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DESCRIBE <http://purl.uniprot.org/SHA-384/BB7C096E152DB1D2A706EEA97F2469E6BCD886FAC2868F60936795CDBC8733E3CBF27916528FDBDA103AC35B2F959E78>
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http://purl.uniprot.org/SHA-384/BB7C096E152DB1D2A706EEA97F2469E6BCD886FAC2868F60936795CDBC8733E3CBF27916528FDBDA103AC35B2F959E78
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/BB7C096E152DB1D2A706EEA97F2469E6BCD886FAC2868F60936795CDBC8733E3CBF27916528FDBDA103AC35B2F959E78
http://www.w3.org/2000/01/rdf-schema#comment
"These findings suggest that basic residues of the C2 domain mediate membrane targeting of Tollip by interaction with phosphoinositides which contribute to the observed partition of the protein in different subcellular compartments."
xsd:string
http://purl.uniprot.org/uniprot/#_4662FC9B4C136B88095DCD607950F7B70B3892172B1319049E48BD222938228F551FDE47788140341DF5AFCCC307B9EF
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/BB7C096E152DB1D2A706EEA97F2469E6BCD886FAC2868F60936795CDBC8733E3CBF27916528FDBDA103AC35B2F959E78
http://purl.uniprot.org/uniprot/F2Z2Y8
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/BB7C096E152DB1D2A706EEA97F2469E6BCD886FAC2868F60936795CDBC8733E3CBF27916528FDBDA103AC35B2F959E78
http://purl.uniprot.org/uniprot/#_F2Z2Y8-mappedCitation-21294713
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/BB7C096E152DB1D2A706EEA97F2469E6BCD886FAC2868F60936795CDBC8733E3CBF27916528FDBDA103AC35B2F959E78