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DESCRIBE <http://purl.uniprot.org/SHA-384/4060CDB598DEB7B1D68B6A4CFF6E993117EED9A23AF1CE3CE01F2C58BC241A16BB8CD6D316F56D11939742538CB4FEB1>
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http://purl.uniprot.org/SHA-384/4060CDB598DEB7B1D68B6A4CFF6E993117EED9A23AF1CE3CE01F2C58BC241A16BB8CD6D316F56D11939742538CB4FEB1
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/4060CDB598DEB7B1D68B6A4CFF6E993117EED9A23AF1CE3CE01F2C58BC241A16BB8CD6D316F56D11939742538CB4FEB1
http://www.w3.org/2000/01/rdf-schema#comment
"E6AP and Enolase1 interacted and colocalized more in the cytoplasmic periphery in breast cancer cells and further demonstrated that E6AP also targeted ENO1 for ubiquitin-mediated degradation in these cells."
xsd:string
http://purl.uniprot.org/uniprot/#_823FD6F934ACF5F9419B72956785CB56E39E1F70D01BA172A11EC068A998EC338A7374078B43387B4578B199037D40EE
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/4060CDB598DEB7B1D68B6A4CFF6E993117EED9A23AF1CE3CE01F2C58BC241A16BB8CD6D316F56D11939742538CB4FEB1
http://purl.uniprot.org/uniprot/E2DRY6
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/4060CDB598DEB7B1D68B6A4CFF6E993117EED9A23AF1CE3CE01F2C58BC241A16BB8CD6D316F56D11939742538CB4FEB1
http://purl.uniprot.org/uniprot/#_E2DRY6-mappedCitation-31329371
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/4060CDB598DEB7B1D68B6A4CFF6E993117EED9A23AF1CE3CE01F2C58BC241A16BB8CD6D316F56D11939742538CB4FEB1