As one of the PTMs with tremendous studies, Phosphorylation regulates a wide variety of biological processes, including signal transduction events (Cohen, 1982). Whereas eukaryotic proteins of phosphorylation have been extensively studied, only limited information is available for phosphorylated proteins in prokaryotic organisms. Previous studies about constructing database of prokaryotic phosphorylation sites mainly focus on tyrosine-, serine, and threonine-phosphorylated proteins (Wurgler-Murphy, King and Kennelly, 2004). However, for the purpose of elucidating the mechanisms of phosphorylation in prokaryotic organisms, other residues which can also be phosphorylated should not be neglected. For example, protein histidine or aspartate phosphorylation plays important roles in two-signal-transduction events (Galperin, Nikolskaya, Koonin, 2001; Swanson, Alex and Simon, 1994).
To settle these challenges, we provide a comprehensive database of Prokaryotic Protein Phosphorylation Sites for 7 types of residues, including 7,391 phosphorylation sites in 3,750 proteins.
For publication of results please cite the following article:
dbPSP: a curated database for phosphorylation sites in prokaryotes.
Zhicheng Pan, Bangshan Wang, Ying Zhang, Yongbo Wang, Shahid Ullah, Jian Ren, Zexian Liu ,Yu Xue.
Database, 2015, 2015: bav031
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