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http://purl.uniprot.org/citations/10358138http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10358138http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10358138http://www.w3.org/2000/01/rdf-schema#comment"The genetic defect in X-linked lymphoproliferative syndrome (XLP) is the Src homology 2 domain-containing protein SAP. SAP constitutively associates with the cell surface molecule, signaling lymphocytic activation molecule (SLAM), and competes with SH2-domain containing protein tyrosine phosphatase-2 (SHP-2) for recruitment to SLAM. SLAM exhibits homology with the mouse cell surface receptor 2B4. The human homologue of 2B4 has now been identified. It is recognized by the c1.7 mAb, a mAb capable of activating human NK cells. Human 2B4 became tyrosine phosphorylated following pervanadate-treatment of transfected cells and recruited SHP-2. SAP was also recruited to 2B4 in activated cells. Importantly, the 2B4-SAP interaction prevented the association between 2B4 and SHP-2. These results suggest that the phenotype of XLP may result from perturbed signaling not only through SLAM, but also other cell surface molecules that utilize SAP as a signaling adaptor protein."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/author"Sutherland G.R."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/author"Sutherland G.R."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/author"Woollatt E."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/author"Woollatt E."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/author"Lanier L.L."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/author"Lanier L.L."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/author"Tangye S.G."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/author"Tangye S.G."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/author"Lazetic S."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/author"Lazetic S."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/author"Phillips J.H."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/author"Phillips J.H."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/name"J. Immunol."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/name"J. Immunol."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/pages"6981-6985"xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/pages"6981-6985"xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/title"Human 2B4, an activating NK cell receptor, recruits the protein tyrosine phosphatase SHP-2 and the adaptor signaling protein SAP."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/title"Human 2B4, an activating NK cell receptor, recruits the protein tyrosine phosphatase SHP-2 and the adaptor signaling protein SAP."xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/volume"162"xsd:string
http://purl.uniprot.org/citations/10358138http://purl.uniprot.org/core/volume"162"xsd:string