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DESCRIBE <http://purl.uniprot.org/SHA-384/54B21F9A0F74E15B4D6375802B87D3D59466A6BF9555F725A3B7A4BA5584D6F1EFF9ACEFA872EA87202A1A7BC7EEF5FF>
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http://purl.uniprot.org/SHA-384/54B21F9A0F74E15B4D6375802B87D3D59466A6BF9555F725A3B7A4BA5584D6F1EFF9ACEFA872EA87202A1A7BC7EEF5FF
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/54B21F9A0F74E15B4D6375802B87D3D59466A6BF9555F725A3B7A4BA5584D6F1EFF9ACEFA872EA87202A1A7BC7EEF5FF
http://www.w3.org/2000/01/rdf-schema#comment
"Mutation or inhibition of Hsp90 resulted in decreased accumulation of Ura2 indicating it is an Hsp90 client. Cpr6 interacted with Ura2 in the absence of stable Cpr6-Hsp90 interaction suggesting a direct interaction."
xsd:string
http://purl.uniprot.org/uniprot/#_B90D44B5D270DE4435AF01E4BEEE670F22EC2B51A9F0E5F90FD72379B9ABCCB1D4C4675DB11936DAA80576F0D8BF8E41
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/54B21F9A0F74E15B4D6375802B87D3D59466A6BF9555F725A3B7A4BA5584D6F1EFF9ACEFA872EA87202A1A7BC7EEF5FF
http://purl.uniprot.org/uniprot/P53691
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/54B21F9A0F74E15B4D6375802B87D3D59466A6BF9555F725A3B7A4BA5584D6F1EFF9ACEFA872EA87202A1A7BC7EEF5FF
http://purl.uniprot.org/uniprot/#_P53691-mappedCitation-23926110
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/54B21F9A0F74E15B4D6375802B87D3D59466A6BF9555F725A3B7A4BA5584D6F1EFF9ACEFA872EA87202A1A7BC7EEF5FF