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http://purl.uniprot.org/citations/17287358http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17287358http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17287358http://www.w3.org/2000/01/rdf-schema#comment"We present a strategy for the analysis of the yeast phosphoproteome that uses endo-Lys C as the proteolytic enzyme, immobilized metal affinity chromatography for phosphopeptide enrichment, a 90-min nanoflow-HPLC/electrospray-ionization MS/MS experiment for phosphopeptide fractionation and detection, gas phase ion/ion chemistry, electron transfer dissociation for peptide fragmentation, and the Open Mass Spectrometry Search Algorithm for phosphoprotein identification and assignment of phosphorylation sites. From a 30-microg (approximately 600 pmol) sample of total yeast protein, we identify 1,252 phosphorylation sites on 629 proteins. Identified phosphoproteins have expression levels that range from <50 to 1,200,000 copies per cell and are encoded by genes involved in a wide variety of cellular processes. We identify a consensus site that likely represents a motif for one or more uncharacterized kinases and show that yeast kinases, themselves, contain a disproportionately large number of phosphorylation sites. Detection of a pHis containing peptide from the yeast protein, Cdc10, suggests an unexpected role for histidine phosphorylation in septin biology. From diverse functional genomics data, we show that phosphoproteins have a higher number of interactions than an average protein and interact with each other more than with a random protein. They are also likely to be conserved across large evolutionary distances."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0607084104"xsd:string
http://purl.uniprot.org/citations/17287358http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0607084104"xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Chi A."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Chi A."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Hunt D.F."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Hunt D.F."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Shabanowitz J."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Shabanowitz J."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Coon J.J."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Coon J.J."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Bai D.L."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Bai D.L."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Burke D.J."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Burke D.J."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Geer L.Y."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Geer L.Y."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Huttenhower C."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Huttenhower C."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Syka J.E.P."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Syka J.E.P."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Troyanskaya O.G."xsd:string
http://purl.uniprot.org/citations/17287358http://purl.uniprot.org/core/author"Troyanskaya O.G."xsd:string