Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation.

Abstract

This is a sequence that is recognized efficiently by a tyrosine protein kinase in vivo. Phosphorylation of tyrosine in cellular proteins appears to play a role in malignant transformation by 4 classes of genetically distinct RNA tumor viruses. Phosphorylated tyrosines in several other proteins resemble the tyrosine in p60src in that they are located 7 residues to the COOH-terminal side of a basic amino acid and either 4 residues to the COOH-terminal side of, or in close proximity to, a glutamic acid residue. These features may play a role in the selection of sites of phosphorylation by some tyrosine protein kinases. Several clear exceptions to this rule exist.