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http://purl.uniprot.org/citations/8769125http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8769125http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8769125http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/8769125http://www.w3.org/2000/01/rdf-schema#comment"Distinct inositol and phosphatidylinositol polyphosphate 5-phosphatases have recently been cloned. Primers were designated coding for highly conserved amino acid regions that are shared between sequences of 5-phosphatases. We used degenerate primers to amplify polymerase chain reaction products from rat brain cDNA. A product with a novel sequence was identified and used to clone a 4.9 kb cDNA from human placenta cDNA libraries (hp51CN). COS-7 cells transfected with a C-terminal truncated form of this cDNA showed an increase in Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3 hydrolyzing activity, but not in Ins(1,4,5)P3 5-phosphatase. Enzymatic activity was inhibited in the presence of 2,3-bisphosphoglycerate and p-hydroxymercuribenzoate. The presence of an SH2 domain and proline-rich sequence motifs within hp51CN suggests that this 5-phosphatase interacts with various proteins in signal transduction."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1996.1161"xsd:string
http://purl.uniprot.org/citations/8769125http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1996.1161"xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/author"Drayer A.L."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/author"Drayer A.L."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/author"Erneux C."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/author"Erneux C."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/author"Woscholski R."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/author"Woscholski R."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/author"Parker P."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/author"Parker P."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/author"De Smedt F."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/author"De Smedt F."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/author"Pesesse X."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/author"Pesesse X."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/pages"243-249"xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/pages"243-249"xsd:string
http://purl.uniprot.org/citations/8769125http://purl.uniprot.org/core/title"Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase."xsd:string