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DESCRIBE <http://purl.uniprot.org/SHA-384/CBB1BCCB89D4100987112897B6051B0CCA6D33523A7C273853538207FCDBBD0AF92EB2540C68E00FA4CA4B823058A48A>
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http://purl.uniprot.org/SHA-384/CBB1BCCB89D4100987112897B6051B0CCA6D33523A7C273853538207FCDBBD0AF92EB2540C68E00FA4CA4B823058A48A
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/CBB1BCCB89D4100987112897B6051B0CCA6D33523A7C273853538207FCDBBD0AF92EB2540C68E00FA4CA4B823058A48A
http://www.w3.org/2000/01/rdf-schema#comment
"Virus infection and RNase L activation disrupt its association with Filamin A and release RNase L to mediate its canonical nuclease-dependent antiviral activities."
xsd:string
http://purl.uniprot.org/uniprot/#_DE9B1A17FB4BEB922917EFEF4B02EBC0B0408B1C28F98C92F420735755BD05777CB0E0C4091A4EA0904928B8F961664C
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/CBB1BCCB89D4100987112897B6051B0CCA6D33523A7C273853538207FCDBBD0AF92EB2540C68E00FA4CA4B823058A48A
http://purl.uniprot.org/uniprot/Q1RLL8
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/CBB1BCCB89D4100987112897B6051B0CCA6D33523A7C273853538207FCDBBD0AF92EB2540C68E00FA4CA4B823058A48A
http://purl.uniprot.org/uniprot/#_Q1RLL8-mappedCitation-25352621
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/CBB1BCCB89D4100987112897B6051B0CCA6D33523A7C273853538207FCDBBD0AF92EB2540C68E00FA4CA4B823058A48A