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DESCRIBE <http://purl.uniprot.org/SHA-384/4C6B6A6DD017A976587D9D7A239D02483943E1E8683876A91AE7951641745AB0B12ADE2284E2B25F5EB5C2C62A6C5FCD>
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http://purl.uniprot.org/SHA-384/4C6B6A6DD017A976587D9D7A239D02483943E1E8683876A91AE7951641745AB0B12ADE2284E2B25F5EB5C2C62A6C5FCD
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/4C6B6A6DD017A976587D9D7A239D02483943E1E8683876A91AE7951641745AB0B12ADE2284E2B25F5EB5C2C62A6C5FCD
http://www.w3.org/2000/01/rdf-schema#comment
"RanBP2 associates in vitro and in vivo and colocalizes with the mitochondrial metallochaperone Cox11 and the pacemaker of glycolysis hexokinase type I (HKI) via its leucine-rich domain."
xsd:string
http://purl.uniprot.org/uniprot/#_127AB22664EBA25E28A813608F242C9C1B73CB9B0F392661494B3949486BFC62B62FAD4A47CB97ACD7CF4C44CF19F3CB
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/4C6B6A6DD017A976587D9D7A239D02483943E1E8683876A91AE7951641745AB0B12ADE2284E2B25F5EB5C2C62A6C5FCD
http://purl.uniprot.org/uniprot/B4YB29
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/4C6B6A6DD017A976587D9D7A239D02483943E1E8683876A91AE7951641745AB0B12ADE2284E2B25F5EB5C2C62A6C5FCD
http://purl.uniprot.org/uniprot/#_B4YB29-mappedCitation-17069463
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/4C6B6A6DD017A976587D9D7A239D02483943E1E8683876A91AE7951641745AB0B12ADE2284E2B25F5EB5C2C62A6C5FCD