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http://purl.uniprot.org/citations/14528312http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14528312http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14528312http://www.w3.org/2000/01/rdf-schema#comment"The concentrations and functions of many cellular proteins are regulated by the ubiquitin pathway. Cullin family proteins bind with the RING-finger protein Roc1 to recruit the ubiquitin-conjugating enzyme (E2) to the ubiquitin ligase complex (E3). Cul1 and Cul7, but not other cullins, bind to an adaptor protein, Skp1. Cul1 associates with one of many F-box proteins through Skp1 to assemble various SCF-Roc1 E3 ligases that each selectively ubiquitinate one or more specific substrates. Here, we show that Cul3, but not other cullins, binds directly to multiple BTB domains through a conserved amino-terminal domain. In vitro, Cul3 promoted ubiquitination of Caenorhabditis elegans MEI-1, a katanin-like protein whose degradation requires the function of both Cul3 and BTB protein MEL-26. We suggest that in vivo there exists a potentially large number of BCR3 (BTB-Cul3-Roc1) E3 ubiquitin ligases."xsd:string
http://purl.uniprot.org/citations/14528312http://purl.org/dc/terms/identifier"doi:10.1038/ncb1056"xsd:string
http://purl.uniprot.org/citations/14528312http://purl.org/dc/terms/identifier"doi:10.1038/ncb1056"xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/author"Xiong Y."xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/author"Xiong Y."xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/author"He Y.J."xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/author"He Y.J."xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/author"Furukawa M."xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/author"Furukawa M."xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/author"Borchers C."xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/author"Borchers C."xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/name"Nat. Cell Biol."xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/name"Nat. Cell Biol."xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/pages"1001-1007"xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/pages"1001-1007"xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/title"Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases."xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/title"Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases."xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/14528312http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/14528312http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14528312
http://purl.uniprot.org/citations/14528312http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14528312