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DESCRIBE <http://purl.uniprot.org/SHA-384/7A300017856A0616996DB92C7C16EE81DA3B1896637F2594577A76FFCB3DD1188DD8404DE90367B1145177BE524119FB>
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http://purl.uniprot.org/SHA-384/7A300017856A0616996DB92C7C16EE81DA3B1896637F2594577A76FFCB3DD1188DD8404DE90367B1145177BE524119FB
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/7A300017856A0616996DB92C7C16EE81DA3B1896637F2594577A76FFCB3DD1188DD8404DE90367B1145177BE524119FB
http://www.w3.org/2000/01/rdf-schema#comment
"Data suggest that CNT3 forms a homotrimer in solution and membrane-bound inside cells; the quaternary structure creates an aqueous basin that significantly shortens the substrate translocation distance."
xsd:string
http://purl.uniprot.org/uniprot/#_09193D8330FEE0AD1EBF84B8924116C9F6ECA536D4AA3F6ACB8D87FD912CB93E4F6BEB3CFB38F34C0A4235660EB70EC8
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/7A300017856A0616996DB92C7C16EE81DA3B1896637F2594577A76FFCB3DD1188DD8404DE90367B1145177BE524119FB
http://purl.uniprot.org/uniprot/Q9HAS3
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/7A300017856A0616996DB92C7C16EE81DA3B1896637F2594577A76FFCB3DD1188DD8404DE90367B1145177BE524119FB
http://purl.uniprot.org/uniprot/#_Q9HAS3-mappedCitation-28661652
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/7A300017856A0616996DB92C7C16EE81DA3B1896637F2594577A76FFCB3DD1188DD8404DE90367B1145177BE524119FB