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http://purl.uniprot.org/citations/15824120http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15824120http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15824120http://www.w3.org/2000/01/rdf-schema#comment"SUMO (small ubiquitin-like modifier) is a member of the ubiquitin family of proteins. SUMO targets include proteins involved in numerous roles including nuclear transport and transcriptional regulation. The previous finding that mutant ataxin-1[82Q] disrupted promyelocytic leukemia (PML) oncogenic domains prompted us to determine whether ataxin-1 disrupts another component of PML oncogenic domains, Sp100 (100-kDa Speckled protein). Similar to the PML protein, mutant ataxin-1[82Q] redistributed Sp100 to mutant ataxin-1[82Q] nuclear inclusions. Based on the ability of PML and Sp100 to be covalently modified by SUMO, we investigated the ability of ataxin-1 to be SUMOylated. SUMO-1 was found to covalently modify the polyglutamine repeat protein ataxin-1. There was a decrease in ataxin-1 SUMOylation in the presence of the expanded polyglutamine tract, ataxin-1[82Q]. The phospho-mutant, ataxin-1[82Q]-S776A, restored SUMO levels to those of wild-type ataxin-1[30Q]. SUMOylation of ataxin-1 was dependent on a functional nuclear localization signal. Ataxin-1 SUMOylation was mapped to at least five lysine residues. Lys(16), Lys(194) preceding the polyglutamine tract, Lys(610)/Lys(697) in the C-terminal ataxin high mobility group domain, and Lys(746) all contribute to ataxin-1 SUMOylation."xsd:string
http://purl.uniprot.org/citations/15824120http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m501677200"xsd:string
http://purl.uniprot.org/citations/15824120http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m501677200"xsd:string
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/author"Orr H.T."xsd:string
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/author"Orr H.T."xsd:string
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/author"Zoghbi H.Y."xsd:string
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/author"Zoghbi H.Y."xsd:string
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/author"Riley B.E."xsd:string
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/author"Riley B.E."xsd:string
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/pages"21942-21948"xsd:string
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/pages"21942-21948"xsd:string
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/title"SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal."xsd:string
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/title"SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal."xsd:string
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/volume"280"xsd:string
http://purl.uniprot.org/citations/15824120http://purl.uniprot.org/core/volume"280"xsd:string
http://purl.uniprot.org/citations/15824120http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15824120
http://purl.uniprot.org/citations/15824120http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15824120
http://purl.uniprot.org/citations/15824120http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15824120
http://purl.uniprot.org/citations/15824120http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15824120