Cell Signaling Technology Inc. Announces the Launch of the PhosphoSite® Database, a Database Dedicated to Phosphorylation Sites in Human and Mouse Proteins
BEVERLY, MA - November 17, 2003 - Cell Signaling Technology, Inc. (CST) announced today the launch of the PhosphoSite® Database, a database dedicated to in vivo protein phosphorylation sites within human and mouse proteins. The database will be freely available for education purposes, while proprietary information will be available on a subscription basis.
PhosphoSite®, developed by CST scientists with support from the National Institute of General Medical Sciences (NIGMS) and the National Institute on Alcohol Abuse and Alcoholism (NIAAA), is a curated protein database dedicated to phosphorylation sites in humans, mice and related species. The site is populated with information from literature reports as well as from high-throughput phosphosite discovery programs. The scientific community, as users of PhosphoSite®, will have the opportunity to enhance the site by sending information about missing or novel sites to CST editors.
“Protein phosphorylation is one of the most critical and widespread regulatory mechanisms of complex organisms. Its deregulation is implicated in many cancers, immunodeficiencies and development disorders. Detailed knowledge of protein phosphorylation will play a critical role in the development of diagnostics and therapeutics in the coming years,” Said Peter Hornbeck, Director of Bioinformatics, CST. “The PhosphoSite® Database will help elucidate these complex regulatory mechanisms by organizing complex signaling information in a central and accessible location.”
The site will contain basic information about the parent protein, including a function statement, accession number, alternative names and links to other useful websites. More detailed information will include a linear representation of the protein, predicted domains, the location of known phosphosites relative to the domain structure, sequences of phosphosites in the parent protein and orthologous sites in other species. Future releases of PhosphoSite® will include the kinases, phosphatases, ligands and receptors that regulate the phosphorylation status of the sites, and pathways in which the phosphosites function, along with structural viewers that allow users to examine the topography of phosphosites.