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DESCRIBE <http://purl.uniprot.org/SHA-384/B1DA2A8FFB0C3E7832467A9D5BA58C55B6B803DBE42138BDE7D7676B2A1832DE0861FC0DA27482FA23F96F0791A9D62C>
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http://purl.uniprot.org/SHA-384/B1DA2A8FFB0C3E7832467A9D5BA58C55B6B803DBE42138BDE7D7676B2A1832DE0861FC0DA27482FA23F96F0791A9D62C
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/B1DA2A8FFB0C3E7832467A9D5BA58C55B6B803DBE42138BDE7D7676B2A1832DE0861FC0DA27482FA23F96F0791A9D62C
http://www.w3.org/2000/01/rdf-schema#comment
"Data show that the C-terminal alpha-helix of human apoC-I contains major lipid-binding determinants which play a role in stabilizing the structure of apoC-I mediating phospholipid interactions and promoting discoidal particle morphology."
xsd:string
http://purl.uniprot.org/uniprot/#_D12FA233E01B83E3F8D343DAA4231684E3E5295BADDC7B3A1ED18254D9662277BC855E24CA475737A5F1644760368C86
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/B1DA2A8FFB0C3E7832467A9D5BA58C55B6B803DBE42138BDE7D7676B2A1832DE0861FC0DA27482FA23F96F0791A9D62C
http://purl.uniprot.org/uniprot/P02654
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/B1DA2A8FFB0C3E7832467A9D5BA58C55B6B803DBE42138BDE7D7676B2A1832DE0861FC0DA27482FA23F96F0791A9D62C
http://purl.uniprot.org/uniprot/#_P02654-mappedCitation-18984910
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/B1DA2A8FFB0C3E7832467A9D5BA58C55B6B803DBE42138BDE7D7676B2A1832DE0861FC0DA27482FA23F96F0791A9D62C