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http://purl.uniprot.org/citations/12037680http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12037680http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12037680http://www.w3.org/2000/01/rdf-schema#comment"Protein kinase CK2 is a ubiquitous and pleiotropic Ser/Thr protein kinase involved in cell growth and transformation. Here we report the identification by yeast interaction trap of a CK2 interacting protein, UBC3B, which is highly homologous to the E2 ubiquitin conjugating enzyme UBC3/CDC34. UBC3B complements the yeast cdc34-2 cell cycle arrest mutant in S. cerevisiae and transfers ubiquitin to a target substrate in vitro. UBC3B is specifically phosphorylated by CK2 in vitro and in vivo. We mapped by deletions and site directed mutagenesis the phosphorylation site to a serine residue within the C-terminal domain in position 233 of UBC3B and in the corresponding serine residue of UBC3. Following CK2-dependent phosphorylation both UBC3B and UBC3 bind to the F-box protein beta-TrCP, the substrate recognition subunit of an SCF (Skp1, Cul1, F-box) ubiquitin ligase. Furthermore, we observed that co-transfection of CK2alpha' together with UBC3B, but not with UBC3DeltaC, enhances the degradation of beta-catenin. Taken together these data suggest that CK2-dependent phosphorylation of UBC3 and UBC3B functions by regulating beta-TrCP substrate recognition."xsd:string
http://purl.uniprot.org/citations/12037680http://purl.org/dc/terms/identifier"doi:10.1038/sj.onc.1205574"xsd:string
http://purl.uniprot.org/citations/12037680http://purl.org/dc/terms/identifier"doi:10.1038/sj.onc.1205574"xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/author"Pinna L.A."xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/author"Pinna L.A."xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/author"Semplici F."xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/author"Semplici F."xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/author"Meggio F."xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/author"Meggio F."xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/author"Oliviero S."xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/author"Oliviero S."xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/name"Oncogene"xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/name"Oncogene"xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/pages"3978-3987"xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/pages"3978-3987"xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/title"CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with beta-TrCP and enhances beta-catenin degradation."xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/title"CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with beta-TrCP and enhances beta-catenin degradation."xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/12037680http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/12037680http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12037680
http://purl.uniprot.org/citations/12037680http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12037680