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DESCRIBE <http://purl.uniprot.org/SHA-384/A9527BC4DB91637DC2D514B8A095B6F22F5A38DC15C2F4DD7F17EA141A6EBB6F988F4A8BD23236BAC1D0946E5E0D1675>
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http://purl.uniprot.org/SHA-384/A9527BC4DB91637DC2D514B8A095B6F22F5A38DC15C2F4DD7F17EA141A6EBB6F988F4A8BD23236BAC1D0946E5E0D1675
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/A9527BC4DB91637DC2D514B8A095B6F22F5A38DC15C2F4DD7F17EA141A6EBB6F988F4A8BD23236BAC1D0946E5E0D1675
http://www.w3.org/2000/01/rdf-schema#comment
"the physiological relevance of the interaction of both Ira2 and Hsp60 with Bcy1. Bcy1 interacts with Ira2 tethering PKA to the Ras complex and Hsp60 chaperone localizes PKA to mitochondria and has a role in the kinase stability."
xsd:string
http://purl.uniprot.org/uniprot/#_86923C03D603262653996245FBA2457017B03D0737313E9A94869151FC73D28A0719265CB7E8E0CC96D97ACA89DB519B
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/A9527BC4DB91637DC2D514B8A095B6F22F5A38DC15C2F4DD7F17EA141A6EBB6F988F4A8BD23236BAC1D0946E5E0D1675
http://purl.uniprot.org/uniprot/P19158
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/A9527BC4DB91637DC2D514B8A095B6F22F5A38DC15C2F4DD7F17EA141A6EBB6F988F4A8BD23236BAC1D0946E5E0D1675
http://purl.uniprot.org/uniprot/#_P19158-mappedCitation-25065647
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/A9527BC4DB91637DC2D514B8A095B6F22F5A38DC15C2F4DD7F17EA141A6EBB6F988F4A8BD23236BAC1D0946E5E0D1675