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DESCRIBE <http://purl.uniprot.org/SHA-384/D8C0A4D14ACEE0218A55BCAB058DEBAD62D4D444B0A90AC7AEEBE0B49CDE4A23A5F6AFDF95C01B69AE078D23F1C9FEEF>
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http://purl.uniprot.org/SHA-384/D8C0A4D14ACEE0218A55BCAB058DEBAD62D4D444B0A90AC7AEEBE0B49CDE4A23A5F6AFDF95C01B69AE078D23F1C9FEEF
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/D8C0A4D14ACEE0218A55BCAB058DEBAD62D4D444B0A90AC7AEEBE0B49CDE4A23A5F6AFDF95C01B69AE078D23F1C9FEEF
http://www.w3.org/2000/01/rdf-schema#comment
"Data show that YB-1 disrupts MutSalpha/PCNA/G/T heteroduplex ternary complex formation through competing with MutSa for PCNA binding on G/T heteroduplex."
xsd:string
http://purl.uniprot.org/uniprot/#_0217BBC0E893DD8644DACEFA72B065BF37DACD14248468EB7243539F65335E0534853396CEDB5CC4BDE7AC70638E9B23
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/D8C0A4D14ACEE0218A55BCAB058DEBAD62D4D444B0A90AC7AEEBE0B49CDE4A23A5F6AFDF95C01B69AE078D23F1C9FEEF
http://purl.uniprot.org/uniprot/Q7Z6A3
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/D8C0A4D14ACEE0218A55BCAB058DEBAD62D4D444B0A90AC7AEEBE0B49CDE4A23A5F6AFDF95C01B69AE078D23F1C9FEEF
http://purl.uniprot.org/uniprot/#_Q7Z6A3-mappedCitation-24141788
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/D8C0A4D14ACEE0218A55BCAB058DEBAD62D4D444B0A90AC7AEEBE0B49CDE4A23A5F6AFDF95C01B69AE078D23F1C9FEEF