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http://purl.uniprot.org/citations/12615067http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12615067http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12615067http://www.w3.org/2000/01/rdf-schema#comment"Btn2p is a novel coiled coil cytosolic protein in Saccharomyces cerevisiae. We report that Btn2p interacts with Yif1p, a component of a protein complex at the Golgi that functions in ER to Golgi transport. Deletion of Btn2p, btn2-delta, results in mis-localiztion of Yif1p to the vacuole. Therefore, Btn2p may have an apparent role in intracellular trafficking of proteins. Btn2p was originally identified as being up-regulated in a btn1-delta strain, which exhibits dysregulation of vacuolar pH, and this up-regulation of Btn2p was presumed to contribute to maintaining a stable vacuolar pH [Pearce et al. Nat. Genet. 22 (1999) 55]. We propose that up-regulation of Btn2p in btn1-delta is an indicator of altered trafficking within the cell, and as btn1-delta serves as a model for the lysosomal storage disorder Batten disease, that altered intracellular trafficking may contribute to some of the cellular pathological hallmarks of this disease."xsd:string
http://purl.uniprot.org/citations/12615067http://purl.org/dc/terms/identifier"doi:10.1016/s0006-291x(03)00209-2"xsd:string
http://purl.uniprot.org/citations/12615067http://purl.org/dc/terms/identifier"doi:10.1016/s0006-291x(03)00209-2"xsd:string
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/author"Pearce D.A."xsd:string
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/author"Pearce D.A."xsd:string
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/author"Chattopadhyay S."xsd:string
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/author"Chattopadhyay S."xsd:string
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/author"Roberts P.M."xsd:string
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/author"Roberts P.M."xsd:string
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/pages"534-538"xsd:string
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/pages"534-538"xsd:string
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/title"The yeast model for Batten disease: a role for Btn2p in the trafficking of the Golgi-associated vesicular targeting protein, Yif1p."xsd:string
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/title"The yeast model for Batten disease: a role for Btn2p in the trafficking of the Golgi-associated vesicular targeting protein, Yif1p."xsd:string
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/volume"302"xsd:string
http://purl.uniprot.org/citations/12615067http://purl.uniprot.org/core/volume"302"xsd:string
http://purl.uniprot.org/citations/12615067http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12615067
http://purl.uniprot.org/citations/12615067http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12615067
http://purl.uniprot.org/citations/12615067http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12615067
http://purl.uniprot.org/citations/12615067http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12615067