※ Overview

    Protein phosphorylation is one of the most indispensable post-translational modifications (PTMs), participates in almost all of biological processes and pathways, and reversibly determines the cellular dynamics and plasticity (Linding, et al., 2007; Jin, et al., 2012; Olsen, et al., 2006; Ptacek, et al., 2005; Ptacek and Snyder, 2006; Ubersax and Ferrell, 2007). In eukaryotes, protein phosphorylation mainly occurs on a specific subset of three types of amino acids, including serine (S), threonine (T) and tyrosine (Y) residues. The identification and functional analysis of phosphorylation sites (p-sites) are fundamental to understand the molecular mechanisms and regulatory roles of protein phosphorylation in eukaryotes.

    The Eukaryotic Phosphorylation Site Database (EPSD) is a comprehensive data resource updated from two databases of dbPPT (Cheng, et al., 2014) and dbPAF (Ullah, et al., 2016), which contained 82,175 p-sites of 20 plants and 483,001 p-sites of 7 animals and fungi, respectively. We carefully re-checked all entries in dbPPT and dbPAF, and further collected 1,451,629 known p-sites newly identified from high-throughput phosphoproteomic studies. Also, known p-sites in 13 additional databases including PhosphoSitePlus, Phospho.ELM, UniProt, PhosphoPep, BioGRID, dbPTM, FPD, HPRD, MPPD, P3DB, PHOSIDA, PhosPhAt and SysPTM were integrated. In total, EPSD contains 1,616,804 experimentally identified p-sites in 209,326 phosphoproteins from 68 eukaryotes. Moreover, we carefully annotated the phosphoproteins and p-sites of eight model organisms with the knowledge from additional 100 public resources that cover 15 distinct 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.

※ Substrate Search



  ▼ Statistics

※ Example

Serine/threonine-protein kinase PLK1 (Homo sapiens)


For publication of results please cite the following articles:

EPSD: a well-annotated database of protein phosphorylation sites in eukaryotes.
Shaofeng Lin, Chenwei Wang, Jiaqi Zhou, Ying Shi, Chen Ruan, Yiran Tu, Lan Yao, Di Peng and Yu Xue.
Briefings in Bioinformatics, 2020, bbz169.
[Abstract] [FREE Full Text] [PDF][Supplementary Data]

dbPAF: an integrative database of protein phosphorylation in animals and fungi.
Shahid Ullah, Shaofeng Lin, Yang Xu, Wankun Deng, Lili Ma, Ying Zhang, Zexian Liu and Yu Xue.
Scientific Reports, 2016, 6:23534, doi:10.1038/srep23534
[Abstract] [FREE Full Text] [PDF] [Supplementary Data]

dbPPT: a comprehensive database of protein phosphorylation in plants.
Han Cheng, Wankun Deng, Yongbo Wang, Jian Ren, Zexian Liu and Yu Xue.
Database, 2014, 2014: bau121
[Abstract] [FREE Full Text] [PDF] [Supplementary Data]