What you can do:
Search for information on prokaryotic proteins that undergo serine, threonine, or tyrosine phosphorylation.
  • The Phosphorylation Site Database provides ready access to information from the primary scientific literature concerning proteins in prokaryotic organisms 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, SwissProt, and PIR.
  • The database may be searched by the name of the protein or gene of interest, the gene or protein GenBank, SwissProt, or PIR accession number, the sequence of the phosphorylation site, the phosphorylated amino acid residue, or literature citation.
  • All information in the database comes from the primary scientific literature.
  • phosphorylation
  • protein phosphorylation
  • phosphorylation sites
  • phosphorylated residues
  • phosphatases
  • phosphoproteins
  • post-translational modifications
  • protein modifications
  • kinases
  • protein kinases
  • signal transduction pathways
  • prokaryotic proteins
  • prokaryotic phosphoproteins
This record last updated: 04-21-2014
Report a missing or misdirected URL.

The Health Sciences Library System supports the Health Sciences at the University of Pittsburgh.

© 1996 - 2023 Health Sciences Library System, University of Pittsburgh. All rights reserved.