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http://purl.uniprot.org/citations/1656454http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1656454http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1656454http://www.w3.org/2000/01/rdf-schema#comment"Light-dependent deactivation of rhodopsin as well as homologous desensitization of beta-adrenergic receptors involves receptor phosphorylation that is mediated by the highly specific protein kinases rhodopsin kinase (RK) and beta-adrenergic receptor kinase (beta ARK), respectively. We report here the cloning of a complementary DNA for RK. The deduced amino acid sequence shows a high degree of homology to beta ARK. In a phylogenetic tree constructed by comparing the catalytic domains of several protein kinases, RK and beta ARK are located on a branch close to, but separate from the cyclic nucleotide-dependent protein kinase and protein kinase C subfamilies. From the common structural features we conclude that both RK and beta ARK are members of a newly delineated gene family of guanine nucleotide-binding protein (G protein)-coupled receptor kinases that may function in diverse pathways to regulate the function of such receptors."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.org/dc/terms/identifier"doi:10.1073/pnas.88.19.8715"xsd:string
http://purl.uniprot.org/citations/1656454http://purl.org/dc/terms/identifier"doi:10.1073/pnas.88.19.8715"xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/author"Caron M.G."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/author"Caron M.G."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/author"Lefkowitz R.J."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/author"Lefkowitz R.J."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/author"Palczewski K."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/author"Palczewski K."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/author"Onorato J.J."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/author"Onorato J.J."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/author"Lorenz W."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/author"Lorenz W."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/author"Inglese J."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/author"Inglese J."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/pages"8715-8719"xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/pages"8715-8719"xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/title"The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase."xsd:string
http://purl.uniprot.org/citations/1656454http://purl.uniprot.org/core/title"The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase."xsd:string