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The incorporation of iron into a 4Fe-4S iron-sulfur cluster via tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide. The incorporation of molybdenum into a protein by L-cysteinyl copper sulfido molybdopterin cytosine dinucleotide. The formation of a selenide-sulfide bond to form the cystine-like L-cysteinyl-L-selenocysteine, as in vertebrate selenopeptide P. The incorporation of iron into a 4Fe-4S iron-sulfur cluster via tris-L-cysteinyl L-arginyl diiron disulfide. The dehydration of peptidyl-S-carbamoyl-L-cysteine to form peptidyl-S-cyano-L-cysteine. The carbamoylation of peptidyl-cysteine to form peptidyl-S-carbamoyl-L-cysteine. The transient amidinylation of peptidyl-cysteine to form peptidyl-S-amidino-L-cysteine. The incorporation of iron into an iron-sulfur cluster by tris-L-cysteinyl-L-cysteine persulfido-bis-L-glutamato-L-histidino tetrairon. The incorporation of iron into an L-cysteinyl diiron subcluster, found in Fe-hydrogenase. The incorporation of iron into a 4Fe-4S iron-sulfur cluster via tris-L-cysteinyl-L-N1'-histidino tetrairon tetrasulfide. The incorporation of iron into a 4Fe-4S iron-sulfur cluster via tris-L-cysteinyl-L-N3'-histidino tetrairon tetrasulfide. The incorporation of iron into a 4Fe-4S iron-sulfur cluster via tris-L-cysteinyl-L-aspartato tetrairon tetrasulfide. The incorporation of iron into a 4Fe-4S iron-sulfur cluster via tris-L-cysteinyl-L-serinyl tetrairon tetrasulfide. The chemical reactions and pathways resulting in the formation of a peptidyl serine-peptidyl cysteine cross-link by the condensation of a serine hydroxyl with the carbonyl of the preceding residue. The incorporation of nickel into a nickel-iron-sulfur cluster via pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide, found in carbon monoxide dehydrogenase. The chemical reactions and pathways resulting in the formation of a peptidyl cysteine-peptidyl glycine cross-link by the condensation of a cysteine thiol with the carbonyl of the preceding residue and alpha-beta dehydrogenation. The chemical reactions and pathways resulting in the formation of a peptidyl cysteine-peptidyl serine cross-link by the condensation of a cysteine thiol with the carbonyl of the preceding residue and alpha-beta dehydrogenation. The chemical reactions and pathways resulting in the formation of a peptidyl cysteine-peptidyl phenylalanine cross-link by the condensation of a cysteine thiol with the carbonyl of the preceding residue and alpha-beta dehydrogenation. The acetylation of peptidyl-cysteine. The chemical reactions and pathways resulting in the formation of a peptidyl serine-peptidyl cysteine cross-link by the condensation of a serine hydroxyl with the carbonyl of the preceding residue and alpha-beta dehydrogenation. The posttranslational cross-linking of a cysteine residue to an L-phenylalanine residue to form 2-(S-L-cysteinyl)-L-phenylalanine. The incorporation of copper into a protein by L-cysteinyl copper sulfido molybdopterin cytosine dinucleotide. The formation of a protein active site cross-link from the alpha-carboxyl carbon of residue N, a cysteine, to the alpha-amino nitrogen of residue N+2, a glycine, coupled with the formation of a double bond to the alpha-amino nitrogen of residue N+1 which loses one hydrogen, and the loss of a molecule of water. The posttranslational cross-linking of a cysteine residue to an L-phenylalanine residue to form 2-(S-L-cysteinyl)-D-phenylalanine. The posttranslational S-nitrosylation of peptidyl-cysteine to form peptidyl-S-nitrosyl-L-cysteine. The formation of a protein-FMN linkage via S-(6-FMN)-L-cysteine. The post-translational cross-linking of a cysteine residue to an L-threonine residue to form 2-(S-L-cysteinyl)-D-allo-threonine. The incorporation of nickel into a 3Fe-2S complex by tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide. The oxidation of two peptidyl-cysteine residues to form a peptidyl-L-cystine (dicysteine) in which segments of peptide chain are linked by a disulfide bond; the cross-link may be between different or the same peptide chain. The incorporation of nickel into a 3Fe-2S complex by tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide. The incorporation of iron into a 3Fe-2S cluster by tris-L-cysteinyl L-cysteine persulfido L-glutamato L-histidino L-serinyl nickel triiron disulfide trioxide. The formation of an isopeptide cross-link between peptidyl-asparagine and peptidyl-cysteine to produce N-(L-isoaspartyl)-L-cysteine. The methylation of peptidyl-cysteine to form peptidyl-S-methyl-L-cysteine. The transfer, from NAD, of ADP-ribose to peptidyl-cysteine to form peptidyl-S-(ADP-ribosyl)-L-cysteine. The incorporation of iron into a 4Fe-4S iron-sulfur cluster via bis-L-cysteinyl-L-N3'-histidino-L-serinyl tetrairon