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Subject: RE: Neighboring Phosphorylation Sites
Date: Mon, 11 Jun 2001 17:32:54 -0700
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Mike,
There are several examples of kinases that doubly phosphorylate sites with
one intervening residue. MKK7 doubly phosphorylates JNK on the Tyr and Thr
residues separated by a proline (FMMTPYVV) and MEK1 doubly phosphorylates
ERK (on a TEY motif).
In terms of adjacent phosphorylation, the BMP receptor phosphorylates SMAD
proteins on the three serines in the C-terminus (NPSSVS).
--------------------------------------------------------------
Gordon Alton, Ph.D.
Lead Scientist
Assay Development / Analytical Protein Chemistry
Department of Informatics and Functional Genomics
Signal Research Division of Celgene
5555 Oberlin Drive, San Diego, CA 92121
858-558-7500
858-623-0870 (fax)
www.signalpharm.com <http://www.signalpharm.com>
---------------------------------------------------------
-----Original Message-----
From: Michael Curtis [mailto:curtism@mail.upstate.edu]
Sent: Monday, June 11, 2001 1:24 PM
To: Recipients of ABRF List
Subject: Neighboring Phosphorylation Sites
Hello.
I am currently working on a phosphorylation project and have a question
concerning neighboring phosphorylation sites. Does anyone know of an
example of
two phosphorylateable residues being directly next to each other and both
being
phosphorylated? Or sites that are very close?
For example:
Directly next to each other:
i.e XXSTXX giving XXSpTpXX upon phosphorylation
Or very close by:
i.e. XXS(X1-2)TXX giving XXSp(X1-2)TpXX upon phosphorylation
I am wondering if phosphorylation of one would sterically hinder the
phosphorylation of the other. Any instance of these cases that you know
about or
any insight you have on this issue would be greatly appreciated.
Thanks in advance.
Mike
Mike Curtis
UMU
curtism@mail.upstate.edu
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