Analysis of the Sequence of Amino Acids Surrounding Sites of Tyrosine Phosphorylation

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. Phospho...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1982-02, Vol.79 (4), p.973-977
Main Authors: Patschinsky, Tilo, Hunter, Tony, Esch, Fred S., Cooper, Jonathan A., Sefton, Bartholomew M.
Format: Article
Language:English
Subjects:
Abelson murine leukemia virus
Acidic amino acids
Alpharetrovirus
Amino Acid Sequence
Amino acids
Avian Sarcoma Viruses
Basic amino acids
Cell Transformation, Neoplastic
Cell Transformation, Viral
Electrophoresis
Gels
Immunoglobulin Heavy Chains
Peptides - metabolism
Phosphorylation
protein kinase
Protein Kinases - metabolism
proteins
Rous sarcoma virus
Sarcoma
Sequence analysis
transformation
Transforming Growth Factors
Tyrosine - metabolism
Viral Proteins - metabolism
Virology
Viruses
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Summary: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 the tyrosine in p60srcin 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.79.4.973