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DESCRIBE <http://purl.uniprot.org/SHA-384/2C4A8E6400BE3E22FBE0F4C0F5F0BF8DE41FC11395D8DE5A86618886E5F59AE982360A5FA85C2633BDD95E5D1736A349>
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http://purl.uniprot.org/SHA-384/2C4A8E6400BE3E22FBE0F4C0F5F0BF8DE41FC11395D8DE5A86618886E5F59AE982360A5FA85C2633BDD95E5D1736A349
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/2C4A8E6400BE3E22FBE0F4C0F5F0BF8DE41FC11395D8DE5A86618886E5F59AE982360A5FA85C2633BDD95E5D1736A349
http://www.w3.org/2000/01/rdf-schema#comment
"IP6 synthase Ins(1 3 4 5 6)P5 2-kinase (IPPK/IP5K) binds to cullins. Depleting IP5K increases the percentage of neddylated active Cul1 and Cul4A and decreases levels of the Cul1/4A substrates p27 and p21."
xsd:string
http://purl.uniprot.org/uniprot/#_95B20193F97D8819C6BD973138785FDE0791020D6B42B817818EC1C4A584EA130CC2DF25507B8F4F66F5E0C32F47616C
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/2C4A8E6400BE3E22FBE0F4C0F5F0BF8DE41FC11395D8DE5A86618886E5F59AE982360A5FA85C2633BDD95E5D1736A349
http://purl.uniprot.org/uniprot/Q9H8X2
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/2C4A8E6400BE3E22FBE0F4C0F5F0BF8DE41FC11395D8DE5A86618886E5F59AE982360A5FA85C2633BDD95E5D1736A349
http://purl.uniprot.org/uniprot/#_Q9H8X2-mappedCitation-26976604
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/2C4A8E6400BE3E22FBE0F4C0F5F0BF8DE41FC11395D8DE5A86618886E5F59AE982360A5FA85C2633BDD95E5D1736A349