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http://purl.uniprot.org/citations/18257517http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18257517http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18257517http://www.w3.org/2000/01/rdf-schema#comment"Phosphorylation is a key regulator of many events in eukaryotic cells. The acquisition of large-scale phosphorylation data sets from model organisms can pinpoint conserved regulatory inputs and reveal kinase-substrate relationships. Here, we provide the first large-scale phosphorylation analysis of the fission yeast, Schizosaccharomyces pombe. Protein from thiabendazole-treated cells was separated by preparative SDS-PAGE and digested with trypsin. The resulting peptides were subjected to either IMAC or TiO2 phosphopeptide enrichment methods and then analyzed by LC-MS/MS using an LTQ-Orbitrap mass spectrometer. In total, 2887 distinct phosphorylation sites were identified from 1194 proteins with an estimated false-discovery rate of <0.5% at the peptide level. A comparison of the two different enrichment methods is presented, supporting the finding that they are complementary. Finally, phosphorylation sites were examined for phosphorylation-specific motifs and evolutionary conservation. These analyses revealed both motifs and specific phosphorylation events identified in S. pombe were conserved and predicted novel phosphorylation in mammals."xsd:string
http://purl.uniprot.org/citations/18257517http://purl.org/dc/terms/identifier"doi:10.1021/pr7006335"xsd:string
http://purl.uniprot.org/citations/18257517http://purl.org/dc/terms/identifier"doi:10.1021/pr7006335"xsd:string
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/author"Gygi S.P."xsd:string
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/author"Gygi S.P."xsd:string
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/author"Villen J."xsd:string
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/author"Villen J."xsd:string
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/author"Wilson-Grady J.T."xsd:string
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/author"Wilson-Grady J.T."xsd:string
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/name"J. Proteome Res."xsd:string
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/name"J. Proteome Res."xsd:string
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/pages"1088-1097"xsd:string
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/pages"1088-1097"xsd:string
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/title"Phosphoproteome analysis of fission yeast."xsd:string
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/title"Phosphoproteome analysis of fission yeast."xsd:string
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/18257517http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/18257517http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18257517
http://purl.uniprot.org/citations/18257517http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18257517
http://purl.uniprot.org/citations/18257517http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18257517
http://purl.uniprot.org/citations/18257517http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18257517