FPD: A comprehensive phosphorylation database in fungi. Issue 10 (October 2017)

• Record Type: Journal Article
• Authors: Bai, Youhuang; Chen, Bin; Li, Mingzhu; Zhou, Yincong; Ren, Silin; Xu, Qin; Chen, Ming; Wang, Shihua
• Is Part Of: Fungal biology. Volume 121:Issue 10(2017:Oct.)
• Page Start: 869
• Page End: 875
• Publication Date: 2017-10
• Subjects: Fungal -- Motif -- Phosphosites -- Protein database; Mycology -- Periodicals; Fungi -- Periodicals; 579.505
• DOI: 10.1016/j.funbio.2017.06.004
• Languages: English
• ISSNs: 1878-6146

Abstract

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.