| http://purl.uniprot.org/citations/9830063 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9830063 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9830063 | http://www.w3.org/2000/01/rdf-schema#comment | "The cDNA for a human Class II phosphoinositide 3-kinase (PI 3-kinase C2beta) with a C2 domain was cloned from a U937 monocyte cDNA library and the enzyme expressed in mammalian and insect cells. Like other Class II PI 3-kinases in vitro, PI 3-kinase C2beta utilizes phosphatidylinositol (PI) and PI 4-monophosphate but not PI 4, 5-biphosphate as substrates in the presence of Mg2+. Remarkably, and unlike other PI 3-kinases, the enzyme can use either Mg-ATP or Ca-ATP to generate PI 3-monophosphate. PI 3-kinase C2beta, like the Class I PI 3-kinases, but unlike PI 3-kinase C2alpha, is sensitive to low nanomolar levels of the inhibitor wortmannin. The enzyme is not regulated by the small GTP-binding protein Ras. The C2 domain of the enzyme bound anionic phospholipids such as PI and phosphatidylserine in vitro, but did not co-operatively bind Ca2+ and phospholipids. Deletion of the C2 domain increased the lipid kinase activity suggesting that it functions as a negative regulator of the catalytic domain. Although presently it is not known whether PI 3-kinase C2beta is regulated by Ca2+ in vivo, our results suggest a novel role for Ca2+ ions in phosphate transfer reactions."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.273.49.33082"xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.273.49.33082"xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Volinia S."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Volinia S."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Stein R.C."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Stein R.C."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Waterfield M.D."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Waterfield M.D."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Zvelebil M.J."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Zvelebil M.J."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Gout I."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Gout I."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Downward J."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Downward J."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Arcaro A."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Arcaro A."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Layton M.J."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Layton M.J."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Watton S.J."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Watton S.J."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Ahmadi K."xsd:string |
| http://purl.uniprot.org/citations/9830063 | http://purl.uniprot.org/core/author | "Ahmadi K."xsd:string |