RT Journal Article
SR Electronic
T1 FPD: A comprehensive phosphorylation database in fungi
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 058867
DO 10.1101/058867
A1 Youhuang Bai
A1 Bin Chen
A1 Yincong Zhou
A1 Silin Ren
A1 Qin Xu
A1 Ming Chen
A1 Shihua Wang
YR 2016
UL http://biorxiv.org/content/early/2016/06/14/058867.abstract
AB Protein phosphorylation, one of the most classic post-translational modification, plays a critical role in the diverse cellular processes including cell cycle, growth and signal transduction pathways. However, the available information of 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 motif were discovered by comparatively analyzing the pattern of phosphorylation sites in fungi, plants and animals.Database URL: http://bis.zju.edu.cn/FPD/index.php