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The modification of peptidyl-asparagine. The formation of a covalent cross-link between or within protein chains. The formation of isopeptide bonds by ligation of peptidyl-lysine and peptidyl-asparagine residues. The alteration of an amino acid residue in a peptide. The autocatalytic formation of isopeptide bonds by ligation of peptidyl-lysine and peptidyl-asparagine residues; known to occur in the capsid of some bacteriophage, such as HK97, where it is thought to provide a mechanism for stabilizing the capsid. The modification of peptidyl-lysine. The formation of isopeptide bonds by ligation of peptidyl-lysine and peptidyl-asparagine residues; occurs in mammals in proteins as yet unidentified by a mechanism probably analogous to that of transglutaminase reactions. The covalent alteration of one or more amino acids occurring in a protein after the protein has been completely translated and released from the ribosome.

View Gene Ontology (GO) Term

GO TERM SUMMARY

Name: peptide cross-linking via N6-(L-isoaspartyl)-L-lysine
Acc: GO:0018420
Aspect: Biological Process
Desc: The formation of isopeptide bonds by ligation of peptidyl-lysine and peptidyl-asparagine residues.
Proteins in PDR annotated with:
   This term: 0
   Term or descendants: 0


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0018420 - peptide cross-linking via N6-(L-isoaspartyl)-L-lysine (interactive image map)

YRC Informatics Platform - Version 3.0
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