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http://purl.uniprot.org/citations/11448987http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11448987http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11448987http://www.w3.org/2000/01/rdf-schema#comment"The formation of the active spliceosome, its recruitment to active areas of transcription, and its role in pre-mRNA splicing depends on the association of a number of multifunctional serine/arginine-rich (SR) proteins. ZNF265 is an arginine/serine-rich (RS) domain containing zinc finger protein with conserved pre-mRNA splicing protein motifs. Here we show that ZNF265 immunoprecipitates from splicing extracts in association with mRNA, and that it is able to alter splicing patterns of Tra2-beta1 transcripts in a dose-dependent manner in HEK 293 cells. Yeast two-hybrid analysis and immunoprecipitation indicated interaction of ZNF265 with the essential splicing factor proteins U1-70K and U2AF(35). Confocal microscopy demonstrated colocalization of ZNF265 with the motor neuron gene product SMN, the snRNP protein U1-70K, the SR protein SC35, and with the transcriptosomal components p300 and YY1. Transfection of HT-1080 cells with ZNF265-EGFP fusion constructs showed that nuclear localization of ZNF265 required the RS domain. Alignment with other RS domain-containing proteins revealed a high degree of SR dipeptide conservation. These data show that ZNF265 functions as a novel component of the mRNA processing machinery."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200010059"xsd:string
http://purl.uniprot.org/citations/11448987http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200010059"xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/author"Adams D.J."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/author"Adams D.J."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/author"Rasko J.E.J."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/author"Rasko J.E.J."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/author"van der Weyden L."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/author"van der Weyden L."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/author"Morris B.J."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/author"Morris B.J."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/author"Stamm S."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/author"Stamm S."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/author"Mayeda A."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/author"Mayeda A."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/pages"25-32"xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/pages"25-32"xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/title"ZNF265 -- a novel spliceosomal protein able to induce alternative splicing."xsd:string
http://purl.uniprot.org/citations/11448987http://purl.uniprot.org/core/title"ZNF265 -- a novel spliceosomal protein able to induce alternative splicing."xsd:string