| http://purl.uniprot.org/citations/10336483 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10336483 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10336483 | http://www.w3.org/2000/01/rdf-schema#comment | "Mammalian Ca2+/CaM-dependent protein kinase kinase (CaM-KK) has been identified and cloned as an activator for two kinases, CaM kinase I (CaM-KI) and CaM kinase IV (CaM-KIV), and a recent report (Yano, S., Tokumitsu, H., and Soderling, T. R. (1998) Nature 396, 584-587) demonstrates that CaM-KK can also activate and phosphorylate protein kinase B (PKB). In this study, we identify a CaM-KK from Caenorhabditis elegans, and comparison of its sequence with the mammalian CaM-KK alpha and beta shows a unique Arg-Pro (RP)-rich insert in their catalytic domains relative to other protein kinases. Deletion of the RP-domain resulted in complete loss of CaM-KIV activation activity and physical interaction of CaM-KK with glutathione S-transferase-CaM-KIV (T196A). However, CaM-KK autophosphorylation and phosphorylation of a synthetic peptide substrate were normal in the RP-domain mutant. Site-directed mutagenesis of three conserved Arg in the RP-domain of CaM-KK confirmed that these positive charges are important for CaM-KIV activation. The RP-domain deletion mutant also failed to fully activate and phosphorylate CaM-KI, but this mutant was indistinguishable from wild-type CaM-KK for the phosphorylation and activation of PKB. These results indicate that the RP-domain in CaM-KK is critical for recognition of downstream CaM-kinases but not for its catalytic activity (i.e. autophosphorylation) and PKB activation."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.22.15803"xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.22.15803"xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/author | "Takahashi N."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/author | "Takahashi N."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/author | "Yano S."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/author | "Yano S."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/author | "Muramatsu M.-A."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/author | "Muramatsu M.-A."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/author | "Eto K."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/author | "Eto K."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/author | "Tokumitsu H."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/author | "Tokumitsu H."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/author | "Soderling T.R."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/author | "Soderling T.R."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/pages | "15803-15810"xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/pages | "15803-15810"xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/title | "Substrate recognition by Ca2+/Calmodulin-dependent protein kinase kinase. Role of the arg-pro-rich insert domain."xsd:string |
| http://purl.uniprot.org/citations/10336483 | http://purl.uniprot.org/core/title | "Substrate recognition by Ca2+/Calmodulin-dependent protein kinase kinase. Role of the arg-pro-rich insert domain."xsd:string |