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DESCRIBE <http://purl.uniprot.org/SHA-384/C6E3DF69BD7D3FB2F0C5751822E2477D67B7141B125D60705A5C70DCB4AE24EFD4F5437DB5CDA79603082A4FE3DFC546>
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http://purl.uniprot.org/SHA-384/C6E3DF69BD7D3FB2F0C5751822E2477D67B7141B125D60705A5C70DCB4AE24EFD4F5437DB5CDA79603082A4FE3DFC546
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/C6E3DF69BD7D3FB2F0C5751822E2477D67B7141B125D60705A5C70DCB4AE24EFD4F5437DB5CDA79603082A4FE3DFC546
http://www.w3.org/2000/01/rdf-schema#comment
"The crystal structure of a histone deacetylase 9 (HDAC9)/myocyte enhancer factor-2 (MEF2)/DNA complex reveals that HDAC9 binds to a hydrophobic groove of the MEF2 dimer."
xsd:string
http://purl.uniprot.org/uniprot/#_98941DA0F120BDE818CCEFBA1E7FE18FF3DA4D6E575446586DE34F4A409C9B6F71931E7B533FB328FBD48250D07A5D00
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/C6E3DF69BD7D3FB2F0C5751822E2477D67B7141B125D60705A5C70DCB4AE24EFD4F5437DB5CDA79603082A4FE3DFC546
http://purl.uniprot.org/uniprot/B3KQ23
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/C6E3DF69BD7D3FB2F0C5751822E2477D67B7141B125D60705A5C70DCB4AE24EFD4F5437DB5CDA79603082A4FE3DFC546
http://purl.uniprot.org/uniprot/#_B3KQ23-mappedCitation-15567413
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/C6E3DF69BD7D3FB2F0C5751822E2477D67B7141B125D60705A5C70DCB4AE24EFD4F5437DB5CDA79603082A4FE3DFC546