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http://purl.uniprot.org/citations/8246984http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8246984http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8246984http://www.w3.org/2000/01/rdf-schema#comment"Phosphatidylinositol 3-kinase (PI 3-kinase) has been implicated as a participant in signaling pathways regulating cell growth by virtue of its activation in response to various mitogenic stimuli. Here we describe the cloning of a novel and ubiquitously expressed human PI 3-kinase. The 4.8-kb cDNA encodes a putative translation product of 1,070 amino acids which is 42% identical to bovine PI 3-kinase and 28% identical to Vps34, a Saccharomyces cerevisiae PI 3-kinase involved in vacuolar protein sorting. Human PI 3-kinase is also similar to Tor2, a yeast protein required for cell cycle progression. Northern (RNA) analysis demonstrated expression of human PI 3-kinase in all tissues and cell lines tested. Protein synthesized from an epitope-tagged cDNA had intrinsic PI 3-kinase activity and associated with the adaptor 85-kDa subunit of PI 3-kinase (p85) in intact cells, as did endogenous human PI 3-kinase. Coprecipitation assays showed that a 187-amino-acid domain between the two src homology 2 domains of p85 mediates interaction with PI 3-kinase in vitro and in intact cells. These results demonstrate the existence of different PI 3-kinase isoforms and define a family of genes encoding distinct PI 3-kinase catalytic subunits that can associate with p85."xsd:string
http://purl.uniprot.org/citations/8246984http://purl.org/dc/terms/identifier"doi:10.1128/mcb.13.12.7677-7688.1993"xsd:string
http://purl.uniprot.org/citations/8246984http://purl.org/dc/terms/identifier"doi:10.1128/mcb.13.12.7677-7688.1993"xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/author"Hu P."xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/author"Hu P."xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/author"Schlessinger J."xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/author"Schlessinger J."xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/author"Skolnik E.Y."xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/author"Skolnik E.Y."xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/author"Mondino A."xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/author"Mondino A."xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/pages"7677-7688"xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/pages"7677-7688"xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/title"Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85."xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/title"Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85."xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/8246984http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/8246984http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8246984
http://purl.uniprot.org/citations/8246984http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8246984