{"database":"GPMDB","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":28,"searchCount":5},"additional":{"omics_type":["Other"],"submitter":["Willger SD, et al."],"instrument_platform":["Instrument"],"disease":["Not Available"],"brenda_tissue":["Not available"],"species":["Candida_albicans_refseq"],"publication":["25750214"],"submitter_mail":["dhogan@dartmouth.edu."],"model":["http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014313","http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014314","http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014315","http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014304","http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014316","http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014317","http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014318","http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014307","http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014309","http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014310","http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014311","http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014312"],"submitter_affiliation":["Department of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, et al."],"cell_type":["Not available"],"repository":["GPMDB"],"pubmed_abstract":["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 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. The majority of proteins (2,111) contained at least two detected phosphorylation sites. Consistent with findings in other fungi, cytoskeletal proteins were among the most highly phosphorylated proteins, and there were differences in Gene Ontology (GO) terms for proteins with serine and threonine versus tyrosine phosphorylation sites. This large-scale analysis identified phosphosites in protein components of Mediator, an important transcriptional coregulatory protein complex. A targeted analysis of the phosphosites in Mediator complex proteins confirmed the large-scale studies, and further in vitro assays identified a subset of these phosphorylations that were catalyzed by Cdk8 (Ssn3), a kinase within the Mediator complex. These data represent the deepest single analysis of a fungal phosphoproteome and lay the groundwork for future analyses of the C. albicans phosphoproteome and specific phosphoproteins."],"pubmed_title":["Analysis of the Candida albicans Phosphoproteome."],"pubmed_authors":["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,","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"],"name_synonyms":["albicans, Candida stellatoidea type I., Candida stellatoidea, assay, Candida, Candida albican, determination, chemical analysis"],"description_synonyms":["deep, data, para Tyrosine, IRF-1, determination, cell, 2-amino-3-(4-hydroxyphenyl)propanoic acid, 3-(p-Hydroxyphenyl)alanine, Proteins, 2-Amino-3-(p-hydroxyphenyl)propionic acid, L-isomer, Phosphorylations, Gene, L-Threonine, proteins, L Threonine, Understanding, C9H11NO3, para-Tyrosine, Cell, phosphorylation, Protein Gene Products, Tyrosine, Gene Proteins, polypeptide, Polypeptides, Readability, L Tyrosine, tirosina, Tyr, chemical analysis, Protein, Gene Products, L Serine, regulation, L-Tyrosine, L isomer., assay, threonine, Tyrosin, L-Serine, MAR"],"pubmed_title_synonyms":["albicans, Candida stellatoidea type I., Candida stellatoidea, assay, Candida, Candida albican, determination, chemical analysis"],"pubmed_abstract_synonyms":["cell wall anabolism, big, cell wall assembly, p-nitrophenylphosphatase activity, Astrin, para Tyrosine, scale tissue, human being, Gene Ontology Projects, nitrophenyl phosphatase activity, determination, PNPPase activity, mating, peltate hair, NPPase activity, Gene, Mitotic spindle-associated protein p126, L-Threonine, Homo sapiense, phosphorylation, Gene Ontology Project, Gene Ontology, protein amino acid phosphorylation, Polypeptides, Homo spaiens, Readability, large, Homo sapien, conclusions, Roles, Mediator Like Complex, Homo sapians, DEEPEST, resistance, Thyroid Hormone-Associated Protein Complex, Gene Products, symptoms, Concepts, Project, Thyroid Hormone Associated Protein Complex, Kinase, fungal-, cell