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Omics score: 1009

Analysis of the Candida albicans phosphoproteome.

ABSTRACT: Data from ProteomeXchange, PXD ID: PXD001844. File: qe+00163.mzml. Published as part of Eukaryot Cell. 2015 Mar 6. pii: EC.00011-15 . From the Abstract: {{i}} ... Here, we contribute to our understanding of phosphorylation in C. albicans regulation, we performed a deep analysis of the phosphoproteome in C. albicans. We identified 19,590 unique peptides that corresponded to 15,906 unique phosphosites on 2,896 proteins. The ratios of serine, threonine and tyrosine phosphosites were 80.01%, 18.11%, and 1.81%, respectively ... {{/i}}

INSTRUMENT(S): Instrument

ORGANISM(S): Candida_albicans_refseq

DISEASE(S): Not Available

SUBMITTER: Willger SD, et al.

PROVIDER: GPM32320014317 | GPMDB |

REPOSITORIES: GPMDB

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Analysis of the Candida albicans Phosphoproteome.

Willger S D SD Liu Z Z Olarte R A RA Adamo M E ME Stajich J E JE Myers L C LC Kettenbach A N AN Hogan D A DA

Eukaryotic cell 20150306 5

Candida albicans is an important human fungal pathogen in both immunocompetent and immunocompromised individuals. C. albicans regulation has been studied in many contexts, including morphological transitions, mating competence, biofilm formation, stress resistance, and cell wall synthesis. Analysis of kinase- and phosphatase-deficient mutants has made it clear that protein phosphorylation plays an important role in the regulation of these pathways. In this study, to further our understanding of ...[more]

PMID: 25750214

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