleic acid 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.
http://purl.obolibrary.org/obo/MOD_02089	O-(phospho-5'-uridine)-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_02090	O-(phospho-5'-uridine)-L-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_02091	O-(phospho-5'-adenosine)-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_02092	S-methylbutanedioic acid-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_02093	N6-(2-hydroxyisobutanoyl)-L-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-(2-hydroxyisobutanoyl)-L-lysine.
http://purl.obolibrary.org/obo/MOD_02094	N6-((3R)-3-hydroxybutanoyl)-L-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-((3R)-3-hydroxybutanoyl)-L-lysine.
http://purl.obolibrary.org/obo/MOD_02095	N6-glutaryl-L-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-glutaryl-L-lysine.
http://purl.obolibrary.org/obo/MOD_02096	N4-methyl-D-asparagine	http://purl.obolibrary.org/obo/MOD_00599	monomethylated residue		A protein modification that effectively converts a D-asparagine residue to N4-methyl-D-asparagine.
http://purl.obolibrary.org/obo/MOD_02097	modified D-asparagine residue	http://purl.obolibrary.org/obo/MOD_00203	D-asparagine		A protein modification that modifies a D-asparagine residue.
http://purl.obolibrary.org/obo/MOD_00001	alkylated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively replaces a hydrogen atom with an alkyl group.
http://purl.obolibrary.org/obo/MOD_00002	O-glycosyl-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O3-glycosylserine.
http://purl.obolibrary.org/obo/MOD_00003	Unimod	http://purl.obolibrary.org/obo/MOD_00032	uncategorized protein modification		Entry from Unimod.
http://purl.obolibrary.org/obo/MOD_00005	O-glycosyl-L-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to O3-glycosylthreonine.
http://purl.obolibrary.org/obo/MOD_00007	selenium substitution for sulfur	http://purl.obolibrary.org/obo/MOD_00745	selenium containing residue		A protein modification that effectively substitutes a selenium atom for a sulfur atom.
http://purl.obolibrary.org/obo/MOD_00009	natural residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that removes a residue, or inserts or replaces a residue with a natural, standard or nonstandard, encoded residue.
http://purl.obolibrary.org/obo/MOD_00010	L-alanine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to an L-alanine.
http://purl.obolibrary.org/obo/MOD_00011	L-arginine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to an L-arginine.
http://purl.obolibrary.org/obo/MOD_00012	L-asparagine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to an L-asparagine.
http://purl.obolibrary.org/obo/MOD_00013	L-aspartic acid residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to an L-aspartic acid.
http://purl.obolibrary.org/obo/MOD_00014	L-cysteine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to an L-cysteine.
http://purl.obolibrary.org/obo/MOD_00015	L-glutamic acid residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to an L-glutamic acid.
http://purl.obolibrary.org/obo/MOD_00016	L-glutamine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to an L-glutamine.
http://purl.obolibrary.org/obo/MOD_00017	glycine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to a glycine.
http://purl.obolibrary.org/obo/MOD_00018	L-histidine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to an L-histidine.
http://purl.obolibrary.org/obo/MOD_00019	L-isoleucine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to an L-isoleucine.
http://purl.obolibrary.org/obo/MOD_00020	L-leucine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to an L-leucine.
http://purl.obolibrary.org/obo/MOD_00021	L-lysine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to L-lysine.
http://purl.obolibrary.org/obo/MOD_00022	L-methionine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to L-methionine.
http://purl.obolibrary.org/obo/MOD_00023	L-phenylalanine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to L-phenylalanine.
http://purl.obolibrary.org/obo/MOD_00024	L-proline residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to L-proline.
http://purl.obolibrary.org/obo/MOD_00025	L-serine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to L-serine.
http://purl.obolibrary.org/obo/MOD_00026	L-threonine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to L-threonine.
http://purl.obolibrary.org/obo/MOD_00027	L-tryptophan residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to L-tryptophan.
http://purl.obolibrary.org/obo/MOD_00028	L-tyrosine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to L-tyrosine.
http://purl.obolibrary.org/obo/MOD_00029	L-valine residue	http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue		A protein modification that effectively converts a source amino acid residue to an L-valine.
http://purl.obolibrary.org/obo/MOD_00032	uncategorized protein modification	http://purl.obolibrary.org/obo/MOD_00000	protein modification		A protein modification that is not chemically categorized.
http://purl.obolibrary.org/obo/MOD_00034	L-cystine (cross-link)	http://purl.obolibrary.org/obo/MOD_00689	disulfide crosslinked residues		A protein modification that effectively cross-links two L-cysteine residues to form L-cystine.
http://purl.obolibrary.org/obo/MOD_00035	(2S,3R)-3-hydroxyasparagine	http://purl.obolibrary.org/obo/MOD_01688	3-hydroxy-L-asparagine		A protein modification that effectively converts an L-asparagine residue to (2S,3R)-3-hydroxyasparagine.
http://purl.obolibrary.org/obo/MOD_00043	S-phospho-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-phospho-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00044	1'-phospho-L-histidine	http://purl.obolibrary.org/obo/MOD_00890	phosphorylated 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).
http://purl.obolibrary.org/obo/MOD_00049	2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to diphthamide.
http://purl.obolibrary.org/obo/MOD_00051	N-acetyl-L-aspartic acid	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to N-acetyl-L-aspartic acid.
http://purl.obolibrary.org/obo/MOD_00052	N-acetyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_01458	alpha-amino acetylated residue		A protein modification that effectively converts an L-cysteine residue to N-acetyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00054	N-acetyl-L-glutamine	http://purl.obolibrary.org/obo/MOD_00907	modified L-glutamine residue		A protein modification that effectively converts an L-glutamine residue to N-acetyl-L-glutamine.
http://purl.obolibrary.org/obo/MOD_00056	N-acetyl-L-isoleucine	http://purl.obolibrary.org/obo/MOD_00910	modified L-isoleucine residue		A protein modification that effectively converts an L-isoleucine residue to N-acetyl-L-isoleucine.
http://purl.obolibrary.org/obo/MOD_00057	N2-acetyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00723	N-acetylated L-lysine		A protein modification that effectively converts an L-lysine residue to N2-acetyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00059	N-acetyl-L-proline	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively converts an L-proline residue to N-acetyl-L-proline.
http://purl.obolibrary.org/obo/MOD_00061	N-acetyl-L-threonine	http://purl.obolibrary.org/obo/MOD_01458	alpha-amino acetylated residue		A protein modification that effectively converts an L-threonine residue to N-acetyl-L-threonine.
http://purl.obolibrary.org/obo/MOD_00062	N-acetyl-L-tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an L-tyrosine residue to N-acetyl-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_00063	N-acetyl-L-valine	http://purl.obolibrary.org/obo/MOD_00920	modified L-valine residue		A protein modification that effectively converts an L-valine residue to N-acetyl-L-valine.
http://purl.obolibrary.org/obo/MOD_00065	S-acetyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00646	monoacetylated L-cysteine		A protein modification that effectively converts an L-cysteine residue to S-acetyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00066	N-formylglycine	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to N-formylglycine.
http://purl.obolibrary.org/obo/MOD_00067	N-D-glucuronoylglycine	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to N-D-glucuronoylglycine.
http://purl.obolibrary.org/obo/MOD_00070	N-methyl-L-alanine	http://purl.obolibrary.org/obo/MOD_01680	alpha-amino monomethylated residue		A protein modification that effectively converts an L-alanine residue to N-methyl-L-alanine.
http://purl.obolibrary.org/obo/MOD_00071	N,N,N-trimethyl-L-alanine	http://purl.obolibrary.org/obo/MOD_01698	alpha-amino trimethylated protonated-residue		A protein modification that effectively converts an L-alanine residue to N,N,N-trimethyl-L-alanine.
http://purl.obolibrary.org/obo/MOD_00072	N-methylglycine	http://purl.obolibrary.org/obo/MOD_01680	alpha-amino monomethylated residue		A protein modification that effectively converts a glycine residue to N-methylglycine.
http://purl.obolibrary.org/obo/MOD_00073	N-methyl-L-methionine	http://purl.obolibrary.org/obo/MOD_01680	alpha-amino monomethylated residue		A protein modification that effectively converts an L-methionine residue to N-methyl-L-methionine.
http://purl.obolibrary.org/obo/MOD_00074	N-methyl-L-phenylalanine	http://purl.obolibrary.org/obo/MOD_01680	alpha-amino monomethylated residue		A protein modification that effectively converts an L-phenylalanine residue to N-methyl-L-phenylalanine.
http://purl.obolibrary.org/obo/MOD_00075	N,N-dimethyl-L-proline	http://purl.obolibrary.org/obo/MOD_01462	N-methylated proline		A protein modification that effectively converts an L-proline residue to N,N-dimethyl-L-proline.
http://purl.obolibrary.org/obo/MOD_00079	N4-methyl-L-asparagine	http://purl.obolibrary.org/obo/MOD_00599	monomethylated residue		A protein modification that effectively converts an L-asparagine residue to N4-methyl-L-asparagine.
http://purl.obolibrary.org/obo/MOD_00080	N5-methyl-L-glutamine	http://purl.obolibrary.org/obo/MOD_00722	monomethylated L-glutamine		A protein modification that effectively converts an L-glutamine residue to N5-methyl-L-glutamine.
http://purl.obolibrary.org/obo/MOD_00081	L-glutamic acid 5-methyl ester (Glu)	http://purl.obolibrary.org/obo/MOD_01453	L-glutamic acid 5-methyl ester		A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-methyl ester.
http://purl.obolibrary.org/obo/MOD_00082	3'-methyl-L-histidine	http://purl.obolibrary.org/obo/MOD_02038	monomethylated 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).
http://purl.obolibrary.org/obo/MOD_00086	N6-palmitoyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-palmitoyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00088	O-palmitoyl-L-threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine.
http://purl.obolibrary.org/obo/MOD_00089	O-palmitoyl-L-serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively converts an L-serine residue to O-palmitoyl-L-serine.
http://purl.obolibrary.org/obo/MOD_00090	L-alanine amide	http://purl.obolibrary.org/obo/MOD_00901	modified L-alanine residue		A protein modification that effectively converts an L-alanine residue to L-alanine amide.
http://purl.obolibrary.org/obo/MOD_00091	L-arginine amide	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		A protein modification that effectively converts an L-arginine residue to L-arginine amide.
http://purl.obolibrary.org/obo/MOD_00092	L-asparagine amide	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively converts an L-asparagine residue to L-asparagine amide.
http://purl.obolibrary.org/obo/MOD_00093	L-aspartic acid 1-amide	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to L-aspartic acid 1-amide.
http://purl.obolibrary.org/obo/MOD_00094	L-cysteine amide	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to L-cysteine amide.
http://purl.obolibrary.org/obo/MOD_00095	L-glutamine amide	http://purl.obolibrary.org/obo/MOD_00907	modified L-glutamine residue		A protein modification that effectively converts an L-glutamine residue to L-glutamine amide.
http://purl.obolibrary.org/obo/MOD_00096	L-glutamic acid 1-amide	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to L-glutamic acid 1-amide.
http://purl.obolibrary.org/obo/MOD_00097	glycine amide	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to glycine amide.
http://purl.obolibrary.org/obo/MOD_00098	L-histidine amide	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to L-histidine amide.
http://purl.obolibrary.org/obo/MOD_00099	L-isoleucine amide	http://purl.obolibrary.org/obo/MOD_00910	modified L-isoleucine residue		A protein modification that effectively converts an L-isoleucine residue to L-isoleucine amide.
http://purl.obolibrary.org/obo/MOD_00100	L-leucine amide	http://purl.obolibrary.org/obo/MOD_00911	modified L-leucine residue		A protein modification that effectively converts an L-leucine residue to L-leucine amide.
http://purl.obolibrary.org/obo/MOD_00101	L-lysine amide	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to L-lysine amide.
http://purl.obolibrary.org/obo/MOD_00102	L-methionine amide	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine residue to L-methionine amide.
http://purl.obolibrary.org/obo/MOD_00103	L-phenylalanine amide	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively converts an L-phenylalanine residue to L-phenylalanine amide.
http://purl.obolibrary.org/obo/MOD_00104	L-proline amide	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively converts an L-proline residue to L-proline amide.
http://purl.obolibrary.org/obo/MOD_00105	L-serine amide	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to L-serine amide.
http://purl.obolibrary.org/obo/MOD_00106	L-threonine amide	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to L-threonine amide.
http://purl.obolibrary.org/obo/MOD_00107	L-tryptophan amide	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to L-tryptophan amide.
http://purl.obolibrary.org/obo/MOD_00108	L-tyrosine amide	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide.
http://purl.obolibrary.org/obo/MOD_00109	L-valine amide	http://purl.obolibrary.org/obo/MOD_00920	modified L-valine residue		A protein modification that effectively converts an L-valine residue to L-valine amide.
http://purl.obolibrary.org/obo/MOD_00110	L-cysteine methyl disulfide	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl disulfide.
http://purl.obolibrary.org/obo/MOD_00112	S-12-hydroxyfarnesyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_01110	isoprenylated cysteine		A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00116	S-diacylglycerol-L-cysteine	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively converts an L-cysteine residue to S-diacylglycerol-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00117	S-(L-isoglutamyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_02046	crosslinked L-glutamine residue		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.
http://purl.obolibrary.org/obo/MOD_00118	2'-(S-L-cysteinyl)-L-histidine	http://purl.obolibrary.org/obo/MOD_02048	crosslinked L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00119	L-lanthionine (Cys-Ser)	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form L-lanthionine.
http://purl.obolibrary.org/obo/MOD_00120	meso-lanthionine	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		A protein modification that effectively cross-links an L-cysteine residue and an L-serine residue by a thioether bond to form meso-lanthionine.
http://purl.obolibrary.org/obo/MOD_00121	(2S,3S,2'R)-3-methyllanthionine	http://purl.obolibrary.org/obo/MOD_01981	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.
http://purl.obolibrary.org/obo/MOD_00122	3'-(S-L-cysteinyl)-L-tyrosine	http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00123	N6-carboxy-L-lysine	http://purl.obolibrary.org/obo/MOD_01152	carboxylated residue		A protein modification that effectively converts an L-lysine residue to N6-carboxy-L-lysine.
http://purl.obolibrary.org/obo/MOD_00124	N6-1-carboxyethyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to N6-1-carboxyethyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00125	hypusine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to hypusine, N6-(4-amino-2-hydroxybutyl)-L-lysine.
http://purl.obolibrary.org/obo/MOD_00129	N6-retinylidene-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine, the adduct of retinal.
http://purl.obolibrary.org/obo/MOD_00130	L-allysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to L-allysine.
http://purl.obolibrary.org/obo/MOD_00131	L-2-aminoadipic acid	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to L-2-aminoadipic acid.
http://purl.obolibrary.org/obo/MOD_00132	L-lysinoalanine (Lys-Ser)	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_00134	N6-glycyl-L-lysine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		A protein modification that effectively crosslinks an L-lysine residue and a glycine residue by an isopeptide bond to form N6-glycyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00135	N-(L-isoaspartyl)-glycine (Asn)	http://purl.obolibrary.org/obo/MOD_02042	crosslinked L-asparagine residue		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.
http://purl.obolibrary.org/obo/MOD_00136	pyruvic acid (Cys)	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to pyruvic acid.
http://purl.obolibrary.org/obo/MOD_00137	L-3-phenyllactic acid	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively converts an L-phenylalanine residue into L-3-phenyllactic acid.
http://purl.obolibrary.org/obo/MOD_00138	2-oxobutanoic acid	http://purl.obolibrary.org/obo/MOD_01160	deaminated residue		A protein modification that effectively converts an L-threonine residue into 2-oxobutanoic acid.
http://purl.obolibrary.org/obo/MOD_00139	N2-succinyl-L-tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to N2-succinyl-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_00140	S-phycocyanobilin-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycocyanobilin.
http://purl.obolibrary.org/obo/MOD_00141	S-phycoerythrobilin-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoerythrobilin.
http://purl.obolibrary.org/obo/MOD_00142	S-phytochromobilin-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phytochromobilin.
http://purl.obolibrary.org/obo/MOD_00143	heme-bis-L-cysteine	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_00144	heme-L-cysteine	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_00145	tetrakis-L-cysteinyl iron	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		A protein modification that effectively converts four L-cysteine residues iron atom to tetrakis-L-cysteinyl iron.
http://purl.obolibrary.org/obo/MOD_00146	tetrakis-L-cysteinyl diiron disulfide	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to tetrakis-L-cysteinyl diiron disulfide.
http://purl.obolibrary.org/obo/MOD_00147	hexakis-L-cysteinyl triiron trisulfide	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		A protein modification that effectively converts six L-cysteine residues and a three-iron three-sulfur cluster to hexakis-L-cysteinyl triiron trisulfide.
http://purl.obolibrary.org/obo/MOD_00148	tris-L-cysteinyl triiron tetrasulfide	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		A protein modification that effectively converts three L-cysteine residues and a three-iron four-sulfur cluster to tris-L-cysteinyl triiron tetrasulfide.
http://purl.obolibrary.org/obo/MOD_00149	tetrakis-L-cysteinyl tetrairon tetrasulfide	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		A protein modification that effectively converts four L-cysteine residues and a four-iron four-sulfur cluster to tetrakis-L-cysteinyl tetrairon tetrasulfide.
http://purl.obolibrary.org/obo/MOD_00150	L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00151	L-cysteinyl molybdopterin	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdopterin.
http://purl.obolibrary.org/obo/MOD_00152	S-(8alpha-FAD)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S'-(8alpha-FAD)-L-cystine.
http://purl.obolibrary.org/obo/MOD_00153	3'-(8alpha-FAD)-L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FAD)-L-histidine.
http://purl.obolibrary.org/obo/MOD_00154	O4'-(8alpha-FAD)-L-tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an L-tyrosine residue to O4'-(8alpha-FAD)-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_00155	L-3',4'-dihydroxyphenylalanine	http://purl.obolibrary.org/obo/MOD_00707	hydroxylated tyrosine		A protein modification that effectively converts an L-tyrosine residue to L-3',4'-dihydroxyphenylalanine.
http://purl.obolibrary.org/obo/MOD_00156	L-2',4',5'-topaquinone	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an L-tyrosine residue to an L-2',4',5'-topaquinone.
http://purl.obolibrary.org/obo/MOD_00157	L-tryptophyl quinone	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to an L-tryptophan quinone.
http://purl.obolibrary.org/obo/MOD_00158	4'-(L-tryptophan)-L-tryptophyl quinone	http://purl.obolibrary.org/obo/MOD_02057	crosslinked L-tryptophan residue		A protein modification that effectively cross-links two L-tryptophan residues by a carbon-carbon bond to form 4'-(L-tryptophan)-L-tryptophyl quinone.
http://purl.obolibrary.org/obo/MOD_00161	S-glucosyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-glucosylated L-cysteine.
http://purl.obolibrary.org/obo/MOD_00162	O5-glucosylgalactosyl-L-hydroxylysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to O5-glucosylgalactosyl-L-hydroxylysine.
http://purl.obolibrary.org/obo/MOD_00163	O-(N-acetylamino)galactosyl-L-serine	http://purl.obolibrary.org/obo/MOD_01675	O-(N-acetylamino)hexosyl-L-serine		A protein modification that effectively converts an L-serine residue to O-(N-acetylaminogalactosyl)-L-serine.
http://purl.obolibrary.org/obo/MOD_00165	1'-mannosyl-L-tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to 1'-mannosyl-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_00166	O4'-glucosyl-L-tyrosine	http://purl.obolibrary.org/obo/MOD_01927	O-glycosyl-L-tyrosine		A protein modification that effectively converts an L-tyrosine residue to O4'-glucosyl-tyrosine.
http://purl.obolibrary.org/obo/MOD_00168	N-aspartyl-glycosylphosphatidylinositolethanolamine	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to N-(aspart-1-yl)-glycosylphosphatidylinositolethanolamine.
http://purl.obolibrary.org/obo/MOD_00169	N-cysteinyl-glycosylphosphatidylinositolethanolamine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to N-cysteinyl-glycosylphosphatidylinositolethanolamine.
http://purl.obolibrary.org/obo/MOD_00170	N-glycyl-glycosylphosphatidylinositolethanolamine	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to N-glycyl-glycosylphosphatidylinositolethanolamine.
http://purl.obolibrary.org/obo/MOD_00171	N-seryl-glycosylphosphatidylinositolethanolamine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to N-seryl-glycosylphosphatidylinositolethanolamine.
http://purl.obolibrary.org/obo/MOD_00172	N-alanyl-glycosylphosphatidylinositolethanolamine	http://purl.obolibrary.org/obo/MOD_00901	modified L-alanine residue		A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylphosphatidylinositolethanolamine.
http://purl.obolibrary.org/obo/MOD_00173	N-threonyl-glycosylphosphatidylinositolethanolamine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to N-threonyl-glycosylphosphatidylinositolethanolamine.
http://purl.obolibrary.org/obo/MOD_00174	N-glycyl-glycosylsphingolipidinositolethanolamine	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to N-glycyl-glycosylsphingolipidinositolethanolamine.
http://purl.obolibrary.org/obo/MOD_00175	N-seryl-glycosylsphingolipidinositolethanolamine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to N-seryl-glycosylsphingolipidinositolethanolamine.
http://purl.obolibrary.org/obo/MOD_00176	O-(phosphoribosyl dephospho-coenzyme A)-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-(phosphoribosyl dephospho-coenzyme A)-L-serine.
http://purl.obolibrary.org/obo/MOD_00177	omega-N-(ADP-ribosyl)-L-arginine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		A protein modification that effectively converts an L-argininine residue to omega-N-(ADP-ribosyl)-L-arginine.
http://purl.obolibrary.org/obo/MOD_00178	S-(ADP-ribosyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-(ADP-ribosyl)-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00179	L-glutamyl 5-glycerylphosphorylethanolamine	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-glycerylphosphorylethanolamine.
http://purl.obolibrary.org/obo/MOD_00180	S-sulfo-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-sulfo-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00181	O4'-sulfo-L-tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an L-tyrosine residue to O4'-sulfo-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_00182	L-bromohistidine	http://purl.obolibrary.org/obo/MOD_01912	monobrominated residue		A protein modification that effectively converts an L-histidine residue to L-bromohistidine.
http://purl.obolibrary.org/obo/MOD_00183	L-2'-bromophenylalanine	http://purl.obolibrary.org/obo/MOD_00972	monobrominated L-phenylalanine		A protein modification that effectively converts an L-phenylalanine residue to L-2'-bromophenylalanine.
http://purl.obolibrary.org/obo/MOD_00184	L-3'-bromophenylalanine	http://purl.obolibrary.org/obo/MOD_00972	monobrominated L-phenylalanine		A protein modification that effectively converts an L-phenylalanine residue to L-3'-bromophenylalanine.
http://purl.obolibrary.org/obo/MOD_00185	L-4'-bromophenylalanine	http://purl.obolibrary.org/obo/MOD_00972	monobrominated L-phenylalanine		A protein modification that effectively converts an L-phenylalanine residue to L-4'-bromophenylalanine.
http://purl.obolibrary.org/obo/MOD_00186	3,3',5-triiodo-L-thyronine	http://purl.obolibrary.org/obo/MOD_00998	iodinated tyrosine		A protein modification that effectively substitutes an L-tyrosine residue with 3,3',5-triiodo-L-thyronine.
http://purl.obolibrary.org/obo/MOD_00187	L-thyroxine	http://purl.obolibrary.org/obo/MOD_00998	iodinated tyrosine		A protein modification that effectively substitutes an L-tyrosine residue with L-thyroxine.
http://purl.obolibrary.org/obo/MOD_00188	6'-bromo-L-tryptophan	http://purl.obolibrary.org/obo/MOD_01912	monobrominated residue		A protein modification that effectively converts an L-tryptophan residue to 6'-bromo-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_00189	dehydroalanine (Ser)	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to dehydroalanine.
http://purl.obolibrary.org/obo/MOD_00190	dehydrobutyrine (Thr)	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to dehydrobutyrine.
http://purl.obolibrary.org/obo/MOD_00191	(Z)-2,3-didehydrotyrosine	http://purl.obolibrary.org/obo/MOD_00706	dehydrogenated tyrosine		A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine.
http://purl.obolibrary.org/obo/MOD_00192	L-serine 5-imidazolinone glycine	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		A protein modification that effectively crosslinks an L-serine residue and a glycine residue to form L-serine 5-imidazolinone glycine.
http://purl.obolibrary.org/obo/MOD_00193	L-3-oxoalanine (Cys)	http://purl.obolibrary.org/obo/MOD_01169	L-3-oxoalanine		A protein modification that effectively converts an L-cysteine residue to L-oxoalanine.
http://purl.obolibrary.org/obo/MOD_00194	lactic acid	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to an amino-terminal lactic acid.
http://purl.obolibrary.org/obo/MOD_00195	L-alanine 5-imidazolinone glycine	http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue		A protein modification that effectively crosslinks an L-alanine residue and a glycine residue to form L-alanine 5-imidazolinone glycine.
http://purl.obolibrary.org/obo/MOD_00196	L-cysteine 5-imidazolinone glycine	http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue		A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form L-cysteine 5-imidazolinone glycine.
http://purl.obolibrary.org/obo/MOD_00197	2-imino-glutamine 5-imidazolinone glycine	http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue		A protein modification that effectively crosslinks an L-glutamine residue and a glycine residue to form 2-imino-glutamine 5-imidazolinone glycine.
http://purl.obolibrary.org/obo/MOD_00198	D-alanine (Ala)	http://purl.obolibrary.org/obo/MOD_00901	modified L-alanine residue		A protein modification that effectively converts an L-alanine residue to D-alanine.
http://purl.obolibrary.org/obo/MOD_00199	D-allo-isoleucine	http://purl.obolibrary.org/obo/MOD_00910	modified L-isoleucine residue		A protein modification that effectively converts an L-isoleucine residue to a D-allo-isoleucine.
http://purl.obolibrary.org/obo/MOD_00200	D-methionine	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine residue to D-methionine.
http://purl.obolibrary.org/obo/MOD_00201	D-phenylalanine	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively converts an L-phenylalanine residue to D-phenylalanine.
http://purl.obolibrary.org/obo/MOD_00202	D-serine (Ser)	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to D-serine.
http://purl.obolibrary.org/obo/MOD_00203	D-asparagine	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively converts an L-asparagine residue to D-asparagine.
http://purl.obolibrary.org/obo/MOD_00204	D-leucine	http://purl.obolibrary.org/obo/MOD_00911	modified L-leucine residue		A protein modification that effectively converts an L-leucine residue to D-leucine.
http://purl.obolibrary.org/obo/MOD_00205	D-tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to D-tryptophan.
http://purl.obolibrary.org/obo/MOD_00206	L-isoglutamyl-polyglycine	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to L-isoglutamyl-polyglycine.
http://purl.obolibrary.org/obo/MOD_00207	L-isoglutamyl-polyglutamic acid	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to isoglutamyl-polyglutamic acid, forming an isopeptide bond with a polyglutamic acid.
http://purl.obolibrary.org/obo/MOD_00208	O4'-(phospho-5'-adenosine)-L-tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00209	S-(2-aminovinyl)-D-cysteine (Cys-Ser)	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_00210	L-cysteine sulfenic acid	http://purl.obolibrary.org/obo/MOD_01854	sulfur monooxygenated residue		A protein modification that effectively monooxygenates an L-cysteine residue to L-cysteine sulfenic acid.
http://purl.obolibrary.org/obo/MOD_00211	S-(glycyl)-L-cysteine (Cys-Gly)	http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue		A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a thioester bond to form S-glycyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00212	S-4-hydroxycinnamyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-4-hydroxycinnamyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00214	dermatan 4-sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine	http://purl.obolibrary.org/obo/MOD_00002	O-glycosyl-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.
http://purl.obolibrary.org/obo/MOD_00216	N6-formyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-formyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00217	O4-arabinosyl-L-hydroxyproline	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively converts an L-proline residue to O4-arabinosyl-L-hydroxyproline.
http://purl.obolibrary.org/obo/MOD_00218	O-(phospho-5'-RNA)-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_00220	4-hydroxy-L-arginine	http://purl.obolibrary.org/obo/MOD_00682	hydroxylated arginine		A protein modification that effectively converts an L-arginine residue to a 4-hydroxy-L-arginine.
http://purl.obolibrary.org/obo/MOD_00221	N-(L-isoaspartyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		A protein modification that effectively crosslinks L-aspartic acid and L-cysteine residues via an isopeptide bond to form N-(L-isoaspartyl)-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00223	N6-mureinyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-mureinyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00224	1-chondroitin sulfate-L-aspartic acid ester	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to 1-chondroitin sulfate-L-aspartic acid ester
http://purl.obolibrary.org/obo/MOD_00225	S-(6-FMN)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-(6-FMN)-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00226	1'-(8alpha-FAD)-L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FAD)-L-histidine.
http://purl.obolibrary.org/obo/MOD_00227	omega-N-phospho-L-arginine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		A protein modification that effectively converts an L-arginine residue to omega-N-phospho-L-arginine.
http://purl.obolibrary.org/obo/MOD_00228	S-diphytanylglycerol diether-L-cysteine	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively converts an L-cysteine residue to S-diphytanylglycerol diether-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00229	alpha-1-microglobulin-Ig alpha complex chromophore	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		A protein modification that effectively converts two L-cysteine residues to form alpha-1-microglobulin-Ig alpha complex chromophore.
http://purl.obolibrary.org/obo/MOD_00230	bis-L-cysteinyl bis-L-histidino diiron disulfide	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00231	hexakis-L-cysteinyl hexairon hexasulfide	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		A protein modification that effectively converts six L-cysteine residues and a six-iron six-sulfur cluster to hexakis-L-cysteinyl hexairon hexasulfide.
http://purl.obolibrary.org/obo/MOD_00232	N6-(phospho-5'-adenosine)-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_00233	N6-(phospho-5'-guanosine)-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_00234	L-cysteine glutathione disulfide	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-glutathionyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00236	N4-(ADP-ribosyl)-L-asparagine	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively converts an L-asparagine residue to N4-(ADP-ribosyl)-L-asparagine.
http://purl.obolibrary.org/obo/MOD_00238	5'-(N6-L-lysine)-L-topaquinone	http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00239	S-methyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_01682	monomethylated L-cysteine		A protein modification that effectively converts an L-cysteine residue to S-methyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00240	4-hydroxy-L-lysine	http://purl.obolibrary.org/obo/MOD_01047	monohydroxylated lysine		A protein modification that effectively converts an L-lysine residue to 4-hydroxy-L-lysine.
http://purl.obolibrary.org/obo/MOD_00241	N4-hydroxymethyl-L-asparagine	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively converts an L-asparagine residue to N4-hydroxymethyl-L-asparagine.
http://purl.obolibrary.org/obo/MOD_00242	O-(ADP-ribosyl)-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-(ADP-ribosyl)-L-serine.
http://purl.obolibrary.org/obo/MOD_00243	L-cysteine oxazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_00244	L-cysteine oxazoline-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazoline-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_00245	glycine oxazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue		A protein modification that effectively crosslinks a glycine residue and an L-serine residue to form glycine oxazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_00246	glycine thiazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue		A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form glycine thiazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_00247	L-serine thiazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-serine thiazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_00248	L-phenylalanine thiazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02053	crosslinked L-phenylalanine residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_00249	L-cysteine thiazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_01420	thiazole/thiazoline ring crosslinked residues		A protein modification that effectively crosslinks two L-cysteine residues to form L-cysteine thiazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_00250	L-lysine thiazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to form L-lysine thiazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_00251	O-(phospho-5'-DNA)-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_00252	keratan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-threonine	http://purl.obolibrary.org/obo/MOD_00005	O-glycosyl-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.
http://purl.obolibrary.org/obo/MOD_00253	L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (Sec)	http://purl.obolibrary.org/obo/MOD_01158	modified L-selenocysteine residue		A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide).
http://purl.obolibrary.org/obo/MOD_00254	O4'-(phospho-5'-RNA)-L-tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00255	3-(3'-L-histidyl)-L-tyrosine	http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00256	L-methionine sulfone	http://purl.obolibrary.org/obo/MOD_01855	sulfur dioxygenated residue		A protein modification that dioxygenates an L-methionine residue to L-methionine sulfone.
http://purl.obolibrary.org/obo/MOD_00257	dipyrrolylmethanemethyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to dipyrrolylmethanemethyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00258	S-(2-aminovinyl)-3-methyl-D-cysteine	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_00259	O4'-(phospho-5'-DNA)-L-tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00260	O-(phospho-5'-DNA)-L-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_00261	O4'-(phospho-5'-uridine)-L-tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00262	N-(L-glutamyl)-L-tyrosine	http://purl.obolibrary.org/obo/MOD_02045	crosslinked L-glutamic acid residue		A protein modification that effectively forms a peptide bond between a C-terminal L-glutamic acid residue and a free L-tyrosine.
http://purl.obolibrary.org/obo/MOD_00263	S-phycoviolobilin-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoviolobilin.
http://purl.obolibrary.org/obo/MOD_00264	phycoerythrobilin-bis-L-cysteine	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycoerythrobilin.
http://purl.obolibrary.org/obo/MOD_00265	phycourobilin-bis-L-cysteine	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycourobilin.
http://purl.obolibrary.org/obo/MOD_00266	N-L-glutamyl-poly-L-glutamic acid	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		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.
http://purl.obolibrary.org/obo/MOD_00267	L-cysteine sulfinic acid	http://purl.obolibrary.org/obo/MOD_01855	sulfur dioxygenated residue		A protein modification that effectively dioxygenates an L-cysteine residue to L-cysteine sulfinic acid.
http://purl.obolibrary.org/obo/MOD_00268	L-3',4',5'-trihydroxyphenylalanine	http://purl.obolibrary.org/obo/MOD_00707	hydroxylated tyrosine		A protein modification that effectively converts an L-tyrosine residue to L-3',4',5'-trihydroxyphenylalanine.
http://purl.obolibrary.org/obo/MOD_00269	O-(sn-1-glycerophosphoryl)-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-(sn-1-glycerophosphoryl)-L-serine.
http://purl.obolibrary.org/obo/MOD_00270	1-thioglycine (internal)	http://purl.obolibrary.org/obo/MOD_01625	1-thioglycine		A protein modification that effectively converts a glycine residue to an internal 1-thioglycine.
http://purl.obolibrary.org/obo/MOD_00271	heme P460-bis-L-cysteine-L-tyrosine	http://purl.obolibrary.org/obo/MOD_02075	metal or metal cluster coordinated L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00272	O-(phospho-5'-adenosine)-L-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_00273	tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino tetrairon disulfide trioxide	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00274	L-cysteine persulfide	http://purl.obolibrary.org/obo/MOD_01886	thiolated residue		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.
http://purl.obolibrary.org/obo/MOD_00275	3'-(1'-L-histidyl)-L-tyrosine	http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00276	heme P460-bis-L-cysteine-L-lysine	http://purl.obolibrary.org/obo/MOD_02074	metal or metal cluster coordinated L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_00277	5-methyl-L-arginine	http://purl.obolibrary.org/obo/MOD_00414	monomethylated L-arginine		A protein modification that effectively converts an L-arginine residue to 5-methyl-L-arginine.
http://purl.obolibrary.org/obo/MOD_00278	2-methyl-L-glutamine	http://purl.obolibrary.org/obo/MOD_00722	monomethylated L-glutamine		A protein modification that effectively converts an L-glutamine residue to 2-methyl-L-glutamine.
http://purl.obolibrary.org/obo/MOD_00279	N-pyruvic acid 2-iminyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to N-pyruvic acid 2-iminyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00280	N-pyruvic acid 2-iminyl-L-valine	http://purl.obolibrary.org/obo/MOD_00920	modified L-valine residue		A protein modification that effectively converts an L-valine residue to N-pyruvic acid 2-iminyl-L-valine.
http://purl.obolibrary.org/obo/MOD_00281	3'-heme-L-histidine	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00282	S-selenyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-selenyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00283	N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to an N6-propylamino-poly(propylmethylamino)-propyldimethylamine-L-lysine.
http://purl.obolibrary.org/obo/MOD_00284	dihydroxyheme-L-aspartate ester-L-glutamate ester	http://purl.obolibrary.org/obo/MOD_02068	metal or metal cluster coordinated L-glutamic acid residue		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.
http://purl.obolibrary.org/obo/MOD_00285	dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium	http://purl.obolibrary.org/obo/MOD_02071	metal or metal cluster coordinated L-methionine residue		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.
http://purl.obolibrary.org/obo/MOD_00286	L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide)	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to L-cysteinyl molybdenum bis(molybdopterin guanine dinucleotide).
http://purl.obolibrary.org/obo/MOD_00287	(2S,3R,4S)-3,4-dihydroxyproline	http://purl.obolibrary.org/obo/MOD_00866	dihydroxylated proline		A protein modification that effectively converts an L-proline residue to a (2S,3R,4S)-3,4-dihydroxyproline.
http://purl.obolibrary.org/obo/MOD_00288	pyrroloquinoline quinone	http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00289	tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00290	tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00291	tris-L-cysteinyl L-aspartato tetrairon tetrasulfide	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_00292	N6-pyruvic acid 2-iminyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to N6-pyruvic acid 2-iminyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00293	tris-L-cysteinyl L-serinyl tetrairon tetrasulfide	http://purl.obolibrary.org/obo/MOD_02072	metal or metal cluster coordinated L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_00294	bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide	http://purl.obolibrary.org/obo/MOD_02072	metal or metal cluster coordinated L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_00296	O-D-glucuronosyl-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-D-glucuronosyl-L-serine.
http://purl.obolibrary.org/obo/MOD_00297	tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00298	tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide	http://purl.obolibrary.org/obo/MOD_02072	metal or metal cluster coordinated L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_00299	N6-(L-isoaspartyl)-L-lysine (Asn)	http://purl.obolibrary.org/obo/MOD_02042	crosslinked L-asparagine residue		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.
http://purl.obolibrary.org/obo/MOD_00301	O-(N-acetylglucosamine-1-phosphoryl)-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-(N-acetylglucosamine-1-phosphoryl)-L-serine.
http://purl.obolibrary.org/obo/MOD_00302	O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-(phosphoglycosyl-D-mannose-1-phosphoryl)-L-serine.
http://purl.obolibrary.org/obo/MOD_00303	heptakis-L-histidino tetracopper mu4-sulfide hydroxide	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00304	L-leucine methyl ester	http://purl.obolibrary.org/obo/MOD_00599	monomethylated residue		A protein modification that effectively converts an L-leucine residue to L-leucine methyl ester.
http://purl.obolibrary.org/obo/MOD_00305	hexakis-L-cysteinyl L-serinyl octairon heptasulfide	http://purl.obolibrary.org/obo/MOD_02072	metal or metal cluster coordinated L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_00306	residues isobaric at 113.084064 Da	http://purl.obolibrary.org/obo/MOD_00624	residues isobaric at 113.0-113.1 Da		Natural or modified residues with a mass of 113.084064 Da.
http://purl.obolibrary.org/obo/MOD_00307	L-aspartimide	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively cyclizes an L-asparagine residue to form a carboxyl-terminal L-aspartimide.
http://purl.obolibrary.org/obo/MOD_00308	L-glutamimide	http://purl.obolibrary.org/obo/MOD_00907	modified L-glutamine residue		A protein modification that effectively cyclizes an L-glutamine residue to form a carboxyl-terminal L-glutamimide.
http://purl.obolibrary.org/obo/MOD_00309	L-beta-carboxyaspartic acid	http://purl.obolibrary.org/obo/MOD_01152	carboxylated residue		A protein modification that effectively converts an L-aspartic acid residue to L-beta-carboxyaspartic acid.
http://purl.obolibrary.org/obo/MOD_00310	N5-methyl-L-arginine	http://purl.obolibrary.org/obo/MOD_00414	monomethylated L-arginine		A protein modification that effectively converts an L-arginine residue to N5-methyl-L-arginine.
http://purl.obolibrary.org/obo/MOD_00311	L-cysteine coenzyme A disulfide	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to L-cysteine coenzyme A disulfide.
http://purl.obolibrary.org/obo/MOD_00312	S-myristoyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-myristoyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00313	S-palmitoleyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_02002	S-palmitoleylated residue		A protein modification that effectively converts an L-cysteine residue to S-palmitoleyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00315	pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00316	N4,N4-dimethyl-L-asparagine	http://purl.obolibrary.org/obo/MOD_00673	methylated asparagine		A protein modification that effectively converts an L-asparagine residue to N4,N4-dimethyl-L-asparagine.
http://purl.obolibrary.org/obo/MOD_00317	N6-3,4-didehydroretinylidene-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to N6-3,4-didehydroretinylidene-L-lysine.
http://purl.obolibrary.org/obo/MOD_00318	4'-(S-L-cysteinyl)-L-tryptophyl quinone	http://purl.obolibrary.org/obo/MOD_02057	crosslinked L-tryptophan residue		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.
http://purl.obolibrary.org/obo/MOD_00319	3-(S-L-cysteinyl)-L-aspartic acid	http://purl.obolibrary.org/obo/MOD_02043	crosslinked L-aspartic acid residue		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.
http://purl.obolibrary.org/obo/MOD_00320	4-(S-L-cysteinyl)-L-glutamic acid	http://purl.obolibrary.org/obo/MOD_02045	crosslinked L-glutamic acid residue		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.
http://purl.obolibrary.org/obo/MOD_00321	cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively converts an L-aspartic acid residue to cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid L-aspartate ester.
