dbPSP 2.0, an updated database of protein phosphorylation sites in prokaryotes

Sci Data. 2020 May 29;7(1):164. doi: 10.1038/s41597-020-0506-7.


In prokaryotes, protein phosphorylation plays a critical role in regulating a broad spectrum of biological processes and occurs mainly on various amino acids, including serine (S), threonine (T), tyrosine (Y), arginine (R), aspartic acid (D), histidine (H) and cysteine (C) residues of protein substrates. Through literature curation and public database integration, here we reported an updated database of phosphorylation sites (p-sites) in prokaryotes (dbPSP 2.0) that contains 19,296 experimentally identified p-sites in 8,586 proteins from 200 prokaryotic organisms, which belong to 12 phyla of two kingdoms, bacteria and archaea. To carefully annotate these phosphoproteins and p-sites, we integrated the knowledge from 88 publicly available resources that covers 9 aspects, namely, taxonomy annotation, genome annotation, function annotation, transcriptional regulation, sequence and structure information, family and domain annotation, interaction, orthologous information and biological pathway. In contrast to version 1.0 (~30 MB), dbPSP 2.0 contains ~9 GB of data, with a 300-fold increased volume. We anticipate that dbPSP 2.0 can serve as a useful data resource for further investigating phosphorylation events in prokaryotes. dbPSP 2.0 is free for all users to access at: http://dbpsp.biocuckoo.cn.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaea / chemistry
  • Archaeal Proteins / chemistry*
  • Bacteria / chemistry
  • Bacterial Proteins / chemistry*
  • Databases, Protein*
  • Datasets as Topic
  • Phosphoproteins / chemistry*
  • Phosphorylation*


  • Archaeal Proteins
  • Bacterial Proteins
  • Phosphoproteins