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http://purl.uniprot.org/citations/20956537http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20956537http://www.w3.org/2000/01/rdf-schema#comment"The Syk protein-tyrosine kinase is phosphorylated on multiple tyrosines after the aggregation of the B cell antigen receptor. However, metabolic labeling experiments indicate that Syk is inducibly phosphorylated to an even greater extent on serine after receptor ligation. A combination of phosphopeptide mapping and mass spectrometric analyses indicates that serine 291 is a major site of phosphorylation. Serine 291 lies within a 23-amino acid insert located within the linker B region that distinguishes Syk from SykB and Zap-70. The phosphorylation of serine-291 by protein kinase C enhances the ability of Syk to couple the antigen receptor to the activation of the transcription factors NFAT and Elk-1. Protein interaction studies indicate a role for the phosphorylated linker insert in promoting an interaction between Syk and the chaperone protein, prohibitin."xsd:string
http://purl.uniprot.org/citations/20956537http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.164509"xsd:string
http://purl.uniprot.org/citations/20956537http://purl.uniprot.org/core/author"Hu J."xsd:string
http://purl.uniprot.org/citations/20956537http://purl.uniprot.org/core/author"Ma H."xsd:string
http://purl.uniprot.org/citations/20956537http://purl.uniprot.org/core/author"Tao W.A."xsd:string
http://purl.uniprot.org/citations/20956537http://purl.uniprot.org/core/author"Harrison M.L."xsd:string
http://purl.uniprot.org/citations/20956537http://purl.uniprot.org/core/author"Galan J."xsd:string
http://purl.uniprot.org/citations/20956537http://purl.uniprot.org/core/author"Geahlen R.L."xsd:string
http://purl.uniprot.org/citations/20956537http://purl.uniprot.org/core/author"Ong S.S."xsd:string
http://purl.uniprot.org/citations/20956537http://purl.uniprot.org/core/author"Paris L.L."xsd:string
http://purl.uniprot.org/citations/20956537http://purl.uniprot.org/core/author"Martin V.A."xsd:string
http://purl.uniprot.org/citations/20956537http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20956537http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/20956537http://purl.uniprot.org/core/pages"39844-39854"xsd:string
http://purl.uniprot.org/citations/20956537http://purl.uniprot.org/core/title"Regulation of Syk by phosphorylation on serine in the linker insert."xsd:string
http://purl.uniprot.org/citations/20956537http://purl.uniprot.org/core/volume"285"xsd:string
http://purl.uniprot.org/citations/20956537http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20956537
http://purl.uniprot.org/citations/20956537http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20956537
http://purl.uniprot.org/uniprot/#_A8K4G2-mappedCitation-20956537http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20956537
http://purl.uniprot.org/uniprot/#_B3KQJ1-mappedCitation-20956537http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20956537
http://purl.uniprot.org/uniprot/#_C3W980-mappedCitation-20956537http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20956537
http://purl.uniprot.org/uniprot/#_C3W981-mappedCitation-20956537http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20956537
http://purl.uniprot.org/uniprot/#_Q13196-mappedCitation-20956537http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20956537
http://purl.uniprot.org/uniprot/#_P43405-mappedCitation-20956537http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20956537