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http://purl.uniprot.org/citations/11980906http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11980906http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11980906http://www.w3.org/2000/01/rdf-schema#comment"We report the cDNA cloning and functional characterization of human cyclin L, a novel cyclin related to the C-type cyclins that are involved in regulation of RNA polymerase II (pol II) transcription. Cyclin L also contains a COOH-terminal dipeptide repeat of alternating arginines and serines, a hallmark of the SR family of splicing factors. We show that recombinant cyclin L interacts with p110 PITSLRE kinase, and that cyclin L antibody co-immunoprecipitates a kinase activity from HeLa nuclear extracts that phosphorylates the carboxyl-terminal domain (CTD) of pol II and splicing factor SC35, and is inhibited by the cdk inhibitor p21. Cyclin L antibody inhibits the second step of RNA splicing in vitro, and recombinant cyclin L protein stimulates splicing under suboptimal conditions. Significantly, the IC(50) for splicing inhibition by p21 is similar to the IC(50) for inhibition of the cyclin L-associated kinase activity. Cyclin L and its associated kinase are thus new members of the pre-mRNA processing machinery."xsd:string
http://purl.uniprot.org/citations/11980906http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m202266200"xsd:string
http://purl.uniprot.org/citations/11980906http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m202266200"xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/author"Edgar A.J."xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/author"Edgar A.J."xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/author"Dickinson L.A."xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/author"Dickinson L.A."xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/author"Ehley J."xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/author"Ehley J."xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/author"Gottesfeld J.M."xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/author"Gottesfeld J.M."xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/pages"25465-25473"xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/pages"25465-25473"xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/title"Cyclin L is an RS domain protein involved in pre-mRNA splicing."xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/title"Cyclin L is an RS domain protein involved in pre-mRNA splicing."xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11980906http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11980906http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11980906
http://purl.uniprot.org/citations/11980906http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11980906