wall formation, study, Pilz, Filamentous Fungi, cellulose and pectin-containing cell wall biogenesis, Homo sapients, cell fusion, Mediator-Like Complex, hMAP126, Candida stellatoidea type I, Cytoskeletal, plant peltate hair, 2-amino-3-(4-hydroxyphenyl)propanoic acid, 3-(p-Hydroxyphenyl)alanine, Mediator Transcription Complex, Mediator Like Complexes, chemical analysis., cell wall biosynthetic process, proteins, L Threonine, Filamentous Fungus, cell envelope biosynthesis, man, cell wall synthesis, D11Bhm180e, Srb-mediator complex, cell envelope biosynthetic process, MAP126, Homo sapience, L Tyrosine, Homo sampiens, Tyr, great, Role Concepts, TRAP (Thyroid Hormone Associated Protein) Complex, L mediator complex, fungi, Candida, Tyrosin, p-nitrophenylphosphate phosphohydrolase activity, ATP Phosphotransferases, Home sapiens, phosphatase, ATP, screening, bacteria, data, findings, Molds, protein complex, para-nitrophenyl phosphatase activity, Proteins, Fungi, 2-Amino-3-(p-hydroxyphenyl)propionic acid, Fungus, Phosphorylations, TR-Associated Protein (TRAP) Complex, macromolecule complex, para-Tyrosine, Phosphotransferases, Mold, Concept, Tyrosine, polypeptide, AI874642, 1-2nm peptidoglycan-based cell wall biogenesis, Role Concept, tirosina, Homo sapian, chemical analysis, Protein, CDK8-containing TRAP/mediator complex, Role, Mastrin, concluding remarks, Ontology Projects, 4-nitrophenylphosphate phosphohydrolase activity, Homo sapeins, scales, Mediator-Like Complexes, S17, Deepest, Ontology Project, deep, Gene Ontologies, Transphosphorylases, Ontology, macromolecular complex, Ontologies, Projects, scale, Kinases, ecto-p-nitrophenyl phosphatase activity, conclusion, protein containing complex, L-isomer, expanded, Humo sapiens, signs, fungus, phosphoric monoester hydrolase activity, 4-nitrophenylphosphatase activity, Understanding, C9H11NO3, K-pNPPase activity, Homo sapines, human, TRAP complex, L isomer, Protein Gene Products, summary, Gene Proteins, Homo spiens, Candida albican, \"human\" EXACT genbank_common_name [], clear, Filamentous, enlarged, K35, albicans, L Serine, Candida stellatoidea, regulation, L-Tyrosine, assay, threonine, L-Serine, protein-protein complex"],"view_count":["28"],"citation_count":["0"],"search_count":["5"],"full_dataset_link":["http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014317"],"search_domains":["dbgap_ncbi~0","patentfamilies~0","rfam~0","merops~0","complex-portal~0","uniprot~0","wormbaseparasite~0","embl-covid19~0","reactome~0","emdb~0","wgs_masters~0","ebiweb_resources~0","opentargets_genetics~0","biomodels_all~0","ipd-mhc~0","ebiweb_teams~0","taxonomy~0","genome_assembly~0","sc-experiments~0","ebiweb_people~0","enzymeportal_enzymes~0","ipd-nhkir~0","cellosaurus~0","pdbe~0","chebi~0","patentproteins~0","interpro7~0","uniref~0","chembl~0","pdbekb~0","gpcrdb~0","hgnc~0","sc-genes~0","intact~0","rhea~0","ebiweb_training~0","alphafold~0","imgt-hla~0","patentnucleotides~0","ensemblroot~0","eva_studies~0","non-coding~0","europepmc~0","pubmed~1","identifiers_registry~0","pdbechem~0","hpa-covid19~0","eva-variants-covid19~0","biosamples~0","gwas_catalog~0","biotools~0","tls_masters~0","mesh~0","coding~0","sra~0","opentargets~0","efo~0","embl-pathogen~0","project~0","pride~1","human_diseases~0","geo_datasets~0","embl~0","treefam~0","uniparc~0","ols~0","dgva~0","intenz~0","go~0","tsa_masters~0","biosamples-covid19~0","ebiweb_corporate~0","omim~0","lrg~0","earlycause-molecular-sequences~0","ipd-kir~0","empiar~0","rnacentral~0","orcid_data_claims~0","gpmdb~2","lineage-covid19~0","metagenomics~0","pfam~0","pride archive~1","varsite~0"],"reanalysis_count":["0"],"submitter_keywords":["Resource Reanalysis"],"citation_count_scaled":["0.0"],"reanalysis_count_scaled":["0.0"],"view_count_scaled":["0.00863664404688464"],"download_count_scaled":["0.0"],"normalized_connections":["1.0"],"additional_accession":[]},"is_claimable":false,"name":"Analysis of the Candida albicans phosphoproteome.","description":"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}}","dates":{"submission":"2015-03-25"},"accession":"GPM32320014317","cross_references":{"pubmed":["25750214"],"Pride":["PXD001844"],"pride":[],"Pride Archive":["PXD001844"]}}