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http://purl.uniprot.org/citations/10400669http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10400669http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10400669http://www.w3.org/2000/01/rdf-schema#comment"The interferon-induced double-stranded RNA-activated protein kinase PKR is the prototype of a class of double-stranded (dsRNA)-binding proteins (DRBPs) which share a dsRNA-binding motif conserved from Drosophila to humans. Here we report the purification of DRBP76, a new human member of this class of proteins. Sequence from the amino terminus of DRBP76 matched that of the M phase-specific protein, MPP4. DRBP76 was also cloned by the yeast two-hybrid screening of a cDNA library using a mutant PKR as bait. Analysis of the cDNA sequence revealed that it is the full-length version of MPP4, has a bipartite nuclear localization signal, two motifs that can mediate interactions with both dsRNA and PKR, five epitopes for potential M phase-specific phosphorylation, two potential sites for phosphorylation by cyclin-dependent kinases, a RG2 motif present in many RNA-binding proteins and predicts a protein of 76 kDa. DsRNA and PKR interactions of DRBP76 were confirmed by analysis of in vitro translated and purified native proteins. Cellular expression of an epitope-tagged DRBP76 demonstrated its nuclear localization, and its co-immunoprecipitation with PKR demonstrated that the two proteins interact in vivo. Finally, purified DRBP76 was shown to be a substrate of PKR in vitro, indicating that this protein's cellular activities may be regulated by PKR-mediated phosphorylation."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.29.20432"xsd:string
http://purl.uniprot.org/citations/10400669http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.29.20432"xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Guo W."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Guo W."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Xu Z."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Xu Z."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Sen G.C."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Sen G.C."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Bandyopadhyay S."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Bandyopadhyay S."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Vestal D.J."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Vestal D.J."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Williams B.R."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Williams B.R."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Patel R.C."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Patel R.C."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Erme S.M."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/author"Erme S.M."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10400669http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string