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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 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 aggregation, arrangement and bonding together of a protein structure comprising two or more rings that are interlocked but not covalently joined; resembling the links of a chain. The aggregation, arrangement and bonding together of a set of components to form a protein complex, occurring at the level of an individual cell.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: protein catenane formation via N6-(L-isoaspartyl)-L-lysine, autocatalytic
Acc: GO:0019937
Aspect: Biological Process
Desc: 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.
Proteins in PDR annotated with:
   This term: 0
   Term or descendants: 0


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0019937 - protein catenane formation via N6-(L-isoaspartyl)-L-lysine, autocatalytic (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle