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	PROSITE documentation PDOC00007

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.

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!)

• Consensus pattern:
  [RK]-x(2)-[DE]-x(3)-Yor[RK]-x(3)-[DE]-x(2)-Y
  Y is the phosphorylation site
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS00007
• View ligand binding statistics of PS00007

1	Authors	Patschinsky T., Hunter T., Esch F.S., Cooper J.A., Sefton B.M.
	Title	Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation.
	Source	Proc. Natl. Acad. Sci. U.S.A. 79:973-977(1982).
	PubMed ID	6280176

2	Authors	Hunter T.
	Title	Synthetic peptide substrates for a tyrosine protein kinase.
	Source	J. Biol. Chem. 257:4843-4848(1982).
	PubMed ID	6279650

3	Authors	Cooper J.A., Esch F.S., Taylor S.S., Hunter T.
	Title	Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro.
	Source	J. Biol. Chem. 259:7835-7841(1984).
	PubMed ID	6330085

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