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http://purl.uniprot.org/citations/9049300http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9049300http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9049300http://www.w3.org/2000/01/rdf-schema#comment"Shc proteins are targets of activated tyrosine kinases and are implicated in the transmission of activation signals to Ras. The p46shc and p52shc isoforms share a C-terminal SH2 domain, a proline- and glycine-rich region (collagen homologous region 1; CH1) and a N-terminal PTB domain. We have isolated cDNAs encoding for a third Shc isoform, p66shc. The predicted amino acid sequence of p66shc overlaps that of p52shc and contains a unique N-terminal region which is also rich in glycines and prolines (CH2). p52shc/p46shc is found in every cell type with invariant reciprocal relationship, whereas p66shc expression varies from cell type to cell type. p66shc differs from p52shc/p46shc in its inability to transform mouse fibroblasts in vitro. Like p52shc/p46shc, p66shc is tyrosine-phosphorylated upon epidermal growth factor (EGF) stimulation, binds to activated EGF receptors (EGFRs) and forms stable complexes with Grb2. However, unlike p52shc/p46shc it does not increase EGF activation of MAP kinases, but inhibits fos promoter activation. The isolated CH2 domain retains the inhibitory effect of p66shc on the fos promoter. p52shc/p46shc and p66shc, therefore, appear to exert different effects on the EGFR-MAP kinase and other signalling pathways that control fos promoter activity. Regulation of p66shc expression might, therefore, influence the cellular response to growth factors."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.org/dc/terms/identifier"doi:10.1093/emboj/16.4.706"xsd:string
http://purl.uniprot.org/citations/9049300http://purl.org/dc/terms/identifier"doi:10.1093/emboj/16.4.706"xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Pawson T."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Pawson T."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Superti-Furga G."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Superti-Furga G."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Pelicci G."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Pelicci G."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Di Fiore P.P."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Di Fiore P.P."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Salcini A.E."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Salcini A.E."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Migliaccio E."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Migliaccio E."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Lanfrancone L."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Lanfrancone L."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Mele S."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Mele S."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Pelicci P.-G."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Pelicci P.-G."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Lai K.M."xsd:string
http://purl.uniprot.org/citations/9049300http://purl.uniprot.org/core/author"Lai K.M."xsd:string