Welcome to the

PHOSPHORYLATION SITE DATABASE



Purpose.
The Phosphorylation Site Database provides ready access to information from the primary scientific literature concerning proteins in prokaryotic organisms (i.e. members of the domains Archaea and Bacteria) that undergo covalent phosphorylation on the hydroxyl side chains of serine, threonine, and/or tyrosine residues. Where known, the sequence of the site(s) phosphorylated and the functional consequences of phosphorylation also are included. Links enable users to quickly access further information concerning the protein in question from PubMed, GenBank, and UniProt.

Go To Database


This database has been constructed and is maintained by:

Peter J. Kennelly http://www.biochem.vt.edu/faculty/kennelly.html
Susannah Wurgler-Murphy
Douglas M. King

with the support of the Department of Biochemistry (http://www.biochem.vt.edu), the Virginia Institute for Genomics [VIGEN], and AHNR-Information Technology in the College of Agriculture and Life Sciences at Virginia Polytechnic Institute and State University, and the National Science Foundation.


Sources for the information contained in the database.
It is the explicit policy of the Phosphorylation Site Database to only include information from journals subject to scientific peer review. No unpublished information or information from unrefereed sources (e.g. published abstracts) will be included. Literature citations are provided for all information contained in the Phosphorylation Site Database. Users are encouraged to access the references cited for more complete and detailed data. Because space limitations preclude the inclusion of every relevant paper, users are encouraged to supplement the list of references provided by the Phosphorylation Site Database through their own independent literature searches.


Search options.
The Phosphorylation Site Database may be searched using a variety of criteria either singly or in combination. These include:

  • the name of the protein of interest
  • the name of the gene encoding the protein
  • the accession number for a gene or protein from the GenBank or UniProt database
  • the sequence of a protein's site of phosphorylation
  • the nature of the amino acid residue phosphorylated
  • literature citation by author name, etc.
For additional information,
Go To Database

A note concerning proteins phosphorylated at multiple sites.

For proteins that undergo phosphorylation at multiple sites, the amino acid sequences for which have been identified, a separate entry has been provided for each phosphorylation site.


How to contact us.
Email us at psite@vt.edu

or write:

Peter J. Kennelly
Department of Biochemistry-0308
Virginia Polytechnic Institute and State University
Blacksburg, VA 24061


Related links.
Prokaryotic Protein Phosphatase Database: http://www.phosphatase.biochem.vt.edu/
PhosphoSite: http://www.phosphosite.org/Login.jsp
PhosphoBase: http://phospho.elm.eu.org/
Protein Kinase Resource: http://pkr.genomics.purdue.edu/pkr/Welcome.do