| http://purl.uniprot.org/citations/1730692 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1730692 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1730692 | http://www.w3.org/2000/01/rdf-schema#comment | "The primary structure of bovine rhodopsin kinase (RK), which phosphorylates light-activated rhodopsin (Rho*), terminates with the amino acid sequence Cys558-Val-Leu-Ser561, a motif that has been shown to direct the isoprenylation and alpha-carboxyl methylation of many proteins (e.g. p21Ha-ras). Transient expression of RK in COS-7 cells revealed the presence of two immunoreactive protein species. Consistent with RK being modified by isoprenylation, interconversion of these two species was dependent upon isoprenoid biosynthesis in the cells. Moreover, a serine substitution for Cys558 resulted in a single RK species whose migration on sodium dodecyl sulfate-polyacrylamide gels was identical to that of RK from cells treated with mevinolin, an inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme A reductase and, thus, of isoprenoid biosynthesis. This finding indicates that isoprenylation of RK requires Cys558. The electrophoretic mobility of isoprenylated RK synthesized in COS-7 cells was identical to that of RK from bovine rod outer segments, suggesting that RK is isoprenylated in vivo. RK was determined to be modified by a farnesyl moiety and alpha-carboxyl-methylated. A time course of Rho* phosphorylation revealed that non-processed RK is approximately 4-fold less active than wild-type RK. This is the first demonstration of isoprenylation/alpha-carboxyl methylation of a protein kinase, and suggests that these modifications markedly influence enzymatic activity in vivo."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)45960-1"xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)45960-1"xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/author | "Caron M.G."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/author | "Caron M.G."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/author | "Lefkowitz R.J."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/author | "Lefkowitz R.J."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/author | "Lorenz W."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/author | "Lorenz W."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/author | "Glickman J.F."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/author | "Glickman J.F."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/author | "Inglese J."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/author | "Inglese J."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/pages | "1422-1425"xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/pages | "1422-1425"xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/title | "Isoprenylation of a protein kinase. Requirement of farnesylation/alpha-carboxyl methylation for full enzymatic activity of rhodopsin kinase."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/title | "Isoprenylation of a protein kinase. Requirement of farnesylation/alpha-carboxyl methylation for full enzymatic activity of rhodopsin kinase."xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/volume | "267"xsd:string |
| http://purl.uniprot.org/citations/1730692 | http://purl.uniprot.org/core/volume | "267"xsd:string |