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Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). Interacting selectively and non-covalently with a protein N-terminus, the end of any peptide chain at which the 2-amino (or 2-imino) function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue. Interacting selectively and non-covalently with the N-terminus of a protein that has the potential to be, or has been, modified by N-terminal myristoylation. Binding affinity is typically altered by myristoylation; for example, N-terminal myristoylation of HIV Nef increases its affinity for calmodulin.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: N-terminal myristoylation domain binding
Acc: GO:0031997
Aspect: Molecular Function
Desc: Interacting selectively and non-covalently with the N-terminus of a protein that has the potential to be, or has been, modified by N-terminal myristoylation. Binding affinity is typically altered by myristoylation; for example, N-terminal myristoylation of HIV Nef increases its affinity for calmodulin.
Proteins in PDR annotated with:
   This term: 1 [Search]
   Term or descendants: 1 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0031997 - N-terminal myristoylation domain binding (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle