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http://purl.uniprot.org/citations/18356159http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18356159http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18356159http://www.w3.org/2000/01/rdf-schema#comment"ISG15 (interferon-stimulated gene 15) is a novel ubiquitin-like (UbL) modifier with two UbL domains in its architecture. We investigated different roles for the two UbL domains in protein modification by ISG15 (ISGylation) and the impact of Influenza B virus NS1 protein (NS1B) on regulation of the pathway. The results show that, although the C-terminal domain is sufficient to link ISG15 to UBE1L and UbcH8, the N-terminal domain is dispensable in the activation and transthiolation steps but required for efficient E3-mediated transfer of ISG15 from UbcH8 to its substrates. NS1B specifically binds to the N-terminal domain of ISG15 but does not affect ISG15 linkage via a thioester bond to its activating and conjugating enzymes. However, it does inhibit the formation of cellular ISG15 conjugates upon interferon treatment. We propose that the N-terminal UbL domain of ISG15 mainly functions in the ligation step and NS1B inhibits ISGylation by competing with E3 ligases for binding to the N-terminal domain."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m800162200"xsd:string
http://purl.uniprot.org/citations/18356159http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m800162200"xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/author"Zhang D.E."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/author"Zhang D.E."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/author"Chang Y.G."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/author"Chang Y.G."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/author"Hu H.Y."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/author"Hu H.Y."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/author"Gao X.C."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/author"Gao X.C."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/author"Song A.X."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/author"Song A.X."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/author"Xie Y.Y."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/author"Xie Y.Y."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/author"Yan X.Z."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/author"Yan X.Z."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/pages"13370-13377"xsd:string
http://purl.uniprot.org/citations/18356159http://purl.uniprot.org/core/pages"13370-13377"xsd:string