tetrasulfide. The posttranslational modification of peptidyl-cysteine by covalent addition of glutathione to form peptidyl-L-cysteine glutathione disulfide. The co- or posttranslational modification of cysteine to form peptidyl-S-diphytanylglycerol diether-L-cysteine. The chemical reactions and pathways resulting in the formation of a C-terminal peptidyl-cysteine ethanolamide-linked glycosylphosphatidylinositol (GPI) anchor following hydrolysis of a cysteinyl-peptide bond in the carboxy-terminal region of a membrane-associated protein. The oxidative deamination of the alpha carbon of an encoded N-terminal amino acid, to form pyruvic acid retaining an amide bond between its 1-carboxyl group and the adjacent residue. The pyruvate 2-oxo group may become an enzyme active site, or it may be reduced to an alcohol. The linkage of protein to heme P460 via heme P460-bis-L-cysteine-L-lysine. The posttranslational modification of peptidyl-cysteine to form peptidyl-S-palmitoleyl-L-cysteine specifically. The formation of a protein-protein cross-link between peptidyl-serine and peptidyl-cysteine by the synthesis of sn-(2S,6R)-lanthionine (meso-lanthione). The formation of a protein-protein cross-link between peptidyl-threonine and peptidyl-cysteine by the synthesis of (2S,3S,6R)-3-methyl-lanthionine (3-methyl-L-lanthionine). The incorporation of iron into a 3Fe-2S cluster via tris-L-cysteinyl L-cysteine persulfido bis-L-glutamato L-histidino nickel triiron disulfide trioxide. The formation of S-(peptidyl-glycyl)-peptidyl-cysteine cross-links by the formation of a thiolester between cysteine and the carboxy-terminal glycine of ubiquitin and other proteins. The formation of a protein-protein cross-link between peptidyl-serine and peptidyl-cysteine by the synthesis of (2R,6R)-lanthionine (L-lanthionine). The linkage of cytochromes and other heme proteins to heme via heme-bis-L-cysteine. The linkage of cytochromes and other heme proteins to heme via heme-L-cysteine. The posttranslational cross-linking of a cysteine residue to an aspartic acid residue to form 3-(S-L-cysteinyl)-L-aspartic acid. The posttranslational cross-linking of a cysteine residue to tryptophyl quinone to form 4'-(S-L-cysteinyl)-L-tryptophyl quinone, a cofactor found at the active site of amine dehydrogenase. The posttranslational cross-linking of a cysteine residue to a glutamic acid residue to form 4-(S-L-cysteinyl)-L-glutamic acid. The posttranslational glycosylation of protein via the sulfur atom of peptidyl-cysteine, forming S-glycosyl-L-cysteine. The chemical reactions and pathways resulting in the formation of a peptidyl cysteine-peptidyl cysteine cross-link by the condensation of a cysteine thiol with the carbonyl of the preceding residue and alpha-beta dehydrogenation. The chemical reactions and pathways resulting in the formation of a peptidyl cysteine-peptidyl lysine cross-link by the condensation of a cysteine thiol with the carbonyl of the preceding residue and alpha-beta dehydrogenation. The transient sulfation of peptidyl-cysteine to form S-sulfo-L-cysteine. The formation of a C-terminal peptidyl-cysteine amide by hydrolysis and oxidation of an interior Cys-Gly peptide in a secreted protein. The oxidation of peptidyl-cysteine to peptidyl-L-cysteine sulfinic acid or peptidyl-L-cysteine sulfenic acid. The posttranslation modification of peptidyl-aspartic acid to form peptidyl-L-beta-methylthioaspartic acid, typical of bacterial ribosomal protein S12. The covalent linking of a chromophore to a protein via peptidyl-cysteines. The linkage of the chromophore phycocyanobilin to phycocyanin or allophycocyanin via S-phycocyanobilin-L-cysteine. The linkage of protein to heme P460 via heme P460-bis-L-cysteine-L-tyrosine. The linkage of the chromophore phytochromobilin to phycocyanin or allophycocyanin via S-phytochromobilin-L-cysteine. The linkage of the chromophore phycourobilin to phycoerythrins via phycourobilin-bis-L-cysteine. The addition of an ester group to a cysteine residue in a protein. The covalent binding of a pyrromethane (dipyrrin) cofactor to protein via the sulfur atom of cysteine forming dipyrrolylmethanemethyl-L-cysteine. The formation of a cross-link between peptidyl-cysteine and peptidyl-threonine via the formation of S-(2-aminovinyl)-3-methyl-D-cysteine. The linkage of the chromophore phycoerythrobilin to phycoerythrocyanin via S-phycoerythrobilin-L-cysteine. The linkage of the chromophore phycoerythrobilin to phycoerythrin via phycoerythrobilin-bis-L-cysteine. The incorporation of iron into a nickel-iron-sulfur cluster via pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide, found in carbon monoxide dehydrogenase. The posttranslational modification of peptidyl-cysteine to form peptidyl-S-myristoyl-L-cysteine. The covalent linkage of coenzyme A and peptidyl-cysteine