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.
Dates
Type | When |
---|---|
Created | 19 years, 2 months ago (May 31, 2006, 5 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 11:48 a.m.) |
Indexed | 1 month, 2 weeks ago (July 11, 2025, 6:21 a.m.) |
Issued | 43 years, 6 months ago (Feb. 1, 1982) |
Published | 43 years, 6 months ago (Feb. 1, 1982) |
Published Online | 43 years, 6 months ago (Feb. 1, 1982) |
Published Print | 43 years, 6 months ago (Feb. 1, 1982) |
@article{Patschinsky_1982, title={Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation.}, volume={79}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.79.4.973}, DOI={10.1073/pnas.79.4.973}, number={4}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Patschinsky, T and Hunter, T and Esch, F S and Cooper, J A and Sefton, B M}, year={1982}, month=feb, pages={973–977} }