http://purl.obolibrary.org/obo/MOD_00322	1'-methyl-L-histidine	http://purl.obolibrary.org/obo/MOD_02038	monomethylated L-histidine		A protein modification that effectively converts an L-histidine residue to tele-methyl-L-histidine.
http://purl.obolibrary.org/obo/MOD_00323	L-lysine methyl ester	http://purl.obolibrary.org/obo/MOD_01683	monomethylated L-lysine		A protein modification that effectively converts an L-lysine residue to L-lysine methyl ester.
http://purl.obolibrary.org/obo/MOD_00324	L-serinyl molybdenum bis(molybdopterin guanine dinucleotide)	http://purl.obolibrary.org/obo/MOD_02072	metal or metal cluster coordinated L-serine residue		A protein modification that effectively converts an L-serine residue to L-serinyl molybdenum bis(molybdopterin guanine dinucleotide).
http://purl.obolibrary.org/obo/MOD_00325	L-beta-methylthioasparagine	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively converts an L-asparagine residue to L-beta-methylthioasparagine.
http://purl.obolibrary.org/obo/MOD_00326	L-pyrrolysine (Lys)	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to L-pyrrolysine (not known as a natural, post-translational modification process).
http://purl.obolibrary.org/obo/MOD_00327	3-hydroxy-L-tryptophan	http://purl.obolibrary.org/obo/MOD_01622	monohydroxylated tryptophan		A protein modification that effectively converts an L-tryptophan residue to a 3-hydroxy-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_00328	O4'-(phospho-3'-DNA)-L-tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00329	hydroxyheme-L-glutamate ester	http://purl.obolibrary.org/obo/MOD_02068	metal or metal cluster coordinated L-glutamic acid residue		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.
http://purl.obolibrary.org/obo/MOD_00330	(phospho-5'-guanosine)-L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to a (phospho-5'-guanosine)-L-histidine.
http://purl.obolibrary.org/obo/MOD_00331	tetrakis-L-cysteinyl triiron tetrasulfide	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		A protein modification that effectively converts four L-cysteine residues and a three-iron four-sulfur cluster to tetrakis-L-cysteinyl triiron tetrasulfide.
http://purl.obolibrary.org/obo/MOD_00332	omega-N-glucosyl-L-arginine	http://purl.obolibrary.org/obo/MOD_01980	omega-N-glycosyl-L-arginine		A protein modification that effectively converts an L-arginine residue to N4-glucosyl-arginine.
http://purl.obolibrary.org/obo/MOD_00333	(3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively converts an L-asparagine residue to (3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine.
http://purl.obolibrary.org/obo/MOD_00334	1'-heme-L-histidine	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00335	(2S,3S,2'R)-3-methyllanthionine sulfoxide	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_00336	tris-L-cysteinyl L-aspartato diiron disulfide	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_00337	S-carbamoyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-carbamoyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00338	S-cyano-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-cyano-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00339	L-cysteinyl hydrogenase diiron subcluster	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to L-cysteinyl hydrogenase diiron subcluster.
http://purl.obolibrary.org/obo/MOD_00340	S-amidino-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-amidino-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00341	N-methyl-L-isoleucine	http://purl.obolibrary.org/obo/MOD_01680	alpha-amino monomethylated residue		A protein modification that effectively converts an L-isoleucine residue to N-methyl-L-isoleucine.
http://purl.obolibrary.org/obo/MOD_00342	N-methyl-L-leucine	http://purl.obolibrary.org/obo/MOD_01808	N-methylated leucine		A protein modification that effectively converts an L-leucine residue to N-methyl-L-leucine.
http://purl.obolibrary.org/obo/MOD_00343	N-methyl-L-tyrosine	http://purl.obolibrary.org/obo/MOD_01680	alpha-amino monomethylated residue		A protein modification that effectively converts an L-tyrosine residue to N-methyl-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_00344	N-palmitoylglycine	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to N-palmitoylglycine.
http://purl.obolibrary.org/obo/MOD_00345	2-(S-L-cysteinyl)-L-phenylalanine	http://purl.obolibrary.org/obo/MOD_02053	crosslinked L-phenylalanine residue		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.
http://purl.obolibrary.org/obo/MOD_00346	2-(S-L-cysteinyl)-D-phenylalanine	http://purl.obolibrary.org/obo/MOD_02053	crosslinked L-phenylalanine residue		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.
http://purl.obolibrary.org/obo/MOD_00347	2-(S-L-cysteinyl)-D-allo-threonine	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_00348	N-carbamoyl-L-alanine	http://purl.obolibrary.org/obo/MOD_00901	modified L-alanine residue		A protein modification that effectively converts an L-alanine residue to N-carbamoyl-L-alanine.
http://purl.obolibrary.org/obo/MOD_00349	4-amino-3-isothiazolidinone-L-serine	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form 4-amino-3-isothiazolidinone-L-serine.
http://purl.obolibrary.org/obo/MOD_00350	L-threonyl-pentaglycyl-murein peptidoglycan	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively attaches an L-threonine residue to murein peptidoglycan by a pentaglycine linker peptide.
http://purl.obolibrary.org/obo/MOD_00351	N-glycyl-1-(phosphatidyl)ethanolamine	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively converts a glycine residue to N-glycyl-1-(phosphatidyl)ethanolamine.
http://purl.obolibrary.org/obo/MOD_00352	L-glutamyl 5-omega-hydroxyceramide ester	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl 5-omega-hydroxyceramide ester.
http://purl.obolibrary.org/obo/MOD_00353	S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium	http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00354	O-(riboflavin phosphoryl)-L-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to O-(riboflavin phosphoryl)-L-threonine.
http://purl.obolibrary.org/obo/MOD_00355	O-(riboflavin phosphoryl)-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-(riboflavin phosphoryl)-L-serine.
http://purl.obolibrary.org/obo/MOD_00356	S-(4alpha-FMN)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-(4a-FMN)-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00357	1'-(8alpha-FMN)-L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FMN)-L-histidine.
http://purl.obolibrary.org/obo/MOD_00358	3'-(8alpha-FMN)-L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FMN)-L-histidine.
http://purl.obolibrary.org/obo/MOD_00359	N2-acetyl-L-arginine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		A protein modification that effectively converts an L-arginine residue to N2-acetyl-L-arginine.
http://purl.obolibrary.org/obo/MOD_00360	L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide.
http://purl.obolibrary.org/obo/MOD_00361	tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_00362	tris-L-cysteinyl L-arginyl diiron disulfide	http://purl.obolibrary.org/obo/MOD_02076	metal or metal cluster coordinated L-arginine residue		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.
http://purl.obolibrary.org/obo/MOD_00363	L-cysteinyl-L-selenocysteine (Cys-Sec)	http://purl.obolibrary.org/obo/MOD_02061	crosslinked L-selenocysteine residue		A protein modification that effectively cross-links an L-cysteine residue and an L-selenocysteine residues to form L-cysteinyl-L-selenocystine.
http://purl.obolibrary.org/obo/MOD_00364	5-hydroxy-N6,N6,N6-trimethyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to 5-hydroxy-N6,N6,N6-trimethyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00365	N-(L-isoglutamyl)-glycine	http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue		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.
http://purl.obolibrary.org/obo/MOD_00366	O-sulfo-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-sulfo-L-serine.
http://purl.obolibrary.org/obo/MOD_00367	O-sulfo-L-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to O-sulfo-L-threonine.
http://purl.obolibrary.org/obo/MOD_00368	N-carboxy-L-methionine	http://purl.obolibrary.org/obo/MOD_01152	carboxylated residue		A protein modification that effectively converts an L-methionine residue to N-carboxy-L-methionine.
http://purl.obolibrary.org/obo/MOD_00369	O-acetyl-L-serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively converts an L-serine residue to O-acetyl-L-serine.
http://purl.obolibrary.org/obo/MOD_00370	(E)-2,3-didehydrotyrosine	http://purl.obolibrary.org/obo/MOD_00706	dehydrogenated tyrosine		A protein modification that effectively converts an L-tyrosine residue to (E)-2,3-didehydrotyrosine.
http://purl.obolibrary.org/obo/MOD_00371	bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00372	3'-(3'-L-tyrosinyl)-L-tyrosine	http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue		A protein modification that effectively cross-links two L-tyrosine residues with a carbon-carbon bond to form 3'-(3'-L-tyrosinyl)-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_00373	3'-(O4'-L-tyrosinyl)-L-tyrosine	http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue		A protein modification that effectively cross-links L-tyrosine residues with an ether bond to form 3'-(O4'-L-tyrosinyl)-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_00374	3,4-dihydroxy-L-arginine	http://purl.obolibrary.org/obo/MOD_00682	hydroxylated arginine		A protein modification that effectively converts an L-arginine residue to 3,4-dihydroxy-L-arginine.
http://purl.obolibrary.org/obo/MOD_00375	4,5-dihydroxy-L-lysine	http://purl.obolibrary.org/obo/MOD_00681	hydroxylated lysine		A protein modification that effectively converts an L-lysine residue to 4,5-dihydroxy-L-lysine.
http://purl.obolibrary.org/obo/MOD_00376	1'-(phospho-5'-adenosine)-L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00377	1'-(phospho-5'-uridine)-L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00378	L-aspartyl semialdehyde	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl semialdehyde.
http://purl.obolibrary.org/obo/MOD_00379	L-serine microcin E492 siderophore ester	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to L-serine microcin E492 siderophore ester.
http://purl.obolibrary.org/obo/MOD_00380	L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide)	http://purl.obolibrary.org/obo/MOD_02066	metal or metal cluster coordinated L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to L-aspartyl molybdenum bis(molybdopterin guanine dinucleotide).
http://purl.obolibrary.org/obo/MOD_00381	L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (Sec)	http://purl.obolibrary.org/obo/MOD_02073	metal or metal cluster coordinated L-selenocysteine residue		A protein modification that effectively converts an L-selenocysteine residue to L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide).
http://purl.obolibrary.org/obo/MOD_00382	3-(2-methylthio)ethyl-6-(4-hydroxybenzylidene)-5-iminopiperazin-2-one	http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00383	2-imino-glutamic acid 5-imidazolinone glycine	http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue		A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue to form 2-imino-glutamic acid 5-imidazolinone glycine.
http://purl.obolibrary.org/obo/MOD_00384	2-imino-methionine 5-imidazolinone glycine	http://purl.obolibrary.org/obo/MOD_02052	crosslinked L-methionine residue		A protein modification that effectively crosslinks an L-methionine residue and a glycine residue to form 2-imino-methionine 5-imidazolinone glycine.
http://purl.obolibrary.org/obo/MOD_00385	L-asparagine 5-imidazolinone glycine	http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue		A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue to form L-asparagine 5-imidazolinone glycine.
http://purl.obolibrary.org/obo/MOD_00386	L-lysine 5-imidazolinone glycine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form L-lysine 5-imidazolinone glycine.
http://purl.obolibrary.org/obo/MOD_00387	2-tetrahydropyridinyl-5-imidazolinone glycine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form 2-tetrahydropyridinyl-5-imidazolinone glycine.
http://purl.obolibrary.org/obo/MOD_00388	L-alanyl-pentaglycyl-murein peptidoglycan	http://purl.obolibrary.org/obo/MOD_00901	modified L-alanine residue		A protein modification that effectively attaches an L-alanine residue to murein peptidoglycan by a pentaglycine linker peptide.
http://purl.obolibrary.org/obo/MOD_00389	N-formyl-L-proline	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively converts an L-proline residue to N-formyl-L-proline.
http://purl.obolibrary.org/obo/MOD_00390	O-decanoyl-L-serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively converts an L-serine residue to O-decanoyl-L-serine.
http://purl.obolibrary.org/obo/MOD_00391	O-octanoyl-L-threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively converts an L-threonine residue to O-octanoyl-L-threonine.
http://purl.obolibrary.org/obo/MOD_00392	O-decanoyl-L-threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively converts an L-threonine residue to O-decanoyl-L-threonine.
http://purl.obolibrary.org/obo/MOD_00393	O-methylated residue	http://purl.obolibrary.org/obo/MOD_00427	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.
http://purl.obolibrary.org/obo/MOD_00395	thioester crosslinked residues	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_00397	iodoacetamide derivatized residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that is produced by reaction with iodoacetamide, usually replacement of a reactive hydrogen with a methylcarboxamido group.
http://purl.obolibrary.org/obo/MOD_00398	carbamoylated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively replaces a hydrogen atom with a carbamoyl (carboxamido) group. Replacement of an amino hydrogen produces a ureido group.
http://purl.obolibrary.org/obo/MOD_00399	iodoacetic acid derivatized residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that is produced by reaction with iodoacetic acid, usually replacement of a reactive hydrogen with a methylcarboxy group.
http://purl.obolibrary.org/obo/MOD_00400	deamidated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		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.
http://purl.obolibrary.org/obo/MOD_00402	Gygi ICAT(TM) d8 modified cysteine	http://purl.obolibrary.org/obo/MOD_01820	isotope tagged sufhydryl reagent 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.
http://purl.obolibrary.org/obo/MOD_00403	homoserine	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine residue to homoserine.
http://purl.obolibrary.org/obo/MOD_00404	homoserine lactone	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine residue to homoserine lactone.
http://purl.obolibrary.org/obo/MOD_00405	Applied Biosystems original ICAT(TM) d8 modified cysteine	http://purl.obolibrary.org/obo/MOD_01820	isotope tagged sufhydryl reagent 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.
http://purl.obolibrary.org/obo/MOD_00406	Applied Biosystems original ICAT(TM) d0 modified cysteine	http://purl.obolibrary.org/obo/MOD_01820	isotope tagged sufhydryl reagent 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.
http://purl.obolibrary.org/obo/MOD_00408	mono N-acetylated residue	http://purl.obolibrary.org/obo/MOD_00670	N-acylated residue		A protein modification that effectively replaces a residue amino or imino hydrogen with an acetyl group.
http://purl.obolibrary.org/obo/MOD_00409	N-formylated residue	http://purl.obolibrary.org/obo/MOD_00670	N-acylated residue		A protein modification that effectively replaces a residue amino group with a formamido group.
http://purl.obolibrary.org/obo/MOD_00410	S-(N-isopropylcarboxamidomethyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-(N-isopropylcarboxamidomethyl)-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00413	biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine derivatized cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that is produced by reaction of a cysteine residue with biotinyl-iodoacetamidyl-3,6-dioxaoctanediamine.
http://purl.obolibrary.org/obo/MOD_00416	phosphorylation of an hydroxyl amino acid with prompt loss of phosphate	http://purl.obolibrary.org/obo/MOD_00704	dehydrated residue		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.
http://purl.obolibrary.org/obo/MOD_00417	S-carboxamidoethyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-carboxamidoethyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00418	pyridylacetylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated residue		A protein modification that effectively replaces a hydrogen atom with an (pyridin-3-yl)acetyl group.
http://purl.obolibrary.org/obo/MOD_00419	(R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to (R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_00420	2-pyrrolidone-5-carboxylic acid (Glu)	http://purl.obolibrary.org/obo/MOD_01048	2-pyrrolidone-5-carboxylic acid		A protein modification that effectively converts an L-glutamic acid residue to 2-pyrrolidone-5-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_00421	C-glycosylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated residue		A protein modification that effectively replaces a residue hydrogen atom on a carbon with a carbohydrate-like group through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_00422	alpha-amino morpholine-2-acetylated residue	http://purl.obolibrary.org/obo/MOD_01813	morpholine-2-acetylated residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a morpholine-2-acetyl group.
http://purl.obolibrary.org/obo/MOD_00423	monosodium salt	http://purl.obolibrary.org/obo/MOD_00747	sodium containing modified residue		A protein modification that effectively substitutes one sodium atom for one hydrogen atom.
http://purl.obolibrary.org/obo/MOD_00424	S-pyridylethyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-pyridylethyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00425	monohydroxylated residue	http://purl.obolibrary.org/obo/MOD_00677	hydroxylated residue		A protein modification that effectively replaces one hydrogen atom with a hydroxyl group.
http://purl.obolibrary.org/obo/MOD_00426	S-glycosylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated residue		A protein modification that effectively replaces a residue hydrogen atom on a sulfur with a carbohydrate-like group through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_00428	dihydroxylated residue	http://purl.obolibrary.org/obo/MOD_00677	hydroxylated residue		A protein modification that effectively replaces two hydrogen atoms with two hydroxyl groups.
http://purl.obolibrary.org/obo/MOD_00429	dimethylated residue	http://purl.obolibrary.org/obo/MOD_00427	methylated residue		A protein modification that effectively replaces two hydrogen atoms with two methyl groups.
http://purl.obolibrary.org/obo/MOD_00430	trimethylated residue	http://purl.obolibrary.org/obo/MOD_00427	methylated residue		A protein modification that effectively replaces three hydrogen atoms with three methyl groups.
http://purl.obolibrary.org/obo/MOD_00431	modified residue with a secondary neutral loss	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		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.
http://purl.obolibrary.org/obo/MOD_00432	modified residue with neutral loss of phosphate	http://purl.obolibrary.org/obo/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 trihydrogen phosphate molecular fragment.
http://purl.obolibrary.org/obo/MOD_00433	monoglucosylated residue	http://purl.obolibrary.org/obo/MOD_00761	monohexosylated residue		A protein modification that effectively replaces a hydrogen atom with an glucose group through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_00434	hexosylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated 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.
http://purl.obolibrary.org/obo/MOD_00435	O-phospho-L-serine with neutral loss of phosphate	http://purl.obolibrary.org/obo/MOD_01151	phosphorylated residue 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.
http://purl.obolibrary.org/obo/MOD_00436	N-acetylhexosaminylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated 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.
http://purl.obolibrary.org/obo/MOD_00439	O-phospho-L-threonine with neutral loss of phosphate	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		Covalent modification of a peptide or protein amino acid phosphorylated threonine with a secondary loss of a neutral trihydrogen phosphate molecular fragment.
http://purl.obolibrary.org/obo/MOD_00441	geranylgeranylated residue	http://purl.obolibrary.org/obo/MOD_00703	isoprenylated residue		A protein modification that effectively replaces a hydrogen atom with a geranylgeranyl group.
http://purl.obolibrary.org/obo/MOD_00442	protonated omega-N,omega-N'-dimethylated L-arginine with secondary neutral loss of N,N'-carbodiimide	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		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.
http://purl.obolibrary.org/obo/MOD_00443	protonated omega-N,omega-N-dimethlyated L-arginine with secondary neutral loss of N,N-dimethylamine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		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.
http://purl.obolibrary.org/obo/MOD_00444	N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine	http://purl.obolibrary.org/obo/MOD_00899	N-palmitoyl-S-diacylglycerol-L-cysteine		A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine.
http://purl.obolibrary.org/obo/MOD_00445	L-homoarginine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to L-homoarginine, such as reaction with O-methylisourea.
http://purl.obolibrary.org/obo/MOD_00446	4-hydroxynonenal adduct	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal.
http://purl.obolibrary.org/obo/MOD_00447	N-glucuronylated residue	http://purl.obolibrary.org/obo/MOD_00764	glycoconjugated 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.
http://purl.obolibrary.org/obo/MOD_00449	acetate labeling reagent (N-term) (heavy form, +3amu)	http://purl.obolibrary.org/obo/MOD_01431	(2)H deuterium tagged reagent		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00451	alpha-amino propanoylated residue	http://purl.obolibrary.org/obo/MOD_01894	propanoylated residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a propanoyl group.
http://purl.obolibrary.org/obo/MOD_00452	alpha-amino 3x(13)C-labeled propanoylated residue	http://purl.obolibrary.org/obo/MOD_01428	(13)C isotope tagged reagent		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(13)C-labeled propanoyl group.
http://purl.obolibrary.org/obo/MOD_00453	quaternary amine labeling reagent light form (N-term & K)	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent light form group.
http://purl.obolibrary.org/obo/MOD_00454	quaternary amine labeling reagent heavy form (+3amu) (N-term & K)	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+3amu) form group.
http://purl.obolibrary.org/obo/MOD_00455	quaternary amine labeling reagent heavy form (+6amu) (N-term & K)	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+6amu) form group.
http://purl.obolibrary.org/obo/MOD_00456	quaternary amine labeling reagent heavy form (+9amu) (N-term & K)	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a quaternary amine reagent heavy (+9amu) form group.
http://purl.obolibrary.org/obo/MOD_00457	4x(12)C, 4x(1)H labeled alpha-amino succinylated residue	http://purl.obolibrary.org/obo/MOD_01696	alpha-amino acylated residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a light succinyl group.
http://purl.obolibrary.org/obo/MOD_00458	4x(2)H labeled alpha-amino succinylated residue	http://purl.obolibrary.org/obo/MOD_01696	alpha-amino acylated residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(2)H labeled succinyl group.
http://purl.obolibrary.org/obo/MOD_00459	4x(13)C labeled alpha-amino succinylated residue	http://purl.obolibrary.org/obo/MOD_01696	alpha-amino acylated residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 4x(13)C labeled succinyl group.
http://purl.obolibrary.org/obo/MOD_00460	L-cysteic acid (L-cysteine sulfonic acid)	http://purl.obolibrary.org/obo/MOD_00708	sulfur oxygenated L-cysteine		A protein modification that effectively trioxygenates an L-cysteine residue to L-cysteine sulfonic acid.
http://purl.obolibrary.org/obo/MOD_00461	nitrated residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a nitrite (NO2) group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_00462	L-kynurenine	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to L-kynurenine.
http://purl.obolibrary.org/obo/MOD_00463	3'-hydroxy-L-kynurenine	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to 3'-hydroxy-L-kynurenine.
http://purl.obolibrary.org/obo/MOD_00464	N'-formyl-L-kynurenine	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to N'-formyl-L-kynurenine.
http://purl.obolibrary.org/obo/MOD_00465	dihydroxyphenylalanine (Phe)	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively converts an L-phenylalanine residue to a dihydroxyphenylalanine.
http://purl.obolibrary.org/obo/MOD_00466	glycosylsphingolipidinositolated residue	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively converts a residue to a glycosylsphingolipidinositolethanolamidated.
http://purl.obolibrary.org/obo/MOD_00467	iminobiotinyl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes an iminobiotinyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_00468	ESP-Tag light d0	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00469	ESP-Tag heavy d10	http://purl.obolibrary.org/obo/MOD_01431	(2)H deuterium tagged reagent		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00470	NHS-LC-Biotin	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00471	EDT-maleimide-PEO-biotin	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00472	IMID d0	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00473	IMID d4	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00474	S-([1,1,2-(2)H3]-carboxamidoethyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		A protein modification that effectively converts an L-cysteine residue to S-(1,1,2-(2)H3)-propanamide-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00475	2-amino-L-tyrosine	http://purl.obolibrary.org/obo/MOD_02039	aminated residue		A protein modification that effectively converts an L-tyrosine residue to 2-amino-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_00476	monogalactosylated residue	http://purl.obolibrary.org/obo/MOD_00761	monohexosylated residue		A protein modification that effectively replaces a hydrogen atom with an galactose group through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_00477	2-pyrrolidone	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively converts, by oxidative decarboxylation, an L-proline residue to 2-pyrrolidone with breakage of the peptide chain.
http://purl.obolibrary.org/obo/MOD_00478	glutamyl semialdehyde (Pro)	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively converts an L-proline residue to L-glutamyl semialdehyde.
http://purl.obolibrary.org/obo/MOD_00479	glutamyl semialdehyde (Arg)	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		A protein modification that effectively converts an L-arginine residue to L-glutamyl semialdehyde.
http://purl.obolibrary.org/obo/MOD_00480	Applied Biosystems cleavable ICAT(TM) light	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00481	Applied Biosystems cleavable ICAT(TM) heavy	http://purl.obolibrary.org/obo/MOD_01428	(13)C isotope tagged reagent		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00482	N-formyl-L-methionine (Met)	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine residue to N-formyl-L-methionine (not known as a natural, post-translational modification process).
http://purl.obolibrary.org/obo/MOD_00483	N-ethylmaleimide derivatized cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that is produced by reaction with N-ethylmaleimide.
http://purl.obolibrary.org/obo/MOD_00484	oxidized lysine biotinylated with biotin-LC-hydrazide, reduced	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00485	oxidized lysine biotinylated with biotin-LC-hydrazide	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00486	oxidized proline biotinylated with biotin-LC-hydrazide, reduced	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00487	oxidized proline biotinylated with biotin-LC-hydrazide	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00488	oxidized arginine biotinylated with biotin-LC-hydrazide	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00489	oxidized arginine biotinylated with biotin-LC-hydrazide, reduced	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00490	EDT-iodo-PEO-biotin	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00491	thio ether formation - BTP Adduct	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00492	ubiquitination signature dipeptidyl lysine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_00494	N-iodoacetyl, p-chlorobenzyl-12C6-glucamine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00495	N-iodoacetyl, p-chlorobenzyl-13C6-glucamine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00497	3-sulfanylpropanoyl (N-term and Lys)	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod [(35)S]dithiobis(succinimidyl propionate) crosslinking
http://purl.obolibrary.org/obo/MOD_00498	fluorinated residue	http://purl.obolibrary.org/obo/MOD_00694	halogen containing residue		A protein modification that effectively substitutes a hydrogen of a residue with a fluorine atom.
http://purl.obolibrary.org/obo/MOD_00499	5-iodoacetamidofluorescein	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00500	monoiodinated residue	http://purl.obolibrary.org/obo/MOD_00755	iodinated residue		A protein modification that effectively substitutes one hydrogen atom of a residue with one iodine atom.
http://purl.obolibrary.org/obo/MOD_00501	diiodinated residue	http://purl.obolibrary.org/obo/MOD_00755	iodinated residue		A protein modification that effectively substitutes two hydrogen atoms of a residue with two iodine atoms.
http://purl.obolibrary.org/obo/MOD_00502	triiodinated residue	http://purl.obolibrary.org/obo/MOD_00755	iodinated residue		A protein modification that effectively substitutes three hydrogen atoms of a residue with three iodine atoms.
http://purl.obolibrary.org/obo/MOD_00503	N-(cis-delta 5)-tetradecaenoylglycine	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to N-(cis-delta 5)-tetradecaenoylglycine.
http://purl.obolibrary.org/obo/MOD_00504	N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to N-(cis,cis-delta 5,delta 8)-tetradecadienoylglycine.
http://purl.obolibrary.org/obo/MOD_00505	benzoyl labeling reagent light form (N-term and K)	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00506	N-linked glycan core N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation, Hex(5) HexNAc(2)
http://purl.obolibrary.org/obo/MOD_00509	amidination of lysines or N-terminal amines with methyl acetimidate	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00510	HexNAc1dHex1 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation, dHex HexNAc
http://purl.obolibrary.org/obo/MOD_00511	HexNAc2 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation, HexNAc(2)
http://purl.obolibrary.org/obo/MOD_00512	Hex3 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation, Hex3
http://purl.obolibrary.org/obo/MOD_00513	HexNAc1dHex2 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation, dHex(2) HexNAc
http://purl.obolibrary.org/obo/MOD_00514	Hex1HexNAc1dHex1 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation, dHex Hex HexNAc
http://purl.obolibrary.org/obo/MOD_00515	HexNAc2dHex1 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation, dHex HexNAc(2)
http://purl.obolibrary.org/obo/MOD_00516	Hex1HexNAc2 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00517	Hex1HexNAc1NeuAc1 glycosylated residue	http://purl.obolibrary.org/obo/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 composed of Hex1HexNAc1NeuAc1 linked through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_00518	HexNAc2dHex2 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00519	Hex1HexNAc2Pent1 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00520	Hex1HexNAc2dHex1 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00521	Hex2HexNAc2 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00522	Hex3HexNAc1Pent1 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00523	Hex1HexNAc2dHex1Pent1 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00524	Hex1HexNAc2dHex2 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00525	Hex2HexNAc2Pent1 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00526	Hex2HexNAc2dHex1 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00527	Hex3HexNAc2 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00528	Hex1HexNAc1NeuAc2 glycosylated residue	http://purl.obolibrary.org/obo/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 composed of Hex1HexNAc1NeuAc2 linked through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_00529	Hex3HexNAc2P1 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00530	L-selenomethionine	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine residue to L-selenomethionine.
http://purl.obolibrary.org/obo/MOD_00531	(18)O labeled deglycosylated asparagine	http://purl.obolibrary.org/obo/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 as the result of having been deglycosylated in (18)O water.
http://purl.obolibrary.org/obo/MOD_00532	Shimadzu 13CNBS	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00533	Shimadzu 12CNBS	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00534	Michael addition of BHT quinone methide to cysteine and lysine	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Post-translational
http://purl.obolibrary.org/obo/MOD_00535	phosphorylation to amine thiol	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00537	L-alanine residue (Thr)	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to L-alanine.
http://purl.obolibrary.org/obo/MOD_00538	protein modification categorized by isobaric sets	http://purl.obolibrary.org/obo/MOD_00000	protein modification		Modified amino acid residues groups into isobaric sets at particular mass resolution cut-offs.
http://purl.obolibrary.org/obo/MOD_00540	9x(13)C labeled residue	http://purl.obolibrary.org/obo/MOD_00842	(13)C labeled residue		A protein modification that effectively converts a residue containing common isotopes to a 9x(13)C labeled residue.
http://purl.obolibrary.org/obo/MOD_00541	9x(13)C labeled L-phosphotyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-phosphotyrosine.
http://purl.obolibrary.org/obo/MOD_00542	hydroxyphenylglyoxal arginine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00543	bis(hydroxyphenylglyoxal) arginine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00544	6x(13)C labeled residue	http://purl.obolibrary.org/obo/MOD_00842	(13)C labeled residue		A protein modification that effectively converts a residue containing common isotopes to a 6x(13)C labeled residue.
http://purl.obolibrary.org/obo/MOD_00546	(18)O label at both C-terminal oxygens	http://purl.obolibrary.org/obo/MOD_00847	(18)O disubstituted residue		A protein modification that effectively substitutes two (18)O atom for the two (16)O atoms of an alpha-carboxyl (1-carboxyl) group.
http://purl.obolibrary.org/obo/MOD_00547	6-aminoquinolyl-N-hydroxysuccinimidyl carbamate	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative used for amino acid analysis
http://purl.obolibrary.org/obo/MOD_00548	APTA	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00549	APTA d3	http://purl.obolibrary.org/obo/MOD_01431	(2)H deuterium tagged reagent		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00550	EAPTA d0	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00551	EAPTA d5	http://purl.obolibrary.org/obo/MOD_01431	(2)H deuterium tagged reagent		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00552	4x(2)H labeled dimethylated residue	http://purl.obolibrary.org/obo/MOD_00839	(2)H deuterium labeled residue		A protein modification that effectively converts a residue containing common isotopes to a 4x(2)H labeled dimethylated residue.
http://purl.obolibrary.org/obo/MOD_00553	1,2-ethanedithiol modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a (2-sulfanylethyl)sulfanyl (or thioethylthiol) group for a hydroxy group.
http://purl.obolibrary.org/obo/MOD_00561	N-ethyl iodoacetamide-	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00562	N-ethyl iodoacetamide-d5	http://purl.obolibrary.org/obo/MOD_01431	(2)H deuterium tagged reagent		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00563	mono-N-acetylaminogalactosylated residue	http://purl.obolibrary.org/obo/MOD_01673	N-acetylaminohexosylated residue		A protein modification that effectively replaces a hydrogen atom with an N-acetylaminogalactose group through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_00565	deglycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00566	label cysteine with IGBP reagent	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00569	residues isobaric at a resolution below 0.000001 Da	http://purl.obolibrary.org/obo/MOD_00770	residues isobaric at a resolution below 0.01 Da		Natural or modified residues that are isobaric at a resolution below 0.000001 Da.
http://purl.obolibrary.org/obo/MOD_00570	residues isobaric at 71.037114 Da	http://purl.obolibrary.org/obo/MOD_00769	residues isobaric at 71.0-71.1 Da		Natural or modified residues with a mass of 71.037114 Da.
http://purl.obolibrary.org/obo/MOD_00571	2-pyrrolidone-5-carboxylic acid (Pro)	http://purl.obolibrary.org/obo/MOD_01048	2-pyrrolidone-5-carboxylic acid		A modification that effectively oxygenates C5 of an L-proline residue to form a 2-pyrrolidone-5-carboxylic acid, pyroglutamic acid.
http://purl.obolibrary.org/obo/MOD_00572	oxidized arginine biotinylated with biotin hydrazide	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00573	oxidized lysine biotinylated with biotin hydrazide	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00574	oxidized proline biotinylated with biotin hydrazide	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00575	oxidized threonine biotinylated with biotin hydrazide	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00576	crotonylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated residue		modification from Unimod Other
http://purl.obolibrary.org/obo/MOD_00577	acetaldehyde crosslinked penta-L-lysine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		modification occurs as a Schiff base in the presence of pentalysine
http://purl.obolibrary.org/obo/MOD_00581	(18)O monosubstituted residue	http://purl.obolibrary.org/obo/MOD_00845	(18)O substituted residue		A protein modification that effectively substitutes one (18)O atom for one (16)O atom.
http://purl.obolibrary.org/obo/MOD_00582	6x(13)C,2x(15)N labeled L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to 6x(13)C,2x(15)N labeled L-lysine.
http://purl.obolibrary.org/obo/MOD_00583	thiophosphorylated residue	http://purl.obolibrary.org/obo/MOD_00861	phosphorus containing modified residue		A protein modification that effectively replaces a hydrogen atom with a thiophosphono group (H2PO2S, 'thiophosphate').
http://purl.obolibrary.org/obo/MOD_00584	4-sulfophenyl isothiocyanate derivatized residue	http://purl.obolibrary.org/obo/MOD_00841	isothiocyanate reagent derivatized residue		A protein modification produced by formation of an adduct with 4-sulfophenyl isothiocyanate.
http://purl.obolibrary.org/obo/MOD_00585	deuterium trisubstituted residue	http://purl.obolibrary.org/obo/MOD_00786	deuterium substituted residue		A protein modification that effectively substitutes three (2)H deuterium atoms for three (1)H protium atoms.
http://purl.obolibrary.org/obo/MOD_00586	pyridyl thiol modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00587	6x(13)C,4x(15)N labeled L-arginine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		A protein modification that effectively converts an L-arginine residue to 6x(13)C, 4x(15)N labeled L-arginine.
http://purl.obolibrary.org/obo/MOD_00588	5x(13)C,1x(15)N labeled L-valine	http://purl.obolibrary.org/obo/MOD_00920	modified L-valine residue		A protein modification that effectively converts an L-valine residue to 5x(13)C,1x(15)N labeled L-valine.
http://purl.obolibrary.org/obo/MOD_00589	9x(13)C,1x(15)N labeled L-phenylalanine	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively converts an L-phenylalanine residue to (13)C,(15)N labeled L-phenylalanine.
http://purl.obolibrary.org/obo/MOD_00592	sulfonation of N-terminal	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00594	residues isobaric at 113.047678 Da	http://purl.obolibrary.org/obo/MOD_00624	residues isobaric at 113.0-113.1 Da		Natural or modified resiues with a mass of 113.047678 Da.
http://purl.obolibrary.org/obo/MOD_00595	monomannosylated residue	http://purl.obolibrary.org/obo/MOD_00761	monohexosylated residue		A protein modification that effectively replaces a hydrogen atom with an manose group through a glycosidic bond
http://purl.obolibrary.org/obo/MOD_00596	4-(2-aminoethyl)benzenesulfonyl fluoride derivatized residue	http://purl.obolibrary.org/obo/MOD_01652	sulfonyl halide reagent derivatized residue		A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS.
http://purl.obolibrary.org/obo/MOD_00598	S-(2-hydroxyethyl)cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-(2-hydroxyethyl)cysteine
http://purl.obolibrary.org/obo/MOD_00600	L-glutamic acid 5-ethyl ester	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to L-glutamate 5-ethyl ester.
http://purl.obolibrary.org/obo/MOD_00602	N-methylated residue	http://purl.obolibrary.org/obo/MOD_00427	methylated residue		A protein modification that effectively replaces a hydrogen atom of a residue amino or imino group with an methyl group.
http://purl.obolibrary.org/obo/MOD_00604	2x(2)H monomethylated L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to 2x(2)H labeled monomethylated L-lysine.
http://purl.obolibrary.org/obo/MOD_00605	Sulfanilic Acid (SA), light C12	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		modification from Unimod Chemical derivative, C-Terminal/Glutamate/Aspartate sulfonation
http://purl.obolibrary.org/obo/MOD_00606	Sulfanilic Acid (SA), heavy C13	http://purl.obolibrary.org/obo/MOD_01428	(13)C isotope tagged reagent		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00607	dioxoindolealanine lactone	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00608	biotin polyethyleneoxide amine	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00609	Pierce EZ-Link Biotin-HPDP modified L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00610	cysteinyl mercury	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00611	iodouridine monophosphate derivatized residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that is produced by reaction of iodouridine monophosphate with a residue.
http://purl.obolibrary.org/obo/MOD_00612	3-(carboxamidomethylthio)propanoylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated 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.
http://purl.obolibrary.org/obo/MOD_00613	biotinoyl-iodoacetyl-ethylenediamine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00614	fucosylated residue	http://purl.obolibrary.org/obo/MOD_00736	deoxyhexosylated 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.
http://purl.obolibrary.org/obo/MOD_00616	residues isobaric at a resolution below 0.1 Da	http://purl.obolibrary.org/obo/MOD_00538	protein modification categorized by isobaric sets		Natural or modified residues that are isobaric at a resolution below 0.1 Da.
http://purl.obolibrary.org/obo/MOD_00617	3x(2)H residue methyl ester	http://purl.obolibrary.org/obo/MOD_00839	(2)H deuterium labeled residue		A protein modification that effectively converts a residue containing common isotopes to a 3x(2)H labeled residue methyl ester.
http://purl.obolibrary.org/obo/MOD_00618	tryptophan carboxylation	http://purl.obolibrary.org/obo/MOD_01152	carboxylated residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00620	cysteine monobromobimane derivative	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00621	menadione quinone derivative	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00622	cysteine mercaptoethanol	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00623	fucosylated biantennary (-2 galactose) N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00624	residues isobaric at 113.0-113.1 Da	http://purl.obolibrary.org/obo/MOD_00616	residues isobaric at a resolution below 0.1 Da		Natural or modified residues with a mass of 113.0-113.1 Da.
http://purl.obolibrary.org/obo/MOD_00625	N-methylmaleimide derivatized residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00626	fluorescein-5-thiosemicarbazide modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00627	2,5-dimethylpyrrole lysine from 2,5-hexanedione adduct	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00628	Hex2	http://purl.obolibrary.org/obo/MOD_00725	complex glycosylation		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
http://purl.obolibrary.org/obo/MOD_00629	MDA adduct +62	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00630	C3-H2-O adduct (+54 amu) of malondialdehyde with lysine or methylglyoxal with arginine.	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00631	hydrolyzed N-ethylmaleimide adduct	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00633	bis-N-I-sulfonerahodamine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00634	dimethyl 3,3'-dithiobispropionimidate	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00635	10-fluoroethoxyphosphinyl-N-(biotinamidopentyl)decanamide	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00636	S-ethylcysteine (Ser)	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to S-ethylcysteine.
http://purl.obolibrary.org/obo/MOD_00637	1x(13)C,3x(2)H labeled monomethylated L-arginine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		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.
http://purl.obolibrary.org/obo/MOD_00638	2x(13)C,6x(2)H labeled dimethylated L-arginine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		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.
http://purl.obolibrary.org/obo/MOD_00639	thiophosphate labeled with biotin-HPDP	http://purl.obolibrary.org/obo/MOD_00861	phosphorus containing modified residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00640	6-N-biotinylaminohexyl isopropyl phosphorofluoridate	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00642	reduced 4-hydroxynonenal adduct	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification produced by formation of an adduct of a residue with 4-hydroxynonenal artificially reduced by a reagent such as NaBH4.
http://purl.obolibrary.org/obo/MOD_00643	methylamine Michael addition derivatized residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Artifact
http://purl.obolibrary.org/obo/MOD_00644	mono O-acetylated residue	http://purl.obolibrary.org/obo/MOD_00394	monoacetylated residue		A protein modification that effectively replaces a residue hydroxyl group with an acetoxy group.
http://purl.obolibrary.org/obo/MOD_00645	mono S-acetylated residue	http://purl.obolibrary.org/obo/MOD_00394	monoacetylated residue		A protein modification that effectively replaces a residue sulfanyl group with an acetylsulfanyl group.
http://purl.obolibrary.org/obo/MOD_00646	monoacetylated L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to either N-acetyl-L-cysteine or S-acetyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00647	monoacetylated L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_00648	N,O-diacetylated L-serine	http://purl.obolibrary.org/obo/MOD_02080	diacetylated L-serine		A protein modification that effectively converts an L-serine residue to N,O-diacetyl-L-serine.
http://purl.obolibrary.org/obo/MOD_00650	N-myristoylated residue	http://purl.obolibrary.org/obo/MOD_00670	N-acylated residue		A protein modification that effectively replaces a residue amino group with a myristoylamino group.
http://purl.obolibrary.org/obo/MOD_00651	N-palmitoylated residue	http://purl.obolibrary.org/obo/MOD_00670	N-acylated residue		A protein modification that effectively replaces a residue amino group with a palmitoylamino group.
http://purl.obolibrary.org/obo/MOD_00652	O-palmitoylated residue	http://purl.obolibrary.org/obo/MOD_00440	palmitoylated residue		A protein modification that effectively replaces a residue hydroxyl group with a palmitoyloxy group.
