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DESCRIBE <http://purl.uniprot.org/SHA-384/00E9734137AFC038D4F417210F6946347E70363F6F3353C68FF1A72FA4B3899FA9982E74AC652AFF21466E26F0659438>
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http://purl.uniprot.org/SHA-384/00E9734137AFC038D4F417210F6946347E70363F6F3353C68FF1A72FA4B3899FA9982E74AC652AFF21466E26F0659438
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/00E9734137AFC038D4F417210F6946347E70363F6F3353C68FF1A72FA4B3899FA9982E74AC652AFF21466E26F0659438
http://www.w3.org/2000/01/rdf-schema#comment
"Importantly receptor sialylation and N-glycosylation participate with disulfide bonding in the stabilization of the cell surface human B2 receptor dimers."
xsd:string
http://purl.uniprot.org/uniprot/#_0061ED7DC1301C0A5C69C47262FB7FAA6A73552620189B2A6B799A9EE5C6A9A046C71192BB64EAFB60C705CB02ED9E05
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/00E9734137AFC038D4F417210F6946347E70363F6F3353C68FF1A72FA4B3899FA9982E74AC652AFF21466E26F0659438
http://purl.uniprot.org/uniprot/P30411
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/00E9734137AFC038D4F417210F6946347E70363F6F3353C68FF1A72FA4B3899FA9982E74AC652AFF21466E26F0659438
http://purl.uniprot.org/uniprot/#_P30411-mappedCitation-16489763
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/00E9734137AFC038D4F417210F6946347E70363F6F3353C68FF1A72FA4B3899FA9982E74AC652AFF21466E26F0659438