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. 1982 Feb;79(4):973–977. doi: 10.1073/pnas.79.4.973

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

T Patschinsky, T Hunter, F S Esch, J A Cooper, B M Sefton
PMCID: PMC345881  PMID: 6280176

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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