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

Proc Natl Acad Sci U S A. 1982 Feb;79(4):973-7. doi: 10.1073/pnas.79.4.973.

Abstract

We have identified the single phosphorylated tyrosine in p60src, the transforming protein of Rous sarcoma virus, as part of the sequence. NH2-Arg-Leu-Ile-Glu-Asp-Asn-Glu-Tyr(P)-Thr-Ala-Arg-COOH. Therefore, 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 four classes of genetically distinct RNA tumor viruses. Phosphorylated tyrosines in several other proteins resemble of 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. Therefore it is possible that these features play a role in the selection of sites of phosphorylation by some tyrosine protein kinases. However, several clear exceptions to this rule exist.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Abelson murine leukemia virus
  • Alpharetrovirus
  • Amino Acid Sequence
  • Avian Sarcoma Viruses
  • Cell Transformation, Neoplastic
  • Cell Transformation, Viral*
  • Immunoglobulin Heavy Chains
  • Peptides* / metabolism
  • Phosphorylation
  • Protein Kinases / metabolism*
  • Transforming Growth Factors
  • Tyrosine / metabolism*
  • Viral Proteins* / metabolism

Substances

  • Immunoglobulin Heavy Chains
  • Peptides
  • Viral Proteins
  • Tyrosine
  • Transforming Growth Factors
  • Protein Kinases