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PROSITE documentation PDOC00007

Tyrosine kinase phosphorylation site





Description

Substrates of tyrosine protein kinases are generally characterized by a lysine or an arginine seven residues to the N-terminal side of the phosphorylated tyrosine. An acidic residue (Asp or Glu) is often found at either three or four residues to the N-terminal side of the tyrosine [1,2,3]. There are a number of exceptions to this rule such as the tyrosine phosphorylation sites of enolase and lipocortin II.

Last update:

June 1988 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

TYR_PHOSPHO_SITE, PS00007; Tyrosine kinase phosphorylation site  (PATTERN with a high probability of occurrence!)


References

1AuthorsPatschinsky T. Hunter T. Esch F.S. Cooper J.A. Sefton B.M.
TitleAnalysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation.
SourceProc. Natl. Acad. Sci. U.S.A. 79:973-977(1982).
PubMed ID6280176

2AuthorsHunter T.
TitleSynthetic peptide substrates for a tyrosine protein kinase.
SourceJ. Biol. Chem. 257:4843-4848(1982).
PubMed ID6279650

3AuthorsCooper J.A. Esch F.S. Taylor S.S. Hunter T.
TitlePhosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro.
SourceJ. Biol. Chem. 259:7835-7841(1984).
PubMed ID6330085



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