http://purl.obolibrary.org/obo/MOD_00653	S-palmitoylated residue	http://purl.obolibrary.org/obo/MOD_00440	palmitoylated residue		A protein modification that effectively replaces a residue sulfanyl group with an palmitoylsulfanyl group.
http://purl.obolibrary.org/obo/MOD_00654	S-methylated residue	http://purl.obolibrary.org/obo/MOD_00427	methylated residue		a protein modification that effectively replaces a sulfanyl group with a methylsulfanyl group
http://purl.obolibrary.org/obo/MOD_00655	S-myristoylated residue	http://purl.obolibrary.org/obo/MOD_00438	myristoylated residue		A protein modification that effectively replaces a residue sulfanyl group with an myristoylsulfanyl group.
http://purl.obolibrary.org/obo/MOD_00656	C-methylated residue	http://purl.obolibrary.org/obo/MOD_00427	methylated residue		A protein modification that effectively replaces a residue hydrocarbyl hydrogen with an methyl group.
http://purl.obolibrary.org/obo/MOD_00657	L-glutamic acid 5-methyl ester (Gln)	http://purl.obolibrary.org/obo/MOD_01453	L-glutamic acid 5-methyl ester		A protein modification that effectively converts an L-glutamine residue to L-glutamate 5-methyl ester.
http://purl.obolibrary.org/obo/MOD_00658	methylated arginine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		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.
http://purl.obolibrary.org/obo/MOD_00660	methylated cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to a methylated cysteine, either S-methylcysteine, or cysteine methyl ester.
http://purl.obolibrary.org/obo/MOD_00661	methylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to a methylated histidine, such as pros-methylhistidine, or tele-methylhistidine.
http://purl.obolibrary.org/obo/MOD_00662	methylated leucine	http://purl.obolibrary.org/obo/MOD_00911	modified L-leucine residue		A protein modification that effectively converts an L-leucine residue to a methylated leucine, either N-methylleucine, or leucine methyl ester.
http://purl.obolibrary.org/obo/MOD_00664	stereoisomerized residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively replaces a residue L-enantiomer (stereoisomer) with a D-enantiomer or with a different diastereomeric isomer.
http://purl.obolibrary.org/obo/MOD_00665	methylated alanine	http://purl.obolibrary.org/obo/MOD_00901	modified L-alanine residue		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.
http://purl.obolibrary.org/obo/MOD_00667	decanoylated residue	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively replaces a hydrogen atom with a decanoyl group.
http://purl.obolibrary.org/obo/MOD_00668	O-decanoylated residue	http://purl.obolibrary.org/obo/MOD_00671	O-acylated residue		A protein modification that effectively replaces a residue hydroxyl group with a decanoyloxy group.
http://purl.obolibrary.org/obo/MOD_00669	O-octanoylated residue	http://purl.obolibrary.org/obo/MOD_00666	octanoylated residue		A protein modification that effectively replaces a residue hydroxyl group with a octanoyloxy group.
http://purl.obolibrary.org/obo/MOD_00671	O-acylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated residue		A protein modification that effectively replaces a residue hydroxyl group with a acyloxy group.
http://purl.obolibrary.org/obo/MOD_00672	S-acylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated residue		A protein modification that effectively replaces a residue sulfanyl group with an acylsulfanyl group.
http://purl.obolibrary.org/obo/MOD_00673	methylated asparagine	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		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.
http://purl.obolibrary.org/obo/MOD_00674	amidated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively replaces a carboxyl group with a carboxamido group.
http://purl.obolibrary.org/obo/MOD_00675	oxidized residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		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.
http://purl.obolibrary.org/obo/MOD_00676	oxygenated residue	http://purl.obolibrary.org/obo/MOD_00675	oxidized residue		A protein modification that effectively adds oxygen atoms to a residue with or without the removal of hydrogen atoms.
http://purl.obolibrary.org/obo/MOD_00678	hydroxylated proline	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively converts an L-proline residue to an hydroxylated L-proline.
http://purl.obolibrary.org/obo/MOD_00679	carbon oxygenated residue	http://purl.obolibrary.org/obo/MOD_00676	oxygenated residue		A protein modification that effectively adds oxygen atoms to a carbon atom of a residue and removes hydrogen atoms.
http://purl.obolibrary.org/obo/MOD_00680	sulfur oxygenated residue	http://purl.obolibrary.org/obo/MOD_00676	oxygenated residue		A protein modification that effectively adds oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms.
http://purl.obolibrary.org/obo/MOD_00681	hydroxylated lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to a hydroxylated L-lysine.
http://purl.obolibrary.org/obo/MOD_00682	hydroxylated arginine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		A protein modification that effectively converts an L-arginine residue to a hydroxylated L-arginine.
http://purl.obolibrary.org/obo/MOD_00683	dehydrogenated residue	http://purl.obolibrary.org/obo/MOD_00675	oxidized residue		A protein modification that effectively removes neutral hydrogen atoms (proton and electron) from a residue.
http://purl.obolibrary.org/obo/MOD_00684	deamidated L-asparagine	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively converts an L-asparagine residue to L-aspartic acid.
http://purl.obolibrary.org/obo/MOD_00685	deamidated L-glutamine	http://purl.obolibrary.org/obo/MOD_00907	modified L-glutamine residue		A protein modification that effectively converts an L-glutamine residue to L-glutamic acid.
http://purl.obolibrary.org/obo/MOD_00686	L-selenocysteine (Cys)	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to L-selenocysteine (not known as a natural, post-translational modification process).
http://purl.obolibrary.org/obo/MOD_00687	thioether crosslinked residues	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_00688	isopeptide crosslinked residues	http://purl.obolibrary.org/obo/MOD_00033	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.
http://purl.obolibrary.org/obo/MOD_00689	disulfide crosslinked residues	http://purl.obolibrary.org/obo/MOD_01619	multisulfide crosslinked residues		A protein modification that crosslinks two cysteine residues by formation of a disulfide bond.
http://purl.obolibrary.org/obo/MOD_00690	oxazole/thiazole ring crosslinked residues	http://purl.obolibrary.org/obo/MOD_00033	crosslinked residues		A protein modification that crosslinks two residues by formation of an oxazole or thiazole ring.
http://purl.obolibrary.org/obo/MOD_00691	5-imidazolinone ring crosslinked residues	http://purl.obolibrary.org/obo/MOD_00033	crosslinked residues		A protein modification that crosslinks two residues by formation of an 5-imidazolinone ring.
http://purl.obolibrary.org/obo/MOD_00692	uncategorized crosslinked residues	http://purl.obolibrary.org/obo/MOD_00033	crosslinked residues		A protein crosslink modification that is not chemically categorized.
http://purl.obolibrary.org/obo/MOD_00694	halogen containing residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively substitutes a halogen atom for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_00695	sulfated residue	http://purl.obolibrary.org/obo/MOD_00860	sulfur containing modified residue		A protein modification that effectively substitutes a sulfonyl group for the hydrogen atom of a hydroxyl or sulfanyl group.
http://purl.obolibrary.org/obo/MOD_00697	flavin modified residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively results from forming an adduct with a compound containing a flavin group.
http://purl.obolibrary.org/obo/MOD_00698	metal or metal cluster containing modified residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively substitutes a metal atom or a metal cluster for hydrogen atoms, or coordinates a metal ion.
http://purl.obolibrary.org/obo/MOD_00699	porphyrin modified residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively results from forming an adduct with a compound containing a porphyrin group.
http://purl.obolibrary.org/obo/MOD_00700	tetrapyrrole modified residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively results from forming an adduct with a compound containing a tetrapyrrole group.
http://purl.obolibrary.org/obo/MOD_00702	isotope labeled residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively substitutes atoms of particular common isotopes with atoms or groups containing isotopes that are not the most common.
http://purl.obolibrary.org/obo/MOD_00704	dehydrated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively forms a double bond by removing a molecule of water from a residue.
http://purl.obolibrary.org/obo/MOD_00705	D-valine	http://purl.obolibrary.org/obo/MOD_00664	stereoisomerized residue		A protein modification that effectively converts an L-valine residue to D-valine.
http://purl.obolibrary.org/obo/MOD_00706	dehydrogenated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts L-tyrosine to 2,3-didehydrotyrosine.
http://purl.obolibrary.org/obo/MOD_00707	hydroxylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		a protein modification that effectively converts an L-tyrosine residue to a multihydroxylated L-phenylalanine
http://purl.obolibrary.org/obo/MOD_00708	sulfur oxygenated L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively adds oxygen atoms to a sulfur atom of L-cysteine residue without removing hydrogen atoms.
http://purl.obolibrary.org/obo/MOD_00709	sulfur oxygenated L-methionine	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively adds oxygen atoms to a sulfur atom of L-methionine residue without removing hydrogen atoms.
http://purl.obolibrary.org/obo/MOD_00710	protonated-dimethylated residue	http://purl.obolibrary.org/obo/MOD_00429	dimethylated residue		A protein modification that effectively adds a proton and replaces two hydrogen atoms with two methyl groups.
http://purl.obolibrary.org/obo/MOD_00711	trimethylated protonated-residue	http://purl.obolibrary.org/obo/MOD_00427	methylated 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.
http://purl.obolibrary.org/obo/MOD_00712	methylated proline	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively converts an L-proline residue to a methylated proline, such as N,N-dimethylproline.
http://purl.obolibrary.org/obo/MOD_00713	methylated glutamic acid	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to a methylated glutamic acid, such as L-glutamate 5-methyl ester.
http://purl.obolibrary.org/obo/MOD_00714	methylated glycine	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to a methylated glycine, such as N-methylglycine.
http://purl.obolibrary.org/obo/MOD_00715	methylated isoleucine	http://purl.obolibrary.org/obo/MOD_00910	modified L-isoleucine residue		A protein modification that effectively converts an L-isoleucine residue to a methylated isoleucine residue, such as N-methyl-L-isoleucine.
http://purl.obolibrary.org/obo/MOD_00716	methylated methionine	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine residue to a methylated methionine, such as N-methyl-L-methionine.
http://purl.obolibrary.org/obo/MOD_00717	methylated phenylalanine	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively converts an L-phenylalanine residue to a methylated phenylalanine, such as N-methyl-L-phenylalanine.
http://purl.obolibrary.org/obo/MOD_00718	methylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an L-tyrosine residue to a methylated tyrosine, such as N-methyl-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_00719	L-methionine sulfoxide	http://purl.obolibrary.org/obo/MOD_01854	sulfur monooxygenated residue		A protein modification that oxygenates an L-methionine residue to one of the diastereomeric L-methionine sulfoxide residues.
http://purl.obolibrary.org/obo/MOD_00720	L-methionine (R)-sulfoxide	http://purl.obolibrary.org/obo/MOD_00719	L-methionine sulfoxide		A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide R-diastereomer.
http://purl.obolibrary.org/obo/MOD_00721	L-methionine (S)-sulfoxide	http://purl.obolibrary.org/obo/MOD_00719	L-methionine sulfoxide		A protein modification that effectively oxygenates an L-methionine residue to L-methionine sulfoxide S-diastereomer.
http://purl.obolibrary.org/obo/MOD_00722	monomethylated L-glutamine	http://purl.obolibrary.org/obo/MOD_00599	monomethylated residue		A protein modification that effectively replaces one hydrogen atom of an L-glutamine residue with one methyl group.
http://purl.obolibrary.org/obo/MOD_00724	N-methylated L-histidine	http://purl.obolibrary.org/obo/MOD_00599	monomethylated residue		A protein modification that effectively replaces one hydrogen atom on a nitrogen of an L-histidine residue with one methyl group.
http://purl.obolibrary.org/obo/MOD_00725	complex glycosylation	http://purl.obolibrary.org/obo/MOD_00693	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 linked through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_00726	glucosylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated 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.
http://purl.obolibrary.org/obo/MOD_00727	mannosylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated 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,
http://purl.obolibrary.org/obo/MOD_00728	galactosylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated 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.
http://purl.obolibrary.org/obo/MOD_00729	pentosylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated 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
http://purl.obolibrary.org/obo/MOD_00730	arabinosylated residue	http://purl.obolibrary.org/obo/MOD_00729	pentosylated 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
http://purl.obolibrary.org/obo/MOD_00731	ribosylated residue	http://purl.obolibrary.org/obo/MOD_00729	pentosylated 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
http://purl.obolibrary.org/obo/MOD_00732	xylosylated residue	http://purl.obolibrary.org/obo/MOD_00729	pentosylated 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
http://purl.obolibrary.org/obo/MOD_00733	N-acetylaminoglucosylated residue	http://purl.obolibrary.org/obo/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-acetylglucosamine group through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_00734	N-acetylaminogalactosylated residue	http://purl.obolibrary.org/obo/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-acetylgalactosamine group through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_00735	hexosuronylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated 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.
http://purl.obolibrary.org/obo/MOD_00736	deoxyhexosylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated 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
http://purl.obolibrary.org/obo/MOD_00737	N-acetylneuraminylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated 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.
http://purl.obolibrary.org/obo/MOD_00738	iron containing modified residue	http://purl.obolibrary.org/obo/MOD_00698	metal or metal cluster 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.
http://purl.obolibrary.org/obo/MOD_00739	iron-sulfur cluster containing modification	http://purl.obolibrary.org/obo/MOD_00860	sulfur containing modified residue		A protein modification that effectively substitutes a cluster of iron and sulfur atoms for hydrogen atoms.
http://purl.obolibrary.org/obo/MOD_00740	manganese containing modified residue	http://purl.obolibrary.org/obo/MOD_00698	metal or metal cluster 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.
http://purl.obolibrary.org/obo/MOD_00741	nickel containing modified residue	http://purl.obolibrary.org/obo/MOD_00698	metal or metal cluster 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.
http://purl.obolibrary.org/obo/MOD_00742	copper containing modified residue	http://purl.obolibrary.org/obo/MOD_00698	metal or metal cluster 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.
http://purl.obolibrary.org/obo/MOD_00743	molybdenum containing modified residue	http://purl.obolibrary.org/obo/MOD_00698	metal or metal cluster 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.
http://purl.obolibrary.org/obo/MOD_00744	molybdenum pterin containing modification	http://purl.obolibrary.org/obo/MOD_00748	pterin modified residue		A protein modification containing a molybdenum atom in a pterin ring system.
http://purl.obolibrary.org/obo/MOD_00745	selenium containing residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively substitutes a selenium atom or a cluster containing selenium for hydrogen atoms.
http://purl.obolibrary.org/obo/MOD_00746	tungsten containing modified residue	http://purl.obolibrary.org/obo/MOD_00698	metal or metal cluster 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.
http://purl.obolibrary.org/obo/MOD_00747	sodium containing modified residue	http://purl.obolibrary.org/obo/MOD_00698	metal or metal cluster containing modified residue		A protein modification that effectively substitutes a sodium atom for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_00748	pterin modified residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively results from forming an adduct with a compound containing a pterin group.
http://purl.obolibrary.org/obo/MOD_00749	sulfur substitution for oxygen	http://purl.obolibrary.org/obo/MOD_00860	sulfur containing modified residue		A protein modification that effectively substitutes a sulfur atom for an oxygen atom.
http://purl.obolibrary.org/obo/MOD_00750	deoxyribonucleic acid linked residue	http://purl.obolibrary.org/obo/MOD_00701	nucleotide or nucleic acid modified residue		A protein modification that effectively crosslinks an amino acid residue and the 3'- or 5'-end of DNA through a phosphodiester bond.
http://purl.obolibrary.org/obo/MOD_00751	ribonucleic acid linked residue	http://purl.obolibrary.org/obo/MOD_00701	nucleotide or nucleic acid modified residue		a protein modification
http://purl.obolibrary.org/obo/MOD_00753	chlorinated residue	http://purl.obolibrary.org/obo/MOD_00694	halogen containing residue		A protein modification that effectively substitutes a chlorine atom for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_00755	iodinated residue	http://purl.obolibrary.org/obo/MOD_00694	halogen containing residue		A protein modification that effectively substitutes an iodine atom of a residue for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_00756	4-hydroxy-D-valine	http://purl.obolibrary.org/obo/MOD_00664	stereoisomerized residue		A protein modification that effectively converts an L-valine residue to 4-hydroxy-D-valine.
http://purl.obolibrary.org/obo/MOD_00757	O4-galactosyl-L-hydroxyproline	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively converts an L-proline residue to O4-galactosyl-L-hydroxyproline.
http://purl.obolibrary.org/obo/MOD_00758	O4-(N-acetylamino)glucosyl-L-hydroxyproline	http://purl.obolibrary.org/obo/MOD_01677	O4-(N-acetylamino)hexosyl-L-hydroxyproline		A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)glucosyl-L-hydroxyproline.
http://purl.obolibrary.org/obo/MOD_00759	fucosylated biantennary (-1 galactose) N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00760	biantennary N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation - missing ref
http://purl.obolibrary.org/obo/MOD_00761	monohexosylated residue	http://purl.obolibrary.org/obo/MOD_00434	hexosylated 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.
http://purl.obolibrary.org/obo/MOD_00762	biantennary (-2 galactose) N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation - missing ref
http://purl.obolibrary.org/obo/MOD_00763	biantennary (-1 galactose) N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation - missing ref
http://purl.obolibrary.org/obo/MOD_00765	cysteinylation (disulfide with free L-cysteine)	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-(L-cysteinyl)-L-cysteine, forming a disulfide bond with free cysteine.
http://purl.obolibrary.org/obo/MOD_00767	glycated residue	http://purl.obolibrary.org/obo/MOD_00764	glycoconjugated 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.
http://purl.obolibrary.org/obo/MOD_00768	methionine oxidation with neutral loss of 80 Da	http://purl.obolibrary.org/obo/MOD_00431	modified residue with a secondary neutral loss		Oxidation of methionine to methionine sulfone with neutral loss of CH3SO2H.
http://purl.obolibrary.org/obo/MOD_00769	residues isobaric at 71.0-71.1 Da	http://purl.obolibrary.org/obo/MOD_00616	residues isobaric at a resolution below 0.1 Da		Natural or modified residues with a mass of 71.0-71.1 Da.
http://purl.obolibrary.org/obo/MOD_00770	residues isobaric at a resolution below 0.01 Da	http://purl.obolibrary.org/obo/MOD_00616	residues isobaric at a resolution below 0.1 Da		Natural or modified residues that are isobaric at a resolution below 0.01 Da.
http://purl.obolibrary.org/obo/MOD_00771	residues isobaric at 166.98-167.00 Da	http://purl.obolibrary.org/obo/MOD_00770	residues isobaric at a resolution below 0.01 Da		Natural or modified residues with a mass of 166.98-167.00 Da.
http://purl.obolibrary.org/obo/MOD_00772	vanadium containing modified residue	http://purl.obolibrary.org/obo/MOD_00698	metal or metal cluster 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.
http://purl.obolibrary.org/obo/MOD_00773	residues isobaric at 181.00-181.02 Da	http://purl.obolibrary.org/obo/MOD_00770	residues isobaric at a resolution below 0.01 Da		Natural or modified residues with a mass of 181.00-181.02 Da.
http://purl.obolibrary.org/obo/MOD_00774	residues isobaric at 243.02-243.03 Da	http://purl.obolibrary.org/obo/MOD_00770	residues isobaric at a resolution below 0.01 Da		Natural or modified residues with a mass of 243.02-243.03 Da.
http://purl.obolibrary.org/obo/MOD_00775	L-asparagine (His)	http://purl.obolibrary.org/obo/MOD_02088	natural, standard, encoded residue substitution		An artifactual protein modification that converts an L-histidine residue to L-asparagine by oxidative degradation.
http://purl.obolibrary.org/obo/MOD_00776	L-aspartic acid (His)	http://purl.obolibrary.org/obo/MOD_02088	natural, standard, encoded residue substitution		An artifactual protein modification that converts an L-histidine residue to L-aspartic acid by oxidative degradation.
http://purl.obolibrary.org/obo/MOD_00777	residues isobaric at 182.96-182.98 Da	http://purl.obolibrary.org/obo/MOD_00778	residues isobaric at 182.9-183.0 Da		Natural or modified residues with a mass of 182.96-182.98 Da.
http://purl.obolibrary.org/obo/MOD_00778	residues isobaric at 182.9-183.0 Da	http://purl.obolibrary.org/obo/MOD_00616	residues isobaric at a resolution below 0.1 Da		Natural or modified residues with a mass of 182.9-183.0 Da.
http://purl.obolibrary.org/obo/MOD_00780	N-acetyl-L-asparagine	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively converts an L-asparagine residue to N-acetyl-L-asparagine.
http://purl.obolibrary.org/obo/MOD_00781	N2-acetyl-L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to N2-acetyl-L-histidine.
http://purl.obolibrary.org/obo/MOD_00782	N-acetyl-L-leucine	http://purl.obolibrary.org/obo/MOD_00911	modified L-leucine residue		A protein modification that effectively converts an L-leucine residue to N-acetyl-L-leucine.
http://purl.obolibrary.org/obo/MOD_00784	N-acetyl-L-phenylalanine	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively converts an L-phenylalanine residue to N-acetyl-L-phenylalanine.
http://purl.obolibrary.org/obo/MOD_00785	N2-acetyl-L-tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to N2-acetyl-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_00786	deuterium substituted residue	http://purl.obolibrary.org/obo/MOD_00839	(2)H deuterium labeled residue		A protein modification that effectively substitutes one or more (2)H deuterium atoms for (1)H protium atoms.
http://purl.obolibrary.org/obo/MOD_00787	diisopropylphosphoserine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		modification from Unimod - label for the active site serine of the serine esterase/protease family also shown to label tyrosine in serum albumin
http://purl.obolibrary.org/obo/MOD_00788	isopropylphosphotyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		modification from Unimod
http://purl.obolibrary.org/obo/MOD_00789	Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form	http://purl.obolibrary.org/obo/MOD_01428	(13)C isotope tagged reagent		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.
http://purl.obolibrary.org/obo/MOD_00790	Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		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.
http://purl.obolibrary.org/obo/MOD_00791	1x(18)O labeled deamidated L-glutamine	http://purl.obolibrary.org/obo/MOD_00852	1x(18)O labeled deamidated residue		A protein modification that effectively converts an L-glutamine residue to L-glutamic acid with one (18)O.
http://purl.obolibrary.org/obo/MOD_00792	deuterium monosubstituted residue	http://purl.obolibrary.org/obo/MOD_00786	deuterium substituted residue		A protein modification that effectively substitutes one (2)H deuterium atom for one (1)H protium atom.
http://purl.obolibrary.org/obo/MOD_00793	dehydroalanine (Cys)	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to dehydroalanine.
http://purl.obolibrary.org/obo/MOD_00795	Michael addition of hydroxymethylvinyl ketone to cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod
http://purl.obolibrary.org/obo/MOD_00796	L-ornithine (Arg)	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		A protein modification that effectively converts an L-arginine residue to L-ornithine.
http://purl.obolibrary.org/obo/MOD_00797	2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		a protein modification that effectively converts an L-cysteine residue to the PEP adduct, 2-(S-L-cysteinyl)pyruvic acid O-phosphothioketal
http://purl.obolibrary.org/obo/MOD_00798	half cystine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_00799	S-galactosyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-galactosyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00800	L-cysteinyl-L-histidino-homocitryl vanadium heptairon nonasulfide	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00801	L-cysteinyl-L-histidino-homocitryl octairon nonasulfide	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00802	L-histidino vanadium tetraoxide	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		a protein modification that effectively converts an L-histidine residue to L-histidino vanadium tetraoxide
http://purl.obolibrary.org/obo/MOD_00803	3-(S-L-cysteinyl)-L-tyrosine	http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00804	O-glucosyl-L-serine	http://purl.obolibrary.org/obo/MOD_00433	monoglucosylated residue		A protein modification that effectively converts an L-serine residue to O3-beta-glucosylated L-serine.
http://purl.obolibrary.org/obo/MOD_00807	pyruvic acid (Ser)	http://purl.obolibrary.org/obo/MOD_01160	deaminated residue		A protein modification that effectively converts an L-serine residue to pyruvic acid.
http://purl.obolibrary.org/obo/MOD_00808	O-galactosyl-L-serine	http://purl.obolibrary.org/obo/MOD_00476	monogalactosylated residue		A protein modification that effectively converts an L-serine residue to O3-galactosylserine.
http://purl.obolibrary.org/obo/MOD_00809	O-galactosyl-L-threonine	http://purl.obolibrary.org/obo/MOD_01348	O-hexosylated threonine		A protein modification that effectively converts an L-threonine residue to O3-galactosylthreonine.
http://purl.obolibrary.org/obo/MOD_00810	O-mannosyl-L-serine	http://purl.obolibrary.org/obo/MOD_00595	monomannosylated residue		A protein modification that effectively converts an L-serine residue to O3-mannosylserine.
http://purl.obolibrary.org/obo/MOD_00811	O-mannosyl-L-threonine	http://purl.obolibrary.org/obo/MOD_01348	O-hexosylated threonine		a protein modification that effectively forms a O3-mannosylthreonine
http://purl.obolibrary.org/obo/MOD_00816	S-stearoyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_02006	S-stearoylated residue		A protein modification that effectively converts an L-cysteine residue to S-stearoyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00817	3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan	http://purl.obolibrary.org/obo/MOD_00601	cyclized residue		A protein modification that effectively converts an L-tryptophan residue to 3'-geranyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_00819	L-2-aminobutanoic acid (Glu)	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to L-2-aminobutanoic acid.
http://purl.obolibrary.org/obo/MOD_00820	2-imino-alanine 5-imidazolinone glycine	http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue		A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue to form 2-imino-alanine 5-imidazolinone glycine.
http://purl.obolibrary.org/obo/MOD_00821	S-(L-alanyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_02040	crosslinked L-alanine residue		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.
http://purl.obolibrary.org/obo/MOD_00822	S-(L-leucyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_02050	crosslinked L-leucine residue		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.
http://purl.obolibrary.org/obo/MOD_00823	S-(L-methionyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_02052	crosslinked L-methionine residue		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.
http://purl.obolibrary.org/obo/MOD_00824	dehydroalanine (Tyr)	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an L-tyrosine residue to dehydroalanine.
http://purl.obolibrary.org/obo/MOD_00825	S-(L-phenylalanyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_02053	crosslinked L-phenylalanine residue		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.
http://purl.obolibrary.org/obo/MOD_00826	S-(L-threonyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_00827	S-(L-tyrosyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_00828	S-(L-tryptophanyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_02057	crosslinked L-tryptophan residue		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.
http://purl.obolibrary.org/obo/MOD_00829	O-(L-phenylalanyl)-L-serine	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_00830	N-methyl-L-proline	http://purl.obolibrary.org/obo/MOD_01680	alpha-amino monomethylated residue		A protein modification that effectively converts an L-proline residue to an N-methyl-L-proline.
http://purl.obolibrary.org/obo/MOD_00832	N4-(N-acetylamino)galactosyl-L-asparagine	http://purl.obolibrary.org/obo/MOD_01674	N4-(N-acetylamino)hexosyl-L-asparagine		A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminogalactosyl)-L-asparagine.
http://purl.obolibrary.org/obo/MOD_00833	N4-glucosyl-L-asparagine	http://purl.obolibrary.org/obo/MOD_01346	N4-hexosylated asparagine		A protein modification that effectively converts an L-asparagine residue to N4-glucosyl-asparagine.
http://purl.obolibrary.org/obo/MOD_00834	O-(N-acetylamino)fucosyl-L-serine	http://purl.obolibrary.org/obo/MOD_00002	O-glycosyl-L-serine		A protein modification that effectively converts an L-serine residue to O3-(N-acetamino)fucosylserine.
http://purl.obolibrary.org/obo/MOD_00835	L-3-oxoalanine (Ser)	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to L-oxoalanine.
http://purl.obolibrary.org/obo/MOD_00836	deuterium disubstituted residue	http://purl.obolibrary.org/obo/MOD_00786	deuterium substituted residue		A protein modification that effectively substitutes two (2)H deuterium atoms for two (1)H protium atoms.
http://purl.obolibrary.org/obo/MOD_00837	deuterium tetrasubstituted residue	http://purl.obolibrary.org/obo/MOD_00786	deuterium substituted residue		A protein modification that effectively substitutes four (2)H deuterium atoms for four (1)H protium atoms.
http://purl.obolibrary.org/obo/MOD_00838	3x(2)H labeled L-leucine	http://purl.obolibrary.org/obo/MOD_00911	modified L-leucine residue		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.
http://purl.obolibrary.org/obo/MOD_00839	(2)H deuterium labeled residue	http://purl.obolibrary.org/obo/MOD_00702	isotope labeled residue		A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing deuteriumm, (2)H.
http://purl.obolibrary.org/obo/MOD_00840	isocyanate reagent derivatized residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification produced by formation of an adduct with an isocyanate compound.
http://purl.obolibrary.org/obo/MOD_00841	isothiocyanate reagent derivatized residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification produced by formation of an adduct with an isothiocyanate compound.
http://purl.obolibrary.org/obo/MOD_00842	(13)C labeled residue	http://purl.obolibrary.org/obo/MOD_00702	isotope labeled residue		A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (13)C.
http://purl.obolibrary.org/obo/MOD_00843	(15)N labeled residue	http://purl.obolibrary.org/obo/MOD_00702	isotope labeled residue		A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (15)N.
http://purl.obolibrary.org/obo/MOD_00844	(18)O labeled residue	http://purl.obolibrary.org/obo/MOD_00702	isotope labeled residue		A protein modification that effectively substitutes atoms of particular common isotopes with atoms of or groups containing (18)O.
http://purl.obolibrary.org/obo/MOD_00845	(18)O substituted residue	http://purl.obolibrary.org/obo/MOD_00844	(18)O labeled residue		A protein modification that effectively substitutes one or more (18)O atoms for (16)O atoms.
http://purl.obolibrary.org/obo/MOD_00846	levuglandinyl (prostaglandin H2) adduct	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		stub
http://purl.obolibrary.org/obo/MOD_00847	(18)O disubstituted residue	http://purl.obolibrary.org/obo/MOD_00845	(18)O substituted residue		A protein modification that effectively substitutes two (18)O atom for two (16)O atoms.
http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that is produced by formation of an adduct with a particular compound used as a reagent.
http://purl.obolibrary.org/obo/MOD_00849	potassium containing modified residue	http://purl.obolibrary.org/obo/MOD_00698	metal or metal cluster containing modified residue		A protein modification that effectively substitutes a potassium atom for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_00850	unnatural residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		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.
http://purl.obolibrary.org/obo/MOD_00851	(18)O labeled deamidated residue	http://purl.obolibrary.org/obo/MOD_00844	(18)O labeled residue		A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with (18)O.
http://purl.obolibrary.org/obo/MOD_00852	1x(18)O labeled deamidated residue	http://purl.obolibrary.org/obo/MOD_00851	(18)O labeled deamidated residue		A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with one (18)O.
http://purl.obolibrary.org/obo/MOD_00853	2x(18)O labeled deamidated residue	http://purl.obolibrary.org/obo/MOD_00851	(18)O labeled deamidated residue		A protein modification that effectively replaces a carboxamido group with a carboxyl group labeled with two (18)O.
http://purl.obolibrary.org/obo/MOD_00854	protonated L-lysine (L-lysinium) residue	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine to L-lysinium (protonated L-lysine).
http://purl.obolibrary.org/obo/MOD_00855	N6,N6,N6-trimethyl-L-lysine (from L-lysinium residue)	http://purl.obolibrary.org/obo/MOD_00430	trimethylated residue		A protein modification that effectively converts an L-lysinium (N6-protonated L-lysine) residue to an N6,N6,N6-trimethyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00856	protonated L-alanine (L-alaninium) residue	http://purl.obolibrary.org/obo/MOD_00901	modified L-alanine residue		A protein modification that effectively converts an L-alanine residue to an L-alaninium (protonated L-alanine).
http://purl.obolibrary.org/obo/MOD_00857	N,N,N-trimethyl-L-alanine (from L-alaninium)	http://purl.obolibrary.org/obo/MOD_01687	alpha-amino trimethylated residue		A protein modification that effectively converts an L-alaninium (protonated L-alanine) residue to an N,N,N-trimethyl-L-alanine.
http://purl.obolibrary.org/obo/MOD_00858	D-alanine (Ser)	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to D-alanine.
http://purl.obolibrary.org/obo/MOD_00859	modified residue that can arise from different natural residues	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that can be derived from different natural residues by different chemical processes.
http://purl.obolibrary.org/obo/MOD_00860	sulfur containing modified residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that produces an amino acid residue containing an exogenous sulfur atom.
http://purl.obolibrary.org/obo/MOD_00861	phosphorus containing modified residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that produces an amino acid residue containing a phosphorus atom.
http://purl.obolibrary.org/obo/MOD_00862	D-alanine	http://purl.obolibrary.org/obo/MOD_00859	modified residue that can arise from different natural residues		A protein modification that effectively converts a source amino acid residue to D-alanine.
http://purl.obolibrary.org/obo/MOD_00863	D-allo-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to D-allo-threonine.
http://purl.obolibrary.org/obo/MOD_00864	tris-L-cysteinyl L-histidino diiron disulfide	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_00865	N-aspartyl-glycosylsphingolipidinositolethanolamine	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to N-aspartyl-glycosylsphingolipidinositolethanolamine.
http://purl.obolibrary.org/obo/MOD_00866	dihydroxylated proline	http://purl.obolibrary.org/obo/MOD_00678	hydroxylated 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.
http://purl.obolibrary.org/obo/MOD_00867	L-cysteinyl-L-selenocysteine (Cys-Cys)	http://purl.obolibrary.org/obo/MOD_01627	L-cysteinyl-L-selenocysteine		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.
http://purl.obolibrary.org/obo/MOD_00868	natural, non-standard encoded residue	http://purl.obolibrary.org/obo/MOD_00009	natural 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.
http://purl.obolibrary.org/obo/MOD_00869	L-alanine residue (Asp)	http://purl.obolibrary.org/obo/MOD_02088	natural, standard, encoded residue substitution		A protein modification that effectively converts an L-aspartic acid residue to L-alanine.
http://purl.obolibrary.org/obo/MOD_00870	phenyl isocyanate derivatized residue	http://purl.obolibrary.org/obo/MOD_00840	isocyanate reagent derivatized residue		A protein modification produced by formation of an adduct with phenyl isocyanate.
http://purl.obolibrary.org/obo/MOD_00871	(2)H5-phenyl isocyanate derivatized residue	http://purl.obolibrary.org/obo/MOD_01431	(2)H deuterium tagged reagent		A protein modification produced by formation of an adduct with (2)H5-phenyl isocyanate.
http://purl.obolibrary.org/obo/MOD_00873	L-isoglutamyl diglutamic acid	http://purl.obolibrary.org/obo/MOD_00207	L-isoglutamyl-polyglutamic 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.
http://purl.obolibrary.org/obo/MOD_00874	L-isoglutamyl triglutamic acid	http://purl.obolibrary.org/obo/MOD_00207	L-isoglutamyl-polyglutamic 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.
http://purl.obolibrary.org/obo/MOD_00875	L-isoglutamyl tetraglutamic acid	http://purl.obolibrary.org/obo/MOD_00207	L-isoglutamyl-polyglutamic 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.
http://purl.obolibrary.org/obo/MOD_00876	hexosaminylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated 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.
http://purl.obolibrary.org/obo/MOD_00877	imidoester crosslink dimethyl pimelimidate singly attached	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		dimethyl pimelimidate modification from Unimod
http://purl.obolibrary.org/obo/MOD_00878	imidoester crosslink dimethyl pimelimidate doubly attached	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		dimethyl pimelimidate modification from Unimod - Mechanism of the reaction of imidoesters with amines
http://purl.obolibrary.org/obo/MOD_00879	naphthalene-2,3-dicarboxaldehyde	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod
http://purl.obolibrary.org/obo/MOD_00880	6x(13)C labeled 4-sulfophenyl isothiocyanate derivatized residue	http://purl.obolibrary.org/obo/MOD_01428	(13)C isotope tagged reagent		A protein modification produced by formation of an adduct with 6x(13)C labeled 4-sulfophenyl isothiocyanate.
http://purl.obolibrary.org/obo/MOD_00882	S-(2-aminoethyl)cysteine (Ser)	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to S-(2-aminoethyl)cysteine.
http://purl.obolibrary.org/obo/MOD_00883	C1-amidated residue	http://purl.obolibrary.org/obo/MOD_00674	amidated residue		A protein modification that effectively replaces a 1-carboxyl group (usually referred to as the alpha-carboxyl) with a carboxamido group.
http://purl.obolibrary.org/obo/MOD_00884	S-aminoethylcysteine (Cys)	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-2-aminoethylcysteine.
http://purl.obolibrary.org/obo/MOD_00885	ester crosslinked residues	http://purl.obolibrary.org/obo/MOD_00033	crosslinked residues		A protein modification that crosslinks two residues by formation of an ester bond.
http://purl.obolibrary.org/obo/MOD_00886	6'-chloro-L-tryptophan	http://purl.obolibrary.org/obo/MOD_01913	monochlorinated L-tryptophan		A protein modification that effectively converts an L-tryptophan residue to 6'-chloro-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_00887	methylated aspartic acid	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to a methylated aspartic acid, such as aspartic acid 4-methyl ester.
http://purl.obolibrary.org/obo/MOD_00888	protonated L-proline (L-prolinium) residue	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively converts an L-proline to an L-prolinium (protonated L-proline).
http://purl.obolibrary.org/obo/MOD_00889	N,N-dimethyl-L-proline (from L-prolinium)	http://purl.obolibrary.org/obo/MOD_01686	alpha-amino dimethylated residue		A protein modification that effectively converts an L-prolinium (charged L-proline) residue to N,N-dimethyl-L-proline.
http://purl.obolibrary.org/obo/MOD_00890	phosphorylated L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to a phosphorylated L-histidine, such as pros-phosphohistidine, or tele-phosphohistidine.
http://purl.obolibrary.org/obo/MOD_00891	D-serine	http://purl.obolibrary.org/obo/MOD_00859	modified residue that can arise from different natural residues		A protein modification that effectively converts a source amino acid residue to D-serine.
http://purl.obolibrary.org/obo/MOD_00892	D-serine (Cys)	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to D-serine.
http://purl.obolibrary.org/obo/MOD_00893	residues isobaric at 128.0-128.1	http://purl.obolibrary.org/obo/MOD_00616	residues isobaric at a resolution below 0.1 Da		Natural or modified residues with a mass of 128.0-128.1 Da.
http://purl.obolibrary.org/obo/MOD_00894	residues isobaric at 128.058578 Da	http://purl.obolibrary.org/obo/MOD_00893	residues isobaric at 128.0-128.1		Natural or modified resiues with a mass of 128.058578 Da.
http://purl.obolibrary.org/obo/MOD_00895	FAD modified residue	http://purl.obolibrary.org/obo/MOD_00861	phosphorus containing modified residue		A protein modification that effectively results from forming an adduct with a compound containing a flavin adenine dinucleotide (FAD) group.
http://purl.obolibrary.org/obo/MOD_00896	FMN modified residue	http://purl.obolibrary.org/obo/MOD_00861	phosphorus containing modified residue		A protein modification that effectively results from forming an adduct with a compound containing a riboflavin phosphate (flavin mononucleotide, FMN) group.
http://purl.obolibrary.org/obo/MOD_00897	N-acetyl-S-archeol-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to N-acetyl-S-archeol-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00898	S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine	http://purl.obolibrary.org/obo/MOD_00116	S-diacylglycerol-L-cysteine		A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine.
http://purl.obolibrary.org/obo/MOD_00899	N-palmitoyl-S-diacylglycerol-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-diacylglycerol-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00900	N-palmitoyl-S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine	http://purl.obolibrary.org/obo/MOD_00899	N-palmitoyl-S-diacylglycerol-L-cysteine		A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-S-(sn-1-2-oleoyl-3-palmitoyl-glycerol)cysteine.
http://purl.obolibrary.org/obo/MOD_00922	Cy3 CyDye DIGE Fluor saturation dye	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00923	Cy5 CyDye DIGE Fluor saturation dye	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00924	N6-(L-threonyl)-L-lysine	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_00925	heptosylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated 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.
http://purl.obolibrary.org/obo/MOD_00927	2x(13)C,4x(2)H labeled dimethylated residue	http://purl.obolibrary.org/obo/MOD_00842	(13)C labeled 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.
http://purl.obolibrary.org/obo/MOD_00928	[3-(2,5)-dioxopyrrolidin-1-yloxycarbonyl)-propyl]dimethyloctylammonium	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00929	lactose glycated lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_00930	propyl-NAG tyrosine adduct	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		tyrosine adduct with substrate analog inhibitor 1,2-dideoxy-2'-methyl-alpha-D-glucopyranoso-[2,1-d]-Delta2'-thiazoline.
http://purl.obolibrary.org/obo/MOD_00931	Michael addition of t-butyl hydroxylated BHT (BHTOH) to C, H or K	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		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
http://purl.obolibrary.org/obo/MOD_00932	IDBEST tag for quantitation	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00933	methylglyoxal arginine adduct (+54 amu)	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		modification from Unimod Chemical derivative - 5-hydro-5-methylimidazol-4-one, arginine methylglyoxal arginine adduct (+54 amu)
http://purl.obolibrary.org/obo/MOD_00934	Levuglandinyl - arginine hydroxylactam adduct	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		modification from Unimod Post-translational
http://purl.obolibrary.org/obo/MOD_00935	methionine oxidation with neutral loss of 64 Da	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		Oxidation of methionine to methionine sulfoxide with neutral loss of CH3SOH.
