Allows the retrieval of phosphorylation, acetylation, and N-glycosylation data of any protein of interest. PHOSIDA lists posttranslational modification sites associated with particular projects and proteomes or, alternatively, displays posttranslational modifications found for any protein or protein group of interest. In addition, structural and evolutionary information on each modified protein and posttranslational modification site is integrated. Importantly, Phosida links extensive peptide information to the sites, such as several peptides implicating the same site and temporal profiles of each site in response to stimulus (e.g., EGF stimulation).
Department for Proteomics and Signal Transduction, Max-Planck Institute for Biochemistry, Am Klopferspitz, Martinsried, Germany
PHOSIDA funding source(s)
National Institutes of Health Grant R01 GM081578-02 on “Complex dynamics in multisite phosphorylation”; PROSPECT, a 7th framework program of the European Union (grant agreement HEALTH-F4-2008-201648/PROSPECTS)