dbPSP: a curated database for protein phosphorylation sites in prokaryotes

• DOI: 10.1093/database/bav031
• Publication Date: 2015-04-05T01:38:23Z
• Authors: Zhicheng Pan; Bangshan Wang; Ying Zhang; Yongbo Wang; Shahid Ullah; Ren Jian; Zexian Liu; Yu Xue
• Keywords: Phosphorylation cascade

As one of the most important post-translational modifications, phosphorylation is highly involved in almost all biological processes through temporally and spatially modifying substrate proteins. Recently, prokaryotes attracted much attention for its critical roles various cellular such as signal transduction. Thus, an integrative data resource prokaryotic will be useful further analysis. In this study, we presented a curated database sites (dbPSP, Database URL: http://dbpsp.biocuckoo.org) 96 organisms, which belong to 11 phyla two domains including bacteria archaea. From scientific literature, manually collected experimentally identified on seven types residues, serine, threonine, tyrosine, aspartic acid, histidine, cysteine arginine. total, dbPSP contains 7391 3750 With dataset, sequence preferences functional annotations phosphoproteins were analyzed, while results shows that there obvious differences among bacteria, archaea eukaryotes. All annotated with original references other descriptions database, could easily accessed user-friendly website interface search browse options. Taken together, provides comprehensive studies protein prokaryotes. http://dbpsp.biocuckoo.org