Journal
FUNGAL BIOLOGY
Volume 121, Issue 10, Pages 869-875Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.funbio.2017.06.004
Keywords
Fungal; Motif; Phosphosites; Protein database
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Funding
- Ministry of Science and Technology of China [2013CB127802]
- National Natural Science Foundation of China [31172297, 31400100, 31601069]
- Natural Science Foundation of Fujian Province [2016J05065]
- Foundation of Education Bureau of Fujian Province [JA15163]
- Fujian Agriculture and Forestry University [KXR14043A, xjq201615]
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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 62272 non-redundant phosphorylation sites in 11222 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. (C) 2017 British Mycological Society. Published by Elsevier Ltd. All rights reserved.
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