http://purl.obolibrary.org/obo/MOD_00936	Levuglandinyl - hydroxylactam adduct, K and N-term	http://purl.obolibrary.org/obo/MOD_00846	levuglandinyl (prostaglandin H2) adduct		modification from Unimod Post-translational
http://purl.obolibrary.org/obo/MOD_00937	Levuglandinyl - arginine lactam adduct	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		modification from Unimod Post-translational
http://purl.obolibrary.org/obo/MOD_00938	Levuglandinyl - lactam adduct, K and N-term	http://purl.obolibrary.org/obo/MOD_00846	levuglandinyl (prostaglandin H2) adduct		modification from Unimod Post-translational
http://purl.obolibrary.org/obo/MOD_00939	hydrolyzed N-methylmaleimide cysteine adduct	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00940	3-methyl-2-pyridyl isocyanate derivatized residue	http://purl.obolibrary.org/obo/MOD_00840	isocyanate reagent derivatized residue		A protein modification produced by formation of an adduct with 3-methyl-2-pyridyl isocyanate.
http://purl.obolibrary.org/obo/MOD_00941	dehydropyrrolizidine alkaloid (dehydroretronecine) derivatized cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00942	(4,4,5,5-(2)H4)-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_00943	4-trimethylammoniumbutanoyl derivatized residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00944	d9-4-trimethylammoniumbutanoyl derivatized residue	http://purl.obolibrary.org/obo/MOD_01431	(2)H deuterium tagged reagent		modification from Unimod Isotopic label
http://purl.obolibrary.org/obo/MOD_00946	crosslinked residues with loss of ammonia	http://purl.obolibrary.org/obo/MOD_00033	crosslinked residues		A protein modification that crosslinks two residues with a covalent bond and the loss of ammonia.
http://purl.obolibrary.org/obo/MOD_00947	DeltaMass	http://purl.obolibrary.org/obo/MOD_00032	uncategorized protein modification		Entries from DeltaMass see http://www.abrf.org/index.cfm/dm.home?AvgMass=all.
http://purl.obolibrary.org/obo/MOD_00951	L-gamma-carboxyglutamic acid with neutral loss of carbon dioxide	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		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.
http://purl.obolibrary.org/obo/MOD_00952	(2-aminosuccinimidyl)acetic acid (Asp)	http://purl.obolibrary.org/obo/MOD_02043	crosslinked L-aspartic acid residue		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.
http://purl.obolibrary.org/obo/MOD_00953	O-(L-isoglutamyl)-L-serine (Glu-Ser)	http://purl.obolibrary.org/obo/MOD_02045	crosslinked L-glutamic acid residue		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.
http://purl.obolibrary.org/obo/MOD_00954	crosslinked residues with loss of water	http://purl.obolibrary.org/obo/MOD_00033	crosslinked residues		A protein modification that crosslinks two residues with a covalent bond and the loss of water.
http://purl.obolibrary.org/obo/MOD_00955	alaninohistidine (serine crosslinked to tele or pros nitrogen of histidine)	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_00956	misincorporation of norleucine for methionine	http://purl.obolibrary.org/obo/MOD_01026	norleucine residue (Nle)		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00957	modified residue with neutral loss of carbon dioxide	http://purl.obolibrary.org/obo/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 carbon dioxide molecular fragment.
http://purl.obolibrary.org/obo/MOD_00958	crosslink between Arg and His sidechains	http://purl.obolibrary.org/obo/MOD_00692	uncategorized crosslinked residues		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00959	3,3',5,5'-TerTyr (Crosslink)	http://purl.obolibrary.org/obo/MOD_00692	uncategorized crosslinked residues		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00960	decarboxylated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively replaces a carboxylic acid group with a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_00961	reduction of disulfide crosslink in cystine to two cysteines	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively reduces the disulfide bond of cystine to form two cysteine residues.
http://purl.obolibrary.org/obo/MOD_00962	2',3'-dihydrotryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that by reducing the indole ring system of tryptophan to indoline effectively converts an L-tryptophan residue to 2',3'-dihydrotryptophan.
http://purl.obolibrary.org/obo/MOD_00964	lysine epsilon amino to imine + 12 amu	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00965	4-thiazolidinecarboxylic acid	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an N-terminal L-cysteine residue by a formadehyde adduct to 4-thiazolidinecarboxylic acid.
http://purl.obolibrary.org/obo/MOD_00966	1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acid	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		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.
http://purl.obolibrary.org/obo/MOD_00967	syndesine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		A protein modification that effectively cross-links two L-lysine residues to form syndesine, hydroxylysinohydroxynorleucine.
http://purl.obolibrary.org/obo/MOD_00970	delta-hydroxy-allysine (Lys)	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00971	2-Oxohistidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to 2-oxohistidine.
http://purl.obolibrary.org/obo/MOD_00972	monobrominated L-phenylalanine	http://purl.obolibrary.org/obo/MOD_01912	monobrominated residue		A protein modification that effectively converts an L-phenylalanine residue to a monobrominated L-phenylalanine, such as L-2'-bromophenylalanine.
http://purl.obolibrary.org/obo/MOD_00973	Oxidation of proline (to glutamic acid)	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00974	(35)Cl labeled 3'-chlorotyrosine	http://purl.obolibrary.org/obo/MOD_00987	chlorinated tyrosine		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00975	(37)Cl labeled 3'-chlorotyrosine	http://purl.obolibrary.org/obo/MOD_00987	chlorinated tyrosine		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00977	disodium salt	http://purl.obolibrary.org/obo/MOD_00747	sodium containing modified residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00978	piperidine adduct to C-terminal Cys	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00979	t-butyl ester (OtBu) and t-butyl (tBu)	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00981	sodium and potassium salt	http://purl.obolibrary.org/obo/MOD_00849	potassium containing modified residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00982	L-selenocysteine (Ser)	http://purl.obolibrary.org/obo/MOD_02088	natural, standard, encoded residue substitution		A protein modification that effectively converts an L-serine residue to L-selenocysteine (not known as a natural post-translational modification process).
http://purl.obolibrary.org/obo/MOD_00983	Asp transamidation with piperidine	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00984	(35)Cl labeled 3',5'-dichlorotyrosine	http://purl.obolibrary.org/obo/MOD_00987	chlorinated tyrosine		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00985	halogenated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a halogen atom.
http://purl.obolibrary.org/obo/MOD_00986	(35)Cl and (37)Cl labeled 3',5'-dichlorotyrosine	http://purl.obolibrary.org/obo/MOD_00987	chlorinated tyrosine		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00987	chlorinated tyrosine	http://purl.obolibrary.org/obo/MOD_00985	halogenated tyrosine		A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a chlorine atom.
http://purl.obolibrary.org/obo/MOD_00988	brominated tyrosine	http://purl.obolibrary.org/obo/MOD_00754	brominated residue		A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with a bromine atom.
http://purl.obolibrary.org/obo/MOD_00990	(37)Cl labeled 3',5'-dichlorotyrosine	http://purl.obolibrary.org/obo/MOD_00987	chlorinated tyrosine		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00991	S-(sn-1-glyceryl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00992	glutamate 5-glycerol ester	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00993	phenyl ester	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00994	(79)Br labeled 3'-bromotyrosine	http://purl.obolibrary.org/obo/MOD_01000	monobrominated tyrosine		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00995	(81)Br labeled 2'-bromophenylalanine	http://purl.obolibrary.org/obo/MOD_02086	brominated phenylalanine		A protein modification that effectively converts an L-phenylalanine residue to (81)Br-L-2'-bromophenylalanine.
http://purl.obolibrary.org/obo/MOD_00996	(81)Br labeled 3'-bromotyrosine	http://purl.obolibrary.org/obo/MOD_01000	monobrominated tyrosine		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00997	cyclohexyl ester	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00998	iodinated tyrosine	http://purl.obolibrary.org/obo/MOD_00985	halogenated tyrosine		A protein modification that effectively substitutes a hydrogen atom of an L-tyrosine residue with an iodine atom.
http://purl.obolibrary.org/obo/MOD_01000	monobrominated tyrosine	http://purl.obolibrary.org/obo/MOD_00988	brominated tyrosine		A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one bromine atom.
http://purl.obolibrary.org/obo/MOD_01001	2-aminoisobutyric acid residue (Aib)	http://purl.obolibrary.org/obo/MOD_00850	unnatural residue		A protein modification that inserts or replaces a residue with a 2-aminoisobutyric acid.
http://purl.obolibrary.org/obo/MOD_01002	gamma-aminobutyryl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01003	t-butyloxymethyl (Bum)	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01004	diaminopropionyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01005	t-butylsulfenyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01006	dibrominated tyrosine	http://purl.obolibrary.org/obo/MOD_00988	brominated tyrosine		A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two bromine atoms.
http://purl.obolibrary.org/obo/MOD_01007	anisyl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes an anisyl (methoxyphenyl) group for a hydroxyl group, typically at the 4 or para position.
http://purl.obolibrary.org/obo/MOD_01008	benzyl (Bzl) and benzyl ester (OBzl) modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a benzyl (phenylmethyl) group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01009	dehydrogenated proline	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01010	trifluoroacetylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated residue		A protein modification that effectively substitutes a trifluoroacetyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01011	N-hydroxysuccinimide (ONSu, OSu)	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01012	oxidation of disulfide crosslink in cystine to two cysteic acids	http://purl.obolibrary.org/obo/MOD_00675	oxidized residue		A protein modification that effectively oxidizes the disulfide bond of a cystine crosslink to form two cysteic acid residues.
http://purl.obolibrary.org/obo/MOD_01013	tetramethylguanidinium termination by-product on amine	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01014	phosphate/sulphate adduct of proteins	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01015	isovaline residue (Iva)	http://purl.obolibrary.org/obo/MOD_00850	unnatural residue		A protein modification that inserts or replaces a residue with an isovaline.
http://purl.obolibrary.org/obo/MOD_01016	t-butyloxycarbonyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01018	4-methylbenzyl	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01019	hydroxymethylphenyl linker	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01020	thioanisyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01021	thiocresyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01022	2-piperidinecarboxylic acid	http://purl.obolibrary.org/obo/MOD_01160	deaminated residue		A protein modification that effectively converts an L-lysine residue to 2-piperidinecarboxylic acid.
http://purl.obolibrary.org/obo/MOD_01023	3',5'-dibromo-L-tyrosine	http://purl.obolibrary.org/obo/MOD_01006	dibrominated tyrosine		A protein modification that effectively converts an L-tyrosine residue to 3',5'-dibromo-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_01024	monohydroxylated proline	http://purl.obolibrary.org/obo/MOD_00678	hydroxylated 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.
http://purl.obolibrary.org/obo/MOD_01025	3'-bromo-L-tyrosine	http://purl.obolibrary.org/obo/MOD_01000	monobrominated tyrosine		A protein modification that effectively converts an L-tyrosine residue to 3'-bromo-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_01026	norleucine residue (Nle)	http://purl.obolibrary.org/obo/MOD_00850	unnatural residue		A protein modification that inserts or replaces a residue with a norleucine.
http://purl.obolibrary.org/obo/MOD_01027	t-amyloxycarbonyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01028	monochlorinated L-tyrosine	http://purl.obolibrary.org/obo/MOD_01911	monochlorinated residue		A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one chlorine atom.
http://purl.obolibrary.org/obo/MOD_01029	succinylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated residue		A protein modification that effectively replaces a hydrogen atom with a succinyl group linked through a carbonyl carbon.
http://purl.obolibrary.org/obo/MOD_01030	hydroxybenzotriazole ester	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01031	dimethylbenzyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01032	benzyloxymethyl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a benzyloxymethyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01033	p-methoxybenzyl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a p-methoxybenzyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01034	4-nitrophenyl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a 4-nitrophenyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01035	chlorobenzyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01037	dichlorinated tyrosine	http://purl.obolibrary.org/obo/MOD_00987	chlorinated tyrosine		A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two chlorine atoms.
http://purl.obolibrary.org/obo/MOD_01040	penicillamine residue	http://purl.obolibrary.org/obo/MOD_00850	unnatural residue		A protein modification that inserts or replaces a residue with a penicillamine.
http://purl.obolibrary.org/obo/MOD_01041	benzyloxycarbonyl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a benzyloxycarbonyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01042	adamantyl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a adamantyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01043	p-nitrobenzyl ester modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a p-nitrobenzyl group for the hydrogen atom of a carboxyl group.
http://purl.obolibrary.org/obo/MOD_01045	3',5'-dichloro-L-tyrosine	http://purl.obolibrary.org/obo/MOD_01037	dichlorinated tyrosine		A protein modification that effectively converts an L-tyrosine residue to 3',5'-dichloro-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_01046	3'-chloro-L-tyrosine	http://purl.obolibrary.org/obo/MOD_01028	monochlorinated L-tyrosine		A protein modification that effectively converts an L-tyrosine residue to 3'-chloro-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_01047	monohydroxylated lysine	http://purl.obolibrary.org/obo/MOD_00681	hydroxylated lysine		A protein modification that effectively converts an L-lysine residue to a monohydroxylated lysine.
http://purl.obolibrary.org/obo/MOD_01049	halogenated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively substitutes a hydrogen atom of an L-histidine residue with a halogen atom.
http://purl.obolibrary.org/obo/MOD_01050	pyridyl alanyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01051	2-nitrobenzoyl	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01052	dimethoxybenzyl Trp	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01053	2-nitrophenylsulphenyl	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01054	4-toluenesulfonyl	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01055	3-nitro-2-pyridinesulfenyl	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01056	(79)Br labeled 3',5'-dibromotyrosine	http://purl.obolibrary.org/obo/MOD_01006	dibrominated tyrosine		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01057	(79)Br and (81)Br labeled 3',5'-dibromotyrosine	http://purl.obolibrary.org/obo/MOD_01006	dibrominated tyrosine		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01058	dichlorobenzyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01059	(81)Br labeled 3',5'-dibromotyrosine	http://purl.obolibrary.org/obo/MOD_01006	dibrominated tyrosine		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01060	S-carboxamidomethyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_01061	S-carboxymethyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_01063	monomethylated phenylalanine	http://purl.obolibrary.org/obo/MOD_00599	monomethylated residue		A protein modification that effectively converts an L-phenylalanine residue to a monomethylated phenylalanine.
http://purl.obolibrary.org/obo/MOD_01064	inositol	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01065	hexose glycated N-terminal	http://purl.obolibrary.org/obo/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 N-terminal amino group to form a Schiff-base or an Amadori ketosamine  (or aminoketose) residue adduct.
http://purl.obolibrary.org/obo/MOD_01066	halogenated phenylalanine	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively substitutes a hydrogen atom of an L-phenylalanine residue with a halogen atom.
http://purl.obolibrary.org/obo/MOD_01067	linker attached to peptide in Fmoc peptide synthesis	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01068	halogenated tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively substitutes a hydrogen atom of an L-tryptophan residue with a halogen atom.
http://purl.obolibrary.org/obo/MOD_01069	2,4-dinitrophenyl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a 2,4-dinitrophenyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01070	pentafluorophenyl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a pentafluorophenyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01071	diphenylmethyl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a diphenylmethyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01072	monopotassium salt	http://purl.obolibrary.org/obo/MOD_00849	potassium containing modified residue		A protein modification that effectively substitutes one potassium atom for one hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01073	2-chlorobenzyloxycarbonyl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a 2-chlorobenzyloxycarbonyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01074	napthylacetyl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a napthylacetyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01075	mercury containing modified residue	http://purl.obolibrary.org/obo/MOD_00698	metal or metal cluster 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.
http://purl.obolibrary.org/obo/MOD_01077	ethanedithiol/TFA cyclic adduct	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01078	S-(2-aminoethyl)-3-methylcysteine (Thr)	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to S-(2-aminoethyl)-3-methylcysteine.
http://purl.obolibrary.org/obo/MOD_01079	S-(acetylamino)methyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-[(acetylamino)methyl]-L-cysteine.
http://purl.obolibrary.org/obo/MOD_01081	delta-glycosyloxy- (of lysine) or beta-glycosyloxy- (of phenylalanine or tyrosine)	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01083	O-benzyl-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-benzyl-L-serine.
http://purl.obolibrary.org/obo/MOD_01084	iodoacetic acid derivatized amino-terminal residue	http://purl.obolibrary.org/obo/MOD_00399	iodoacetic acid derivatized residue		A protein modification that by reaction of iodoacetic acid effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a carboxymethyl group.
http://purl.obolibrary.org/obo/MOD_01085	alpha-N-gluconoylated L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		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
http://purl.obolibrary.org/obo/MOD_01086	p-nitrobenzyloxycarbonyl	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01087	2,4,5-trichlorophenyl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a 2,4,5-trichlorophenyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01088	2,4,6-trimethyloxybenzyl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a 2,4,6-trimethyloxybenzyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01089	xanthyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01090	iodoacetamide derivatized amino-terminal residue	http://purl.obolibrary.org/obo/MOD_00397	iodoacetamide derivatized residue		A protein modification that by reaction of iodoacetamide effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a carboxamidomethyl group.
http://purl.obolibrary.org/obo/MOD_01091	monochlorinated L-phenylalanine	http://purl.obolibrary.org/obo/MOD_01911	monochlorinated residue		A protein modification that effectively substitutes one hydrogen atom of an L-phenylalanine residue with one chlorine atom.
http://purl.obolibrary.org/obo/MOD_01092	mesitylene-2-sulfonyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01093	isopropyl lysyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01094	N6-carboxymethyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00399	iodoacetic acid derivatized residue		A protein modification that effectively converts an L-lysine residue to N6-carboxymethyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01096	O-benzyl-L-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to O-benzyl-L-threonine.
http://purl.obolibrary.org/obo/MOD_01097	S-benzyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-benzyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_01098	naphthylalanine residue	http://purl.obolibrary.org/obo/MOD_00850	unnatural residue		A protein modification that inserts or replaces a residue with a naphthylalanine.
http://purl.obolibrary.org/obo/MOD_01099	succinyl beta-aspartyl anhydride	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to succinyl beta-aspartyl anhydride.
http://purl.obolibrary.org/obo/MOD_01100	HMP (hydroxymethylphenyl)/TFA adduct	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01104	4-methoxy-2,3,6-trimethylbenzenesulfonyl	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01105	2-bromobenzyloxycarbonyl	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01106	N-formyl-L-tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to N-formyl-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01107	O5-benzyl-L-glutamate	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to O5-benzyl-L-glutamate.
http://purl.obolibrary.org/obo/MOD_01108	2-amino-5-(4-methoxyphenyl)-5-oxopentanoic acid (Glu)	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to 2-amino-5-(4-methoxyphenyl)-5-oxopentanoic acid, glutamtic acid anisole adduct.
http://purl.obolibrary.org/obo/MOD_01111	dimethoxybenzhydryl modified residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that effectively substitutes a dimethoxybenzhydryl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01113	2-(p-biphenyl)isopropyl-oxycarbonyl	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01114	triphenylmethyl	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01115	isoprenylated tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		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).
http://purl.obolibrary.org/obo/MOD_01116	S-farnesyl-L-cysteine methyl ester	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine methyl ester.
http://purl.obolibrary.org/obo/MOD_01117	pentamethyldihydrobenzofuransulfonyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01118	alpha-N-6-phosphogluconoylated L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		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
http://purl.obolibrary.org/obo/MOD_01120	2,2,5,7,8-pentamethylchroman-6-sulfonyl chloride derivatized residue	http://purl.obolibrary.org/obo/MOD_01652	sulfonyl halide reagent 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.
http://purl.obolibrary.org/obo/MOD_01121	monomethoxytrityl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01124	aldohexosyl lysyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01128	N-glycolneuraminic acid	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01130	SucPhencarb Lysyl	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01133	S-12-hydroxyfarnesyl-L-cysteine methyl ester	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-12-hydroxyfarnesyl-L-cysteine methyl ester.
http://purl.obolibrary.org/obo/MOD_01134	fluorescein labelling of peptide N-terminal using NHS ester	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01135	Hex-HexNAc	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01137	N6-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-lysine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		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.
http://purl.obolibrary.org/obo/MOD_01140	diiodinated tyrosine	http://purl.obolibrary.org/obo/MOD_00998	iodinated tyrosine		A protein modification that effectively substitutes two hydrogen atoms of an L-tyrosine residue with two iodine atoms.
http://purl.obolibrary.org/obo/MOD_01141	omega-N-(2,2,5,7,8-pentamethylchroman-6-sulfonyl)-L-arginine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		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.
http://purl.obolibrary.org/obo/MOD_01142	S-15,16-dihydrobiliverdin-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound 15,16-dihydrobiliverdin.
http://purl.obolibrary.org/obo/MOD_01143	15,16-dihydrobiliverdin-bis-L-cysteine	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound 15,16-dihydrobiliverdin.
http://purl.obolibrary.org/obo/MOD_01144	S-(sn-1-2,3-dipalmitoylglycerol)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00116	S-diacylglycerol-L-cysteine		A protein modification that effectively converts an L-cysteine residue to S-(sn-1-2,3-dipalmitoyl-glycerol)cysteine.
http://purl.obolibrary.org/obo/MOD_01145	N-tau-(ADP-ribosyl)diphthamide	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to N-tau-(ADP-ribosyl)diphthamide.
http://purl.obolibrary.org/obo/MOD_01146	S-(6-FAD)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-(6-FAD)-L-cystine.
http://purl.obolibrary.org/obo/MOD_01147	dHex1Hex3HexNAc2 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01151	phosphorylated residue with neutral loss of phosphate	http://purl.obolibrary.org/obo/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 phosphorylated residue with a secondary loss of a neutral trihydrogen phosphate molecular fragment.
http://purl.obolibrary.org/obo/MOD_01153	methylthiolated residue	http://purl.obolibrary.org/obo/MOD_01886	thiolated residue		A protein modification that effectively replaces a hydrogen atom with an methylsulfanyl group (thiomethyl group).
http://purl.obolibrary.org/obo/MOD_01154	pyruvic acid	http://purl.obolibrary.org/obo/MOD_00859	modified residue that can arise from different natural residues		A protein modification that effectively converts a source amino acid to pyruvic acid.
http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process	http://purl.obolibrary.org/obo/MOD_00000	protein modification		Modified amino acid residue derived from a natural amino acid by a real or hypothetical chemical process.
http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified	http://purl.obolibrary.org/obo/MOD_00000	protein modification		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.
http://purl.obolibrary.org/obo/MOD_01158	modified L-selenocysteine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-selenocysteine residue.
http://purl.obolibrary.org/obo/MOD_01159	peptidoglycanated residue	http://purl.obolibrary.org/obo/MOD_00764	glycoconjugated 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.
http://purl.obolibrary.org/obo/MOD_01161	deoxygenated residue	http://purl.obolibrary.org/obo/MOD_01472	reduced residue		A protein modification that effectively removes oxygen atoms from a residue without the removal of hydrogen atoms.
http://purl.obolibrary.org/obo/MOD_01162	fucosylated biantennary	http://purl.obolibrary.org/obo/MOD_00725	complex glycosylation		modification from Unimod N-linked glycosylation
http://purl.obolibrary.org/obo/MOD_01163	guanylated residue	http://purl.obolibrary.org/obo/MOD_00701	nucleotide or nucleic acid modified residue		A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoguanosine through either a phosphodiester or a phosphoramide bond.
http://purl.obolibrary.org/obo/MOD_01164	riboflavin-phosphorylated residue	http://purl.obolibrary.org/obo/MOD_00697	flavin modified 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.
http://purl.obolibrary.org/obo/MOD_01165	adenylated residue	http://purl.obolibrary.org/obo/MOD_00701	nucleotide or nucleic acid modified residue		A protein modification that effectively crosslinks an amino acid residue and 5'-phosphoadenosine through either a phosphodiester or a phosphoramide bond.
http://purl.obolibrary.org/obo/MOD_01166	uridylated residue	http://purl.obolibrary.org/obo/MOD_00701	nucleotide or nucleic acid modified residue		A protein modification that effectively crosslinks an amino acid residue and 5'-phosphouridine through either a phosphodiester or a phosphoramide bond.
http://purl.obolibrary.org/obo/MOD_01167	molybdopterin guanine dinucleotide	http://purl.obolibrary.org/obo/MOD_00744	molybdenum pterin containing modification		modification from Unimod
http://purl.obolibrary.org/obo/MOD_01168	dehydroalanine	http://purl.obolibrary.org/obo/MOD_00859	modified residue that can arise from different natural residues		A protein modification that effectively converts a source amino acid residue to dehydroalanine.
http://purl.obolibrary.org/obo/MOD_01169	L-3-oxoalanine	http://purl.obolibrary.org/obo/MOD_00859	modified residue that can arise from different natural residues		A protein modification that effectively converts a source amino acid residue to L-oxoalanine.
http://purl.obolibrary.org/obo/MOD_01170	pyruvic acid iminylated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively forms a 2-ketoimine of pyruvicacid with a residue amino group.
http://purl.obolibrary.org/obo/MOD_01171	O-acetyl-L-threonine	http://purl.obolibrary.org/obo/MOD_01186	monoacetylated L-threonine		A protein modification that effectively converts an L-threonine residue to O-acetyl-L-threonine.
http://purl.obolibrary.org/obo/MOD_01172	N-alanyl-glycosylsphingolipidinositolethanolamine	http://purl.obolibrary.org/obo/MOD_00901	modified L-alanine residue		A protein modification that effectively converts an L-alanine residue to N-alanyl-glycosylsphingolipidinositolethanolamine.
http://purl.obolibrary.org/obo/MOD_01173	N-asparaginyl-glycosylsphingolipidinositolethanolamine	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylsphingolipidinositolethanolamine.
http://purl.obolibrary.org/obo/MOD_01174	S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively converts an L-cysteine residue to S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)-L-cysteine.
http://purl.obolibrary.org/obo/MOD_01175	S-phycourobilin-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycourobilin.
http://purl.obolibrary.org/obo/MOD_01176	L-dehydrolysinonorleucine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_01177	1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine.
http://purl.obolibrary.org/obo/MOD_01178	S-(aspart-4-yloxy) thiocarbonate	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to S-(aspart-4-yloxy) thiocarbonate.
http://purl.obolibrary.org/obo/MOD_01179	N,N-dimethyl-L-alanine	http://purl.obolibrary.org/obo/MOD_01686	alpha-amino dimethylated residue		A protein modification that effectively converts an L-alanine residue to N,N-dimethyl-L-alanine.
http://purl.obolibrary.org/obo/MOD_01180	2-hydroxyglycine observational artifact	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to 2-hydroxyglycine.
http://purl.obolibrary.org/obo/MOD_01181	L-aspartic acid 4-methyl ester	http://purl.obolibrary.org/obo/MOD_01681	monomethylated L-aspartic acid		A protein modification that effectively converts an L-aspartic acid residue to L-aspartate 4-methyl ester.
http://purl.obolibrary.org/obo/MOD_01182	6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD	http://purl.obolibrary.org/obo/MOD_02048	crosslinked L-histidine residue		A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD.
http://purl.obolibrary.org/obo/MOD_01183	L-selenocystine (oxidized selenocysteine) (Sec-Sec)	http://purl.obolibrary.org/obo/MOD_01158	modified L-selenocysteine residue		A protein modification that effectively cross-links two L-selenocysteine residues to form L-selenocystine,
http://purl.obolibrary.org/obo/MOD_01184	L-selenocystine (selenium disubstituted L-cystine)	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively substitutes two selenium atoms for two sulfur atoms in L-cystine to form L-selenocystine.
http://purl.obolibrary.org/obo/MOD_01185	4-amidated L-aspartic acid	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to L-asparagine.
http://purl.obolibrary.org/obo/MOD_01186	monoacetylated L-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to either N-acetyl-L-threonne, or O-acetyl-Lthreonine.
http://purl.obolibrary.org/obo/MOD_01187	L-pyrrolysine residue	http://purl.obolibrary.org/obo/MOD_00868	natural, non-standard encoded residue		A protein modification that inserts or replaces a residue with an L-pyrrolysine residue, a natural pretranslational modification.
http://purl.obolibrary.org/obo/MOD_01188	N-ethyl iodoacetamide-d5 - site Y	http://purl.obolibrary.org/obo/MOD_00562	N-ethyl iodoacetamide-d5		modification from Unimod Isotopic label -
http://purl.obolibrary.org/obo/MOD_01189	N-ethyl iodoacetamide-d5 - site C	http://purl.obolibrary.org/obo/MOD_00562	N-ethyl iodoacetamide-d5		modification from Unimod Isotopic label -
http://purl.obolibrary.org/obo/MOD_01191	N-ethyl iodoacetamide-d0 - site C	http://purl.obolibrary.org/obo/MOD_00561	N-ethyl iodoacetamide-		modification from Unimod Isotopic label -
http://purl.obolibrary.org/obo/MOD_01192	N-ethyl iodoacetamide-d0 - site Y	http://purl.obolibrary.org/obo/MOD_00561	N-ethyl iodoacetamide-		modification from Unimod Isotopic label -
http://purl.obolibrary.org/obo/MOD_01193	pyridyl thiol modified L-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01194	pyridyl thiol modified L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01195	benzoyl labeling reagent light form - site K	http://purl.obolibrary.org/obo/MOD_00505	benzoyl labeling reagent light form (N-term and K)		modification from Unimod Isotopic label -
http://purl.obolibrary.org/obo/MOD_01197	N-heptosyl-L-glutamine	http://purl.obolibrary.org/obo/MOD_00925	heptosylated residue		A protein modification that effectively converts an L-glutamine residue to N-heptosyl-L-glutamine.
http://purl.obolibrary.org/obo/MOD_01198	O-heptosyl-L-serine	http://purl.obolibrary.org/obo/MOD_00925	heptosylated residue		A protein modification that effectively converts an L-serine residue to O-heptosyl-L-serine.
http://purl.obolibrary.org/obo/MOD_01199	N-heptosyl-L-arginine	http://purl.obolibrary.org/obo/MOD_00925	heptosylated residue		A protein modification that effectively converts an L-arginine residue to an N-heptosyl-L-arginine.
http://purl.obolibrary.org/obo/MOD_01200	O-heptosyl-L-threonine	http://purl.obolibrary.org/obo/MOD_00925	heptosylated residue		A protein modification that effectively converts an L-threonine residue to O-heptosyl-L-threonine.
http://purl.obolibrary.org/obo/MOD_01201	N6-heptosyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00925	heptosylated residue		A protein modification that effectively converts an L-lysine residue to N6-heptosyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01202	N-heptosyl-L-asparagine	http://purl.obolibrary.org/obo/MOD_00925	heptosylated residue		A protein modification that effectively converts an L-asparagine residue to N-heptosyl-L-asparagine.
http://purl.obolibrary.org/obo/MOD_01203	N6-(pyridylacetyl)lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-[(pyrid-3-yl)acetyl]lysine.
http://purl.obolibrary.org/obo/MOD_01205	Hex1HexNAc1NeuAc2 O-glycosylated serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_01206	Hex1HexNAc1NeuAc2 O-glycosylated threonine	http://purl.obolibrary.org/obo/MOD_00528	Hex1HexNAc1NeuAc2 glycosylated residue		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.
http://purl.obolibrary.org/obo/MOD_01207	Hex1HexNAc1NeuAc2 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-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.
http://purl.obolibrary.org/obo/MOD_01208	copper(1+) carboxylate C-terminal residue	http://purl.obolibrary.org/obo/MOD_00742	copper containing modified residue		A protein modification that effectively converts a C-terminal residue to the copper(1+) carboxylate salt.
http://purl.obolibrary.org/obo/MOD_01209	copper(1+) L-aspartate	http://purl.obolibrary.org/obo/MOD_02066	metal or metal cluster coordinated L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to the copper(1+) aspartate salt.
http://purl.obolibrary.org/obo/MOD_01210	copper(1+) L-glutamate	http://purl.obolibrary.org/obo/MOD_02068	metal or metal cluster coordinated L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to the copper(1+) glutamate salt.
http://purl.obolibrary.org/obo/MOD_01211	N6-(morpholine-2-acetyl)-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-(morpholine-2-acetyl)-lysine.
http://purl.obolibrary.org/obo/MOD_01212	iodoacetamide N6-derivatized lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to N6-(carboxamidomethyl)lysine.
http://purl.obolibrary.org/obo/MOD_01213	iodoacetamide derivatized histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to an iodoacetamide derivatized histidine, either 1'- or 3'-(carboxamidolmethyl)histidine.
http://purl.obolibrary.org/obo/MOD_01215	iodoacetamide derivatized aspartic acid	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to O4-(carboxamidomethyl)aspartate.
http://purl.obolibrary.org/obo/MOD_01216	iodoacetamide derivatized glutamic acid	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to O5-(carboxamidomethyl)glutamate.
http://purl.obolibrary.org/obo/MOD_01217	Sulfanilic Acid (SA), light C12 - site D	http://purl.obolibrary.org/obo/MOD_00605	Sulfanilic Acid (SA), light C12		modification from Unimod Isotopic label -
http://purl.obolibrary.org/obo/MOD_01218	Sulfanilic Acid (SA), light C12 - site E	http://purl.obolibrary.org/obo/MOD_00605	Sulfanilic Acid (SA), light C12		modification from Unimod Isotopic label -
http://purl.obolibrary.org/obo/MOD_01219	Sulfanilic Acid (SA), heavy C13 - site D	http://purl.obolibrary.org/obo/MOD_00606	Sulfanilic Acid (SA), heavy C13		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01220	Sulfanilic Acid (SA), heavy C13 - site E	http://purl.obolibrary.org/obo/MOD_00606	Sulfanilic Acid (SA), heavy C13		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01221	O-formyl-L-threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively converts an L-threonine residue to O-formyl-L-threonine.
http://purl.obolibrary.org/obo/MOD_01222	O-formyl-L-serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively converts an L-serine residue to O-formyl-L-serine.
http://purl.obolibrary.org/obo/MOD_01223	thioacylation of primary amines - site N-term	http://purl.obolibrary.org/obo/MOD_00497	3-sulfanylpropanoyl (N-term and Lys)		modification from Unimod Other -
http://purl.obolibrary.org/obo/MOD_01224	thioacylation of primary amines - site K	http://purl.obolibrary.org/obo/MOD_00497	3-sulfanylpropanoyl (N-term and Lys)		modification from Unimod Other -
http://purl.obolibrary.org/obo/MOD_01225	monofluorinated L-tyrosine	http://purl.obolibrary.org/obo/MOD_00985	halogenated tyrosine		A protein modification that effectively converts an L-tyrosine residue into an L-fluorotyrosine.
http://purl.obolibrary.org/obo/MOD_01226	monofluorinated L-tryptophan	http://purl.obolibrary.org/obo/MOD_01068	halogenated tryptophan		A protein modification that effectively converts an L-tryptophan residue to an L-fluorotryptophan.
http://purl.obolibrary.org/obo/MOD_01227	monofluorinated L-phenylalanine	http://purl.obolibrary.org/obo/MOD_01066	halogenated phenylalanine		A protein modification that effectively converts an L-phenylalanine residue to an L-fluorophenylalanine.
http://purl.obolibrary.org/obo/MOD_01228	monoiodinated tyrosine	http://purl.obolibrary.org/obo/MOD_00998	iodinated tyrosine		A protein modification that effectively substitutes one hydrogen atom of an L-tyrosine residue with one iodine atom.
http://purl.obolibrary.org/obo/MOD_01229	L-iodohistidine	http://purl.obolibrary.org/obo/MOD_01049	halogenated histidine		A protein modification that effectively converts an L-histidine residue to an L-iodohistidine.
http://purl.obolibrary.org/obo/MOD_01230	Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form - site K	http://purl.obolibrary.org/obo/MOD_00790	Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, light form		modification from Unimod Isotopic label -
http://purl.obolibrary.org/obo/MOD_01231	3x(13)C labeled N6-propanoyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01428	(13)C isotope tagged reagent		A protein modification that effectively converts an L-lysine residue to 3x(13)C labeled N6-propanoyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01232	3x(12)C labeled N6-propanoyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		A protein modification that effectively converts an L-lysine residue to 3x(12)C labeled N6-propanoyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01233	3x(2)H labeled N6-acetyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00449	acetate labeling reagent (N-term) (heavy form, +3amu)		A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled N6-acetyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01234	(18)O monosubstituted L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate
http://purl.obolibrary.org/obo/MOD_01235	(18)O monosubstituted L-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate
http://purl.obolibrary.org/obo/MOD_01236	(18)O monosubstituted L-tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		modification from Unimod Isotopic label - alkaline phosphatase to dephosphorylate
http://purl.obolibrary.org/obo/MOD_01237	cysteine 4-hydroxynonenal adduct	http://purl.obolibrary.org/obo/MOD_00446	4-hydroxynonenal adduct		A protein modification produced by formation of an adduct of an L-cysteine residue with 4-hydroxynonenal.
http://purl.obolibrary.org/obo/MOD_01238	lysine 4-hydroxynonenal adduct	http://purl.obolibrary.org/obo/MOD_00446	4-hydroxynonenal adduct		A protein modification produced by formation of an adduct of an L-lysine residue with 4-hydroxynonenal.
http://purl.obolibrary.org/obo/MOD_01239	histidine 4-hydroxynonenal adduct	http://purl.obolibrary.org/obo/MOD_00446	4-hydroxynonenal adduct		A protein modification produced by formation of an adduct of an L-histidine residue with 4-hydroxynonenal.
http://purl.obolibrary.org/obo/MOD_01241	3x(2)H labeled L-aspartic acid 4-methyl ester	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled L-aspartic acid 4-methyl ester.
http://purl.obolibrary.org/obo/MOD_01242	3x(2)H labeled L-glutamic acid 5-methyl ester	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-lysine residue to 3x(2)H labeled L-glutamic acid 5-methyl ester.
http://purl.obolibrary.org/obo/MOD_01243	potassium carboxylate C-terminal residue	http://purl.obolibrary.org/obo/MOD_01072	monopotassium salt		A protein modification that effectively converts a C-terminal residue to the potassium carboxylate salt.
http://purl.obolibrary.org/obo/MOD_01244	potassium L-glutamate	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamioc acid residue to the potassium glutamate salt.
http://purl.obolibrary.org/obo/MOD_01245	potassium L-aspartate	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to the potassium aspartate salt.
http://purl.obolibrary.org/obo/MOD_01248	iodouridine monophosphate derivatized tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that is produced by reaction of iodouridine monophosphate with an L-tyrosine residue to form an ether linkage.
http://purl.obolibrary.org/obo/MOD_01249	iodouridine monophosphate derivatized tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that is produced by reaction of iodouridine monophosphate with an L-tryptophan residue.
http://purl.obolibrary.org/obo/MOD_01250	iodouridine monophosphate derivatized phenylalanine	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that is produced by reaction of iodouridine monophosphate with an L-phenylalanine residue.
http://purl.obolibrary.org/obo/MOD_01251	N6-[3-(carboxamidomethylthio)propanoyl]lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-[3-(carboxamidomethylthio)propanoyl]lysine.
http://purl.obolibrary.org/obo/MOD_01253	malondialdehyde lysine adduct (+54 amu)	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Chemical derivative - Malondialdehyde (MDA) adduct
http://purl.obolibrary.org/obo/MOD_01254	4x(2)H labeled dimethylated L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to 4x(2)H labeled dimethylated L-lysine.
http://purl.obolibrary.org/obo/MOD_01255	S-(2-sulfanylethyl)cysteine (Ser)	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to S-(2-sulfanylethyl)cysteine.
http://purl.obolibrary.org/obo/MOD_01256	3-methyl-S-(2-sulfanylethyl)cysteine (Thr)	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to 3-methyl-S-(2-sulfanylethyl)cysteine.
http://purl.obolibrary.org/obo/MOD_01257	6-aminoquinolyl-N-hydroxysuccinimidyl carbamate - site K	http://purl.obolibrary.org/obo/MOD_00547	6-aminoquinolyl-N-hydroxysuccinimidyl carbamate		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01258	N-methylmaleimide modified L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01259	N-methylmaleimide modified L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01272	iminobiotinylation - site K	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01273	O-[4-(2-aminoethyl)benzenesulfonyl] serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-serine residue.
http://purl.obolibrary.org/obo/MOD_01274	N'-[4-(2-aminoethyl)benzenesulfonyl] derivatized histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-histidine residue.
http://purl.obolibrary.org/obo/MOD_01275	N6-[4-(2-aminoethyl)benzenesulfonyl]lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-lysine residue.
http://purl.obolibrary.org/obo/MOD_01276	O4'-[4-(2-aminoethyl)benzenesulfonyl]tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that is produced by formation of an adduct with 4-(2-aminoethyl)benzenesulfonyl fluoride, AEBS, and an L-tyrosine residue.
http://purl.obolibrary.org/obo/MOD_01277	crotonylated L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Other -
http://purl.obolibrary.org/obo/MOD_01278	crotonylated L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Other -
http://purl.obolibrary.org/obo/MOD_01279	crotonylated L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		modification from Unimod Other -
http://purl.obolibrary.org/obo/MOD_01280	EDT-iodo-PEO-biotin - site T	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01281	EDT-iodo-PEO-biotin - site S	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01285	6x(13)C,1x(15)N labeled L-leucine	http://purl.obolibrary.org/obo/MOD_00911	modified L-leucine residue		A protein modification that effectively converts an L-leucine residue to 6x(13)C,1x(15)N isotope labeled L-leucine.
http://purl.obolibrary.org/obo/MOD_01286	6x(13)C,1x(15)N labeled L-isoleucine	http://purl.obolibrary.org/obo/MOD_00910	modified L-isoleucine residue		A protein modification that effectively converts an L-isoleucine residue to 6x(13)C,1x(15)N isotope labeled L-isoleucine.
