| http://purl.uniprot.org/citations/8662856 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8662856 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8662856 | http://www.w3.org/2000/01/rdf-schema#comment | "We report the identification of a novel class of phosphatidylinositol (PtdIns) 3-kinases whose members contain C-terminal C2 domains. We have isolated Drosophila and murine genes (termed cpk and cpk-m respectively) by polymerase chain reaction amplification of cDNA libraries with degenerate primers corresponding to conserved regions of PtdIns kinases. The amino acid sequences of Cpk and Cpk-m are most similar to that of p110, a family of PtdIns 3-kinases that mediates the responses of cells to mitogenic stimuli. The Cpk and Cpk-m sequences are similar to a large, central region of p110, but differ from p110 at their N and C termini. The N termini of the Cpk proteins do not contain any recognizable protein motif, while the C termini contain "C2 domains," a feature unique among PtdIns kinases. Cpk has an intrinsic PtdIns kinase activity and can phosphorylate PtdIns and PtdIns-4-P, but not PtdIns(4,5)P2, at the D3 position of the inositol ring. Cpk is the first PtdIns 3-kinase identified with this particular substrate specificity. We have identified two potential Cpk-binding proteins, p90 and p190, and have determined that both Cpk and p190 may be tyrosine phosphorylated. This finding suggests that Cpk function may be regulated by tyrosine kinases."xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.271.23.13892"xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.271.23.13892"xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/author | "Hirano M."xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/author | "Hirano M."xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/author | "Williams L.T."xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/author | "Williams L.T."xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/author | "Molz L."xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/author | "Molz L."xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/author | "Chen Y.-W."xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/author | "Chen Y.-W."xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/date | "1996"xsd:gYear |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/date | "1996"xsd:gYear |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/pages | "13892-13899"xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/pages | "13892-13899"xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/title | "Cpk is a novel class of Drosophila PtdIns 3-kinase containing a C2 domain."xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/title | "Cpk is a novel class of Drosophila PtdIns 3-kinase containing a C2 domain."xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/volume | "271"xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://purl.uniprot.org/core/volume | "271"xsd:string |
| http://purl.uniprot.org/citations/8662856 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8662856 |
| http://purl.uniprot.org/citations/8662856 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8662856 |