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DESCRIBE <http://purl.uniprot.org/SHA-384/0264610CA2E8FB3EF89422421BED7957218299B7B54465F4792567E6E1832CED92B11871F02E279BD2A4B8A99D076DDF>
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http://purl.uniprot.org/SHA-384/0264610CA2E8FB3EF89422421BED7957218299B7B54465F4792567E6E1832CED92B11871F02E279BD2A4B8A99D076DDF
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/0264610CA2E8FB3EF89422421BED7957218299B7B54465F4792567E6E1832CED92B11871F02E279BD2A4B8A99D076DDF
http://www.w3.org/2000/01/rdf-schema#comment
"downregulation of HSC70 resulted in increased levels of DeltaF508-CFTR complexes with the co-chaperone BAG3 that in addition appeared to co-localize with the mutated protein on the cell surface."
xsd:string
http://purl.uniprot.org/uniprot/#_77AE5AFD999328D42A57FD63A6E5704BE541B45D804FDCE182882005A88AE4A2F2D3FB50E2CC955D239715EDF64BEE05
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/0264610CA2E8FB3EF89422421BED7957218299B7B54465F4792567E6E1832CED92B11871F02E279BD2A4B8A99D076DDF
http://purl.uniprot.org/uniprot/Q53HF2
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/0264610CA2E8FB3EF89422421BED7957218299B7B54465F4792567E6E1832CED92B11871F02E279BD2A4B8A99D076DDF
http://purl.uniprot.org/uniprot/#_Q53HF2-mappedCitation-22170045
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/0264610CA2E8FB3EF89422421BED7957218299B7B54465F4792567E6E1832CED92B11871F02E279BD2A4B8A99D076DDF