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DESCRIBE <http://purl.uniprot.org/SHA-384/B2F6CE845078CF529BCB4E334AC753A70A43855B307741E570667FF7C23D7F47DB08122C3C6E5A12C1EF171453D2D95F>
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http://purl.uniprot.org/SHA-384/B2F6CE845078CF529BCB4E334AC753A70A43855B307741E570667FF7C23D7F47DB08122C3C6E5A12C1EF171453D2D95F
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/B2F6CE845078CF529BCB4E334AC753A70A43855B307741E570667FF7C23D7F47DB08122C3C6E5A12C1EF171453D2D95F
http://www.w3.org/2000/01/rdf-schema#comment
"Our findings reveal that PTPN1/2-mediated dephosphorylation of MITA/STING and its degradation by the 20S proteasomal pathway is an important regulatory mechanism of innate immune response to DNA virus."
xsd:string
http://purl.uniprot.org/uniprot/#_8DD135A61D25ECD06A12B5601ED60DF0BBCD0C897ED65AB1DADEBA8826C251CEB0E31A245CB73987E709E3288865D17F
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/B2F6CE845078CF529BCB4E334AC753A70A43855B307741E570667FF7C23D7F47DB08122C3C6E5A12C1EF171453D2D95F
http://purl.uniprot.org/uniprot/D3DUJ3
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/B2F6CE845078CF529BCB4E334AC753A70A43855B307741E570667FF7C23D7F47DB08122C3C6E5A12C1EF171453D2D95F
http://purl.uniprot.org/uniprot/#_D3DUJ3-mappedCitation-31527250
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/B2F6CE845078CF529BCB4E334AC753A70A43855B307741E570667FF7C23D7F47DB08122C3C6E5A12C1EF171453D2D95F