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The transient guanylylation of peptidyl-histidine to form (phospho-5'-guanosine)-L-histidine. The posttranslational bromination of peptidyl-histidine to form peptidyl-L-bromohistidine; the position of the bromine substitution is unknown. 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 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 copper into a 4Cu-S copper-sulfur cluster via heptakis-L-histidino tetracopper mu4-sulfide hydroxide. The modification of peptidyl-histidine. The incorporation of iron into a Rieske 4Fe-4S iron-sulfur cluster via bis-L-cysteinyl bis-L-histidino diiron disulfide. 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 involving peptidyl-diphthine, a modified histidine residue. The adenylylation of peptidyl-histidine to form peptidyl-1'-(phospho-5'-adenosine)-L-histidine (otherwise known as tau-AMP-histidine, tele-AMP-histidine) or peptidyl-3'-(phospho-5'-adenosine)-L-histidine (otherwise known as pi-AMP-histidine, pros-AMP-histidine). 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 uridylylation of peptidyl-histidine to form peptidyl-1'-(phospho-5'-uridine)-L-histidine (otherwise known as tau-UMP-histidine, tele-UMP-histidine) or peptidyl-3'-(phospho-5'-uridine)-L-histidine (otherwise known as pi-UMP-histidine, pros-UMP-histidine). The alteration of an amino acid residue in a peptide. The posttranslational phosphorylation of peptidyl-histidine to form peptidyl-1'-phospho-L-histidine (otherwise known as tau-phosphohistidine, tele-phosphohistidine) or peptidyl-3'-phospho-L-histidine (otherwise known as pi-phosphohistidine, pros-phosphohistidine). The posttranslation modification of peptidyl-histidine and peptidyl-tyrosine to form a protein cross-link. The formation of a protein-FAD linkage via 3'-(8-alpha-FAD)-L-histidine. The formation of a protein-FAD linkage via 1'-(8-alpha-FAD)-L-histidine. The methylation of peptidyl-L-histidine to form peptidyl-L-1'-methyl-L-histidine (otherwise known as tau-methylhistidine, tele-methylhistidine) or peptidyl-L-3'-methyl-L-histidine (otherwise known as pi-methylhistidine, pros-methylhistidine). The posttranslation modification of peptidyl-histidine and peptidyl-cysteine to form a 2'-(S-L-cysteinyl)-L-histidine protein cross-link. 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 formation of a C-terminal peptidyl-histidine amide by hydrolysis and oxidation of an interior His-Gly peptide in a secreted protein. 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 incorporation of iron into a 4Fe-4S iron-sulfur cluster via bis-L-cysteinyl-L-N3'-histidino-L-serinyl tetrairon tetrasulfide. The covalent linkage of heme and a protein via 3'-L-histidine (otherwise known as pi-heme-histidine, pros-heme-histidine). The chemical reactions and pathways involving peptidyl-diphthamide, a modified histidine residue. 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 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).

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: peptidyl-histidine modification
Acc: GO:0018202
Aspect: Biological Process
Desc: The modification of peptidyl-histidine.
Proteins in PDR annotated with:
   This term: 0
   Term or descendants: 81 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0018202 - peptidyl-histidine modification (interactive image map)
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