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http://purl.uniprot.org/citations/10814712http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10814712http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10814712http://www.w3.org/2000/01/rdf-schema#comment"Spinocerebellar ataxia type 2 (SCA2) is caused by expansion of a polyglutamine tract in ataxin-2, a protein of unknown function. Using the yeast two-hybrid system, we identified a novel protein, A2BP1 (ataxin-2 binding protein 1) which binds to the C-terminus of ataxin-2. Northern blot analysis showed that A2BP1 was predominantly expressed in muscle and brain. By immunocfluorescent staining, A2BP1 and ataxin-2 were both localized to the trans -Golgi network. Immunocytochemistry showed that A2BP1 was expressed in the cytoplasm of Purkinje cells and dentate neurons in a pattern similar to that seen for ataxin-2 labeling. Western blot analysis of subcellular fractions indicated enrichment of A2BP1 in the same fractions as ataxin-2. Sequence analysis of the A2BP1 cDNA revealed an RNP motif that is highly conserved among RNA-binding proteins. A2BP1 had striking homology with a human cDNA clone, P83A20, of unknown function and at least two copies of A2BP1 homologs are found in the Caenorhabditis elegans genome database. A2BP1 and related proteins appear to form a novel gene family sharing RNA-binding motifs."xsd:string
http://purl.uniprot.org/citations/10814712http://purl.org/dc/terms/identifier"doi:10.1093/hmg/9.9.1303"xsd:string
http://purl.uniprot.org/citations/10814712http://purl.org/dc/terms/identifier"doi:10.1093/hmg/9.9.1303"xsd:string
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/author"Shibata H."xsd:string
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/author"Shibata H."xsd:string
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/author"Huynh D.P."xsd:string
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/author"Huynh D.P."xsd:string
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/author"Pulst S.-M."xsd:string
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/author"Pulst S.-M."xsd:string
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/name"Hum. Mol. Genet."xsd:string
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/name"Hum. Mol. Genet."xsd:string
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/pages"1303-1313"xsd:string
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/pages"1303-1313"xsd:string
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/title"A novel protein with RNA-binding motifs interacts with ataxin-2."xsd:string
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/title"A novel protein with RNA-binding motifs interacts with ataxin-2."xsd:string
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/10814712http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/10814712http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10814712
http://purl.uniprot.org/citations/10814712http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10814712
http://purl.uniprot.org/citations/10814712http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10814712
http://purl.uniprot.org/citations/10814712http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10814712