Protein phosphorylation, one of most important post-translational modifications (PTMs), orchestrates a wide spectrum of signal transduction pathways through by mainly modifying specific serine (S), threonine (T) or tyrosine (Y) residues on targeted substrates. (Tim, et al., 2022; Battaglioni, et al., 2022; Shindo, et al., 2023). more details >>>

    Owing to phosphorylation as a key regulatory mechanism conserved across almost all eukaryotic organisms, the collection, curation and integration of experimentally identified p-sites and functional p-sites are essential yet remain a great challenge in the PTMs research community.
   The Eukaryotic Phosphorylation Site Database 2.0 (EPSD) is a comprehensive data resource. Previously we developed the eukaryotic phosphorylation site database 1.0 (EPSD 1.0), which collected 1,616,804 p-sites in 209,326 phosphoproteins from 68 eukaryotic species. Now in the 2.0 version, we carefully re-checked all entries in EPSD 1.0, and further collected 841,963 new non-redundant p-sites from phosphopretome as well as public data resources including PhosphoSitePlus, iPTMnet, UniProt, Pf-phospho, BioGRID, dbPTM, PTMcode2, Plant PTM Viewer, RegPhos, PhosPhAt and Scop3p. In total, EPSD 2.0 contains 2,769,163 experimentally identified p-sites in 362,707 phosphoproteins from 223 eukaryotes. Moreover, we carefully annotated 88,074 functional events of 32,762 p-sites, covering 58 types of downstream effects on phosphoproteins, and regulatory impacts on 107 biological processes. In addition, the phosphoproteins and p-sites of eight model organisms were annotated by integrating the knowledge from 100 additional resources that covered 15 aspects, including (i) Phosphorylation regulator; (ii) Genetic variation & mutation; (iii) Functional annotation; (iv) Structural annotation; (v) Physicochemical property; (vi) Functional domain; (vii) Disease-associated information; (viii) Protein-protein interaction; (ix) Drug-target relation; (x) Orthologous information; (xi) Biological pathway; (xii) Transcriptional regulator; (xiii) mRNA expression; (xiv) Protein expression/proteomics; (xv) Subcellular localization. We anticipate EPSD can serve as a useful resource for further analysis of eukaryotic phosphorylation. Here we confirm that EPSD will be continuously maintained and updated, meanwhile all data sets and annotations are freely accessed for all users. Hide details <<<