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http://purl.uniprot.org/citations/8943344http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8943344http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8943344http://www.w3.org/2000/01/rdf-schema#comment"Protein tyrosine phosphatases (PTPases), such as SHP-1 and SHP-2, that contain Src homology 2 (SH2) domains play important roles in growth factor and cytokine signal transduction pathways. A protein of approximately 115 to 120 kDa that interacts with SHP-1 and SHP-2 was purified from v-src-transformed rat fibroblasts (SR-3Y1 cells), and the corresponding cDNA was cloned. The predicted amino acid sequence of the encoded protein, termed SHPS-1 (SHP substrate 1), suggests that it is a glycosylated receptor-like protein with three immunoglobulin-like domains in its extracellular region and four YXX(L/V/I) motifs, potential tyrosine phosphorylation and SH2-domain binding sites, in its cytoplasmic region. Various mitogens, including serum, insulin, and lysophosphatidic acid, or cell adhesion induced tyrosine phosphorylation of SHPS-1 and its subsequent association with SHP-2 in cultured cells. Thus, SHPS-1 may be a direct substrate for both tyrosine kinases, such as the insulin receptor kinase or Src, and a specific docking protein for SH2-domain-containing PTPases. In addition, we suggest that SHPS-1 may be a potential substrate for SHP-2 and may function in both growth factor- and cell adhesion-induced cell signaling."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.org/dc/terms/identifier"doi:10.1128/mcb.16.12.6887"xsd:string
http://purl.uniprot.org/citations/8943344http://purl.org/dc/terms/identifier"doi:10.1128/mcb.16.12.6887"xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Kasuga M."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Kasuga M."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Iwamatsu A."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Iwamatsu A."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Tsuda M."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Tsuda M."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Takahashi N."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Takahashi N."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Fujioka Y."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Fujioka Y."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Takada T."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Takada T."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Noguchi T."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Noguchi T."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Matozaki T."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Matozaki T."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Yamao T."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/author"Yamao T."xsd:string
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8943344http://purl.uniprot.org/core/date"1996"xsd:gYear