http://purl.obolibrary.org/obo/MOD_01287	Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, heavy form - site K	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Isotopic label -
http://purl.obolibrary.org/obo/MOD_01293	1x(18)O labeled deamidated L-asparagine	http://purl.obolibrary.org/obo/MOD_00852	1x(18)O labeled deamidated residue		A protein modification that effectively converts an L-asparagine residue to L-aspartic acid with one (18)O.
http://purl.obolibrary.org/obo/MOD_01295	monosodium L-aspartate	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to monosodium L-aspartate.
http://purl.obolibrary.org/obo/MOD_01296	monosodium L-glutamate	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to monosodium L-glutamate.
http://purl.obolibrary.org/obo/MOD_01297	5x(13)C labeled L-proline	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively converts an L-proline residue to 5x(13)C labeled L-proline.
http://purl.obolibrary.org/obo/MOD_01298	reduced cysteine 4-hydroxynonenal adduct	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_01299	reduced lysine 4-hydroxynonenal adduct	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_01300	reduced histidine 4-hydroxynonenal adduct	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_01301	methylamine Michael addition derivatized threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to 2-amino-3-(methylamino)butanoic acid.
http://purl.obolibrary.org/obo/MOD_01302	methylamine Michael addition derivatized serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to 2-amino-3-(methylamino)propanoic acid.
http://purl.obolibrary.org/obo/MOD_01303	N4-hexosaminylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		A protein modification that effectively converts an L-asparagine residue to an N4-hexosaminyl-L-asparagine.
http://purl.obolibrary.org/obo/MOD_01304	N6-hexosaminylated lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to an N4-hexosaminyl-L-lysine, as a synthetic peptide protectting group.
http://purl.obolibrary.org/obo/MOD_01305	N1'-hexosaminylated tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to N1'-hexosaminyl-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01306	O-hexosaminylated threonine	http://purl.obolibrary.org/obo/MOD_00876	hexosaminylated residue		A protein modification that effectively converts an L-threonine residue to O-hexosaminyl-L-threonine.
http://purl.obolibrary.org/obo/MOD_01307	thiophosphate labeled with biotin-HPDP -site S	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01308	thiophosphate labeled with biotin-HPDP -site T	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01309	thiophosphate labeled with biotin-HPDP - site Y	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		modification from Unimod Chemical derivative - 
http://purl.obolibrary.org/obo/MOD_01310	quaternary amine labeling reagent light form N6-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent light form group.
http://purl.obolibrary.org/obo/MOD_01311	quaternary amine labeling reagent heavy form (+3amu) N6-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+3amu) form group.
http://purl.obolibrary.org/obo/MOD_01312	quaternary amine labeling reagent heavy form (+6amu) N6-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+6amu) form group.
http://purl.obolibrary.org/obo/MOD_01313	quaternary amine labeling reagent heavy form (+9amu) N6-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively replaces a lysine N6-hydrogen with a quaternary amine reagent heavy (+9amu) form group.
http://purl.obolibrary.org/obo/MOD_01314	4x(1)H,4x(12)C-labeled N6-succinyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00670	N-acylated residue		A protein modification that effectively converts an L-lysine residue to 4x(1)H,4x(12)C-labeled N6-succinyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01315	4x(2)H labeled N6-succinyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00670	N-acylated residue		A protein modification that effectively converts an L-lysine residue to 4x(2)H-labeled N6-succinyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01316	4x(13)C labeled N6-succinyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00670	N-acylated residue		A protein modification that effectively converts an L-lysine residue to 4x(13)C labeled N6-succinyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01317	phosphorylation to amine thiol - site T	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01318	phosphorylation to amine thiol - site S	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01319	Michael addition of BHT quinone methide to histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		modification from Unimod Other
http://purl.obolibrary.org/obo/MOD_01320	Michael addition of BHT quinone methide to lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Other
http://purl.obolibrary.org/obo/MOD_01321	Michael addition of BHT quinone methide to cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Other
http://purl.obolibrary.org/obo/MOD_01326	9x(13)C labeled L-tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an L-tyrosine residue to 9x(13)C labeled L-tyrosine.
http://purl.obolibrary.org/obo/MOD_01327	9x(13)C labeled L-phenylalanine	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively converts an L-phenylalanine residue to 9x(13)C labeled L-phenylalanine.
http://purl.obolibrary.org/obo/MOD_01328	iodoacetic acid - site W	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		modification from Unimod Chemical derivative - hydroxylethanone
http://purl.obolibrary.org/obo/MOD_01331	6x(13)C labeled L-arginine	http://purl.obolibrary.org/obo/MOD_00544	6x(13)C labeled residue		A protein modification that effectively converts an L-arginine residue to 6x(13)C labeled L-arginine.
http://purl.obolibrary.org/obo/MOD_01332	6x(13)C labeled L-leucine	http://purl.obolibrary.org/obo/MOD_00544	6x(13)C labeled residue		A protein modification that effectively converts an L-leucine residue to 6x(13)C labeled L-leucine.
http://purl.obolibrary.org/obo/MOD_01333	6x(13)C labeled L-isoleucine	http://purl.obolibrary.org/obo/MOD_00544	6x(13)C labeled residue		A protein modification that effectively converts an L-isoleucine residue to 6x(13)C labeled L-isoleucine.
http://purl.obolibrary.org/obo/MOD_01334	6x(13)C labeled L-lysine	http://purl.obolibrary.org/obo/MOD_00544	6x(13)C labeled residue		A protein modification that effectively converts an L-lysine residue to 6x(13)C labeled L-lysine.
http://purl.obolibrary.org/obo/MOD_01335	6x(13)C labeled 4-sulfophenyl isothiocyanate derivatized lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01337	deamidated 4-methyl esterified asparagine	http://purl.obolibrary.org/obo/MOD_01369	deamidated and methyl esterified residue		A protein modification that effectively converts an L-asparagine residue to L-aspartate 4-methyl ester.
http://purl.obolibrary.org/obo/MOD_01338	N6-ethyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to N6-ethyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01339	ethylated residue	http://purl.obolibrary.org/obo/MOD_00001	alkylated residue		A protein modification that effectively replaces a hydrogen atom with an ethyl group.
http://purl.obolibrary.org/obo/MOD_01340	ESP-Tag heavy d10 - site K	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Isotopic label -
http://purl.obolibrary.org/obo/MOD_01341	ESP-Tag light d0 - site K	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Isotopic label -
http://purl.obolibrary.org/obo/MOD_01345	2-amino-3-oxobutanoic acid	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to 2-amino-3-oxobutanoic acid.
http://purl.obolibrary.org/obo/MOD_01346	N4-hexosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		A protein modification that effectively converts an L-asparagine residue to an N4-hexosyl-L-asparagine.
http://purl.obolibrary.org/obo/MOD_01347	hexose glycated L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_01348	O-hexosylated threonine	http://purl.obolibrary.org/obo/MOD_00434	hexosylated residue		A protein modification that effectively converts an L-threonine residue to an O-hexosyl-L-threonine.
http://purl.obolibrary.org/obo/MOD_01349	hydrolyzed N-ethylmaleimide cysteine adduct	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01350	hydrolyzed N-ethylmaleimide lysine adduct	http://purl.obolibrary.org/obo/MOD_00631	hydrolyzed N-ethylmaleimide adduct		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01351	nitrated L-tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to a nitrated L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01353	amidination of lysines or N-terminal amines with methyl acetimidate - site K	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01354	Hex1HexNAc1NeuAc1 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-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.
http://purl.obolibrary.org/obo/MOD_01355	Hex1HexNAc1NeuAc1 O-glycosylated threonine	http://purl.obolibrary.org/obo/MOD_00517	Hex1HexNAc1NeuAc1 glycosylated residue		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.
http://purl.obolibrary.org/obo/MOD_01356	Hex1HexNAc1NeuAc1 O-glycosylated serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_01357	2x(13)C,4x(2)H labeled dimethylated L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_01358	Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form - site N-term	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		modification from Unimod Isotopic label - Use when labelling post-digest
http://purl.obolibrary.org/obo/MOD_01359	Bruker Daltonics SERVA-ICPL(TM) quantification chemistry, medium form - site K	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Isotopic label - Use when labelling post-digest
http://purl.obolibrary.org/obo/MOD_01360	4-sulfophenyl isothiocyanate N6-derivatized lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to the 4-sulfophenyl isothiocyanate adduct, N6-[(4-sulfophenyl)carbamothioyl]lysine.
http://purl.obolibrary.org/obo/MOD_01361	O-thiophospho-L-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to O-thiophospho-L-threonine.
http://purl.obolibrary.org/obo/MOD_01362	O-thiophospho-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-thiophospho-L-serine.
http://purl.obolibrary.org/obo/MOD_01363	O4'-thiophospho-L-tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an L-tyrosine residue to O4'-thiophospho-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_01364	fluorescein-5-thiosemicarbazide - site S	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01365	fluorescein-5-thiosemicarbazide - site C	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01366	fluorescein-5-thiosemicarbazide - site K	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01367	fluorescein-5-thiosemicarbazide - site P	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01368	fluorescein-5-thiosemicarbazide - site R	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		modification from Unimod Chemical derivative -
http://purl.obolibrary.org/obo/MOD_01369	deamidated and methyl esterified residue	http://purl.obolibrary.org/obo/MOD_00393	O-methylated residue		A protein modification that effectively replaces a carboxamido group with a carboxyl methyl ester group.
http://purl.obolibrary.org/obo/MOD_01370	6x(13)C,1x(15)N labeled residue	http://purl.obolibrary.org/obo/MOD_00843	(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.
http://purl.obolibrary.org/obo/MOD_01372	(2S)-4-hydroxyleucine	http://purl.obolibrary.org/obo/MOD_01411	monohydroxylated leucine		A protein modification that effectively converts an L-leucine residue to a (2S)-4-hydroxyleucine.
http://purl.obolibrary.org/obo/MOD_01373	(2S,4R)-5-hydroxyleucine	http://purl.obolibrary.org/obo/MOD_01411	monohydroxylated leucine		A protein modification that effectively converts an L-leucine residue to a (2S,4R)-5-hydroxyleucine.
http://purl.obolibrary.org/obo/MOD_01374	(2S,4R)-5-oxoleucine	http://purl.obolibrary.org/obo/MOD_00911	modified L-leucine residue		A modification that effectively oxygenates C5 of an L-leucine residue to form a (2S,4R)-5-oxoleucine.
http://purl.obolibrary.org/obo/MOD_01375	(2S,4R)-4,5-dihydroxyleucine	http://purl.obolibrary.org/obo/MOD_01412	dihydroxylated leucine		A protein modification that effectively converts an L-leucine residue to a (2S,4R)-4,5-dihydroxyleucine.
http://purl.obolibrary.org/obo/MOD_01376	(2S,3S,4R)-3,4-dihydroxyisoleucine	http://purl.obolibrary.org/obo/MOD_01416	dihydroxylated isoleucine		A protein modification that effectively converts an L-isoleucine residue to a (2S,3S,4R)-3,4-dihydroxyisoleucine.
http://purl.obolibrary.org/obo/MOD_01377	(2S,3R,4S)-4-hydroxyisoleucine	http://purl.obolibrary.org/obo/MOD_01415	monohydroxylated isoleucine		A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4S)-4-hydroxyisoleucine.
http://purl.obolibrary.org/obo/MOD_01378	(2S,3R,4R)-4,5-dihydroxyisoleucine	http://purl.obolibrary.org/obo/MOD_01416	dihydroxylated isoleucine		A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4R)-4,5-dihydroxyisoleucine.
http://purl.obolibrary.org/obo/MOD_01379	2'-methylsulfonyl-L-tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to 2'-methylsulfonyl-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01380	2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide	http://purl.obolibrary.org/obo/MOD_02057	crosslinked L-tryptophan residue		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.
http://purl.obolibrary.org/obo/MOD_01381	O-palmitoleyl-L-serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively converts an L-serine residue to O-palmitoleyl-L-serine.
http://purl.obolibrary.org/obo/MOD_01382	N,N,N-trimethyl-L-methionine	http://purl.obolibrary.org/obo/MOD_01698	alpha-amino trimethylated protonated-residue		A protein modification that effectively converts an L-methionine residue to N,N,N-trimethyl-L-methionine.
http://purl.obolibrary.org/obo/MOD_01383	L-cystine S-oxide	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		A protein modification that effectively cross-links two L-cysteine residues and oxidizes a sulfur to form L-cystine S-oxide.
http://purl.obolibrary.org/obo/MOD_01384	aminomalonic acid (Ser)	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to an aminomalonic acid.
http://purl.obolibrary.org/obo/MOD_01385	3-hydroxy-L-phenylalanine	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively converts an L-phenylalanine residue to 3-hydroxy-L-phenylalanine.
http://purl.obolibrary.org/obo/MOD_01386	3-hydroxy-L-valine	http://purl.obolibrary.org/obo/MOD_00920	modified L-valine residue		A protein modification that effectively converts an L-valine residue to 3-hydroxy-L-valine.
http://purl.obolibrary.org/obo/MOD_01387	O-methyl-L-threonine	http://purl.obolibrary.org/obo/MOD_01803	O-methylated threonine		A protein modification that effectively converts an L-threonine residue to O-methyl-L-threonine.
http://purl.obolibrary.org/obo/MOD_01388	1-amino-2-propanol	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue into 1-amino-2-propanol.
http://purl.obolibrary.org/obo/MOD_01389	L-isoleucine thiazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02049	crosslinked L-isoleucine residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-isoleucine residue to form L-isoleucine thiazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01390	L-valine thiazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02059	crosslinked L-valine residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-valine residue to form L-valine thiazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01391	L-valine 5-(methoxymethyl)thiazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02059	crosslinked L-valine residue		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.
http://purl.obolibrary.org/obo/MOD_01392	L-asparagine 5-methylthiazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02042	crosslinked L-asparagine residue		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.
http://purl.obolibrary.org/obo/MOD_01393	L-cysteine pyridine-2,5-dicarboxylic acid	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		A protein modification that crosslinks two serine residues and a cysteine residue by formation of a pyridine-2,5-dicarboxylic acid.
http://purl.obolibrary.org/obo/MOD_01394	L-cysteine 5-amino-3,4,5,6-tetrahydropyridine-2,5-dicarboxylic acid	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_01395	4-(1-hydroxyethyl)-7-isoleucino-2-(threonin-O3-ylcarbonyl)-7,8-dihydroquinolin-8-ol	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_01396	5-hydroxy-3-methyl-L-proline (Pro)	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively converts an L-proline residue to a 5-hydroxy-3-methyl-L-proline.
http://purl.obolibrary.org/obo/MOD_01397	L-serine 5-methyloxazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		A protein modification that effectively crosslinks an L-serine residue and an L-threonine residue to form L-serine 5-methyloxazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01398	N6-propanoyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively converts an L-lysine residue to N6-propanoyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01400	L-lysyl-poly(ADP-ribose)	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to an L-lysyl-poly(ADP-ribose).
http://purl.obolibrary.org/obo/MOD_01401	(2S,3S)-3-hydroxyasparagine	http://purl.obolibrary.org/obo/MOD_01688	3-hydroxy-L-asparagine		A protein modification that effectively converts an L-asparagine residue to a (2S,3S)-3-hydroxyasparagine.
http://purl.obolibrary.org/obo/MOD_01402	(2S,3R,4R)-3,4-dihydroxyproline	http://purl.obolibrary.org/obo/MOD_00866	dihydroxylated proline		A protein modification that effectively converts an L-proline residue to a (2S,3R,4R)-3,4-dihydroxyproline.
http://purl.obolibrary.org/obo/MOD_01403	(2S)-4,5,5'-trihydroxyleucine	http://purl.obolibrary.org/obo/MOD_01413	trihydroxylated leucine		A protein modification that effectively converts an L-leucine residue to a (2S)-4,5,5'-trihydroxyleucine.
http://purl.obolibrary.org/obo/MOD_01404	L-asparagine thiazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02042	crosslinked L-asparagine residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-asparagine residue to form L-asparagine thiazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01405	L-proline thiazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02054	crosslinked L-proline residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-proline residue to form L-proline thiazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01406	L-threonine thiazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-threonine thiazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01407	L-phenylalanine thiazoline-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02053	crosslinked L-phenylalanine residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazoline-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01408	L-threonine thiazoline-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-threonine thiazoline-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01409	trihydroxylated residue	http://purl.obolibrary.org/obo/MOD_00677	hydroxylated residue		A protein modification that effectively replaces three hydrogen atoms with three hydroxyl groups.
http://purl.obolibrary.org/obo/MOD_01410	hydroxylated leucine	http://purl.obolibrary.org/obo/MOD_00911	modified L-leucine residue		A protein modification that effectively converts an L-leucine residue to an hydroxylated leucine.
http://purl.obolibrary.org/obo/MOD_01411	monohydroxylated leucine	http://purl.obolibrary.org/obo/MOD_01410	hydroxylated leucine		A protein modification that effectively converts an L-leucine residue to a monohydroxylated leucine.
http://purl.obolibrary.org/obo/MOD_01412	dihydroxylated leucine	http://purl.obolibrary.org/obo/MOD_01410	hydroxylated leucine		A protein modification that effectively converts an L-leucine residue to a dihydroxylated leucine.
http://purl.obolibrary.org/obo/MOD_01413	trihydroxylated leucine	http://purl.obolibrary.org/obo/MOD_01410	hydroxylated leucine		A protein modification that effectively converts an L-leucine residue to a trihydroxylated leucine.
http://purl.obolibrary.org/obo/MOD_01414	hydroxylated isoleucine	http://purl.obolibrary.org/obo/MOD_00910	modified L-isoleucine residue		A protein modification that effectively converts an L-isoleucine residue to an hydroxylated isoleucine.
http://purl.obolibrary.org/obo/MOD_01415	monohydroxylated isoleucine	http://purl.obolibrary.org/obo/MOD_01414	hydroxylated isoleucine		A protein modification that effectively converts an L-isoleucine residue to a monohydroxylated isoleucine.
http://purl.obolibrary.org/obo/MOD_01416	dihydroxylated isoleucine	http://purl.obolibrary.org/obo/MOD_01414	hydroxylated isoleucine		A protein modification that effectively converts an L-isoleucine residue to a dihydroxylated isoleucine.
http://purl.obolibrary.org/obo/MOD_01417	monomethylated proline	http://purl.obolibrary.org/obo/MOD_00599	monomethylated residue		A protein modification that effectively converts an L-proline residue to a monomethylated proline.
http://purl.obolibrary.org/obo/MOD_01418	methylated threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to a methylated threonine, such as O-methyl-L-threonine.
http://purl.obolibrary.org/obo/MOD_01419	oxazole/oxazoline ring crosslinked residues	http://purl.obolibrary.org/obo/MOD_00690	oxazole/thiazole 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.
http://purl.obolibrary.org/obo/MOD_01420	thiazole/thiazoline ring crosslinked residues	http://purl.obolibrary.org/obo/MOD_00690	oxazole/thiazole 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.
http://purl.obolibrary.org/obo/MOD_01421	oxazole/oxazoline ring crosslinked residues (Ser)	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_01422	oxazole/oxazoline ring crosslinked residues (Thr)	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_01423	palmitoleylated residue	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively replaces a hydrogen atom with a palmitoleyl group.
http://purl.obolibrary.org/obo/MOD_01424	quinaldate modified residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively results from forming an adduct with a compound containing a quinaldate, kynurenate, or xanthurenate group.
http://purl.obolibrary.org/obo/MOD_01425	pyridinyl ring crosslinked residues	http://purl.obolibrary.org/obo/MOD_00033	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.
http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that forms an adduct with a particular isotope labeled compound used as a reagent.
http://purl.obolibrary.org/obo/MOD_01428	(13)C isotope tagged reagent	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		A protein modification that forms an adduct with a (13)C labeled compound used as a reagent.
http://purl.obolibrary.org/obo/MOD_01429	(15)N isotope tagged reagent	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		A protein modification that forms an adduct with a (15)N labeled compound used as a reagent.
http://purl.obolibrary.org/obo/MOD_01430	(18)O isotope tagged reagent	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		A protein modification that forms an adduct with a (13)C labeled compound used as a reagent.
http://purl.obolibrary.org/obo/MOD_01431	(2)H deuterium tagged reagent	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		A protein modification that forms an adduct with a (2)H labeled compound used as a reagent.
http://purl.obolibrary.org/obo/MOD_01432	(2S,4S)-4,5-dihydroxyleucine	http://purl.obolibrary.org/obo/MOD_01412	dihydroxylated leucine		A protein modification that effectively converts an L-leucine residue to a (2S,4S)-4,5-dihydroxyleucine.
http://purl.obolibrary.org/obo/MOD_01433	1-amino-2-propanone	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue into 1-amino-2-propanone.
http://purl.obolibrary.org/obo/MOD_01434	4-hydroxy-L-glutamic acid	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to a 4-hydroxy-L-glutamic acid.
http://purl.obolibrary.org/obo/MOD_01435	2-(cystein-S-ylcarbonyl)-3-methyl-4-(glutam-5-yloxy)methylindole	http://purl.obolibrary.org/obo/MOD_02045	crosslinked L-glutamic acid residue		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.
http://purl.obolibrary.org/obo/MOD_01436	cyclo[(prolylserin)-O-yl] cysteinate (Cys)	http://purl.obolibrary.org/obo/MOD_01629	cyclo[(prolylserin)-O-yl] cysteinate		A protein modification that effectively converts an L-cysteine residue to cyclo[(prolylserin)-O-yl] cysteinate.
http://purl.obolibrary.org/obo/MOD_01437	cyclo[(prolylserin)-O-yl] cysteinate (Cys-Pro-Ser cross-link)	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_01438	S-[2-(pyridin-2-yl)ethyl]-L-cysteine	http://purl.obolibrary.org/obo/MOD_00424	S-pyridylethyl-L-cysteine		A protein modification that effectively converts an L-cysteine residue to S-[2-(pyridin-2-yl)ethyl]-L-cysteine.
http://purl.obolibrary.org/obo/MOD_01439	S-[2-(pyridin-4-yl)ethyl]-L-cysteine	http://purl.obolibrary.org/obo/MOD_00424	S-pyridylethyl-L-cysteine		A protein modification that effectively converts an L-cysteine residue to S-[2-(pyridin-4-yl)ethyl]-L-cysteine.
http://purl.obolibrary.org/obo/MOD_01440	glutamyl semialdehyde	http://purl.obolibrary.org/obo/MOD_00859	modified residue that can arise from different natural residues		A protein modification that effectively converts a source amino acid residue to an L-glutamyl semialdehyde.
http://purl.obolibrary.org/obo/MOD_01441	natural, standard, encoded residue	http://purl.obolibrary.org/obo/MOD_00009	natural residue		A protein modification that inserts or replaces a residue with a natural, standard, encoded residue.
http://purl.obolibrary.org/obo/MOD_01442	3-(O4'-L-tyrosyl)-L-valine	http://purl.obolibrary.org/obo/MOD_02059	crosslinked L-valine residue		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.
http://purl.obolibrary.org/obo/MOD_01443	tetrakis-L-glutamato bis-L-N1'-histidino lipid carboxylato manganese iron oxide	http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue		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.
http://purl.obolibrary.org/obo/MOD_01444	L-3,3-dihydroxyoalanine (Cys)	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to L-3,3-dihydroxyoalanine.
http://purl.obolibrary.org/obo/MOD_01445	L-3,3-dihydroxyoalanine (Ser)	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to L-3,3-dihydroxyoalanine.
http://purl.obolibrary.org/obo/MOD_01446	N-(dihydroxymethyl)-L-methionine (fMet)	http://purl.obolibrary.org/obo/MOD_01450	modified N-formyl-L-methionine residue		A protein modification that effectively converts an N-formyl-Lmethionine residue to N-(dihydroxymethyl)-L-methionine.
http://purl.obolibrary.org/obo/MOD_01447	N-(dihydroxymethyl)-L-methionine (Met)	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine residue to N-(dihydroxymethyl)-L-methionine (not known as a natural, post-translational modification process).
http://purl.obolibrary.org/obo/MOD_01448	L-3,3-dihydroxyoalanine	http://purl.obolibrary.org/obo/MOD_00859	modified residue that can arise from different natural residues		A protein modification that effectively converts a source amino acid residue to L-3,3-dihydroxyoalanine.
http://purl.obolibrary.org/obo/MOD_01449	L-3,3-dihydroxyoalanine (Oxoalanine)	http://purl.obolibrary.org/obo/MOD_01448	L-3,3-dihydroxyoalanine		A protein modification that effectively converts an L-3-oxoalanine residue to L-3,3-dihydroxyoalanine.
http://purl.obolibrary.org/obo/MOD_01450	modified N-formyl-L-methionine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an N-formyl-L-methionine residue.
http://purl.obolibrary.org/obo/MOD_01451	O-phospho-L-serine arising from O-phosphopantetheine-L-serine after neutral loss of pantetheine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_01452	O-phosphopantetheine-L-serine with neutral loss of pantetheine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_01453	L-glutamic acid 5-methyl ester	http://purl.obolibrary.org/obo/MOD_00599	monomethylated residue		A protein modification that effectively converts a source amino acid residue to L-glutamate 5-methyl ester.
http://purl.obolibrary.org/obo/MOD_01454	N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		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.
http://purl.obolibrary.org/obo/MOD_01455	O-phosphorylated residue	http://purl.obolibrary.org/obo/MOD_00696	phosphorylated residue		A protein modification that effectively replaces a residue hydroxyl or carboxyl hydrogen with a phosphono group (H2PO3 or 'phosphate').
http://purl.obolibrary.org/obo/MOD_01456	N-phosphorylated residue	http://purl.obolibrary.org/obo/MOD_00696	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').
http://purl.obolibrary.org/obo/MOD_01457	L-cysteine (Ser)	http://purl.obolibrary.org/obo/MOD_02088	natural, standard, encoded residue substitution		A protein modification that effectively converts an L-serine residue to L-cysteine (not known as a natural, post-translational modification process).
http://purl.obolibrary.org/obo/MOD_01458	alpha-amino acetylated residue	http://purl.obolibrary.org/obo/MOD_01696	alpha-amino acylated residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acetyl group.
http://purl.obolibrary.org/obo/MOD_01459	4x(2)H labeled alpha-dimethylamino N-terminal residue	http://purl.obolibrary.org/obo/MOD_00552	4x(2)H labeled dimethylated residue		A protein modification that effectively converts an N-terminal residue to an 4x(2)H labeled alpha-dimethylamino N-terminal residue.
http://purl.obolibrary.org/obo/MOD_01460	alpha-amino methylated residue	http://purl.obolibrary.org/obo/MOD_00602	N-methylated residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a methyl group.
http://purl.obolibrary.org/obo/MOD_01461	N-methylated alanine	http://purl.obolibrary.org/obo/MOD_01460	alpha-amino methylated residue		A protein modification that effectively replaces an L-alanine alpha amino hydrogen with a methyl group.
http://purl.obolibrary.org/obo/MOD_01462	N-methylated proline	http://purl.obolibrary.org/obo/MOD_01460	alpha-amino methylated residue		A protein modification that effectively replaces an L-proline alpha imino hydrogen with a methyl group.
http://purl.obolibrary.org/obo/MOD_01463	N-methylated methionine	http://purl.obolibrary.org/obo/MOD_01460	alpha-amino methylated residue		A protein modification that effectively replaces an L-methionine alpha amino hydrogen with a methyl group.
http://purl.obolibrary.org/obo/MOD_01464	protonated L-methionine (L-methioninium) residue	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine residue to an L-methioninium (protonated L-methionine).
http://purl.obolibrary.org/obo/MOD_01465	N,N,N-trimethyl-L-methionine (from L-methioninium)	http://purl.obolibrary.org/obo/MOD_01687	alpha-amino trimethylated residue		A protein modification that effectively converts an L-methioninium (protonated L-methionine) residue to an N6,N6,N6-trimethyl-L-methionine.
http://purl.obolibrary.org/obo/MOD_01466	menadione quinone derivative - site C	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_01467	menadione quinone derivative - site K	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_01468	L-selenocysteinyl molybdenum bis(molybdopterin guanine dinucleotide) (Cys)	http://purl.obolibrary.org/obo/MOD_02073	metal or metal cluster coordinated L-selenocysteine residue		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).
http://purl.obolibrary.org/obo/MOD_01469	L-selenocysteinyl tungsten bis(molybdopterin guanine dinucleotide) (Cys)	http://purl.obolibrary.org/obo/MOD_02073	metal or metal cluster coordinated L-selenocysteine residue		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).
http://purl.obolibrary.org/obo/MOD_01470	(E)-dehydrobutyrine (Thr)	http://purl.obolibrary.org/obo/MOD_00190	dehydrobutyrine (Thr)		A protein modification that effectively converts an L-threonine residue to (E)-dehydrobutyrine.
http://purl.obolibrary.org/obo/MOD_01471	(Z)-dehydrobutyrine (Thr)	http://purl.obolibrary.org/obo/MOD_00190	dehydrobutyrine (Thr)		A protein modification that effectively converts an L-threonine residue to (Z)-dehydrobutyrine.
http://purl.obolibrary.org/obo/MOD_01472	reduced residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		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.
http://purl.obolibrary.org/obo/MOD_01473	hydrogenated residue	http://purl.obolibrary.org/obo/MOD_01472	reduced residue		A protein modification that effectively adds neutral hydrogen atoms (proton and electron) to a residue.
http://purl.obolibrary.org/obo/MOD_01474	O-[S-(carboxymethyl)phosphopantetheine]-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-[S-(carboxymethyl)phosphopantetheine]-L-serine.
http://purl.obolibrary.org/obo/MOD_01475	O-[S-(carboxamidomethyl)phosphopantetheine]-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-[S-(carboxamidomethyl)phosphopantetheine]-L-serine.
http://purl.obolibrary.org/obo/MOD_01476	2'-fluoro-L-phenylalanine	http://purl.obolibrary.org/obo/MOD_01227	monofluorinated L-phenylalanine		A protein modification that effectively converts an L-phenylalanine residue to an 2'-fluoro-L-fluorophenylalanine.
http://purl.obolibrary.org/obo/MOD_01477	3'-fluoro-L-phenylalanine	http://purl.obolibrary.org/obo/MOD_01227	monofluorinated L-phenylalanine		A protein modification that effectively converts an L-phenylalanine residue to an 3'-fluoro-L-fluorophenylalanine.
http://purl.obolibrary.org/obo/MOD_01478	4'-fluoro-L-phenylalanine	http://purl.obolibrary.org/obo/MOD_01227	monofluorinated L-phenylalanine		A protein modification that effectively converts an L-phenylalanine residue into an 4'-fluoro-L-fluorophenylalanine.
http://purl.obolibrary.org/obo/MOD_01479	4'-fluoro-L-tryptophan	http://purl.obolibrary.org/obo/MOD_01226	monofluorinated L-tryptophan		A protein modification that effectively converts an L-tryptophan residue into an 4'-fluoro-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01480	5'-fluoro-L-tryptophan	http://purl.obolibrary.org/obo/MOD_01226	monofluorinated L-tryptophan		A protein modification that effectively converts an L-tryptophan residue into an 5'-fluoro-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01481	6'-fluoro-L-tryptophan	http://purl.obolibrary.org/obo/MOD_01226	monofluorinated L-tryptophan		A protein modification that effectively converts an L-tryptophan residue into an 6'-fluoro-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01482	calcium containing modified residue	http://purl.obolibrary.org/obo/MOD_00698	metal or metal cluster 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.
http://purl.obolibrary.org/obo/MOD_01483	O-formylated residue	http://purl.obolibrary.org/obo/MOD_00671	O-acylated residue		A protein modification that effectively replaces a residue hydroxyl group with a formyloxy group.
http://purl.obolibrary.org/obo/MOD_01484	N6-(L-isoglutamyl)-L-lysine (Glu)	http://purl.obolibrary.org/obo/MOD_02045	crosslinked L-glutamic acid residue		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.
http://purl.obolibrary.org/obo/MOD_01485	iTRAQ4plex-114 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01518	iTRAQ4plex 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.
http://purl.obolibrary.org/obo/MOD_01486	iTRAQ4plex-114 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01711	iTRAQ4plex 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.
http://purl.obolibrary.org/obo/MOD_01487	iTRAQ4plex-114 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01488	iTRAQ4plex-114 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01489	iTRAQ4plex-114 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01490	iTRAQ4plex-114 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01491	iTRAQ4plex-114 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-114 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01492	iTRAQ4plex-115 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01518	iTRAQ4plex 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.
http://purl.obolibrary.org/obo/MOD_01493	iTRAQ4plex-115 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01711	iTRAQ4plex 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.
http://purl.obolibrary.org/obo/MOD_01494	iTRAQ4plex-115 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01495	iTRAQ4plex-115 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01496	iTRAQ4plex-115 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01497	iTRAQ4plex-115 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01498	iTRAQ4plex-115 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-115 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01499	iTRAQ4plex-116 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01518	iTRAQ4plex 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.
http://purl.obolibrary.org/obo/MOD_01500	iTRAQ4plex-116 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01711	iTRAQ4plex 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.
http://purl.obolibrary.org/obo/MOD_01501	iTRAQ4plex-116 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01502	iTRAQ4plex-116 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01503	iTRAQ4plex-116 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01504	iTRAQ4plex-116 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01505	iTRAQ4plex-116 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-116 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01506	iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01863	mTRAQ 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.
http://purl.obolibrary.org/obo/MOD_01507	iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01711	iTRAQ4plex 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.
http://purl.obolibrary.org/obo/MOD_01508	iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01509	iTRAQ4plex-117, mTRAQ heavy, reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01510	iTRAQ4plex-117 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01511	iTRAQ4plex-117 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01512	iTRAQ4plex-117 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ4plex-117 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01513	modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.1 Da	http://purl.obolibrary.org/obo/MOD_00538	protein modification categorized by isobaric sets		Modifications that have monoisotopic mass differences from their respective origins that are nominally equal (sometimes called isobaric) at a resolution below 0.1 Da.
http://purl.obolibrary.org/obo/MOD_01514	modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.01 Da	http://purl.obolibrary.org/obo/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 0.01 Da.
http://purl.obolibrary.org/obo/MOD_01515	modifications with monoisotopic mass differences that are nominally equal at a resolution below 0.000001 Da	http://purl.obolibrary.org/obo/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 0.000001 Da.
http://purl.obolibrary.org/obo/MOD_01516	modifications with monoisotopic mass diferences that are nominally equal at 144.099-144.106 Da.	http://purl.obolibrary.org/obo/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 of 144.099-144.106 Da.
http://purl.obolibrary.org/obo/MOD_01517	modifications with monoisotopic mass differences that are nominally equal at 144.102062 Da	http://purl.obolibrary.org/obo/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 144.102062 Da.
http://purl.obolibrary.org/obo/MOD_01518	iTRAQ4plex reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01705	isotope tagged 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.
http://purl.obolibrary.org/obo/MOD_01519	reporter fragment	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A distinct molecular entity produced from a protein or a protein modification as the result of a fragmentation process.
http://purl.obolibrary.org/obo/MOD_01520	modification reporter fragment	http://purl.obolibrary.org/obo/MOD_01519	reporter fragment		A distinct molecular entity produced as the result of a fragmentation process performed on a particular modified residue.
http://purl.obolibrary.org/obo/MOD_01521	iTRAQ4plex reporter fragment	http://purl.obolibrary.org/obo/MOD_01520	modification reporter fragment		A protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01522	iTRAQ4plex-114 reporter fragment	http://purl.obolibrary.org/obo/MOD_01521	iTRAQ4plex reporter fragment		The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 114 reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01523	iTRAQ4plex-115 reporter fragment	http://purl.obolibrary.org/obo/MOD_01521	iTRAQ4plex reporter fragment		The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 115 reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01524	iTRAQ4plex-116 reporter fragment	http://purl.obolibrary.org/obo/MOD_01521	iTRAQ4plex reporter fragment		The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 116 reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01525	iTRAQ4plex-117, mTRAQ heavy, reporter fragment	http://purl.obolibrary.org/obo/MOD_01870	mTRAQ reporter fragment		The protein modification reporter fragment produced by an Applied Biosystems iTRAQ4plex 117 reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01526	iTRAQ8plex reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01705	isotope tagged 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.
http://purl.obolibrary.org/obo/MOD_01527	residue reporter fragment	http://purl.obolibrary.org/obo/MOD_01519	reporter fragment		A distinct molecular entity produced from a particular amino acid residue as the result of a fragmentation process.
http://purl.obolibrary.org/obo/MOD_01528	iTRAQ8plex-113 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01591	modifications with monoisotopic mass differences that are nominally equal at 304.205359 Da		A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01529	iTRAQ8plex-113 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01712	iTRAQ8plex 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.
http://purl.obolibrary.org/obo/MOD_01530	iTRAQ8plex-113 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01531	iTRAQ8plex-113 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01532	iTRAQ8plex-113 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01533	iTRAQ8plex-113 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01534	iTRAQ8plex-113 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-113 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01535	iTRAQ8plex-114 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01591	modifications with monoisotopic mass differences that are nominally equal at 304.205359 Da		A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01536	iTRAQ8plex-114 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01712	iTRAQ8plex 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.
http://purl.obolibrary.org/obo/MOD_01537	iTRAQ8plex-114 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01538	iTRAQ8plex-114 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01539	iTRAQ8plex-114 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01540	iTRAQ8plex-114 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01541	iTRAQ8plex-114 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-114 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01542	iTRAQ8plex-115 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01584	modifications with monoisotopic mass differences that are nominally equal at 304.199039 Da		A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01543	iTRAQ8plex-115 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01712	iTRAQ8plex 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.
http://purl.obolibrary.org/obo/MOD_01544	iTRAQ8plex-115 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01545	iTRAQ8plex-115 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01546	iTRAQ8plex-115 reporter+balance reagent N'-derivatized histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01547	iTRAQ8plex-115 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01548	iTRAQ8plex-115 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-115 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01549	iTRAQ8plex-116 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01591	modifications with monoisotopic mass differences that are nominally equal at 304.205359 Da		A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01550	iTRAQ8plex-116 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01712	iTRAQ8plex 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.
http://purl.obolibrary.org/obo/MOD_01551	iTRAQ8plex-116 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01552	iTRAQ8plex-116 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01553	iTRAQ8plex-116 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01554	iTRAQ8plex-116 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01555	iTRAQ8plex-116 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-116 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01556	iTRAQ8plex-117 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01591	modifications with monoisotopic mass differences that are nominally equal at 304.205359 Da		A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01557	iTRAQ8plex-117 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01712	iTRAQ8plex 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.
http://purl.obolibrary.org/obo/MOD_01558	iTRAQ8plex-117 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01559	iTRAQ8plex-117 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01560	iTRAQ8plex-117 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01561	iTRAQ8plex-117 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01562	iTRAQ8plex-117 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-117 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01563	iTRAQ8plex-118 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01584	modifications with monoisotopic mass differences that are nominally equal at 304.199039 Da		A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01564	iTRAQ8plex-118 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01712	iTRAQ8plex 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.
http://purl.obolibrary.org/obo/MOD_01565	iTRAQ8plex-118 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01566	iTRAQ8plex-118 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01567	iTRAQ8plex-118 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01568	iTRAQ8plex-118 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01569	iTRAQ8plex-118 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-118 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01570	iTRAQ8plex-119 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01584	modifications with monoisotopic mass differences that are nominally equal at 304.199039 Da		A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01571	iTRAQ8plex-119 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01712	iTRAQ8plex 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.
http://purl.obolibrary.org/obo/MOD_01572	iTRAQ8plex-119 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01573	iTRAQ8plex-119 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01574	iTRAQ8plex-119 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01575	iTRAQ8plex-119 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01576	iTRAQ8plex-119 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-119 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01577	iTRAQ8plex-121 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01584	modifications with monoisotopic mass differences that are nominally equal at 304.199039 Da		A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01578	iTRAQ8plex-121 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01712	iTRAQ8plex 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.
http://purl.obolibrary.org/obo/MOD_01579	iTRAQ8plex-121 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01580	iTRAQ8plex-121 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01581	iTRAQ8plex-121 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01582	iTRAQ8plex-121 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01583	iTRAQ8plex-121 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Applied Biosystems iTRAQ8plex-121 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01584	modifications with monoisotopic mass differences that are nominally equal at 304.199039 Da	http://purl.obolibrary.org/obo/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 304.199039 Da.
http://purl.obolibrary.org/obo/MOD_01585	O-glycyl-L-serine	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		A protein modification that effectively crosslinks an L-serine residue and a glycine residue by an ester bond to form O-glycyl-L-serine.
http://purl.obolibrary.org/obo/MOD_01586	O-glycyl-L-threonine	http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue		A protein modification that effectively crosslinks an L-threonine residue and a glycine residue by an ester bond to form O-glycyl-L-threonine.
http://purl.obolibrary.org/obo/MOD_01587	O-(2-aminoethylphosphoryl)-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-(2-aminoethylphosphoryl)-L-serine.
http://purl.obolibrary.org/obo/MOD_01588	O-cholinephosphoryl-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-cholinephosphoryl-L-serine.
http://purl.obolibrary.org/obo/MOD_01589	O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine	http://purl.obolibrary.org/obo/MOD_00002	O-glycosyl-L-serine		A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine.
http://purl.obolibrary.org/obo/MOD_01590	3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan	http://purl.obolibrary.org/obo/MOD_00601	cyclized residue		A protein modification that effectively converts an L-tryptophan residue to 3'-farnesyl-2',3'-dihydro-2',N2-cyclo-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01591	modifications with monoisotopic mass differences that are nominally equal at 304.205359 Da	http://purl.obolibrary.org/obo/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 304.205359 Da.