to form L-cysteine coenzyme A disulfide. The, presumably, posttranslational modification of peptidyl-cysteine to form peptidyl-L-cysteine methyl disulfide. The posttranslational modification of peptidyl-cysteine to form peptidyl-S-farnesyl-L-cysteine; formation of S-farnesycysteine may be coupled with subsequent cleavage of a carboxy-terminal tripeptide for the CXXX motif and methyl esterification of the farnesylated cysteine; the residue may be found at the first position in the sequence motif C-X-X-(SAQCMT)* where the second and third positions are usually aliphatic. The posttranslational modification of peptidyl-cysteine to form peptidyl-S-geranylgeranylcysteine; formation of S-geranylgeranyl-L-cysteine may be coupled with subsequent cleavage of a carboxy-terminal tripeptide for the CAAX motif and methyl esterification of the geranylgeranylated cysteine; methyl esterification but not cleavage occurs for the CXC motif. For the type II geranylgeranyltransferase the residue may be found at the first and final positions in the sequence motif C-X-C* or at the final position in the sequence motif C-C*. These motifs are necessary but not sufficient for modification. The posttranslational modification of peptidyl-cysteine to form S-12-hydroxyfarnesyl-L-cysteine; formation of S-farnesycysteine may be coupled with subsequent cleavage of a carboxy-terminal tripeptide for the CXXX motif and methyl esterification of the farnesylated cysteine. The phosphorylation of peptidyl-cysteine to form peptidyl-S-phospho-L-cysteine. The incorporation of iron into a Rieske 4Fe-4S iron-sulfur cluster via bis-L-cysteinyl bis-L-histidino diiron disulfide. The palmitoylation of the N-terminal cysteine of proteins to form the derivative N-palmitoyl-cysteine. The modification of peptidyl-cysteine. The formation of a protein-protein cross-link between peptidyl-threonine and peptidyl-cysteine by the synthesis of (2S,3S,4Xi,6R)-3-methyl-lanthionine sulfoxide (3-methyl-L-lanthionine sulfoxide), as found in the antibiotic actagardine. The modification of peptidyl-cysteine to form peptidyl-L-cysteine persulfide. A persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii Rhodanese. The posttranslational synthesis of (S,Z)-S-(2-aminovinyl)cysteine forming an intra-polypeptide cross-link between serine and cysteine. The alteration of an amino acid residue in a peptide. The synthesis of the chromophore S-4-hydroxycinnamyl-L-cysteine. The incorporation of iron and molybdenum into a Mo-7Fe-8S iron-molybdenum-sulfur cluster via L-cysteinyl homocitryl molybdenum-heptairon-nonasulfide, found in nitrogenase. The incorporation of molybdenum into a protein via L-cysteinyl molybdopterin. The formation of a protein-FAD linkage via S-(8-alpha-FAD)-L-cysteine. The co- or posttranslational modification of peptidyl-cysteine to form peptidyl-S-diacylglycerol-L-cysteine; the oleate and palmitate actually represent mixtures of saturated (generally at 3') and unsaturated (generally at 2') fatty acids. The posttranslational thioether cross-linking of a cysteine residue to a tyrosine residue to form 3'-(S-L-cysteinyl)-L-tyrosine, found in galactose oxidase. The posttranslation modification of peptidyl-histidine and peptidyl-cysteine to form a 2'-(S-L-cysteinyl)-L-histidine protein cross-link. The posttranslation modification of peptidyl-glutamine and peptidyl-cysteine to form a S-(L-isoglutamyl)-L-cysteine protein cross-link. The incorporation of molybdenum into a protein by L-cysteinyl molybdopterin guanine dinucleotide. The incorporation of iron into a 4Fe-4S iron-sulfur cluster via tetrakis-L-cysteinyl tetrairon tetrasulfide. The posttranslational modification of peptidyl-cysteine or peptidyl-serine to peptidyl-L-3-oxoalanine; characteristic of the active sites of arylsulfatases. The incorporation of iron into a 3Fe-4S iron-sulfur cluster via tris-L-cysteinyl triiron tetrasulfide. The incorporation of iron into a 2Fe-2S iron-sulfur cluster via tetrakis-L-cysteinyl diiron disulfide. The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). The incorporation of iron into a protein via tetrakis-L-cysteinyl iron (there is no exogenous sulfur, so this modification by itself does not produce an iron-sulfur protein). The formation of 4-amino-3-isothiazolinone cross-links by the formation of a sulfenylamide bond between cysteine or cysteine sulfenic acid, and the alpha-amido of the following residue.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: peptidyl-cysteine modification
Acc: GO:0018198
Aspect: Biological Process
Desc: The modification of peptidyl-cysteine.
Proteins in PDR annotated with:
   This term: 0
   Term or descendants: 17 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0018198 - peptidyl-cysteine modification (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle