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DESCRIBE <http://purl.uniprot.org/SHA-384/94460DF48390CC495FF3EF3D0E871AAD8D0E5DB9EDFE1E62FDECBF69407E3C0E611650E0F19F3D3F76A4336BF03140BB>
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http://purl.uniprot.org/SHA-384/94460DF48390CC495FF3EF3D0E871AAD8D0E5DB9EDFE1E62FDECBF69407E3C0E611650E0F19F3D3F76A4336BF03140BB
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/94460DF48390CC495FF3EF3D0E871AAD8D0E5DB9EDFE1E62FDECBF69407E3C0E611650E0F19F3D3F76A4336BF03140BB
http://www.w3.org/2000/01/rdf-schema#comment
"The results suggest that phosphorylation of serine-504 by PKCdelta modulates the biological function of tNOX."
xsd:string
http://purl.uniprot.org/uniprot/#_EB651A8F29CDB562A9B2B9496DE90409F9EBC8693F918514D4C3368951CA8D46039CAF59BA863F487C497B9619E0FEF4
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/94460DF48390CC495FF3EF3D0E871AAD8D0E5DB9EDFE1E62FDECBF69407E3C0E611650E0F19F3D3F76A4336BF03140BB
http://purl.uniprot.org/uniprot/Q32ND0
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/94460DF48390CC495FF3EF3D0E871AAD8D0E5DB9EDFE1E62FDECBF69407E3C0E611650E0F19F3D3F76A4336BF03140BB
http://purl.uniprot.org/uniprot/#_Q32ND0-mappedCitation-22659163
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/94460DF48390CC495FF3EF3D0E871AAD8D0E5DB9EDFE1E62FDECBF69407E3C0E611650E0F19F3D3F76A4336BF03140BB