RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/7721860http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7721860http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7721860http://www.w3.org/2000/01/rdf-schema#comment"We have isolated additional cDNA clones encoding type II inositol polyphosphate 5-phosphatase (5-phosphatase II) resulting in a combined cDNA of 3076 nucleotides encoding a protein of 942 amino acids. The 5-phosphatase II hydrolyzed both Ins(1,4,5)P3 to Ins(1,4)P2 and the phospholipid PtdIns(4,5)P2 to PtdIns(4)P both in vitro and in vivo. There are two motifs highly conserved between types I and II 5-phosphatase and several other proteins presumed to be inositol phosphatases suggesting a possible role in catalysis. The type II 5-phosphatase also contains homology to several GTPase activating proteins although no such activity for 5-phosphatase II was found. The predicted protein ends with the sequence CNPL, suggesting that it is isoprenylated as a mechanism for membrane attachment. We found evidence for isoprenylation by demonstrating incorporation of [3H]mevalonate into native but not C939S mutant 5-phosphatase II expressed in Sf9 insect cells. Furthermore, we showed that membrane localization and the activity of 5-phosphatase II toward its lipid substrate PtdIns(4,5)P2 is reduced by eliminating 5-phosphatase II isoprenylation in the mutant C939S relative to the native enzyme."xsd:string
http://purl.uniprot.org/citations/7721860http://purl.org/dc/terms/identifier"doi:10.1074/jbc.270.16.9370"xsd:string
http://purl.uniprot.org/citations/7721860http://purl.org/dc/terms/identifier"doi:10.1074/jbc.270.16.9370"xsd:string
http://purl.uniprot.org/citations/7721860http://purl.uniprot.org/core/author"Majerus P.W."xsd:string
http://purl.uniprot.org/citations/7721860http://purl.uniprot.org/core/author"Majerus P.W."xsd:string
http://purl.uniprot.org/citations/7721860http://purl.uniprot.org/core/author"Jefferson A.B."xsd:string
http://purl.uniprot.org/citations/7721860http://purl.uniprot.org/core/author"Jefferson A.B."xsd:string
http://purl.uniprot.org/citations/7721860http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7721860http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7721860http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7721860http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7721860http://purl.uniprot.org/core/pages"9370-9377"xsd:string
http://purl.uniprot.org/citations/7721860http://purl.uniprot.org/core/pages"9370-9377"xsd:string
http://purl.uniprot.org/citations/7721860http://purl.uniprot.org/core/title"Properties of type II inositol polyphosphate 5-phosphatase."xsd:string
http://purl.uniprot.org/citations/7721860http://purl.uniprot.org/core/title"Properties of type II inositol polyphosphate 5-phosphatase."xsd:string
http://purl.uniprot.org/citations/7721860http://purl.uniprot.org/core/volume"270"xsd:string
http://purl.uniprot.org/citations/7721860http://purl.uniprot.org/core/volume"270"xsd:string
http://purl.uniprot.org/citations/7721860http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7721860
http://purl.uniprot.org/citations/7721860http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7721860
http://purl.uniprot.org/citations/7721860http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7721860
http://purl.uniprot.org/citations/7721860http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7721860
http://purl.uniprot.org/uniprot/P32019http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7721860
http://purl.uniprot.org/uniprot/P32019#attribution-354CC280BEF93651391ECDF4C5187255http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/7721860