{PDOC00007}
{PS00007; TYR_PHOSPHO_SITE_1}
{PS60007; TYR_PHOSPHO_SITE_2}
{BEGIN}
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* Tyrosine kinase phosphorylation sites *
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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.

We developed  two  signature  patterns for the tyrosine kinase phosphorylation
sites. The  first  pattern  is  directed  against  the  sites where the acidic
residue (Asp  or Glu) is found at three residues to the N-terminal side of the
tyrosine, and the second one against the site where it is at four.

-Consensus pattern: [RK]-x(2)-[DE]-x(3)-Y
                    [Y is the phosphorylation site]

-Consensus pattern: [RK]-x(3)-[DE]-x(2)-Y
                    [Y is the phosphorylation site]

-Last update: March 2019 / Text and pattern revised; pattern added.

[ 1] Patschinsky T., Hunter T., Esch F.S., Cooper J.A., Sefton B.M.
     "Analysis of the sequence of amino acids surrounding sites of tyrosine
     phosphorylation."
     Proc. Natl. Acad. Sci. U.S.A. 79:973-977(1982).
     PubMed=6280176
[ 2] Hunter T.
     "Synthetic peptide substrates for a tyrosine protein kinase."
     J. Biol. Chem. 257:4843-4848(1982).
     PubMed=6279650
[ 3] Cooper J.A., Esch F.S., Taylor S.S., Hunter T.
     "Phosphorylation sites in enolase and lactate dehydrogenase utilized
     by tyrosine protein kinases in vivo and in vitro."
     J. Biol. Chem. 259:7835-7841(1984).
     PubMed=6330085

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