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DESCRIBE <http://purl.uniprot.org/SHA-384/314FE2FEDA4D7FD67350ACCDE714DD3E587BB36E4D1E1E7914AAC822CD8C2FC942244077369DA1E46FCBD5A3DDABBE79>
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http://purl.uniprot.org/SHA-384/314FE2FEDA4D7FD67350ACCDE714DD3E587BB36E4D1E1E7914AAC822CD8C2FC942244077369DA1E46FCBD5A3DDABBE79
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/314FE2FEDA4D7FD67350ACCDE714DD3E587BB36E4D1E1E7914AAC822CD8C2FC942244077369DA1E46FCBD5A3DDABBE79
http://www.w3.org/2000/01/rdf-schema#comment
"Hsc70 interacted with Rab1A in a chaperone-dependent mannerand Hsc70 knockdown decreased the level of Rab1A and increased the level of its ubiquitination under stress conditions."
xsd:string
http://purl.uniprot.org/uniprot/#_154289D08C9FD3EAD3D0E1E2B8131D1926C2229D2C8AED9419B781A8365DB7255B5EEB50726D9E38C62032247E05DE2E
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/314FE2FEDA4D7FD67350ACCDE714DD3E587BB36E4D1E1E7914AAC822CD8C2FC942244077369DA1E46FCBD5A3DDABBE79
http://purl.uniprot.org/uniprot/Q53HF2
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/314FE2FEDA4D7FD67350ACCDE714DD3E587BB36E4D1E1E7914AAC822CD8C2FC942244077369DA1E46FCBD5A3DDABBE79
http://purl.uniprot.org/uniprot/#_Q53HF2-mappedCitation-24801886
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/314FE2FEDA4D7FD67350ACCDE714DD3E587BB36E4D1E1E7914AAC822CD8C2FC942244077369DA1E46FCBD5A3DDABBE79