http://purl.obolibrary.org/obo/MOD_01592	modifications with monoisotopic mass differences that are nominally equal at 304.199-304.206 Da	http://purl.obolibrary.org/obo/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 of 304.199-304.206 Da.
http://purl.obolibrary.org/obo/MOD_01593	iTRAQ8plex reporter fragment	http://purl.obolibrary.org/obo/MOD_01520	modification reporter fragment		A protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01594	iTRAQ8plex-113 reporter fragment	http://purl.obolibrary.org/obo/MOD_01593	iTRAQ8plex reporter fragment		The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-113 reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01595	iTRAQ8plex-114 reporter fragment	http://purl.obolibrary.org/obo/MOD_01593	iTRAQ8plex reporter fragment		The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-114 reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01596	iTRAQ8plex-115 reporter fragment	http://purl.obolibrary.org/obo/MOD_01593	iTRAQ8plex reporter fragment		The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-115 reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01597	iTRAQ8plex-116 reporter fragment	http://purl.obolibrary.org/obo/MOD_01593	iTRAQ8plex reporter fragment		The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-116 reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01598	iTRAQ8plex-117 reporter fragment	http://purl.obolibrary.org/obo/MOD_01593	iTRAQ8plex reporter fragment		The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-117 reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01599	iTRAQ8plex-118 reporter fragment	http://purl.obolibrary.org/obo/MOD_01593	iTRAQ8plex reporter fragment		The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-118 reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01600	iTRAQ8plex-119 reporter fragment	http://purl.obolibrary.org/obo/MOD_01593	iTRAQ8plex reporter fragment		The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-119 reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01601	iTRAQ8plex-121 reporter fragment	http://purl.obolibrary.org/obo/MOD_01593	iTRAQ8plex reporter fragment		The protein modification reporter fragment produced by an Applied Biosystems iTRAQ8plex-121 reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01602	S-(L-lysyl)-L-methionine sulfilimine	http://purl.obolibrary.org/obo/MOD_02052	crosslinked L-methionine residue		A protein modification that effectively converts an L-lysine residue, and an L-methionine residue to S-(L-lysyl)-L-methionine sulfilimine.
http://purl.obolibrary.org/obo/MOD_01603	2x(15)N labeled L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to 2x(15)N labeled L-lysine.
http://purl.obolibrary.org/obo/MOD_01604	4x(15)N labeled L-arginine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		A protein modification that effectively converts an L-arginine residue to 4x(15)N labeled L-arginine.
http://purl.obolibrary.org/obo/MOD_01605	5-glutamyl 2-aminoadipic acid	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl 2-aminoadipic acid.
http://purl.obolibrary.org/obo/MOD_01606	5-glutamyl 2-aminoadipic 6-phosphoric anhydride	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl 2-aminoadipic 6-phosphoric anhydride.
http://purl.obolibrary.org/obo/MOD_01607	5-glutamyl allysine	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl allysine.
http://purl.obolibrary.org/obo/MOD_01608	N2-(L-isoglutamyl)-L-lysine	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to N2-(L-isoglutamyl)-L-lysine. This is not an isopeptide cross-link.
http://purl.obolibrary.org/obo/MOD_01609	7'-hydroxy-2'-alpha-mannosyl-L-tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to 7'-hydroxy-2'-alpha-mannosyl-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01610	L-threonine methyl ester	http://purl.obolibrary.org/obo/MOD_01803	O-methylated threonine		A protein modification that effectively converts an L-threonine residue to L-threonine methyl ester.
http://purl.obolibrary.org/obo/MOD_01611	6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FMN	http://purl.obolibrary.org/obo/MOD_02048	crosslinked L-histidine residue		A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FMN.
http://purl.obolibrary.org/obo/MOD_01612	3'-iodo-L-tyrosine	http://purl.obolibrary.org/obo/MOD_01228	monoiodinated tyrosine		A protein modification that effectively converts an L-tyrosine residue to 3'-iodo-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_01613	3',5'-diiodo-L-tyrosine	http://purl.obolibrary.org/obo/MOD_01140	diiodinated tyrosine		A protein modification that effectively converts an L-tyrosine residue to 3',5'-diiodo-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_01614	glycyl phospho-5'-adenosine	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to glycyl phospho-5'-adenosine.
http://purl.obolibrary.org/obo/MOD_01615	glycyl cysteine dithioester	http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue		A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a dithioester bond to form glycyl cysteine dithioester.
http://purl.obolibrary.org/obo/MOD_01616	trithiocystine	http://purl.obolibrary.org/obo/MOD_01620	polysulfide crosslinked residues		A protein modification that effectively cross-links two L-cysteine residues and adds three sulfur atoms to form trithiocystine.
http://purl.obolibrary.org/obo/MOD_01617	O-(6-phosphomannosyl)-L-threonine	http://purl.obolibrary.org/obo/MOD_01804	glycosylphosphorylated residue		A protein modification that effectively converts an L-threonine residue to O-(6-phosphomannosyl)-L-threonine.
http://purl.obolibrary.org/obo/MOD_01618	L-alanyl-L-isoaspartyl cyclopeptide	http://purl.obolibrary.org/obo/MOD_02042	crosslinked L-asparagine residue		A protein modification that effectively converts an L-alaine residue and an L-asparagine residue to L-alanyl-L-isoaspartyl cyclopeptide.
http://purl.obolibrary.org/obo/MOD_01619	multisulfide crosslinked residues	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		A protein modification that crosslinks two cysteine residues by formation of a chain of two or more bonded sulfur atoms.
http://purl.obolibrary.org/obo/MOD_01620	polysulfide crosslinked residues	http://purl.obolibrary.org/obo/MOD_01619	multisulfide crosslinked residues		A protein modification that crosslinks two cysteine residues by formation of a chain of three or more bonded sulfur atoms.
http://purl.obolibrary.org/obo/MOD_01621	flavin crosslinked residues	http://purl.obolibrary.org/obo/MOD_00033	crosslinked residues		A protein modification that crosslinks two or more amino acid residues by forming an adduct with a compound containing a flavin group.
http://purl.obolibrary.org/obo/MOD_01622	monohydroxylated tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		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.
http://purl.obolibrary.org/obo/MOD_01623	1-thioglycine (C-terminal)	http://purl.obolibrary.org/obo/MOD_01625	1-thioglycine		A protein modification that effectively converts a glycine residue to a C-terminal 1-thioglycine.
http://purl.obolibrary.org/obo/MOD_01624	(2-aminosuccinimidyl)acetic acid (Asn)	http://purl.obolibrary.org/obo/MOD_02042	crosslinked L-asparagine residue		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.
http://purl.obolibrary.org/obo/MOD_01625	1-thioglycine	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to 1-thioglycine.
http://purl.obolibrary.org/obo/MOD_01626	L-cystine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_01627	L-cysteinyl-L-selenocysteine	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_01628	(2-aminosuccinimidyl)acetic acid	http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue		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.
http://purl.obolibrary.org/obo/MOD_01629	cyclo[(prolylserin)-O-yl] cysteinate	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_01630	N6-(L-isoglutamyl)-L-lysine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		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 .
http://purl.obolibrary.org/obo/MOD_01631	L-alanine removal	http://purl.obolibrary.org/obo/MOD_00901	modified L-alanine residue		A protein modification that effectively removes or replaces an L-alanine.
http://purl.obolibrary.org/obo/MOD_01632	L-arginine removal	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		A protein modification that effectively removes or replaces an L-arginine.
http://purl.obolibrary.org/obo/MOD_01633	L-asparagine removal	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively removes or replaces an L-asparagine.
http://purl.obolibrary.org/obo/MOD_01634	L-aspartic acid removal	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively removes or replaces an L-aspartic acid.
http://purl.obolibrary.org/obo/MOD_01635	L-cysteine removal	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively removes or replaces an L-cysteine.
http://purl.obolibrary.org/obo/MOD_01636	L-glutamic acid removal	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively removes or replaces an L-glutamic acid.
http://purl.obolibrary.org/obo/MOD_01637	L-glutamine removal	http://purl.obolibrary.org/obo/MOD_00907	modified L-glutamine residue		A protein modification that effectively removes or replaces an L-glutamine.
http://purl.obolibrary.org/obo/MOD_01638	glycine removal	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively removes or replaces a glycine.
http://purl.obolibrary.org/obo/MOD_01639	L-histidine removal	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively removes or replaces an L-histidine.
http://purl.obolibrary.org/obo/MOD_01640	L-isoleucine removal	http://purl.obolibrary.org/obo/MOD_00910	modified L-isoleucine residue		A protein modification that effectively removes or replaces an L-isoleucine.
http://purl.obolibrary.org/obo/MOD_01641	L-leucine removal	http://purl.obolibrary.org/obo/MOD_00911	modified L-leucine residue		A protein modification that effectively removes or replaces an L-leucine.
http://purl.obolibrary.org/obo/MOD_01642	L-lysine removal	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively removes or replaces an L-lysine.
http://purl.obolibrary.org/obo/MOD_01643	L-methionine removal	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively removes or replaces an L-methionine.
http://purl.obolibrary.org/obo/MOD_01644	L-phenylalanine removal	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively removes or replaces an L-phenylalanine.
http://purl.obolibrary.org/obo/MOD_01645	L-proline removal	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively removes or replaces an L-proline.
http://purl.obolibrary.org/obo/MOD_01646	L-serine removal	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively removes or replaces an L-serine.
http://purl.obolibrary.org/obo/MOD_01647	L-threonine removal	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively removes or replaces an L-threonine.
http://purl.obolibrary.org/obo/MOD_01648	L-tryptophan removal	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively removes or replaces an L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01649	L-tyrosine removal	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively removes or replaces an L-tyrosine.
http://purl.obolibrary.org/obo/MOD_01650	L-valine removal	http://purl.obolibrary.org/obo/MOD_00920	modified L-valine residue		A protein modification that effectively removes or replaces an L-valine.
http://purl.obolibrary.org/obo/MOD_01651	natural, standard, encoded residue removal	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively removes a natural, standard, encoded residue.
http://purl.obolibrary.org/obo/MOD_01652	sulfonyl halide reagent derivatized residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that is produced by formation of an adduct with a sulfonyl halide compound used as a reagent.
http://purl.obolibrary.org/obo/MOD_01653	dansyl chloride derivatized residue	http://purl.obolibrary.org/obo/MOD_01652	sulfonyl halide reagent derivatized residue		A protein modification that is produced by formation of an adduct with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride.
http://purl.obolibrary.org/obo/MOD_01654	N6-Dansyl derivatized lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that is produced by reaction with 5-dimethylaminonaphthalene-1-sulfonyl chloride, dansyl chloride, to form N6-Dansyl-lysine.
http://purl.obolibrary.org/obo/MOD_01655	alpha-amino-Dansyl derivatized residue	http://purl.obolibrary.org/obo/MOD_01653	dansyl chloride 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.
http://purl.obolibrary.org/obo/MOD_01656	Dabsyl chloride derivatized residue	http://purl.obolibrary.org/obo/MOD_01652	sulfonyl halide reagent derivatized residue		A protein modification that is produced by formation of an adduct with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, Dabsyl chloride.
http://purl.obolibrary.org/obo/MOD_01657	N6-Dabsyl derivatized lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that is produced by reaction with 4-(4-dimethylaminophenylazo)benzenesulfonyl chloride, dabsyl chloride, to form N6-Dabsyl-lysine.
http://purl.obolibrary.org/obo/MOD_01658	alpha-amino-Dabsyl derivatized residue	http://purl.obolibrary.org/obo/MOD_01656	Dabsyl chloride 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.
http://purl.obolibrary.org/obo/MOD_01659	Uniblue A derivatized residue	http://purl.obolibrary.org/obo/MOD_00848	reagent 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.
http://purl.obolibrary.org/obo/MOD_01660	Uniblue A derivatized cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_01661	pyruvic acid (Tyr)	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an L-tyrosine residue to pyruvic acid.
http://purl.obolibrary.org/obo/MOD_01662	N5-(ADP-ribosyl)-L-glutamine	http://purl.obolibrary.org/obo/MOD_00907	modified L-glutamine residue		A protein modification that effectively converts an L-glutamine residue to N5-(ADP-ribosyl)-L-glutamine.
http://purl.obolibrary.org/obo/MOD_01663	O-(ADP-ribosyl)-L-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to O-(ADP-ribosyl)-L-threonine.
http://purl.obolibrary.org/obo/MOD_01664	7'-hydroxy-L-tryptophan	http://purl.obolibrary.org/obo/MOD_01622	monohydroxylated tryptophan		A protein modification that effectively converts an L-tryptophan residue to a 7'-hydroxy-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01665	N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-valine	http://purl.obolibrary.org/obo/MOD_00920	modified L-valine residue		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.
http://purl.obolibrary.org/obo/MOD_01666	epicocconone derivatized residue	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		A protein modification that is produced by formation of an adduct with epicocconone.
http://purl.obolibrary.org/obo/MOD_01667	N6-epicoccononyl lysine adduct	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that is produced by formation of an adduct with epicocconone.
http://purl.obolibrary.org/obo/MOD_01668	O4-(8alpha-FAD)-L-aspartate	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to O4-(8alpha-FAD)-L-aspartate.
http://purl.obolibrary.org/obo/MOD_01669	trimethyl-L-arginine	http://purl.obolibrary.org/obo/MOD_00658	methylated arginine		A protein modification that effectively converts an L-arginine residue to N(omega),N(omega),N'(omega)-trimethyl-L-arginine.
http://purl.obolibrary.org/obo/MOD_01670	N6-chloro-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01671	O-(L-isoaspartyl)-L-threonine (active site intermediate)	http://purl.obolibrary.org/obo/MOD_01978	O-(L-isoaspartyl)-L-threonine		A protein modification that effectively converts an L-threonine residue to O-(L-isoaspartyl)-L-threonine, using free L-asparagine and releasing ammonia.
http://purl.obolibrary.org/obo/MOD_01672	halogenated lysine	http://purl.obolibrary.org/obo/MOD_00694	halogen containing residue		A protein modification that effectively substitutes a hydrogen atom of an L-lysine residue with a halogen atom.
http://purl.obolibrary.org/obo/MOD_01673	N-acetylaminohexosylated residue	http://purl.obolibrary.org/obo/MOD_00436	N-acetylhexosaminylated residue		A protein modification that effectively replaces a hydrogen atom with an N-acetylaminohexose group through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_01674	N4-(N-acetylamino)hexosyl-L-asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminohexosyl)-L-asparagine.
http://purl.obolibrary.org/obo/MOD_01675	O-(N-acetylamino)hexosyl-L-serine	http://purl.obolibrary.org/obo/MOD_01673	N-acetylaminohexosylated residue		A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminohexosyl)-L-serine.
http://purl.obolibrary.org/obo/MOD_01676	O-(N-acetylamino)hexosyl-L-threonine	http://purl.obolibrary.org/obo/MOD_01673	N-acetylaminohexosylated residue		A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminohexosyl)-L-threonine.
http://purl.obolibrary.org/obo/MOD_01677	O4-(N-acetylamino)hexosyl-L-hydroxyproline	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively converts an L-proline residue to O4-(N-acetylamino)hexosyl-L-hydroxyproline.
http://purl.obolibrary.org/obo/MOD_01678	N6-carbamoyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively coverts L-lysine to N6-carbamoyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01679	alpha-aminocarbamoylated residue	http://purl.obolibrary.org/obo/MOD_00398	carbamoylated residue		A protein modification that effectively replaces a residue alpha amino or imino hydrogen with a carbamoyl group.
http://purl.obolibrary.org/obo/MOD_01680	alpha-amino monomethylated residue	http://purl.obolibrary.org/obo/MOD_00599	monomethylated residue		A protein modification that effectively replaces one residue alpha amino or imino hydrogen with one methyl group.
http://purl.obolibrary.org/obo/MOD_01681	monomethylated L-aspartic acid	http://purl.obolibrary.org/obo/MOD_00599	monomethylated residue		A protein modification that effectively replaces one hydrogen atom of an L-aspartic acid residue with one methyl group.
http://purl.obolibrary.org/obo/MOD_01682	monomethylated L-cysteine	http://purl.obolibrary.org/obo/MOD_00599	monomethylated residue		A protein modification that effectively replaces one hydrogen atom of an L-cysteine residue with one methyl group.
http://purl.obolibrary.org/obo/MOD_01684	palmitoylated-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_01685	alpha-amino palmitoylated residue	http://purl.obolibrary.org/obo/MOD_01696	alpha-amino acylated residue		A protein modification that effectively replaces a residue alpha-amino group with a alpha-palmitoylamino group.
http://purl.obolibrary.org/obo/MOD_01686	alpha-amino dimethylated residue	http://purl.obolibrary.org/obo/MOD_01460	alpha-amino methylated residue		A protein modification that effectively replaces two alpha amino hydrogen atoms with two methyl group.
http://purl.obolibrary.org/obo/MOD_01687	alpha-amino trimethylated residue	http://purl.obolibrary.org/obo/MOD_01460	alpha-amino methylated residue		A protein modification that effectively replaces an alpha-aminium group with a trimethylaminium group.
http://purl.obolibrary.org/obo/MOD_01688	3-hydroxy-L-asparagine	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively converts an L-asparagine residue to one of the diastereomeric 3-hydroxy-L-asparagine residues.
http://purl.obolibrary.org/obo/MOD_01689	alpha-carboxyl methylated residue	http://purl.obolibrary.org/obo/MOD_00393	O-methylated residue		A protein modification that effectively converts a carboxyl-terminal residue to an alpha-carboxyl (1-carboxyl) methyl ester.
http://purl.obolibrary.org/obo/MOD_01690	N-[(12R)-12-hydroxymyristoyl]-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to N-[(12R)-12-hydroxymyristoyl]-L-cysteine.
http://purl.obolibrary.org/obo/MOD_01691	N-(12-ketomyristoyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to N-(12-ketomyristoyl)-L-cysteine.
http://purl.obolibrary.org/obo/MOD_01692	glutamyl semialdehyde (Glu)	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl semialdehyde.
http://purl.obolibrary.org/obo/MOD_01693	alpha-amino pyridylacetylated residue	http://purl.obolibrary.org/obo/MOD_01696	alpha-amino acylated residue		A protein modification that effectively replaces a residue alpha amino or imino hydrogen with a (pyrid-3-yl)acetyl group.
http://purl.obolibrary.org/obo/MOD_01694	S-(coelenterazin-3a-yl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_01695	alpha-amino 3-(carboxamidomethylthio)propanoylated residue	http://purl.obolibrary.org/obo/MOD_01696	alpha-amino acylated residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an 3-(carboxamidomethylthio)propanoyl group.
http://purl.obolibrary.org/obo/MOD_01696	alpha-amino acylated residue	http://purl.obolibrary.org/obo/MOD_00670	N-acylated residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group.
http://purl.obolibrary.org/obo/MOD_01697	alpha-amino 4-(2-aminoethyl)benzenesulfonylated residue	http://purl.obolibrary.org/obo/MOD_00596	4-(2-aminoethyl)benzenesulfonyl fluoride derivatized residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an 4-(2-aminoethyl)benzenesulfonyl group.
http://purl.obolibrary.org/obo/MOD_01698	alpha-amino trimethylated protonated-residue	http://purl.obolibrary.org/obo/MOD_01460	alpha-amino methylated residue		A protein modification that effectively replaces an amino group with a trimethylaminium group.
http://purl.obolibrary.org/obo/MOD_01699	protonated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively adds a hydrogen cation, a proton, forming a cationic residue.
http://purl.obolibrary.org/obo/MOD_01700	alpha-amino protonated residue	http://purl.obolibrary.org/obo/MOD_01699	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.
http://purl.obolibrary.org/obo/MOD_01701	deprotonated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively removes a hydrogen cation, a proton, forming an anionic residue.
http://purl.obolibrary.org/obo/MOD_01702	alpha-carboxyl deprotonated residue	http://purl.obolibrary.org/obo/MOD_01701	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.
http://purl.obolibrary.org/obo/MOD_01703	dehydrobutyrine	http://purl.obolibrary.org/obo/MOD_00859	modified residue that can arise from different natural residues		A protein modification that effectively converts a source amino acid residue to dehydrobutyrine.
http://purl.obolibrary.org/obo/MOD_01704	dehydrobutyrine (Met)	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine residue to dehydrobutyrine, by neutral loss of methyl sulfide.
http://purl.obolibrary.org/obo/MOD_01705	isotope tagged reagent acylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated residue		A protein modification that effectively replaces a residue hydrogen with an isotope tagged reagent acyl group.
http://purl.obolibrary.org/obo/MOD_01706	isotope tagged reagent N-acylated residue	http://purl.obolibrary.org/obo/MOD_00670	N-acylated residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an isotope tagged reagent acyl group.
http://purl.obolibrary.org/obo/MOD_01707	isotope tagged reagent O-acylated residue	http://purl.obolibrary.org/obo/MOD_00671	O-acylated residue		A protein modification that effectively replaces a residue hydroxyl group with an isotope tagged reagent acyloxy group.
http://purl.obolibrary.org/obo/MOD_01708	isotope tagged reagent alpha-amino acylated residue	http://purl.obolibrary.org/obo/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.
http://purl.obolibrary.org/obo/MOD_01709	iTRAQ4plex reporter+balance reagent N-acylated residue	http://purl.obolibrary.org/obo/MOD_01706	isotope tagged 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.
http://purl.obolibrary.org/obo/MOD_01710	iTRAQ8plex reporter+balance reagent N-acylated residue	http://purl.obolibrary.org/obo/MOD_01706	isotope tagged 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.
http://purl.obolibrary.org/obo/MOD_01711	iTRAQ4plex reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01709	iTRAQ4plex reporter+balance reagent N-acylated residue		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.
http://purl.obolibrary.org/obo/MOD_01712	iTRAQ8plex reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01710	iTRAQ8plex reporter+balance reagent N-acylated residue		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.
http://purl.obolibrary.org/obo/MOD_01713	iTRAQ4plex reporter+balance reagent O-acylated residue	http://purl.obolibrary.org/obo/MOD_01707	isotope tagged 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.
http://purl.obolibrary.org/obo/MOD_01714	iTRAQ8plex reporter+balance reagent O-acylated residue	http://purl.obolibrary.org/obo/MOD_01707	isotope tagged 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.
http://purl.obolibrary.org/obo/MOD_01715	TMT6plex reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01705	isotope tagged reagent acylated residue		A protein modification that effectively replaces a hydrogen atom of a residue with a Proteome Sciences TMT6plex reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01716	TMT6plex reporter fragment	http://purl.obolibrary.org/obo/MOD_01520	modification reporter fragment		The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-126 reagent acylated residue.
http://purl.obolibrary.org/obo/MOD_01717	TMT6plex reporter+balance reagent N-acylated residue	http://purl.obolibrary.org/obo/MOD_01706	isotope tagged reagent N-acylated residue		A protein modification that effectively replaces a residue amino- or imino-hydrogen with a Proteome Sciences TMT6plex reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01718	TMT6plex reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01717	TMT6plex reporter+balance reagent N-acylated residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a Proteome Sciences TMT6plex reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01719	TMT6plex reporter+balance reagent O-acylated residue	http://purl.obolibrary.org/obo/MOD_01707	isotope tagged 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.
http://purl.obolibrary.org/obo/MOD_01720	TMT6plex-126 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01715	TMT6plex 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.
http://purl.obolibrary.org/obo/MOD_01721	TMT6plex-126 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01720	TMT6plex-126 reporter+balance reagent acylated residue		A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-126 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01722	TMT6plex-126 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01723	TMT6plex-126 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01724	TMT6plex-126 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01725	TMT6plex-126 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01726	TMT6plex-126 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-126 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01727	TMT6plex-126 reporter fragment	http://purl.obolibrary.org/obo/MOD_01716	TMT6plex reporter fragment		The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-126 reagent acylated residue.
http://purl.obolibrary.org/obo/MOD_01728	TMT6plex-127 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01715	TMT6plex 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.
http://purl.obolibrary.org/obo/MOD_01729	TMT6plex-127 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01728	TMT6plex-127 reporter+balance reagent acylated residue		A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-127 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01730	TMT6plex-127 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01731	TMT6plex-127 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01732	TMT6plex-127 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01734	TMT6plex-127 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-127 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01735	TMT6plex-127 reporter fragment	http://purl.obolibrary.org/obo/MOD_01716	TMT6plex reporter fragment		The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-127 reagent acylated residue.
http://purl.obolibrary.org/obo/MOD_01736	TMT6plex-128 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01715	TMT6plex 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.
http://purl.obolibrary.org/obo/MOD_01737	TMT6plex-128 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01736	TMT6plex-128 reporter+balance reagent acylated residue		A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-128 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01738	TMT6plex-128 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01739	TMT6plex-128 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01740	TMT6plex-128 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01741	TMT6plex-128 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01742	TMT6plex-128 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-128 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01743	TMT6plex-128 reporter fragment	http://purl.obolibrary.org/obo/MOD_01716	TMT6plex reporter fragment		The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-128 reagent acylated residue.
http://purl.obolibrary.org/obo/MOD_01744	TMT6plex-129 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01715	TMT6plex 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.
http://purl.obolibrary.org/obo/MOD_01745	TMT6plex-129 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01744	TMT6plex-129 reporter+balance reagent acylated residue		A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-129 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01746	TMT6plex-129 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01747	TMT6plex-129 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01748	TMT6plex-129 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01749	TMT6plex-129 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01750	TMT6plex-129 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-129 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01751	TMT6plex-129 reporter fragment	http://purl.obolibrary.org/obo/MOD_01716	TMT6plex reporter fragment		The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-129 reagent acylated residue.
http://purl.obolibrary.org/obo/MOD_01752	TMT6plex-130 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01715	TMT6plex 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.
http://purl.obolibrary.org/obo/MOD_01753	TMT6plex-130 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01752	TMT6plex-130 reporter+balance reagent acylated residue		A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-130 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01754	TMT6plex-130 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01755	TMT6plex-130 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01756	TMT6plex-130 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01757	TMT6plex-130 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01758	TMT6plex-130 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-130 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01759	TMT6plex-130 reporter fragment	http://purl.obolibrary.org/obo/MOD_01716	TMT6plex reporter fragment		The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-130 reagent acylated residue.
http://purl.obolibrary.org/obo/MOD_01760	TMT6plex-131 reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01715	TMT6plex 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.
http://purl.obolibrary.org/obo/MOD_01761	TMT6plex-131 reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01760	TMT6plex-131 reporter+balance reagent acylated residue		A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Proteome Sciences TMT6plex-131 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01762	TMT6plex-131 reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively replaces the N6'-hydrogen atom of a lysine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01763	TMT6plex-131 reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01764	TMT6plex-131 reporter+balance reagent N'-acylated histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively replaces an N'-hydrogen atom of a histidine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01765	TMT6plex-131 reporter+balance reagent O3-acylated serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively replaces an O3-hydrogen atom of a serine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01766	TMT6plex-131 reporter+balance reagent O3-acylated threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively replaces an O3-hydrogen atom of a threonine residue with the Proteome Sciences TMT6plex-131 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01767	TMT6plex-131 reporter fragment	http://purl.obolibrary.org/obo/MOD_01716	TMT6plex reporter fragment		The protein modification reporter fragment produced by an Proteome Sciences TMT6plex-131 reagent acylated residue.
http://purl.obolibrary.org/obo/MOD_01768	O-palmitoleylated residue	http://purl.obolibrary.org/obo/MOD_01423	palmitoleylated residue		A protein modification that effectively replaces a residue hydroxyl group with a palmitoleyloxy group.
http://purl.obolibrary.org/obo/MOD_01769	O-palmitoleyl-L-threonine	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively converts an L-threonine residue to O-palmitoleyl-L-threonine.
http://purl.obolibrary.org/obo/MOD_01770	O-palmitoyl-L-threonine amide	http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine		A protein modification that effectively converts an L-threonine residue to O-palmitoyl-L-threonine amide.
http://purl.obolibrary.org/obo/MOD_01771	farnesyl reporter fragment	http://purl.obolibrary.org/obo/MOD_01520	modification reporter fragment		The farnesyl cation protein modification reporter fragment produced by fragmentation of some farnesyl modified residues.
http://purl.obolibrary.org/obo/MOD_01772	palmityl reporter fragment	http://purl.obolibrary.org/obo/MOD_01520	modification reporter fragment		The palmityl cation protein modification reporter fragment produced by fragmentation of some palmitoyl modified residues.
http://purl.obolibrary.org/obo/MOD_01773	N6,N6,N6-trimethyl-L-lysine with neutral loss of trimethylamine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		Covalent modification of a trimethyllysine residue with secondary loss of a neutral trimethylamine molecular fragment.
http://purl.obolibrary.org/obo/MOD_01774	N6-octanoyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00666	octanoylated residue		A protein modification that effectively converts an L-lysine residue to N6-octanoyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01775	5-glutamyl serotonin	http://purl.obolibrary.org/obo/MOD_00907	modified L-glutamine residue		A protein modification that effectively converts an L-glutamine residue to 5-glutamyl serotonin.
http://purl.obolibrary.org/obo/MOD_01776	S-methylthiocarbonylaminoethylcysteine (Cys)	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-methylthiocarbonylaminoethylcysteine.
http://purl.obolibrary.org/obo/MOD_01777	S-(glycyl)-L-cysteine (Gly)	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		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.
http://purl.obolibrary.org/obo/MOD_01778	N-(glycyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		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.
http://purl.obolibrary.org/obo/MOD_01779	N6-(L-lysyl)-L-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated 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.
http://purl.obolibrary.org/obo/MOD_01780	N6-(beta-lysyl)-L-5-hydroxylysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-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.
http://purl.obolibrary.org/obo/MOD_01781	N6-butanoyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01997	N-butanoylated residue		A protein modification that effectively converts an L-lysine residue to N6-butanoyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01782	N-methyl-L-serine	http://purl.obolibrary.org/obo/MOD_01800	N-methylated serine		A protein modification that effectively converts an L-serine residue to N-methyl-L-serine.
http://purl.obolibrary.org/obo/MOD_01783	N,N-dimethyl-L-serine	http://purl.obolibrary.org/obo/MOD_01800	N-methylated serine		A protein modification that effectively converts an L-serine residue to N,N-dimethyl-L-serine.
http://purl.obolibrary.org/obo/MOD_01784	N,N,N-trimethyl-L-serine	http://purl.obolibrary.org/obo/MOD_01800	N-methylated serine		A protein modification that effectively converts an L-serine residue to N,N,N-trimethyl-L-serine.
http://purl.obolibrary.org/obo/MOD_01785	O-(L-isoglutamyl)-L-threonine (active site intermediate)	http://purl.obolibrary.org/obo/MOD_01979	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.
http://purl.obolibrary.org/obo/MOD_01787	5'-(L-tyros-5'-yl)amino-L-tyrosine	http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_01788	histidine immonium ion	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an N-terminal L-histidine residue to histidine immonium ion.
http://purl.obolibrary.org/obo/MOD_01789	phenylalanine immonium ion	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that effectively converts an N-terminal L-phenylalanine residue to phenylalanine immonium ion.
http://purl.obolibrary.org/obo/MOD_01790	tyrosine immonium ion	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an an N-terminal L-tyrosine residue to tyrosine immonium ion.
http://purl.obolibrary.org/obo/MOD_01791	phosphohistidine immonium ion	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an N-terminal phosphohistidine residue to phosphohistidine immonium ion.
http://purl.obolibrary.org/obo/MOD_01792	phosphotyrosine immonium ion	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an N-terminal O4'-phospho-L-tyrosine residue to tyrosine immonium ion.
http://purl.obolibrary.org/obo/MOD_01793	S-carboxamidomethyl-L-cysteine sulfoxide	http://purl.obolibrary.org/obo/MOD_01854	sulfur monooxygenated residue		A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine sulfoxide.
http://purl.obolibrary.org/obo/MOD_01794	1x(13)C,3x(2)H labeled monomethylated residue	http://purl.obolibrary.org/obo/MOD_00842	(13)C labeled 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.
http://purl.obolibrary.org/obo/MOD_01795	1x(13)C,3x(2)H C(6)-labeled L-methionine	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		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.
http://purl.obolibrary.org/obo/MOD_01796	1x(13)C,3x(2)H C(6)-labeled L-methionine sulfoxide	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		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.
http://purl.obolibrary.org/obo/MOD_01797	1'-phosphohistidine immonium ion	http://purl.obolibrary.org/obo/MOD_01791	phosphohistidine immonium ion		A protein modification that effectively converts an N-terminal 1'-phosphohistidine residue to 1'-phosphohistidine immonium ion.
http://purl.obolibrary.org/obo/MOD_01798	3'-phosphohistidine immonium ion	http://purl.obolibrary.org/obo/MOD_01791	phosphohistidine immonium ion		A protein modification that effectively converts an N-terminal 3'-phosphohistidine residue to 3'-phosphohistidine immonium ion.
http://purl.obolibrary.org/obo/MOD_01799	methylated serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_01800	N-methylated serine	http://purl.obolibrary.org/obo/MOD_01799	methylated serine		A protein modification that effectively replaces an L-serine alpha amino hydrogen with a methyl group.
http://purl.obolibrary.org/obo/MOD_01801	protonated L-serine (L-serinium) residue	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to an L-serinium (protonated L-serine).
http://purl.obolibrary.org/obo/MOD_01802	N,N,N-trimethyl-L-serine (from L-serinium)	http://purl.obolibrary.org/obo/MOD_01687	alpha-amino trimethylated residue		A protein modification that effectively converts an L-serinium (protonated L-serine) residue to an N,N,N-trimethyl-L-serine.
http://purl.obolibrary.org/obo/MOD_01803	O-methylated threonine	http://purl.obolibrary.org/obo/MOD_01418	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.
http://purl.obolibrary.org/obo/MOD_01804	glycosylphosphorylated residue	http://purl.obolibrary.org/obo/MOD_00764	glycoconjugated residue		A protein modification that effectively results from forming an adduct with a glycosylphosphate through a phosphodiester bond.
http://purl.obolibrary.org/obo/MOD_01805	N-(L-isoaspartyl)-glycine (Asp)	http://purl.obolibrary.org/obo/MOD_02043	crosslinked L-aspartic acid residue		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.
http://purl.obolibrary.org/obo/MOD_01806	N,N-dimethyl-L-leucine	http://purl.obolibrary.org/obo/MOD_01808	N-methylated leucine		A protein modification that effectively converts an L-leucine residue to N,N-dimethyl-L-leucine.
http://purl.obolibrary.org/obo/MOD_01807	N-formyl-L-glutamic acid	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to N-formyl-L-glutamic acid.
http://purl.obolibrary.org/obo/MOD_01808	N-methylated leucine	http://purl.obolibrary.org/obo/MOD_01460	alpha-amino methylated residue		A protein modification that effectively replaces an L-leucine alpha amino hydrogen with a methyl group.
http://purl.obolibrary.org/obo/MOD_01809	5x(13)C,1x(15)N labeled residue	http://purl.obolibrary.org/obo/MOD_00843	(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.
http://purl.obolibrary.org/obo/MOD_01810	5x(13)C,1x(15)N labeled L-proline	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that effectively converts an L-proline residue to 5x(13)C,1x(15)N labeled L-proline.
http://purl.obolibrary.org/obo/MOD_01811	5x(13)C,1x(15)N labeled L-methionine	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine residue to 5x(13)C,1x(15)N labeled L-methionine.
http://purl.obolibrary.org/obo/MOD_01812	5x(13)C,1x(15)N labeled L-methionine sulfoxide	http://purl.obolibrary.org/obo/MOD_01809	5x(13)C,1x(15)N labeled residue		A protein modification that effectively converts an L-methionine residue to 5x(13)C,1x(15)N labeled L-methionine sulfoxide.
http://purl.obolibrary.org/obo/MOD_01813	morpholine-2-acetylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated residue		A protein modification that effectively substitutes a morpholine-2-acetyl group for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_01814	L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		A protein modification that effectively cross-links a cysteine and two serine residues to form L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid.
http://purl.obolibrary.org/obo/MOD_01815	L-glutamate thiazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02045	crosslinked L-glutamic acid residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-glutamic acid residue to form L-glutamate thiazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01816	2'-hydroxy-L-tryptophan	http://purl.obolibrary.org/obo/MOD_01622	monohydroxylated tryptophan		A protein modification that effectively converts an L-tryptophan residue to a 2'-hydroxy-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01817	2'-oxo-L-tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to a 2'-oxo-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01818	1'-(L-tryptophan-3'-yl)-L-tryptophan	http://purl.obolibrary.org/obo/MOD_02057	crosslinked L-tryptophan residue		A protein modification that effectively cross-links two tryptophan residues to form 1'-(L-tryptophan-3'-yl)-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01819	N6-succinyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-succinyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01820	isotope tagged sufhydryl reagent modified cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively replaces a cysteine sulhydryl hydrogen with an isotope tagged sulfhydryl reagent group.
http://purl.obolibrary.org/obo/MOD_01821	cysTMT6plex reporter+balance reagent cysteine disulfide	http://purl.obolibrary.org/obo/MOD_01820	isotope tagged sufhydryl reagent modified cysteine		A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01822	cysTMT6plex-zero reporter+balance reagent cysteine disulfide	http://purl.obolibrary.org/obo/MOD_01821	cysTMT6plex reporter+balance reagent cysteine disulfide		A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-zero reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01823	cysTMT6plex-126 reporter+balance reagent cysteine disulfide	http://purl.obolibrary.org/obo/MOD_01821	cysTMT6plex reporter+balance reagent cysteine disulfide		A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-126 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01824	cysTMT6plex-127 reporter+balance reagent cysteine disulfide	http://purl.obolibrary.org/obo/MOD_01821	cysTMT6plex reporter+balance reagent cysteine disulfide		A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-127 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01825	cysTMT6plex-128 reporter+balance reagent cysteine disulfide	http://purl.obolibrary.org/obo/MOD_01821	cysTMT6plex reporter+balance reagent cysteine disulfide		A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-128 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01826	cysTMT6plex-129 reporter+balance reagent cysteine disulfide	http://purl.obolibrary.org/obo/MOD_01821	cysTMT6plex reporter+balance reagent cysteine disulfide		A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-129 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01827	cysTMT6plex-130 reporter+balance reagent cysteine disulfide	http://purl.obolibrary.org/obo/MOD_01821	cysTMT6plex reporter+balance reagent cysteine disulfide		A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-130 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01828	cysTMT6plex-131 reporter+balance reagent cysteine disulfide	http://purl.obolibrary.org/obo/MOD_01821	cysTMT6plex reporter+balance reagent cysteine disulfide		A protein modification that effectively replaces a residue sulfhydryl hydrogen with a Thermo Scientific cysTMT6plex-131 reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01829	S-carboxymethyl-L-cysteine sulfoxide	http://purl.obolibrary.org/obo/MOD_01854	sulfur monooxygenated residue		A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine sulfoxide.
http://purl.obolibrary.org/obo/MOD_01830	S-carboxymethyl-L-cysteine sulfone	http://purl.obolibrary.org/obo/MOD_01855	sulfur dioxygenated residue		A protein modification that effectively converts an L-cysteine residue to S-carboxymethyl-L-cysteine sulfone.
http://purl.obolibrary.org/obo/MOD_01831	S-carboxamidomethyl-L-cysteine sulfone	http://purl.obolibrary.org/obo/MOD_01855	sulfur dioxygenated residue		A protein modification that effectively converts an L-cysteine residue to S-carboxamidomethyl-L-cysteine sulfone.
http://purl.obolibrary.org/obo/MOD_01832	5x(13)C-labeled residue	http://purl.obolibrary.org/obo/MOD_00842	(13)C labeled residue		A protein modification that effectively converts a residue containing common isotopes to a 5x(13)C-labeled residue.
http://purl.obolibrary.org/obo/MOD_01833	5x(13)C-labeled L-methionine	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine.
http://purl.obolibrary.org/obo/MOD_01834	5x(13)C-labeled L-methionine sulfoxide	http://purl.obolibrary.org/obo/MOD_01832	5x(13)C-labeled residue		A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine sulfoxide.
http://purl.obolibrary.org/obo/MOD_01835	5x(13)C-labeled L-methionine sulfone	http://purl.obolibrary.org/obo/MOD_01832	5x(13)C-labeled residue		A protein modification that effectively converts an L-methionine residue containing common isotopes to 5x(13)C-labeled L-methionine sulfone.
http://purl.obolibrary.org/obo/MOD_01836	N6-[([1-(6-nitro-2H-1,3-benzodioxol-5-yl)ethoxy]carbonyl]lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-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.
http://purl.obolibrary.org/obo/MOD_01837	L-lanthionine (Cys-Cys)	http://purl.obolibrary.org/obo/MOD_00687	thioether crosslinked residues		A protein modification that effectively cross-links two L-cysteine residues with a thioether bond to form L-lanthionine.
http://purl.obolibrary.org/obo/MOD_01838	L-lysinoalanine (Lys)	http://purl.obolibrary.org/obo/MOD_01853	L-lysinoalanine		A protein modification that effectively converts an L-lysine residue to L-lysinoalanine.
http://purl.obolibrary.org/obo/MOD_01839	L-lanthionine	http://purl.obolibrary.org/obo/MOD_01841	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.
http://purl.obolibrary.org/obo/MOD_01840	L-allo-isoleucine	http://purl.obolibrary.org/obo/MOD_00910	modified L-isoleucine residue		A protein modification that effectively converts an L-isoleucine residue to L-allo-isoleucine.
