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http://purl.uniprot.org/citations/7515063http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7515063http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7515063http://www.w3.org/2000/01/rdf-schema#comment"The protein tyrosine kinase expressed by the protooncogene c-fgr is phosphorylated and down-regulated in vitro by the c-Src kinase (CSK). CSK catalyzed phosphorylation affects Tyr-511 of c-Fgr, homologous to Tyr-527 of c-Src and it prevents the autophosphorylation normally occurring at c-Fgr Tyr-400, homologous to c-Src Tyr-416. Polylysine, histones H1 and H2A and other polycationic proteins on the other hand stimulate c-Fgr activity while promoting enhanced autophosphorylation of both Tyr-400 and Tyr-511. Once phosphorylated at Tyr-511 and down-regulated by CSK, c-Fgr is no more susceptible to polylysine stimulation. Previous autophosphorylation (at Tyr-400) reduces c-Fgr susceptibility to down-regulation by CSK, although Tyr-511 can be still phosphorylated by it. If a more exhaustive autophosphorylation (of both Tyr-400 and Tyr-511) is performed in the presence of polylysine, c-Fgr becomes totally insensitive to CSK down-regulation. These data support the concept that down-regulation of c-Fgr by Tyr-511 phosphorylation is prevented if Tyr-400 is also phosphorylated and they are consistent with an outcompetition of phospho-Tyr-511 from the Src homology 2 domain by phospho-Tyr-400, which, in c-Fgr, is surrounded by an amino acid sequence divergent from that of the other Src-related protein tyrosine kinases."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)40763-0"xsd:string
http://purl.uniprot.org/citations/7515063http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)40763-0"xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/author"James P."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/author"James P."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/author"Pinna L.A."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/author"Pinna L.A."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/author"Donella-Deana A."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/author"Donella-Deana A."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/author"Ruzzene M."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/author"Ruzzene M."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/author"Brunati A.M."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/author"Brunati A.M."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/pages"15885-15891"xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/pages"15885-15891"xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/title"Regulation of c-Fgr protein kinase by c-Src kinase (CSK) and by polycationic effectors."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/title"Regulation of c-Fgr protein kinase by c-Src kinase (CSK) and by polycationic effectors."xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/volume"269"xsd:string
http://purl.uniprot.org/citations/7515063http://purl.uniprot.org/core/volume"269"xsd:string