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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. The selective, non-covalent, often stoichiometric, interaction of a molecule with one or more specific sites on another molecule. 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: protein N-terminus binding
Acc: GO:0047485
Aspect: Molecular Function
Desc: 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.
Synonyms:
  • NH2-terminal binding
  • NH2-terminus binding
  • amino-terminus binding
  • N-terminal end binding
  • N-terminal binding
  • amino-terminal binding
Proteins in PDR annotated with:
   This term: 164 [Search]
   Term or descendants: 165 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0047485 - protein N-terminus binding (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle