@article {Bai058867, author = {Youhuang Bai and Bin Chen and Yincong Zhou and Silin Ren and Qin Xu and Ming Chen and Shihua Wang}, title = {FPD: A comprehensive phosphorylation database in fungi}, elocation-id = {058867}, year = {2016}, doi = {10.1101/058867}, publisher = {Cold Spring Harbor Laboratory}, abstract = {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}, URL = {https://www.biorxiv.org/content/early/2016/06/14/058867}, eprint = {https://www.biorxiv.org/content/early/2016/06/14/058867.full.pdf}, journal = {bioRxiv} }