http://purl.obolibrary.org/obo/MOD_01841	lanthionine	http://purl.obolibrary.org/obo/MOD_01993	beta-carbon thioether crosslinked residues		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.
http://purl.obolibrary.org/obo/MOD_01842	S-(2-aminovinyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_01851	S-(2-aminovinyl)-cysteine		A protein modification that effectively converts two L-cysteine residues to S-(2-aminovinyl)-L-cysteine.
http://purl.obolibrary.org/obo/MOD_01843	5'-chloro-L-tryptophan	http://purl.obolibrary.org/obo/MOD_01913	monochlorinated L-tryptophan		A protein modification that effectively converts an L-tryptophan residue to 5'-chloro-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01844	2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid	http://purl.obolibrary.org/obo/MOD_02050	crosslinked L-leucine residue		A protein modification that effectively converts an L-cysteine residue and an L-leucine residue to 2-(3-methylbutanoyl)-5-hydroxyoxazole-4-carbothionic acid.
http://purl.obolibrary.org/obo/MOD_01845	L-proline 5-hydroxyoxazole-4-carbothionic acid	http://purl.obolibrary.org/obo/MOD_02054	crosslinked L-proline residue		A protein modification that effectively converts an L-cysteine residue and an L-proline residue to L-proline 5-hydroxyoxazole-4-carbothionic acid.
http://purl.obolibrary.org/obo/MOD_01846	methanobactin OB3b copper complex	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		A protein modification that effectively converts two L-cysteine residues, and a copper atom to the methanobactin OB3b copper complex.
http://purl.obolibrary.org/obo/MOD_01847	L-cysteine sulfinyl phosphate	http://purl.obolibrary.org/obo/MOD_00861	phosphorus containing modified residue		A protein modification that effectively converts an L-cysteine residue to L-cysteine sulfinyl phosphate.
http://purl.obolibrary.org/obo/MOD_01848	S-(spermidinoglutathion-S-yl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-(spermidinoglutathion-S-yl)-L-cysteine.
http://purl.obolibrary.org/obo/MOD_01849	S-(2-aminovinyl)-D-cysteine (Cys-Cys)	http://purl.obolibrary.org/obo/MOD_01850	S-(2-aminovinyl)-D-cysteine		A protein modification that effectively cross-links two L-cysteine residues by a thioether bond to form S-(2-aminovinyl)-D-cysteine.
http://purl.obolibrary.org/obo/MOD_01850	S-(2-aminovinyl)-D-cysteine	http://purl.obolibrary.org/obo/MOD_01851	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)-D-cysteine.
http://purl.obolibrary.org/obo/MOD_01851	S-(2-aminovinyl)-cysteine	http://purl.obolibrary.org/obo/MOD_00859	modified residue that can arise from different natural residues		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.
http://purl.obolibrary.org/obo/MOD_01852	L-lysinoalanine (Lys-Cys)	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_01853	L-lysinoalanine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_01854	sulfur monooxygenated residue	http://purl.obolibrary.org/obo/MOD_00680	sulfur oxygenated residue		A protein modification that effectively adds one oxygen atom to a sulfur atom of a residue without removing hydrogen atoms.
http://purl.obolibrary.org/obo/MOD_01855	sulfur dioxygenated residue	http://purl.obolibrary.org/obo/MOD_00680	sulfur oxygenated residue		A protein modification that effectively adds two oxygen atoms to a sulfur atom of a residue without removing hydrogen atoms.
http://purl.obolibrary.org/obo/MOD_01856	oxazole/oxazoline ring crosslinked residues (Cys)	http://purl.obolibrary.org/obo/MOD_01419	oxazole/oxazoline ring crosslinked residues		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.
http://purl.obolibrary.org/obo/MOD_01857	2-(L-cystein-S-yl)-methionine	http://purl.obolibrary.org/obo/MOD_02052	crosslinked L-methionine residue		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.
http://purl.obolibrary.org/obo/MOD_01858	S-(N-acetylamino)glucosyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-(N-acetylamino)glucosyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_01859	4-amino-3-isothiazolidinone-L-phenylalanine	http://purl.obolibrary.org/obo/MOD_02053	crosslinked L-phenylalanine residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form 4-amino-3-isothiazolidinone-L-phenylalanine.
http://purl.obolibrary.org/obo/MOD_01860	L-cysteine bacillithiol disulfide	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to L-cysteine bacillithiol disulfide.
http://purl.obolibrary.org/obo/MOD_01861	isothiazolidinone ring crosslinked residues	http://purl.obolibrary.org/obo/MOD_00033	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.
http://purl.obolibrary.org/obo/MOD_01862	disulfide conjugated residue	http://purl.obolibrary.org/obo/MOD_01886	thiolated 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.
http://purl.obolibrary.org/obo/MOD_01863	mTRAQ reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01705	isotope tagged 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.
http://purl.obolibrary.org/obo/MOD_01864	mTRAQ light reporter+balance reagent acylated residue	http://purl.obolibrary.org/obo/MOD_01868	modifications with monoisotopic mass differences that are nominally equal at 140.094963 Da		A protein modification that effectively replaces a hydrogen atom of a residue with the Applied Biosystems mTRAQ light reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01865	mTRAQ light reporter+balance reagent acylated N-terminal	http://purl.obolibrary.org/obo/MOD_01864	mTRAQ light reporter+balance reagent acylated residue		A protein modification that effectively replaces a hydrogen atom of a protein N-terminal with the Applied Biosystems mTRAQ light reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01866	mTRAQ light reporter+balance reagent N6-acylated lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-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.
http://purl.obolibrary.org/obo/MOD_01867	mTRAQ light reporter+balance reagent O4'-acylated tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively replaces the O4'-hydrogen atom of a tyrosine residue with the Applied Biosystems mTRAQ light reporter+balance group.
http://purl.obolibrary.org/obo/MOD_01868	modifications with monoisotopic mass differences that are nominally equal at 140.094963 Da	http://purl.obolibrary.org/obo/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 of 140.094963 Da.
http://purl.obolibrary.org/obo/MOD_01869	mTRAQ light reporter fragment	http://purl.obolibrary.org/obo/MOD_01870	mTRAQ reporter fragment		The protein modification reporter fragment produced by an Applied Biosystems mTRAQ light reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01870	mTRAQ reporter fragment	http://purl.obolibrary.org/obo/MOD_01520	modification reporter fragment		A protein modification reporter fragment produced by an Applied Biosystems mTRAQ reagent derivatized residue.
http://purl.obolibrary.org/obo/MOD_01871	cyclized N-terminal S-carboxamidomethyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_01160	deaminated residue		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.
http://purl.obolibrary.org/obo/MOD_01872	cyclized N-terminal S-carboxymethyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00704	dehydrated residue		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.
http://purl.obolibrary.org/obo/MOD_01873	N-carboxy-L-alanine	http://purl.obolibrary.org/obo/MOD_01152	carboxylated residue		A protein modification that effectively converts an L-alanine residue to N-carboxy-L-alanine.
http://purl.obolibrary.org/obo/MOD_01874	N-carboxy-L-valine	http://purl.obolibrary.org/obo/MOD_01152	carboxylated residue		A protein modification that effectively converts an L-alanine residue to N-carboxy-L-valine.
http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively replaces an N6-amino hydrogen atom of L-lysine with an acyl group.
http://purl.obolibrary.org/obo/MOD_01877	2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		A protein modification that effectively converts an L-cysteine residue and an L-arginine residue to 2-(4-guanidinobutanoyl)-5-hydroxyimidazole-4-carbothionic acid.
http://purl.obolibrary.org/obo/MOD_01878	L-threonine 5-hydroxyoxazole-4-carbonthionic acid	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		A protein modification that effectively converts an L-cysteine residue and an L-threonine residue to L-threonine 5-hydroxyoxazole-4-carbothionic acid.
http://purl.obolibrary.org/obo/MOD_01879	methanobactin SB2 copper complex	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_01880	L-deoxyhypusine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from RESID
http://purl.obolibrary.org/obo/MOD_01881	3-(L-phenylalan-2'-yl)-L-valine	http://purl.obolibrary.org/obo/MOD_02059	crosslinked L-valine residue		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.
http://purl.obolibrary.org/obo/MOD_01882	5-imidazolinone ring crosslinked residues (Gly)	http://purl.obolibrary.org/obo/MOD_00691	5-imidazolinone ring crosslinked residues		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.
http://purl.obolibrary.org/obo/MOD_01883	5-imidazolinone ring crosslinked residues (Cys)	http://purl.obolibrary.org/obo/MOD_00691	5-imidazolinone ring crosslinked residues		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.
http://purl.obolibrary.org/obo/MOD_01884	4-aminobutylated residue	http://purl.obolibrary.org/obo/MOD_00001	alkylated residue		A protein modification that effectively replaces a hydrogen atom with a 4-aminobutyl group, usually derived from spermidine.
http://purl.obolibrary.org/obo/MOD_01887	Uniblue A derivatized lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_01888	didehydrogenated residue	http://purl.obolibrary.org/obo/MOD_00683	dehydrogenated residue		A protein modification that effectively removes two neutral hydrogen atoms (proton and electron) from a residue.
http://purl.obolibrary.org/obo/MOD_01889	S-(2-succinyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_01890	N-[(L-histidin-1'-yl)methyl]-L-methionine (fMet)	http://purl.obolibrary.org/obo/MOD_02062	crosslinked N-formyl-L-methionine residue		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.
http://purl.obolibrary.org/obo/MOD_01891	N-[(L-histidin-1'-yl)methyl]-L-methionine (Met)	http://purl.obolibrary.org/obo/MOD_02052	crosslinked L-methionine residue		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.
http://purl.obolibrary.org/obo/MOD_01892	N6-crotonyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-crotonyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01893	N6-malonyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-malonyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01894	propanoylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated residue		A protein modification that effectively replaces a hydrogen atom with an propanoyl group.
http://purl.obolibrary.org/obo/MOD_01895	alpha-amino 3x(12)C-labeled propanoylated residue	http://purl.obolibrary.org/obo/MOD_01426	isotope tagged reagent derivatized residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a 3x(12)C-labeled propanoyl group.
http://purl.obolibrary.org/obo/MOD_01896	trifluoroacetic acid adduct	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		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.
http://purl.obolibrary.org/obo/MOD_01897	5-hydroxy-3-methyl-L-proline (Ile)	http://purl.obolibrary.org/obo/MOD_00910	modified L-isoleucine residue		A protein modification that effectively converts an L-isoleucine residue to 5-hydroxy-3-methyl-L-proline.
http://purl.obolibrary.org/obo/MOD_01898	N2,N2-dimethyl-L-arginine	http://purl.obolibrary.org/obo/MOD_00783	dimethylated L-arginine		modification from RESID
http://purl.obolibrary.org/obo/MOD_01899	L-arginine thiazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02041	crosslinked L-arginine residue		A protein modification that effectively crosslinks an L-arginine residue and an L-cysteine residue to form arginine thiazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01900	L-cysteine 5-methyloxazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		A protein modification that effectively crosslinks an L-cysteine residue and an L-threonine residue to form L-cysteine 5-methyloxazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01901	L-threonine 5-methyloxazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_01422	oxazole/oxazoline ring crosslinked residues (Thr)		A protein modification that effectively crosslinks two L-threonine residues to form L-threonine 5-methyloxazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01902	L-isoleucine oxazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02049	crosslinked L-isoleucine residue		A protein modification that effectively crosslinks an L-isoleucine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01903	L-serine oxazole-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_01421	oxazole/oxazoline ring crosslinked residues (Ser)		A protein modification that effectively crosslinks two L-serine residues to form serine oxazole-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01904	L-serine 5-methyloxazoline-4-carboxylic acid	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		A protein modification that effectively crosslinks an L-serine residue and an L-threonine residue to form L-serine 5-methyloxazoline-4-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01905	5-hydroxy-3-methyl-L-proline	http://purl.obolibrary.org/obo/MOD_00859	modified residue that can arise from different natural residues		A protein modification that effectively converts a source amino acid residue to 5-hydroxy-3-methyl-L-proline.
http://purl.obolibrary.org/obo/MOD_01906	dehydromethionine	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine residue to dehydromethionine.
http://purl.obolibrary.org/obo/MOD_01907	dehydromethionine (from L-methioninium)	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methioninium (protonated L-methionine) residue to dehydromethionine.
http://purl.obolibrary.org/obo/MOD_01908	4-sulfophenyl isothiocyanate alpha-amino derivatized residue	http://purl.obolibrary.org/obo/MOD_00584	4-sulfophenyl isothiocyanate derivatized residue		A protein modification that effectively converts a residue to the 4-sulfophenyl isothiocyanate adduct, alpha-amino-[(4-sulfophenyl)carbamothioyl] residue.
http://purl.obolibrary.org/obo/MOD_01909	6x(13)C labeled 4-sulfophenyl isothiocyanate alpha-amino derivatized residue	http://purl.obolibrary.org/obo/MOD_00880	6x(13)C labeled 4-sulfophenyl isothiocyanate 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.
http://purl.obolibrary.org/obo/MOD_01910	monofluorinated residue	http://purl.obolibrary.org/obo/MOD_00498	fluorinated residue		A protein modification that effectively substitutes one hydrogen atom of a residue with one fluorine atom.
http://purl.obolibrary.org/obo/MOD_01911	monochlorinated residue	http://purl.obolibrary.org/obo/MOD_00753	chlorinated residue		A protein modification that effectively substitutes one hydrogen atom of a residue with one chlorine atom.
http://purl.obolibrary.org/obo/MOD_01912	monobrominated residue	http://purl.obolibrary.org/obo/MOD_00754	brominated residue		A protein modification that effectively substitutes one hydrogen atom of a residue with one bromine atom.
http://purl.obolibrary.org/obo/MOD_01913	monochlorinated L-tryptophan	http://purl.obolibrary.org/obo/MOD_01911	monochlorinated residue		A protein modification that effectively substitutes one hydrogen atom of an L-tryptophan residue with one chlorine atom.
http://purl.obolibrary.org/obo/MOD_01914	O5-galactosyl-L-hydroxylysine	http://purl.obolibrary.org/obo/MOD_00396	O-glycosylated residue		A protein modification that effectively converts a 5-hydroxy-L-lysine residue to O5-galactosyl-L-hydroxylysine.
http://purl.obolibrary.org/obo/MOD_01915	N-formyl-L-alanine	http://purl.obolibrary.org/obo/MOD_00901	modified L-alanine residue		A protein modification that effectively converts an L-alanine residue to N-formyl-L-alanine.
http://purl.obolibrary.org/obo/MOD_01916	O4'-(N-acetylamino)galactosyl-L-tyrosine	http://purl.obolibrary.org/obo/MOD_01927	O-glycosyl-L-tyrosine		A protein modification that effectively converts an L-tyrosine residue to O4'-(N-acetylamino)galactosyl-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_01917	N6-(L-isoaspartyl)-L-lysine (Asp)	http://purl.obolibrary.org/obo/MOD_02043	crosslinked L-aspartic acid residue		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.
http://purl.obolibrary.org/obo/MOD_01918	(2S,5S)-5-hydroxylysine	http://purl.obolibrary.org/obo/MOD_00037	5-hydroxy-L-lysine		A protein modification that effectively converts an L-lysine residue to (2S,5S)-5-hydroxylysine.
http://purl.obolibrary.org/obo/MOD_01919	(2S,3S)-3-hydroxyaspartic acid	http://purl.obolibrary.org/obo/MOD_01926	3-hydroxy-L-aspartic acid		A protein modification that effectively converts an L-aspartic acid residue to (2S,3S)-3-hydroxyaspartic acid.
http://purl.obolibrary.org/obo/MOD_01920	3-hydroxy-L-histidine	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that effectively converts an L-histidine residue to 3-hydroxy-L-histidine.
http://purl.obolibrary.org/obo/MOD_01921	D-aspartic acid (Asp)	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to D-aspartic acid.
http://purl.obolibrary.org/obo/MOD_01922	3-methoxydehydroalanine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to 3-methoxydehydroalanine.
http://purl.obolibrary.org/obo/MOD_01923	N6-(L-aspartyl)-L-lysine	http://purl.obolibrary.org/obo/MOD_02043	crosslinked L-aspartic acid residue		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.
http://purl.obolibrary.org/obo/MOD_01924	S-octanoyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-octanoyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_01925	(2S,5R)-5-hydroxylysine	http://purl.obolibrary.org/obo/MOD_00037	5-hydroxy-L-lysine		A protein modification that effectively converts an L-lysine residue to (2S,5R)-5-hydroxylysine.
http://purl.obolibrary.org/obo/MOD_01926	3-hydroxy-L-aspartic acid	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to one of the diastereomeric 3-hydroxy-L-aspartic acid residues.
http://purl.obolibrary.org/obo/MOD_01927	O-glycosyl-L-tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an L-tyrosine residue to O4'-glycosyltyrosine.
http://purl.obolibrary.org/obo/MOD_01928	N-(L-isoaspartyl)-glycine	http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue		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.
http://purl.obolibrary.org/obo/MOD_01929	N6-(L-isoaspartyl)-L-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated 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.
http://purl.obolibrary.org/obo/MOD_01930	D-aspartic acid (Asn)	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively converts an L-asparagine residue to D-aspartic acid.
http://purl.obolibrary.org/obo/MOD_01931	N6-phospho-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to N6-phospho-L-lysine.
http://purl.obolibrary.org/obo/MOD_01932	L-lysinonorleucine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		A protein modification that effectively cross-links two lysine residues with a carbon-nitrogen bond to form L-lysinonorleucine..
http://purl.obolibrary.org/obo/MOD_01933	desmosine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		A protein modification that effectively cross-links four L-lysine residues to form desmosine.
http://purl.obolibrary.org/obo/MOD_01934	isodesmosine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		A protein modification that effectively cross-links four L-lysine residues to form isodesmosine.
http://purl.obolibrary.org/obo/MOD_01935	O-glucosyl-L-hydroxylysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		modification from RESID
http://purl.obolibrary.org/obo/MOD_01936	N6-oleoyl-L-lysine	http://purl.obolibrary.org/obo/MOD_02011	N-oleoylated residue		A protein modification that effectively converts an L-lysine residue to N6-oleoyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01937	N-palmitoyl-L-methionine	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine residue to N-palmitoyl-L-methionine.
http://purl.obolibrary.org/obo/MOD_01938	2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid (Asn)	http://purl.obolibrary.org/obo/MOD_02042	crosslinked L-asparagine residue		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.
http://purl.obolibrary.org/obo/MOD_01939	2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid (Asp)	http://purl.obolibrary.org/obo/MOD_02043	crosslinked L-aspartic acid residue		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.
http://purl.obolibrary.org/obo/MOD_01940	2-(2-aminosuccinimidyl)pentanedioic acid (Asn)	http://purl.obolibrary.org/obo/MOD_02042	crosslinked L-asparagine residue		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.
http://purl.obolibrary.org/obo/MOD_01941	2-(2-aminosuccinimidyl)pentanedioic acid (Asp)	http://purl.obolibrary.org/obo/MOD_02043	crosslinked L-aspartic acid residue		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.
http://purl.obolibrary.org/obo/MOD_01942	D-aspartic acid	http://purl.obolibrary.org/obo/MOD_00859	modified residue that can arise from different natural residues		A protein modification that effectively converts a source amino acid residue to D-aspartic acid.
http://purl.obolibrary.org/obo/MOD_01943	pyrrolidione ring crosslinked residues	http://purl.obolibrary.org/obo/MOD_00033	crosslinked residues		A protein modification that crosslinks two adjacent residues by formation of a pyrrolidione ring.
http://purl.obolibrary.org/obo/MOD_01944	2-aminosuccinimide ring crosslinked residues	http://purl.obolibrary.org/obo/MOD_00033	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.
http://purl.obolibrary.org/obo/MOD_01945	2-(2-aminosuccinimidyl)-3-sulfanylpropanoic acid	http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_01946	2-(2-aminosuccinimidyl)pentanedioic acid	http://purl.obolibrary.org/obo/MOD_02045	crosslinked L-glutamic acid residue		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.
http://purl.obolibrary.org/obo/MOD_01947	O-(L-isoaspartyl)-L-threonine (cross-link)	http://purl.obolibrary.org/obo/MOD_02043	crosslinked L-aspartic acid residue		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.
http://purl.obolibrary.org/obo/MOD_01948	labionin	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_01949	coelenterazine	http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue		A protein modification that effectively cross-links a phenylalanine and two tyrosine residues to form coelenterazine.
http://purl.obolibrary.org/obo/MOD_01950	L-isoglutamyl histamine	http://purl.obolibrary.org/obo/MOD_00907	modified L-glutamine residue		A protein modification that effectively converts an L-glutamine residue to L-isoglutamyl histamine.
http://purl.obolibrary.org/obo/MOD_01951	O-(L-isoglutamyl)-L-serine (Gln-Ser)	http://purl.obolibrary.org/obo/MOD_02046	crosslinked L-glutamine residue		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.
http://purl.obolibrary.org/obo/MOD_01952	O-(L-isoglutamyl)-L-threonine (Gln-Thr)	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_01953	tetrakis-L-cysteinyl tetrairon octanitrosyl	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		A protein modification that effectively converts four L-cysteine residues and a four-iron cluster to tetrakis-L-cysteinyl tetrairon octanitrosyl.
http://purl.obolibrary.org/obo/MOD_01954	dehydroalanine (Sec)	http://purl.obolibrary.org/obo/MOD_01168	dehydroalanine		A protein modification that effectively converts an L-selenocysteine residue to dehydroalanine.
http://purl.obolibrary.org/obo/MOD_01955	L-alaninato bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese pentoxide	http://purl.obolibrary.org/obo/MOD_02065	metal or metal cluster coordinated L-alanine residue		modification from RESID
http://purl.obolibrary.org/obo/MOD_01956	(3R)-3-hydroxy-L-arginine	http://purl.obolibrary.org/obo/MOD_00682	hydroxylated arginine		A protein modification that effectively converts an L-arginine residue to (3R)-3-hydroxy-L-arginine.
http://purl.obolibrary.org/obo/MOD_01957	2-hydroxyproline	http://purl.obolibrary.org/obo/MOD_01024	monohydroxylated proline		A protein modification that effectively converts an L-proline residue to 2-hydroxyproline.
http://purl.obolibrary.org/obo/MOD_01958	bis-L-cysteinyl bisglutathion-S-yl diiron disulfide	http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_01959	tris-L-cysteinyl L-glutamato tetrairon tetrasulfide	http://purl.obolibrary.org/obo/MOD_02068	metal or metal cluster coordinated L-glutamic acid residue		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.
http://purl.obolibrary.org/obo/MOD_01960	tris-L-cysteinyl L-glutamin-O6-yl tetrairon tetrasulfide	http://purl.obolibrary.org/obo/MOD_02069	metal or metal cluster coordinated L-glutamine residue		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.
http://purl.obolibrary.org/obo/MOD_01962	N4-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-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.
http://purl.obolibrary.org/obo/MOD_01963	O-(2,4-diacetamido-2,4,6-trideoxy-D-glucosyl)-L-serine	http://purl.obolibrary.org/obo/MOD_00002	O-glycosyl-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.
http://purl.obolibrary.org/obo/MOD_01964	O-(2-acetamido-4-glyceramido-2,4,6-trideoxy-D-glucosyl)-L-serine	http://purl.obolibrary.org/obo/MOD_00002	O-glycosyl-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.
http://purl.obolibrary.org/obo/MOD_01965	2xC(13),3x(2)H labeled N6-acetyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01431	(2)H deuterium tagged reagent		A protein modification that effectively converts an L-lysine residue to 2xC(13),3x(2)H labeled N6-acetyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_01967	omega-N-(N-acetylamino)glucosyl-L-arginine	http://purl.obolibrary.org/obo/MOD_00448	mono-N-acetylaminoglucosylated residue		A protein modification that effectively converts an L-arginine residue to  omega-N-(N-acetylamino)glucosyl-L-arginine.
http://purl.obolibrary.org/obo/MOD_01968	(2R,3R,2'R)-3-methyllanthionine	http://purl.obolibrary.org/obo/MOD_01981	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.
http://purl.obolibrary.org/obo/MOD_01969	S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine.
http://purl.obolibrary.org/obo/MOD_01970	5-glutamyl glutamic acid	http://purl.obolibrary.org/obo/MOD_00207	L-isoglutamyl-polyglutamic 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.
http://purl.obolibrary.org/obo/MOD_01971	5-glutamyl N2-ornithine	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to N2-ornithine.
http://purl.obolibrary.org/obo/MOD_01972	5-glutamyl coenzyme A thioester	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to 5-glutamyl coenzyme A thioester.
http://purl.obolibrary.org/obo/MOD_01973	N6-(3-phosphoglyceryl)-L-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-(3-phosphoglyceryl)-L-lysine.
http://purl.obolibrary.org/obo/MOD_01974	S-methyl-L-methionine	http://purl.obolibrary.org/obo/MOD_00716	methylated methionine		A protein modification that effectively converts an L-methionine residue to S-methyl-L-methionine.
http://purl.obolibrary.org/obo/MOD_01975	S-poly(3-hydroxybutyrate)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-(poly-3-hydroxybutyrate)-L-cysteine.
http://purl.obolibrary.org/obo/MOD_01976	O3-(poly-3-hydroxybutyrate)-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O3-(poly-3-hydroxybutyrate)-L-serine.
http://purl.obolibrary.org/obo/MOD_01977	O-(L-isoglutamyl)-L-serine	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_01978	O-(L-isoaspartyl)-L-threonine	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_01979	O-(L-isoglutamyl)-L-threonine	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_01980	omega-N-glycosyl-L-arginine	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		A protein modification that effectively converts an L-arginine residue to N4-glycosyl-arginine.
http://purl.obolibrary.org/obo/MOD_01981	3-methyllanthionine	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_01982	N,N,N-trimethylglycine	http://purl.obolibrary.org/obo/MOD_01698	alpha-amino trimethylated protonated-residue		modification from RESID
http://purl.obolibrary.org/obo/MOD_01983	N,N-dimethylglycine	http://purl.obolibrary.org/obo/MOD_01686	alpha-amino dimethylated residue		A protein modification that effectively converts a glycine residue to N,N-dimethyllglycine.
http://purl.obolibrary.org/obo/MOD_01984	2-(L-cystein-S-yl)-L-alanine	http://purl.obolibrary.org/obo/MOD_02040	crosslinked L-alanine residue		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.
http://purl.obolibrary.org/obo/MOD_01985	2-(L-cystein-S-yl)-D-asparagine	http://purl.obolibrary.org/obo/MOD_02060	crosslinked D-asparagine residue		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.
http://purl.obolibrary.org/obo/MOD_01986	2-(L-cystein-S-yl)-L-serine	http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_01987	2-(L-cystein-S-yl)-D-serine	http://purl.obolibrary.org/obo/MOD_02064	crosslinked D-serine residue		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.
http://purl.obolibrary.org/obo/MOD_01988	2-(L-cystein-S-yl)-L-threonine	http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue		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.
http://purl.obolibrary.org/obo/MOD_01989	2-(L-cystein-S-yl)-D-tyrosine	http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue		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.
http://purl.obolibrary.org/obo/MOD_01990	protonated glycine (glycinium) residue	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to a glycinium (protonated glycine).
http://purl.obolibrary.org/obo/MOD_01991	N,N,N-trimethylglycine (from glycinium)	http://purl.obolibrary.org/obo/MOD_01687	alpha-amino trimethylated residue		A protein modification that effectively converts a glycinium (protonated glycine) residue to an N,N,N-trimethylglycine.
http://purl.obolibrary.org/obo/MOD_01992	alpha-carbon thioether crosslinked residues	http://purl.obolibrary.org/obo/MOD_00687	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.
http://purl.obolibrary.org/obo/MOD_01993	beta-carbon thioether crosslinked residues	http://purl.obolibrary.org/obo/MOD_00687	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.
http://purl.obolibrary.org/obo/MOD_01994	N1'-formyl-L-tryptophan	http://purl.obolibrary.org/obo/MOD_01106	N-formyl-L-tryptophan		A protein modification that effectively converts an L-tryptophan residue to N1'-formyl-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01995	N2-formyl-L-tryptophan	http://purl.obolibrary.org/obo/MOD_01106	N-formyl-L-tryptophan		A protein modification that effectively converts an L-tryptophan residue to N2-formyl-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_01996	butanoylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated residue		A protein modification that effectively replaces a hydrogen atom with an butanoyl group.
http://purl.obolibrary.org/obo/MOD_01997	N-butanoylated residue	http://purl.obolibrary.org/obo/MOD_01996	butanoylated residue		A protein modification that effectively replaces a residue amino or imino hydrogen with a butanoyl group.
http://purl.obolibrary.org/obo/MOD_01998	alpha-amino butanoylated residue	http://purl.obolibrary.org/obo/MOD_01997	N-butanoylated residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with a butanoyl group.
http://purl.obolibrary.org/obo/MOD_01999	N6-(11-cis)-retinylidene-L-lysine	http://purl.obolibrary.org/obo/MOD_02000	N6-retinylidene-L-lysine (unspecified geometric isomer)		A protein modification that effectively converts an L-lysine residue to N6-retinylidene-(11-cis)-L-lysine.
http://purl.obolibrary.org/obo/MOD_02000	N6-retinylidene-L-lysine (unspecified geometric isomer)	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine (unspecified geometric isomer).
http://purl.obolibrary.org/obo/MOD_02077	nitrosylated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively replaces a hydrogen atom with an nitrosyl (NO) group.
http://purl.obolibrary.org/obo/MOD_02078	acetylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated residue		A protein modification that effectively replaces one or more hydrogen atoms with one or more acetyl groups.
http://purl.obolibrary.org/obo/MOD_02079	diacetylated residue	http://purl.obolibrary.org/obo/MOD_02078	acetylated residue		A protein modification that effectively replaces one hydrogen atom with one acetyl group.
http://purl.obolibrary.org/obo/MOD_02080	diacetylated L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		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.
http://purl.obolibrary.org/obo/MOD_01112	nicotinoyl lysine	http://purl.obolibrary.org/obo/MOD_00947	DeltaMass		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_02099	residue modified by radical hydroxylation	http://purl.obolibrary.org/obo/MOD_02098	residue modified by radical mechanism		A hydroxyl substition induced by a radical reaction.
http://purl.obolibrary.org/obo/MOD_02106	4-hydroxy-L-tryptophan	http://purl.obolibrary.org/obo/MOD_01622	monohydroxylated tryptophan		A protein modification that effectively converts an L-tryptophan residue to a 4-hydroxy-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_00401	Gygi ICAT(TM) d0 modified cysteine	http://purl.obolibrary.org/obo/MOD_01820	isotope tagged sufhydryl reagent 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.
http://purl.obolibrary.org/obo/MOD_00659	methylated glutamine	http://purl.obolibrary.org/obo/MOD_00907	modified L-glutamine residue		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.
http://purl.obolibrary.org/obo/MOD_00006	N-glycosylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated residue		A protein modification that effectively replaces a residue hydrogen atom on a nitrogen with a carbohydrate-like group through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_00030	N-formyl-L-methionine residue	http://purl.obolibrary.org/obo/MOD_00868	natural, non-standard encoded residue		A protein modification that effectively converts a source amino acid residue to an N-formyl-L-methionine, a natural pretranslational modification.
http://purl.obolibrary.org/obo/MOD_00031	L-selenocysteine residue	http://purl.obolibrary.org/obo/MOD_00868	natural, non-standard encoded residue		A protein modification that effectively converts a source amino acid residue to an L-selenocysteine, a natural pretranslational modification.
http://purl.obolibrary.org/obo/MOD_00033	crosslinked residues	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that crosslinks two or more amino acid residues with covalent bonds.
http://purl.obolibrary.org/obo/MOD_00036	(2S,3R)-3-hydroxyaspartic acid	http://purl.obolibrary.org/obo/MOD_01926	3-hydroxy-L-aspartic acid		A protein modification that effectively converts an L-aspartic acid residue to (2S,3R)-3-hydroxyaspartic acid.
http://purl.obolibrary.org/obo/MOD_00037	5-hydroxy-L-lysine	http://purl.obolibrary.org/obo/MOD_01047	monohydroxylated lysine		A protein modification that effectively converts an L-lysine  residue to one of the diastereomeric 5-hydroxy-L-lysine  residues.
http://purl.obolibrary.org/obo/MOD_00038	3-hydroxy-L-proline	http://purl.obolibrary.org/obo/MOD_01024	monohydroxylated proline		A protein modification that effectively converts an L-proline residue to 3-hydroxy-L-proline.
http://purl.obolibrary.org/obo/MOD_00039	4-hydroxy-L-proline	http://purl.obolibrary.org/obo/MOD_01024	monohydroxylated proline		A protein modification that effectively converts an L-proline residue to 4-hydroxy-L-proline
http://purl.obolibrary.org/obo/MOD_00040	2-pyrrolidone-5-carboxylic acid (Gln)	http://purl.obolibrary.org/obo/MOD_01160	deaminated residue		A protein modification that effectively converts an L-glutamine residue to 2-pyrrolidone-5-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_00041	L-gamma-carboxyglutamic acid	http://purl.obolibrary.org/obo/MOD_01152	carboxylated residue		A protein modification that effectively converts an L-glutamic acid residue to L-gamma-carboxyglutamic acid.
http://purl.obolibrary.org/obo/MOD_00042	L-aspartic 4-phosphoric anhydride	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to L-aspartic 4-phosphoric anhydride.
http://purl.obolibrary.org/obo/MOD_00045	3'-phospho-L-histidine	http://purl.obolibrary.org/obo/MOD_00890	phosphorylated 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).
http://purl.obolibrary.org/obo/MOD_00046	O-phospho-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-phospho-L-serine.
http://purl.obolibrary.org/obo/MOD_00047	O-phospho-L-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively converts an L-threonine residue to O-phospho-L-threonine.
http://purl.obolibrary.org/obo/MOD_00048	O4'-phospho-L-tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an L-tyrosine residue to O4'-phospho-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_00050	N-acetyl-L-alanine	http://purl.obolibrary.org/obo/MOD_00901	modified L-alanine residue		A protein modification that effectively converts an L-alanine residue to N-acetyl-L-alanine.
http://purl.obolibrary.org/obo/MOD_00053	N-acetyl-L-glutamic acid	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to N-acetyl-L-glutamic acid.
http://purl.obolibrary.org/obo/MOD_00055	N-acetylglycine	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to N-acetylglycine.
http://purl.obolibrary.org/obo/MOD_00058	N-acetyl-L-methionine	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that effectively converts an L-methionine to N-acetyl-L-methionine.
http://purl.obolibrary.org/obo/MOD_00060	N-acetyl-L-serine	http://purl.obolibrary.org/obo/MOD_01458	alpha-amino acetylated residue		A protein modification that effectively converts an L-serine residue to N-acetyl-L-serine.
http://purl.obolibrary.org/obo/MOD_00064	N6-acetyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00723	N-acetylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-acetyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00068	N-myristoylglycine	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that effectively converts a glycine residue to N-myristoylglycine.
http://purl.obolibrary.org/obo/MOD_00069	N-palmitoyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_01685	alpha-amino palmitoylated residue		A protein modification that effectively converts an L-cysteine residue to N-palmitoyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00076	symmetric dimethyl-L-arginine	http://purl.obolibrary.org/obo/MOD_00783	dimethylated L-arginine		A protein modification that effectively converts an L-arginine residue to symmetric dimethylarginine, N(omega),N'(omega)-dimethyl-L-arginine.
http://purl.obolibrary.org/obo/MOD_00077	asymmetric dimethyl-L-arginine	http://purl.obolibrary.org/obo/MOD_00783	dimethylated L-arginine		A protein modification that effectively converts an L-arginine residue to asymmetric dimethylarginine, N(omega),N(omega)-dimethyl-L-arginine.
http://purl.obolibrary.org/obo/MOD_00078	omega-N-methyl-L-arginine	http://purl.obolibrary.org/obo/MOD_00414	monomethylated L-arginine		A protein modification that effectively converts an L-arginine residue to N(omega)-methyl-L-arginine.
http://purl.obolibrary.org/obo/MOD_00083	N6,N6,N6-trimethyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00663	methylated lysine		A protein modification that effectively converts an L-lysine residue to N6,N6,N6-trimethyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00084	N6,N6-dimethyl-L-lysine	http://purl.obolibrary.org/obo/MOD_00663	methylated lysine		A protein modification that effectively converts an L-lysine residue to N6,N6-dimethyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00085	N6-methyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01683	monomethylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00087	N6-myristoyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-myristoyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00111	S-farnesyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_01110	isoprenylated cysteine		A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00113	S-geranylgeranyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_01110	isoprenylated cysteine		A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00114	L-cysteine methyl ester	http://purl.obolibrary.org/obo/MOD_01689	alpha-carboxyl methylated residue		A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl ester.
http://purl.obolibrary.org/obo/MOD_00115	S-palmitoyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_01684	palmitoylated-L-cysteine		A protein modification that effectively converts an L-cysteine residue to S-palmitoyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00126	N6-biotinyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01885	biotinylated residue		A protein modification that effectively converts an L-lysine residue to N6-biotinyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00127	N6-lipoyl-L-lysine	http://purl.obolibrary.org/obo/MOD_01875	N6-acylated L-lysine		A protein modification that effectively converts an L-lysine residue to N6-lipoyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00128	N6-pyridoxal phosphate-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to N6-pyridoxal phosphate-L-lysine.
http://purl.obolibrary.org/obo/MOD_00133	N6-(L-isoglutamyl)-L-lysine (Gln)	http://purl.obolibrary.org/obo/MOD_02046	crosslinked L-glutamine residue		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.
http://purl.obolibrary.org/obo/MOD_00159	O-phosphopantetheine-L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively converts an L-serine residue to O-phosphopantetheine-L-serine.
http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively converts an L-asparagine residue to an N4-glycosyl-L-asparagine.
http://purl.obolibrary.org/obo/MOD_00164	O-(N-acetylamino)galactosyl-L-threonine	http://purl.obolibrary.org/obo/MOD_01676	O-(N-acetylamino)hexosyl-L-threonine		A protein modification that effectively converts an L-asparagine residue to O-(N-acetylaminogalactosyl)-L-threonine.
http://purl.obolibrary.org/obo/MOD_00167	N-asparaginyl-glycosylphosphatidylinositolethanolamine	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that effectively converts an L-asparagine residue to N-asparaginyl-glycosylphosphatidylinositolethanolamine.
http://purl.obolibrary.org/obo/MOD_00213	chondroitin sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine	http://purl.obolibrary.org/obo/MOD_00002	O-glycosyl-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.
http://purl.obolibrary.org/obo/MOD_00215	heparan sulfate D-glucuronosyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine	http://purl.obolibrary.org/obo/MOD_00002	O-glycosyl-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.
http://purl.obolibrary.org/obo/MOD_00219	L-citrulline	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		A protein modification that effectively converts an L-arginine residue to L-citrulline.
http://purl.obolibrary.org/obo/MOD_00222	2'-alpha-mannosyl-L-tryptophan	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that effectively converts an L-tryptophan residue to 2'-alpha-mannosyl-L-tryptophan.
http://purl.obolibrary.org/obo/MOD_00235	S-nitrosyl-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-nitrosyl-L-cysteine.
http://purl.obolibrary.org/obo/MOD_00237	L-beta-methylthioaspartic acid	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that effectively converts an L-aspartic acid residue to L-beta-methylthioaspartic acid.
http://purl.obolibrary.org/obo/MOD_00295	O-octanoyl-L-serine	http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine		A protein modification that effectively converts an L-serine residue to O-octanoyl-L-serine.
http://purl.obolibrary.org/obo/MOD_00300	L-glutamyl-5-poly(ADP-ribose)	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that effectively converts an L-glutamic acid residue to L-glutamyl-5-poly(ADP-ribose).
http://purl.obolibrary.org/obo/MOD_00314	glycine cholesterol ester	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively converts a glycine residue to glycine cholesterol ester.
http://purl.obolibrary.org/obo/MOD_00394	monoacetylated residue	http://purl.obolibrary.org/obo/MOD_02078	acetylated residue		A protein modification that effectively replaces one hydrogen atom with one acetyl group.
http://purl.obolibrary.org/obo/MOD_00396	O-glycosylated residue	http://purl.obolibrary.org/obo/MOD_00693	glycosylated residue		A protein modification that effectively replaces a residue hydrogen atom on an oxygen with a carbohydrate-like group through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_00414	monomethylated L-arginine	http://purl.obolibrary.org/obo/MOD_00599	monomethylated residue		A protein modification that effectively replaces one hydrogen atom of an L-arginine residue with one methyl group.
http://purl.obolibrary.org/obo/MOD_00427	methylated residue	http://purl.obolibrary.org/obo/MOD_00001	alkylated residue		A protein modification that effectively replaces a hydrogen atom with a methyl group.
http://purl.obolibrary.org/obo/MOD_00437	farnesylated residue	http://purl.obolibrary.org/obo/MOD_00703	isoprenylated residue		A protein modification that effectively replaces a hydrogen atom with a farnesyl group.
http://purl.obolibrary.org/obo/MOD_00438	myristoylated residue	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively replaces a hydrogen atom with a myristoyl group.
http://purl.obolibrary.org/obo/MOD_00440	palmitoylated residue	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively replaces a hydrogen atom with a palmitoyl group.
