Home  |  Contact
PROSITE documentation PDOC00007

Tyrosine kinase phosphorylation site


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!)


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

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)