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DESCRIBE <http://purl.uniprot.org/SHA-384/5B6D921624DCC8C6DEE0D39120AE9E21668AB833BB490B8A0AE51B74250FA6DF81893F5908A4D9E902CDBE426325BD68>
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http://purl.uniprot.org/SHA-384/5B6D921624DCC8C6DEE0D39120AE9E21668AB833BB490B8A0AE51B74250FA6DF81893F5908A4D9E902CDBE426325BD68
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/5B6D921624DCC8C6DEE0D39120AE9E21668AB833BB490B8A0AE51B74250FA6DF81893F5908A4D9E902CDBE426325BD68
http://www.w3.org/2000/01/rdf-schema#comment
"the acidic domain of GPIHBP1 is important and electrostatic interactions play a key role in ligand binding"
xsd:string
http://purl.uniprot.org/uniprot/#_08E014C4F211BF92C7C4E82E7EEB80203DAF33B04D5CBE925DB2E45CDA38D90EC7A00DE3DB13700910EF07457D6645F7
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/5B6D921624DCC8C6DEE0D39120AE9E21668AB833BB490B8A0AE51B74250FA6DF81893F5908A4D9E902CDBE426325BD68
http://purl.uniprot.org/uniprot/Q8IV16
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/5B6D921624DCC8C6DEE0D39120AE9E21668AB833BB490B8A0AE51B74250FA6DF81893F5908A4D9E902CDBE426325BD68
http://purl.uniprot.org/uniprot/#_Q8IV16-mappedCitation-18713736
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/5B6D921624DCC8C6DEE0D39120AE9E21668AB833BB490B8A0AE51B74250FA6DF81893F5908A4D9E902CDBE426325BD68