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http://purl.uniprot.org/citations/8663140http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8663140http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8663140http://www.w3.org/2000/01/rdf-schema#comment"Phosphatidylinositol (PI) 3-kinases catalyze the formation of 3'-phosphoinositides, which appear to promote cellular responses to growth factors and such membrane trafficking events as insulin-stimulated translocation of intracellular glucose transporters. We report here the cloning of a novel PI 3-kinase, p170, from cDNA of insulin-sensitive mouse 3T3-L1 adipocytes. Mouse p170 utilizes PI and to a limited extent PI 4-P as substrates, in contrast to the PI-specific yeast VPS34 homolog PtdIns 3-kinase and the p110 PI 3-kinases, which phosphorylate PI, PI 4-P, and PI 4,5-P2. Mouse p170 is also distinct from PtdIns 3-kinase or the p110 PI 3-kinases in exhibiting a 10-fold lower sensitivity to wortmannin. Unique structural elements of p170 include C-terminal sequences strikingly similar to the phosphoinositide-binding C2 domain of protein kinase C isoforms, synaptotagmins, and other proteins. These features of mouse p170 are shared with a recently cloned Drosophila PI 3-kinase, DmPI3K_68D. Together, these proteins define a new class of PI 3-kinase likely influenced by cellular regulators distinct from those acting upon p110- or VPS34-like PI 3-kinases."xsd:string
http://purl.uniprot.org/citations/8663140http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.23.13304"xsd:string
http://purl.uniprot.org/citations/8663140http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.23.13304"xsd:string
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/author"Czech M.P."xsd:string
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/author"Czech M.P."xsd:string
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/author"Guilherme A."xsd:string
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/author"Guilherme A."xsd:string
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/author"Virbasius J.V."xsd:string
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/author"Virbasius J.V."xsd:string
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/pages"13304-13307"xsd:string
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/pages"13304-13307"xsd:string
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/title"Mouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain."xsd:string
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/title"Mouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain."xsd:string
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8663140http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8663140http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8663140
http://purl.uniprot.org/citations/8663140http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8663140
http://purl.uniprot.org/citations/8663140http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8663140
http://purl.uniprot.org/citations/8663140http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8663140