http://purl.obolibrary.org/obo/MOD_00448	mono-N-acetylaminoglucosylated residue	http://purl.obolibrary.org/obo/MOD_01673	N-acetylaminohexosylated residue		A protein modification that effectively replaces a hydrogen atom with an N-acetylaminoglucose group through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_00599	monomethylated residue	http://purl.obolibrary.org/obo/MOD_00427	methylated residue		A protein modification that effectively replaces one hydrogen atom with one methyl group.
http://purl.obolibrary.org/obo/MOD_00601	cyclized residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		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.
http://purl.obolibrary.org/obo/MOD_00649	acylated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively replaces a hydrogen atom with an acyl group.
http://purl.obolibrary.org/obo/MOD_00663	methylated lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to a methylated lysine.
http://purl.obolibrary.org/obo/MOD_00666	octanoylated residue	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively replaces a hydrogen atom with an octanoyl group.
http://purl.obolibrary.org/obo/MOD_00670	N-acylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated residue		A protein modification that effectively replaces a residue alpha-amino- or alpha-imino-hydrogen with an acyl group.
http://purl.obolibrary.org/obo/MOD_00677	hydroxylated residue	http://purl.obolibrary.org/obo/MOD_00679	carbon oxygenated residue		A protein modification that effectively replaces a hydrogen atom with an hydroxyl group.
http://purl.obolibrary.org/obo/MOD_00693	glycosylated residue	http://purl.obolibrary.org/obo/MOD_00764	glycoconjugated residue		A protein modification that effectively replaces a hydrogen atom with an carbohydrate-like group through a glycosidic bond.
http://purl.obolibrary.org/obo/MOD_00696	phosphorylated residue	http://purl.obolibrary.org/obo/MOD_00861	phosphorus containing modified residue		A protein modification that effectively replaces a hydrogen atom with a phosphono group (H2PO3 or 'phosphate').
http://purl.obolibrary.org/obo/MOD_00701	nucleotide or nucleic acid modified residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		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.
http://purl.obolibrary.org/obo/MOD_00703	isoprenylated residue	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated 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.
http://purl.obolibrary.org/obo/MOD_00723	N-acetylated L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to either N2-acetyl-L-lysine, or N6-acetyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_00752	monoadenosine diphosphoribosyl (ADP-ribosyl) modified residue	http://purl.obolibrary.org/obo/MOD_02087	adenosine 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.
http://purl.obolibrary.org/obo/MOD_00754	brominated residue	http://purl.obolibrary.org/obo/MOD_00694	halogen containing residue		A protein modification that effectively substitutes a bromine atom for a hydrogen atom.
http://purl.obolibrary.org/obo/MOD_00764	glycoconjugated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		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.
http://purl.obolibrary.org/obo/MOD_00783	dimethylated L-arginine	http://purl.obolibrary.org/obo/MOD_00658	methylated arginine		A protein modification that effectively replaces two hydrogen atoms of an L-arginine residue with two methyl groups.
http://purl.obolibrary.org/obo/MOD_00805	O-(N-acetylamino)glucosyl-L-serine	http://purl.obolibrary.org/obo/MOD_00448	mono-N-acetylaminoglucosylated residue		A protein modification that effectively converts an L-serine residue to O3-(N-acetylaminoglucosyl)-L-serine.
http://purl.obolibrary.org/obo/MOD_00806	O-(N-acetylamino)glucosyl-L-threonine	http://purl.obolibrary.org/obo/MOD_00448	mono-N-acetylaminoglucosylated residue		A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminoglucosyl)-L-threonine.
http://purl.obolibrary.org/obo/MOD_00812	O-fucosyl-L-serine	http://purl.obolibrary.org/obo/MOD_00614	fucosylated residue		A protein modification that effectively converts an L-serine residue to an O-fucosylserine.
http://purl.obolibrary.org/obo/MOD_00813	O-fucosyl-L-threonine	http://purl.obolibrary.org/obo/MOD_00614	fucosylated residue		A protein modification that effectively converts an threonine residue to an O-fucosylthreonine.
http://purl.obolibrary.org/obo/MOD_00814	O-xylosyl-L-serine	http://purl.obolibrary.org/obo/MOD_00002	O-glycosyl-L-serine		A protein modification that effectively converts an L-serine residue to O3-xylosylserine.
http://purl.obolibrary.org/obo/MOD_00818	glycosylphosphatidylinositolated residue	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively converts a residue to a glycosylphosphatidylinositolethanolamidated.
http://purl.obolibrary.org/obo/MOD_00831	N4-(N-acetylamino)glucosyl-L-asparagine	http://purl.obolibrary.org/obo/MOD_00448	mono-N-acetylaminoglucosylated residue		A protein modification that effectively converts an L-asparagine residue to N4-(N-acetylaminoglucosyl)-L-asparagine.
http://purl.obolibrary.org/obo/MOD_00901	modified L-alanine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-alanine.
http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-arginine residue.
http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-asparagine residue.
http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-aspartic acid residue.
http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-cysteine residue.
http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-glutamic acid residue.
http://purl.obolibrary.org/obo/MOD_00907	modified L-glutamine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-glutamine residue.
http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies a glycine residue.
http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-histidine residue.
http://purl.obolibrary.org/obo/MOD_00910	modified L-isoleucine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-isoleucine residue.
http://purl.obolibrary.org/obo/MOD_00911	modified L-leucine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-leucine residue.
http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-lysine residue.
http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-methionine residue.
http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-phenylalanine residue.
http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-proline residue.
http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-serine residue.
http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-threonine residue.
http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-tryptophan residue.
http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-tyrosine residue.
http://purl.obolibrary.org/obo/MOD_00920	modified L-valine residue	http://purl.obolibrary.org/obo/MOD_01157	protein modification categorized by amino acid modified		A protein modification that modifies an L-valine residue.
http://purl.obolibrary.org/obo/MOD_01048	2-pyrrolidone-5-carboxylic acid	http://purl.obolibrary.org/obo/MOD_00601	cyclized residue		A protein modification that effectively converts a source amino acid residue to 2-pyrrolidone-5-carboxylic acid.
http://purl.obolibrary.org/obo/MOD_01110	isoprenylated cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		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).
http://purl.obolibrary.org/obo/MOD_01119	S-geranylgeranyl-L-cysteine methyl ester	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine methyl ester.
http://purl.obolibrary.org/obo/MOD_01148	ubiquitinylated lysine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a ubiquitin.
http://purl.obolibrary.org/obo/MOD_01149	sumoylated lysine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_01150	neddylated lysine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a nedd8 protein.
http://purl.obolibrary.org/obo/MOD_01152	carboxylated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively replaces a hydrogen atom with a carboxylic acid group.
http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively results from forming an adduct with a compound containing a lipid-like group either through acylation, alkylation, or amidation.
http://purl.obolibrary.org/obo/MOD_01160	deaminated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		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.
http://purl.obolibrary.org/obo/MOD_01240	ubiquitination signature tetrapeptidyl lysine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		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.
http://purl.obolibrary.org/obo/MOD_01352	nitrated L-tyrosine	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that effectively converts an L-tyrosine residue to a nitrated L-tyrosine.
http://purl.obolibrary.org/obo/MOD_01399	N6-(ADP-ribosyl)-L-lysine	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that effectively converts an L-lysine residue to an N6-(ADP-ribosyl)-L-lysine.
http://purl.obolibrary.org/obo/MOD_01683	monomethylated L-lysine	http://purl.obolibrary.org/obo/MOD_00663	methylated lysine		A protein modification that effectively replaces one hydrogen atom of an L-lysine residue with one methyl group.
http://purl.obolibrary.org/obo/MOD_01786	3'-nitro-L-tyrosine	http://purl.obolibrary.org/obo/MOD_01352	nitrated L-tyrosine		A protein modification that effectively converts an L-tyrosine residue to 3'-nitro-L-tyrosine.
http://purl.obolibrary.org/obo/MOD_01885	biotinylated residue	http://purl.obolibrary.org/obo/MOD_00649	acylated residue		A protein modification that effectively replaces a hydrogen atom with a biotinyl group.
http://purl.obolibrary.org/obo/MOD_01886	thiolated residue	http://purl.obolibrary.org/obo/MOD_00860	sulfur containing modified residue		A protein modification that effectively replaces a hydrogen atom with an sulfanyl or substituted sulfanyl group.
http://purl.obolibrary.org/obo/MOD_02039	aminated residue	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively replaces a hydrogen group with a amino group
http://purl.obolibrary.org/obo/MOD_02040	crosslinked L-alanine residue	http://purl.obolibrary.org/obo/MOD_00901	modified L-alanine residue		A protein modification that contains an L-alanine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02041	crosslinked L-arginine residue	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		A protein modification that contains an L-arginine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02042	crosslinked L-asparagine residue	http://purl.obolibrary.org/obo/MOD_00903	modified L-asparagine residue		A protein modification that contains an L-asparagine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02043	crosslinked L-aspartic acid residue	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that contains an L-aspartic acid residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02044	crosslinked L-cysteine residue	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that contains an L-cysteine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02045	crosslinked L-glutamic acid residue	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that contains an L-glutamic acid residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02046	crosslinked L-glutamine residue	http://purl.obolibrary.org/obo/MOD_00907	modified L-glutamine residue		A protein modification that contains an L-glutamine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02047	crosslinked glycine residue	http://purl.obolibrary.org/obo/MOD_00908	modified glycine residue		A protein modification that contains a glycine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02048	crosslinked L-histidine residue	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that contains an L-histidine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02049	crosslinked L-isoleucine residue	http://purl.obolibrary.org/obo/MOD_00910	modified L-isoleucine residue		A protein modification that contains an L-isoleucine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02050	crosslinked L-leucine residue	http://purl.obolibrary.org/obo/MOD_00911	modified L-leucine residue		A protein modification that contains an L-leucine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that contains an L-lysine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02052	crosslinked L-methionine residue	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that contains an L-methionine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02053	crosslinked L-phenylalanine residue	http://purl.obolibrary.org/obo/MOD_00914	modified L-phenylalanine residue		A protein modification that contains an L-phenylalanine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02054	crosslinked L-proline residue	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		A protein modification that contains an L-proline residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02055	crosslinked L-serine residue	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that contains an L-serine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02056	crosslinked L-threonine residue	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that contains an L-threonine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02057	crosslinked L-tryptophan residue	http://purl.obolibrary.org/obo/MOD_00918	modified L-tryptophan residue		A protein modification that contains an L-tryptophan residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02058	crosslinked L-tyrosine residue	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that contains an L-tyrosine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02059	crosslinked L-valine residue	http://purl.obolibrary.org/obo/MOD_00920	modified L-valine residue		A protein modification that contains an L-valine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02061	crosslinked L-selenocysteine residue	http://purl.obolibrary.org/obo/MOD_01158	modified L-selenocysteine residue		A protein modification that contains an L-selenocysteine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02062	crosslinked N-formyl-L-methionine residue	http://purl.obolibrary.org/obo/MOD_01450	modified N-formyl-L-methionine residue		A protein modification that contains an N-formyl-L-methionine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02066	metal or metal cluster coordinated L-aspartic acid residue	http://purl.obolibrary.org/obo/MOD_00904	modified L-aspartic acid residue		A protein modification that contains an L-aspartic acid residue coordinated to one or more metal atoms or metal clusters.
http://purl.obolibrary.org/obo/MOD_02067	metal or metal cluster coordinated L-cysteine residue	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that contains an L-cysteine residue coordinated to one or more metal atoms or metal clusters.
http://purl.obolibrary.org/obo/MOD_02068	metal or metal cluster coordinated L-glutamic acid residue	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid residue		A protein modification that contains an L-glutamic acid residue coordinated to one or more metal atoms or metal clusters.
http://purl.obolibrary.org/obo/MOD_02070	metal or metal cluster coordinated L-histidine residue	http://purl.obolibrary.org/obo/MOD_00909	modified L-histidine residue		A protein modification that contains an L-histidine residue coordinated to one or more metal atoms or metal clusters.
http://purl.obolibrary.org/obo/MOD_02071	metal or metal cluster coordinated L-methionine residue	http://purl.obolibrary.org/obo/MOD_00913	modified L-methionine residue		A protein modification that contains an L-methionine residue coordinated to one or more metal atoms or metal clusters.
http://purl.obolibrary.org/obo/MOD_02072	metal or metal cluster coordinated L-serine residue	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that contains an L-serine residue coordinated to one or more metal atoms or metal clusters.
http://purl.obolibrary.org/obo/MOD_02073	metal or metal cluster coordinated L-selenocysteine residue	http://purl.obolibrary.org/obo/MOD_01158	modified L-selenocysteine residue		A protein modification that contains an L-selenocysteine residue coordinated to one or more metal atoms or metal clusters.
http://purl.obolibrary.org/obo/MOD_02074	metal or metal cluster coordinated L-lysine residue	http://purl.obolibrary.org/obo/MOD_00912	modified L-lysine residue		A protein modification that contains an L-lysine residue coordinated to one or more metal atoms or metal clusters.
http://purl.obolibrary.org/obo/MOD_02075	metal or metal cluster coordinated L-tyrosine residue	http://purl.obolibrary.org/obo/MOD_00919	modified L-tyrosine residue		A protein modification that contains an L-tyrosine residue coordinated to one or more metal atoms or metal clusters.
http://purl.obolibrary.org/obo/MOD_02076	metal or metal cluster coordinated L-arginine residue	http://purl.obolibrary.org/obo/MOD_00902	modified L-arginine residue		A protein modification that contains an L-arginine residue coordinated to one or more metal atoms or metal clusters.
http://purl.obolibrary.org/obo/MOD_02060	crosslinked D-asparagine residue	http://purl.obolibrary.org/obo/MOD_02097	modified D-asparagine residue		A protein modification that contains an D-asparagine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02063	crosslinked D-phenylalanine residue	http://purl.obolibrary.org/obo/MOD_00201	D-phenylalanine		A protein modification that contains an D-phenylalanine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02064	crosslinked D-serine residue	http://purl.obolibrary.org/obo/MOD_00202	D-serine (Ser)		A protein modification that contains an D-serine residue crosslinked to one or more amino acid residues.
http://purl.obolibrary.org/obo/MOD_02065	metal or metal cluster coordinated L-alanine residue	http://purl.obolibrary.org/obo/MOD_00901	modified L-alanine residue		A protein modification that contains an L-alanine residue coordinated to one or more metal atoms or metal clusters.
http://purl.obolibrary.org/obo/MOD_02069	metal or metal cluster coordinated L-glutamine residue	http://purl.obolibrary.org/obo/MOD_00907	modified L-glutamine residue		A protein modification that contains an L-glutamine residue coordinated to one or more metal atoms or metal clusters.
http://purl.obolibrary.org/obo/MOD_01109	9-fluorenylmethyloxycarbonyl (Fmoc)	http://purl.obolibrary.org/obo/MOD_00848	reagent derivatized residue		modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_02088	natural, standard, encoded residue substitution	http://purl.obolibrary.org/obo/MOD_01156	protein modification categorized by chemical process		A protein modification that effectively replaces a natural, standard, encoded residue.
http://purl.obolibrary.org/obo/MOD_02001	stearoylated residue	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively replaces a hydrogen atom with a stearoyl group.
http://purl.obolibrary.org/obo/MOD_02002	S-palmitoleylated residue	http://purl.obolibrary.org/obo/MOD_01423	palmitoleylated residue		A protein modification that effectively replaces a residue sulfanyl group with a palmitoleylsulfanyl group.
http://purl.obolibrary.org/obo/MOD_02003	O3-acylated L-serine	http://purl.obolibrary.org/obo/MOD_00916	modified L-serine residue		A protein modification that effectively replaces an O3-hydroxy hydrogen atom of L-serine with an acyl group.
http://purl.obolibrary.org/obo/MOD_02004	O3-acylated L-threonine	http://purl.obolibrary.org/obo/MOD_00917	modified L-threonine residue		A protein modification that effectively replaces an O3-hydroxy hydrogen atom of L-threonine with an acyl group.
http://purl.obolibrary.org/obo/MOD_02005	S-acylated L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		A protein modification that effectively replaces an sulfanyl hydrogen atom of L-cysteine with an acyl group.
http://purl.obolibrary.org/obo/MOD_02006	S-stearoylated residue	http://purl.obolibrary.org/obo/MOD_02001	stearoylated residue		A protein modification that effectively replaces a residue sulfanyl group with a stearoylsulfanyl group.
http://purl.obolibrary.org/obo/MOD_02007	N6-palmitoleyl-L-lysine	http://purl.obolibrary.org/obo/MOD_02008	N-palmitoleylated residue		A protein modification that effectively converts an L-lysine residue to N6-palmitoleyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_02008	N-palmitoleylated residue	http://purl.obolibrary.org/obo/MOD_00670	N-acylated residue		A protein modification that effectively replaces a residue amino group with a palmitoleylamino group.
http://purl.obolibrary.org/obo/MOD_02009	N6-stearoyl-L-lysine	http://purl.obolibrary.org/obo/MOD_02010	N-stearoylated residue		A protein modification that effectively converts an L-lysine residue to N6-stearoyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_02010	N-stearoylated residue	http://purl.obolibrary.org/obo/MOD_02001	stearoylated residue		A protein modification that effectively replaces a residue amino group with a stearoylamino group.
http://purl.obolibrary.org/obo/MOD_02011	N-oleoylated residue	http://purl.obolibrary.org/obo/MOD_02012	oleoylated residue		A protein modification that effectively replaces a residue amino group with a oleoylamino group.
http://purl.obolibrary.org/obo/MOD_02012	oleoylated residue	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively replaces a hydrogen atom with a oleoyl group.
http://purl.obolibrary.org/obo/MOD_02013	N6-linoloyl-L-lysine	http://purl.obolibrary.org/obo/MOD_02014	N-linoloylated residue		A protein modification that effectively converts an L-lysine residue to N6-linoloyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_02014	N-linoloylated residue	http://purl.obolibrary.org/obo/MOD_02015	linoloylated residue		A protein modification that effectively replaces a residue amino group with a linoloylamino group.
http://purl.obolibrary.org/obo/MOD_02015	linoloylated residue	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively replaces a hydrogen atom with a linoloyl group.
http://purl.obolibrary.org/obo/MOD_02016	N6-arachidonoyl-L-lysine	http://purl.obolibrary.org/obo/MOD_02017	N-arachidonoylated residue		A protein modification that effectively converts an L-lysine residue to N6-arachidonoyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_02017	N-arachidonoylated residue	http://purl.obolibrary.org/obo/MOD_02018	arachidonoylated residue		A protein modification that effectively replaces a residue amino group with an arachidonoylamino group.
http://purl.obolibrary.org/obo/MOD_02018	arachidonoylated residue	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively replaces a hydrogen atom with an arachidonoyl group.
http://purl.obolibrary.org/obo/MOD_02019	N6-timnodonoyl-L-lysine	http://purl.obolibrary.org/obo/MOD_02020	N-timnodonoylated residue		A protein modification that effectively converts an L-lysine residue to N6-timnodonoyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_02020	N-timnodonoylated residue	http://purl.obolibrary.org/obo/MOD_02021	timnodonoylated residue		A protein modification that effectively replaces a residue amino group with a timnodonoylamino group.
http://purl.obolibrary.org/obo/MOD_02021	timnodonoylated residue	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively replaces a hydrogen atom with a timnodonoyl group.
http://purl.obolibrary.org/obo/MOD_02022	N6-cervonoyl-L-lysine	http://purl.obolibrary.org/obo/MOD_02023	N-cervonoylated residue		A protein modification that effectively converts an L-lysine residue to N6-cervonoyl-L-lysine.
http://purl.obolibrary.org/obo/MOD_02023	N-cervonoylated residue	http://purl.obolibrary.org/obo/MOD_02024	cervonoylated residue		A protein modification that effectively replaces a residue amino group with a cervonoylamino group.
http://purl.obolibrary.org/obo/MOD_02024	cervonoylated residue	http://purl.obolibrary.org/obo/MOD_01155	lipoconjugated residue		A protein modification that effectively replaces a hydrogen atom with a cervonoyl group.
http://purl.obolibrary.org/obo/MOD_02025	5-glutaminyl glutamic acid	http://purl.obolibrary.org/obo/MOD_00906	modified L-glutamic acid 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.
http://purl.obolibrary.org/obo/MOD_02026	S-(cysteinyl-glycyl)-L-cysteine	http://purl.obolibrary.org/obo/MOD_00905	modified L-cysteine residue		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.
http://purl.obolibrary.org/obo/MOD_02027	urmylated lysine	http://purl.obolibrary.org/obo/MOD_02051	crosslinked L-lysine residue		A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a URM1 protein.
http://purl.obolibrary.org/obo/MOD_02028	iTRAQ4plex reporter+balance reagent acylated residue, average mass modification	http://purl.obolibrary.org/obo/MOD_01709	iTRAQ4plex reporter+balance reagent N-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.
http://purl.obolibrary.org/obo/MOD_02029	cis-peptidyl-L-proline	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		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)
http://purl.obolibrary.org/obo/MOD_02030	trans-peptidyl-L-proline	http://purl.obolibrary.org/obo/MOD_00915	modified L-proline residue		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)
http://purl.obolibrary.org/obo/MOD_02031	dHex1Hex4HexNAc5 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation, dHex Hex(4) HexNAc(5)
http://purl.obolibrary.org/obo/MOD_02032	dHex2Hex4HexNAc5 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation, dHex(2) Hex(4) HexNAc(5)
http://purl.obolibrary.org/obo/MOD_02033	dHex1Hex5HexNAc3 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation, dHex Hex(5) HexNAc(3)
http://purl.obolibrary.org/obo/MOD_02034	dHex1Hex3HexNAc6 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation, dHex Hex(3) HexNAc(6)
http://purl.obolibrary.org/obo/MOD_02035	dHex1Hex6HexNAc3 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation, dHex Hex(6) HexNAc(3)
http://purl.obolibrary.org/obo/MOD_02036	Hex9HexNAc2 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation, Hex(9)HexNAc(2)
http://purl.obolibrary.org/obo/MOD_02037	Hex7HexNAc2 N4-glycosylated asparagine	http://purl.obolibrary.org/obo/MOD_00160	N4-glycosyl-L-asparagine		modification from Unimod N-linked glycosylation, Hex(7) HexNAc(2)
http://purl.obolibrary.org/obo/MOD_02038	monomethylated L-histidine	http://purl.obolibrary.org/obo/MOD_00599	monomethylated residue		A protein modification that effectively replaces one hydrogen atom of an L-histidine residue with one methyl group.
http://purl.obolibrary.org/obo/MOD_02107	5-hydroxy-L-tryptophan	http://purl.obolibrary.org/obo/MOD_01622	monohydroxylated tryptophan		A protein modification that effectively converts an L-tryptophan residue to a 5-hydroxy-L-tryptophan.
http://purl.obolibrary.org/obo/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.
http://purl.obolibrary.org/obo/MOD_00004	artifact				Artifact entry from Unimod - OBSOLETE because organizational use is no longer required.
http://purl.obolibrary.org/obo/MOD_00008	common				Entry from Unimod representing one or more entries in RESID. OBSOLETE because organizational use is no longer required.
http://purl.obolibrary.org/obo/MOD_00407	residue methyl ester				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.
http://purl.obolibrary.org/obo/MOD_00411	O18 label				modification from Unimod Isotopic label. OBSOLETE because Unimod:18 is now merged with entry 258 remap to MOD:00581 'single 018 label'
http://purl.obolibrary.org/obo/MOD_00412	oxidation				modification from Unimod artifact. OBSOLETE because Unimod entry 19 is now merged with Unimod 35 remap to MOD:00425 'monohydroxylated residue'.
http://purl.obolibrary.org/obo/MOD_00415	phosphorylation without neutral loss				modification from Unimod - OBSOLETE because Unimod entry 22 is now merged with entry 21 remap to MOD:00696 'phosphorylated residue'.
http://purl.obolibrary.org/obo/MOD_00450	acetate labeling reagent light form (K)				OBSOLETE because this isotopic label from Unimod entry 57 is deprecated
http://purl.obolibrary.org/obo/MOD_00496	reductive amination-D				OBSOLETE because Unimod entry 125 is merged with entry 199, remap to id: MOD:00552
http://purl.obolibrary.org/obo/MOD_00507	5-dimethylaminonaphthalene-1-sulfonyl				OBSOLETE because redundant, replaced by MOD:01653. Remap to MOD:01653.
http://purl.obolibrary.org/obo/MOD_00508	ISD a-series (C-Term)				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
http://purl.obolibrary.org/obo/MOD_00536	L-serine to L-alanine replacement				OBSOLETE because Unimod 179 merged with Unimod 447 remap to ??? a protein modification that replaces an L-serine residue with an L-alanine residue
http://purl.obolibrary.org/obo/MOD_00539	threonine reduced to aminobutynate				OBSOLETE because Unimod 179 merged wth Unimod 447 remap to ??? modification from Unimod O-linked glycosylation
http://purl.obolibrary.org/obo/MOD_00545	deuterated dimethyl labeling (D)				OBSOLETE because redundant with MOD:00927. Remap to MOD:00927.
http://purl.obolibrary.org/obo/MOD_00554	APTA-d0 with no neutral loss				OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00555	APTA-d0 with quaternary amine loss				OBSOLETE because Unimod entry 202 was merged with entry 195, remap to MOD:00548. modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00556	acrolein addition +94				OBSOLETE because this modification not supported by any literature that I can find[PMT]
http://purl.obolibrary.org/obo/MOD_00557	acrolein addition +56				OBSOLETE because this modification not supported by the papers listed or any other that I can find[PMT]
http://purl.obolibrary.org/obo/MOD_00558	acrolein addition +38				OBSOLETE because this modification not supported by any literature that I can find[PMT]
http://purl.obolibrary.org/obo/MOD_00559	acrolein addition +76				OBSOLETE because this modification not supported by any literature that I can find[PMT]
http://purl.obolibrary.org/obo/MOD_00560	acrolein addition +112				OBSOLETE because this modification not supported by any literature that I can find[PMT]
http://purl.obolibrary.org/obo/MOD_00564	Applied Biosystems iTRAQ(TM) multiplexed quantitation chemistry				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.
http://purl.obolibrary.org/obo/MOD_00567	histidine oxidation to asparagine				OBSOLETE because Unimod entry 244 is redundant with Unimod 348. Remap to MOD:00775.
http://purl.obolibrary.org/obo/MOD_00568	histidine oxidation to aspartic acid				OBSOLETE because Unimod entry 245 is redundant with Unimod 349. Remap to MOD:00776
http://purl.obolibrary.org/obo/MOD_00578	acetaldehyde +28				OBSOLETE because this modification not supported by any literature that I can find [PMT]
http://purl.obolibrary.org/obo/MOD_00579	propionaldehyde +40				OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other
http://purl.obolibrary.org/obo/MOD_00580	propionaldehyde +42				OBSOLETE because entry removed from Unimod. Remap potentially to MOD:00579 propionaldehyde +40
http://purl.obolibrary.org/obo/MOD_00590	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
http://purl.obolibrary.org/obo/MOD_00591	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
http://purl.obolibrary.org/obo/MOD_00593	covalent modification of lysine by omega-maleimido alkanoyl N-hydroxysuccinimido esters				OBSOLETE because removed from Unimod. modification from Unimod Chemical derivative
http://purl.obolibrary.org/obo/MOD_00597	methyl methanethiosulfonate				OBSOLETE because Unimod entry 277 redundant with Unimod 39. Remap to MOD:00110.
http://purl.obolibrary.org/obo/MOD_00603	N-ethylation				OBSOLETE because Unimod entry 283 is redundant with Unimod 280. Remap to MOD:00600
http://purl.obolibrary.org/obo/MOD_00615	4-sulfophenyl isothiocyante modification to N-term R				OBSOLETE because entry Unimod:261 site N-term R was abandoned. Remap to MOD:00584
http://purl.obolibrary.org/obo/MOD_00619	hydroxylethanone				OBSOLETE because entry 300 is redundant with Unimod 6 remap to MOD:01328
http://purl.obolibrary.org/obo/MOD_00632	N-succinimide				OBSOLETE because this chemical derivative modification from Unimod 321 is deprecated.
http://purl.obolibrary.org/obo/MOD_00641	CAMthiopropanoyl of Lys				OBSOLETE because Unimod entry 334 is merged with Unimod 293. Remap to MOD:00612
http://purl.obolibrary.org/obo/MOD_00766	C terminal -K from HC of MAb				modification from Unimod Post-translational - C-terminal loss of lysine OBSOLETE because the idenical to MOD:01642. Remap to MOD:01642
http://purl.obolibrary.org/obo/MOD_00779	lysine oxidation to aminoadipic semialdehyde				OBSOLETE because redundant with MOD:00130. Remap to MOD:00130.
http://purl.obolibrary.org/obo/MOD_00794	pyrrolidone from proline				OBSOLETE because redundant and identical to MOD:00477. Remap to MOD:00477.
http://purl.obolibrary.org/obo/MOD_00815	molybdopterin				OBSOLETE because redundant with MOD:00151. Remap to MOD:00151.
http://purl.obolibrary.org/obo/MOD_00872	L-isoglutamyl monoglutamic acid				OBSOLETE because redundant and identical to MOD:01970. Remap to MOD:01970.
http://purl.obolibrary.org/obo/MOD_00881	N-reductive amination-D				OBSOLETE because Unimod entry 465 megerd with 199. Remap to MOD:00552 DiMethyl-CH2D.
http://purl.obolibrary.org/obo/MOD_00921	new uncategorized Unimod entries				New uncategorized Unimod. OBSOLETE because organizational use is no longer required.
http://purl.obolibrary.org/obo/MOD_00926	Bisphenol A diglycidyl ether derivative				Modification from Unimod Non-standard residue. OBSOLETE because not an amino acid modification. From Unimod not an approved entry.
http://purl.obolibrary.org/obo/MOD_00945	fluorescein-5-thiosemicarbazide adduct				OBSOLETE because redundant and identical to MOD:00626. Remap to MOD:00626.
http://purl.obolibrary.org/obo/MOD_00948	5'-dephospho				OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00949	desmosine				OBSOLETE because redundant and identical to MOD:01933. Remap to MOD:01933.
http://purl.obolibrary.org/obo/MOD_00950	decomposed carboxymethylated methionine				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
http://purl.obolibrary.org/obo/MOD_00963	Oxidation of Trp to kynurenine				Modification from DeltaMass. OBSOLETE because redundant and identical to MOD:00462. Remap to MOD:00462.
http://purl.obolibrary.org/obo/MOD_00968	CM-Cys vs PAM-Cys				OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00969	CAM-Cys vs PAM-Cys				OBSOLETE because this isn't a protein modification, but rather the difference between two known modifications. modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_00976	potassium salt				modification from DeltaMass - OBSOLETE because redundant and identical to MOD:01072. Remap to MOD:01072.
http://purl.obolibrary.org/obo/MOD_00980	Carboxamidomethyl (on Cysteine)				modification from DeltaMass - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060.
http://purl.obolibrary.org/obo/MOD_00989	acetamidomethyl (Acm)				OBSOLETE because redundant, the difference component of MOD:01079. Remap to MOD:01079.
http://purl.obolibrary.org/obo/MOD_00999	homoseryl lactone				OBSOLETE because redundant and identical to MOD:00404. Remap to MOD:00404.
http://purl.obolibrary.org/obo/MOD_01017	homoseryl (-Hse-)				OBSOLETE because redundant and identical to MOD:00403. Remap to MOD:00403.
http://purl.obolibrary.org/obo/MOD_01036	O-methyl aspartyl				OBSOLETE because redundant and identical to MOD:01181. Remap to MOD:01181.
http://purl.obolibrary.org/obo/MOD_01038	norleucine (Nle)				OBSOLETE because this represents a free amino acid and the corresponding residue is MOD:01026.
http://purl.obolibrary.org/obo/MOD_01039	hydroxy aspartyl				OBSOLETE because redundant and identical to MOD:00036. Remap to MOD:00036.
http://purl.obolibrary.org/obo/MOD_01044	N-methyl glutamyl				OBSOLETE because redundant and identical to MOD:00080. Remap to MOD:00080.
http://purl.obolibrary.org/obo/MOD_01062	carboxymethyl cysteinyl				OBSOLETE because duplicate and redundant with MOD:01061. Remap to MOD:01061
http://purl.obolibrary.org/obo/MOD_01076	N-methyl arginyl				modification from DeltaMass - OBSOLETE because redundant and identical to MOD:00414. Remap to MOD:00414.
http://purl.obolibrary.org/obo/MOD_01080	acrylamidyl cysteinyl				OBSOLETE because this is identical to MOD:00417.  modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01082	4-glycosyloxy- (hexosyl, C6) (of proline)				OBSOLETE because redundant with MOD:00757, remap. modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01095	Matrix alpha cyano MH+				Modification from DeltaMass. OBSOLETE because not an amino acid modification.
http://purl.obolibrary.org/obo/MOD_01101	S-Farnesyl-				OBSOLETE because erroneous and apparently redundant to MOD:00111. Remap to MOD:00111.
http://purl.obolibrary.org/obo/MOD_01102	myristoylation-4H (two double bonds)				OBSOLETE because redundant and identical to MOD:00504. Remap to MOD:00504.
http://purl.obolibrary.org/obo/MOD_01103	myristoleylation (one double bond)				OBSOLETE because redundant and identical to MOD:00503. Remap to MOD:00503.
http://purl.obolibrary.org/obo/MOD_01122	5'phos dCytidinyl				OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01123	monoiodated tyrosine				OBSOLETE because redundant and identical to MOD:01123. Remap to MOD:01123.
http://purl.obolibrary.org/obo/MOD_01125	5'phos dThymidinyl				OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01126	5'phos Cytidinyl				OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01127	5'phos Uridinyl				OBSOLETE because redundant and identical to MOD:01166. Remap to MOD:01166.
http://purl.obolibrary.org/obo/MOD_01129	5'phos dAdenosyl				OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01131	5'phos dGuanosyl				OBSOLETE because this is a modification that occurs to DNA/RNA and not proteins. modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01132	5'phos Adenosinyl				OBSOLETE because redundant and identical to MOD:01165. Remap to MOD:01165.
http://purl.obolibrary.org/obo/MOD_01136	dioctyl phthalate				OBSOLETE because this is a small molecule contaminant and not a modification to a polypeptide. modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01138	Aedans Cystenyl				OBSOLETE because no evidence has been seen for this protein modification. modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01139	dioctyl phthalate sodium adduct				OBSOLETE because this is a MS contaminant, not a known modification to a polypeptide. modification from DeltaMass
http://purl.obolibrary.org/obo/MOD_01190	dibromo				Modification from Unimod Chemical derivative. OBSOLETE because duplicate and redundant with MOD:01006. Remap to MOD:01006.
http://purl.obolibrary.org/obo/MOD_01196	5-dimethylaminonaphthalene-1-sulfonyl - site K				OBSOLETE because redundant, replaced with MOD:01654. Remap to MOD:01654.
http://purl.obolibrary.org/obo/MOD_01214	iodoacetamide - site C				modification from Unimod Chemical derivative - OBSOLETE because redundant, the difference component of MOD:01060. Remap to MOD:01060.
http://purl.obolibrary.org/obo/MOD_01246	fucosylated -site S				OBSOLETE because redundant and identical to MOD:00812 after formula correction. Remap to MOD:00812.
http://purl.obolibrary.org/obo/MOD_01247	fucosylated -site T				OBSOLETE because redundant and identical to MOD:00813 after formula correction. Remap to MOD:00813.
http://purl.obolibrary.org/obo/MOD_01252	5-hydro-5-methylimidazol-4-one, methylglyoxal arginine adduct (+54 amu)				OBSOLETE because redundant and identical to MOD:00933. Remap to MOD:00933.
http://purl.obolibrary.org/obo/MOD_01260	nucleophilic addtion to cytopiloyne - site Y				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 -
http://purl.obolibrary.org/obo/MOD_01261	nucleophilic addtion to cytopiloyne - site S				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 -
http://purl.obolibrary.org/obo/MOD_01262	nucleophilic addition to cytopiloyne - site R				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 -
http://purl.obolibrary.org/obo/MOD_01263	nucleophilic addtion to cytopiloyne - site K				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 -
http://purl.obolibrary.org/obo/MOD_01264	nucleophilic addtion to cytopiloyne - site C				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 -
http://purl.obolibrary.org/obo/MOD_01265	nucleophilic addtion to cytopiloyne - site P				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 -
http://purl.obolibrary.org/obo/MOD_01266	nucleophilic addition to cytopiloyne+H2O - site C				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 -
http://purl.obolibrary.org/obo/MOD_01267	nucleophilic addition to cytopiloyne+H2O - site K				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 -
http://purl.obolibrary.org/obo/MOD_01268	nucleophilic addition to cytopiloyne+H2O - site T				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 -
http://purl.obolibrary.org/obo/MOD_01269	nucleophilic addition to cytopiloyne+H2O - site R				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 -
http://purl.obolibrary.org/obo/MOD_01270	nucleophilic addition to cytopiloyne+H2O - site S				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 -
http://purl.obolibrary.org/obo/MOD_01271	nucleophilic addition to cytopiloyne+H2O - site Y				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 -
http://purl.obolibrary.org/obo/MOD_01282	acrolein addition +56 - site H				OBSOLETE because this modification is not supported by the linked literature [PMT]
http://purl.obolibrary.org/obo/MOD_01283	acrolein addition +56 - site K				OBSOLETE because this modification is not supported by the linked literature [PMT]
http://purl.obolibrary.org/obo/MOD_01284	acrolein addition +56 - site C				OBSOLETE because this modification is not supported by the linked literature [PMT]
http://purl.obolibrary.org/obo/MOD_01288	acetaldehyde +28 - site H				OBSOLETE because this is not supported by the literature [PMT]
http://purl.obolibrary.org/obo/MOD_01289	acetaldehyde +28 - site K				OBSOLETE because this is not supported by the literature [PMT]
http://purl.obolibrary.org/obo/MOD_01290	dihydroxylated residue - site F				OBSOLETE because redundant and identical to MOD:00465. Remap to MOD:00465.
http://purl.obolibrary.org/obo/MOD_01291	dihydroxylated residue - site W				OBSOLETE because redundant and identical to MOD:00464. Remap to MOD:00464.
http://purl.obolibrary.org/obo/MOD_01292	dimethylation of proline residue				OBSOLETE because redundant and identical to MOD:00075. Map to MOD:00075.
http://purl.obolibrary.org/obo/MOD_01294	deamidation in presence of O18 -site Q				OBSOLETE identical and redundant with MOD:00791. Remap to MOD:00791.
http://purl.obolibrary.org/obo/MOD_01322	propionaldehyde +40 - site K				OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other -
http://purl.obolibrary.org/obo/MOD_01323	propionaldehyde +40 - site H				OBSOLETE because not supported by the linked literature [PMT]. modification from Unimod Other -
http://purl.obolibrary.org/obo/MOD_01324	acetaldehyde +26 - site H				OBSOLETE because this is not supported by the linked literature [PMT]
http://purl.obolibrary.org/obo/MOD_01325	acetaldehyde +26 - site K				OBSOLETE because this is not supported by the linked literature [PMT]
http://purl.obolibrary.org/obo/MOD_01329	iodoacetic acid - site C				OBSOLETE because duplicate and redundant with MOD:01061. Remap to MOD:01061
http://purl.obolibrary.org/obo/MOD_01330	iodoacetic acid -site K				OBSOLETE because identical with MOD:01094. Remap to MOD:01094
http://purl.obolibrary.org/obo/MOD_01336	deamidation followed by a methylation -site Q				OBSOLETE - identical and redundant with MOD:00657. Remap to MOD:00657.
http://purl.obolibrary.org/obo/MOD_01342	selenium substitution for sulfur - site M				OBSOLETE because redundant and identical to MOD:00530. Remap to MOD:00530.
http://purl.obolibrary.org/obo/MOD_01343	selenium substitution for sulfur - site C				OBSOLETE because redundant and identical to MOD:00686. Remap to MOD:00686.
http://purl.obolibrary.org/obo/MOD_01344	dehydrogenated residue - site S				OBSOLETE because redundant and identical with MOD:00835. Remap to MOD:00835.
http://purl.obolibrary.org/obo/MOD_01371	deamidation in presence of O18				OBSOLETE bcecause identical and redundant with MOD:00851. Remap to MOD:00851.
http://purl.obolibrary.org/obo/MOD_01427	2-aminobutanoic acid (Abu)				OBSOLETE because redundant and identical to MOD:00819. Remap to MOD:00819.
http://purl.obolibrary.org/obo/MOD_01876	4x(1)H,4x(12)C-labeled alpha-amino succinylated residue				OBSOLETE because identical to MOD:00457
http://purl.obolibrary.org/obo/MOD_01961	O-(L-isoglutamyl)-L-threonine (THR)				OBSOLETE because redundant and identical to MOD:01785. Remap to MOD:01785.
http://purl.obolibrary.org/obo/MOD_01966	L-methionine (R)-sulfoxide				OBSOLETE because redundant and identical to MOD:00720. Remap to MOD:00720.
http://purl.obolibrary.org/obo/MOD_02098	residue modified by radical mechanism				A chemical transformation driven by a radical reaction.
http://purl.obolibrary.org/obo/mod#contains	contains				'Entity A' contains 'Entity B' implies that 'Entity B' is a part of the structure of 'Entity A'.
http://purl.obolibrary.org/obo/mod#derives_from	derives from				'Entity A' derives_from 'Entity B' implies that 'Entity A' is chemically derived from 'Entity B'.
http://purl.obolibrary.org/obo/mod#has_functional_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.
http://purl.obolibrary.org/obo/mod#part_of	part of				'Entity A' part_of 'Entity B' implies that 'Entity A' is a part of the structure of 'Entity B'.