FPD: A comprehensive phosphorylation database in fungi

Fungal Biol. 2017 Oct;121(10):869-875. doi: 10.1016/j.funbio.2017.06.004. Epub 2017 Jun 23.

Abstract

Protein phosphorylation, one of the most classic post-translational modification, plays a critical role in diverse cellular processes including cell cycle, growth, and signal transduction pathways. However, the available information about phosphorylation in fungi is limited. Here, we provided a Fungi Phosphorylation Database (FPD) that comprises high-confidence in vivo phosphosites identified by MS-based proteomics in various fungal species. This comprehensive phosphorylation database contains 62 272 non-redundant phosphorylation sites in 11 222 proteins across eight organisms, including Aspergillus flavus, Aspergillus nidulans, Fusarium graminearum, Magnaporthe oryzae, Neurospora crassa, Saccharomyces cerevisiae, Schizosaccharomyces pombe, and Cryptococcus neoformans. A fungi-specific phosphothreonine motif and several conserved phosphorylation motifs were discovered by comparatively analysing the pattern of phosphorylation sites in plants, animals, and fungi.

Keywords: Fungal; Motif; Phosphosites; Protein database.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Databases, Factual* / standards
  • Fungal Proteins / metabolism*
  • Fungi / metabolism*
  • Humans
  • Phosphorylation
  • Plants / metabolism
  • Protein Processing, Post-Translational / physiology*
  • Serine / metabolism
  • Threonine / metabolism
  • Tyrosine / metabolism

Substances

  • Fungal Proteins
  • Threonine
  • Tyrosine
  • Serine