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DESCRIBE <http://purl.uniprot.org/SHA-384/65A9567AB685179A688E7027412EEF2CF60B0472F7E54F33BA5FBC593B883E6E771F53D01BD15A11B5ABD04F351CF02F>
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http://purl.uniprot.org/SHA-384/65A9567AB685179A688E7027412EEF2CF60B0472F7E54F33BA5FBC593B883E6E771F53D01BD15A11B5ABD04F351CF02F
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/65A9567AB685179A688E7027412EEF2CF60B0472F7E54F33BA5FBC593B883E6E771F53D01BD15A11B5ABD04F351CF02F
http://www.w3.org/2000/01/rdf-schema#comment
"the phosphorylation status of hnRNP A1 serine 199 regulates the AKT-dependent sensitivity of cells to rapamycin and functionally links IRES-transacting factor annealing activity to cellular responses to mTOR complex 1 inhibition."
xsd:string
http://purl.uniprot.org/uniprot/#_C9C5B054723C2E57D062D7A5C3DF0A5613F4E6F60E4421D9A6117C5FFD4E8D6480BE60F8A749385D83E507DEE5F792F6
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/65A9567AB685179A688E7027412EEF2CF60B0472F7E54F33BA5FBC593B883E6E771F53D01BD15A11B5ABD04F351CF02F
http://purl.uniprot.org/uniprot/Q0VAC0
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/65A9567AB685179A688E7027412EEF2CF60B0472F7E54F33BA5FBC593B883E6E771F53D01BD15A11B5ABD04F351CF02F
http://purl.uniprot.org/uniprot/#_Q0VAC0-mappedCitation-21454539
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/65A9567AB685179A688E7027412EEF2CF60B0472F7E54F33BA5FBC593B883E6E771F53D01BD15A11B5ABD04F351CF02F