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http://purl.uniprot.org/citations/7961848http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7961848http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7961848http://www.w3.org/2000/01/rdf-schema#comment"Phosphatidylinositol (PtdIns) 4-kinase catalyzes the first committed step in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. Here we report the first mammalian cDNA clone of a PtdIns 4-kinase (named PI4K alpha). The 2.6-kb cDNA encodes a protein of 854 amino acids that is highly homologous to the recently cloned yeast PtdIns 4-kinase STT4 and is also homologous to a second yeast PtdIns 4-kinase, PIK1. PI4K alpha has more distant sequence homology to the catalytic domains of mammalian and yeast PtdIns 3-kinases and to the yeast Tor family of proteins. It also has a region of similarity to pleckstrin homology domains and a potential ankyrin repeat. Cross-hybridizing messages were detected in all human tissues investigated. The enzymatic properties of the protein expressed in insect cells are characteristic of type II PtdIns 4-kinases (activated by detergent and inhibited by adenosine), and PI4K alpha is recognized by an antibody specific for type II PtdIns 4-kinases."xsd:string
http://purl.uniprot.org/citations/7961848http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)61989-7"xsd:string
http://purl.uniprot.org/citations/7961848http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)61989-7"xsd:string
http://purl.uniprot.org/citations/7961848http://purl.uniprot.org/core/author"Cantley L.C."xsd:string
http://purl.uniprot.org/citations/7961848http://purl.uniprot.org/core/author"Cantley L.C."xsd:string
http://purl.uniprot.org/citations/7961848http://purl.uniprot.org/core/author"Wong K."xsd:string
http://purl.uniprot.org/citations/7961848http://purl.uniprot.org/core/author"Wong K."xsd:string
http://purl.uniprot.org/citations/7961848http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7961848http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7961848http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7961848http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7961848http://purl.uniprot.org/core/pages"28878-28884"xsd:string
http://purl.uniprot.org/citations/7961848http://purl.uniprot.org/core/pages"28878-28884"xsd:string
http://purl.uniprot.org/citations/7961848http://purl.uniprot.org/core/title"Cloning and characterization of a human phosphatidylinositol 4-kinase."xsd:string
http://purl.uniprot.org/citations/7961848http://purl.uniprot.org/core/title"Cloning and characterization of a human phosphatidylinositol 4-kinase."xsd:string
http://purl.uniprot.org/citations/7961848http://purl.uniprot.org/core/volume"269"xsd:string
http://purl.uniprot.org/citations/7961848http://purl.uniprot.org/core/volume"269"xsd:string
http://purl.uniprot.org/citations/7961848http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7961848
http://purl.uniprot.org/citations/7961848http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7961848
http://purl.uniprot.org/citations/7961848http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7961848
http://purl.uniprot.org/citations/7961848http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7961848
http://purl.uniprot.org/uniprot/P42356http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7961848
http://purl.uniprot.org/uniprot/P42356#attribution-214AFB630444E7D066942549CCC93554http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/7961848