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http://purl.uniprot.org/citations/16872604http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16872604http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16872604http://www.w3.org/2000/01/rdf-schema#comment"ISG15, an interferon-upregulated ubiquitin-like protein, is covalently conjugated to various cellular proteins (ISGylation). In this study, we found that protein phosphatase 2Cbeta (PP2Cbeta), which functions in the nuclear factor kappaB (NF-kappaB) pathway via dephosphorylation of TGF-beta-activated kinase, was ISGylated, and analysis by NF-kappaB luciferase reporter assay revealed that PP2Cbeta activity was suppressed by co-expression of ISG15, UBE1L, and UbcH8. We determined the ISGylation sites of PP2Cbeta and constructed its ISGylation-resistant mutant. In contrast to the wild type, this mutant suppressed the NF-kappaB pathway even in the presence of ISG15, UBE1L, and UbcH8. Thus, we propose that ISGylation negatively regulates PP2Cbeta activity."xsd:string
http://purl.uniprot.org/citations/16872604http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2006.07.032"xsd:string
http://purl.uniprot.org/citations/16872604http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2006.07.032"xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/author"Kobayashi T."xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/author"Kobayashi T."xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/author"Takeuchi T."xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/author"Takeuchi T."xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/author"Tamura S."xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/author"Tamura S."xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/author"Yokosawa H."xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/author"Yokosawa H."xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/pages"4521-4526"xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/pages"4521-4526"xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/title"Negative regulation of protein phosphatase 2Cbeta by ISG15 conjugation."xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/title"Negative regulation of protein phosphatase 2Cbeta by ISG15 conjugation."xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/volume"580"xsd:string
http://purl.uniprot.org/citations/16872604http://purl.uniprot.org/core/volume"580"xsd:string
http://purl.uniprot.org/citations/16872604http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16872604
http://purl.uniprot.org/citations/16872604http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16872604