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DESCRIBE <http://purl.uniprot.org/SHA-384/C1AACAC1371AC774AFFE8082137953BA88D446C8D8B9B11E2BF75A4A774DE9ACA3F16312FEE6FBD1113EC4FEE1A95457>
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http://purl.uniprot.org/SHA-384/C1AACAC1371AC774AFFE8082137953BA88D446C8D8B9B11E2BF75A4A774DE9ACA3F16312FEE6FBD1113EC4FEE1A95457
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/C1AACAC1371AC774AFFE8082137953BA88D446C8D8B9B11E2BF75A4A774DE9ACA3F16312FEE6FBD1113EC4FEE1A95457
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/#_4F9B739E2E346FB112A2B56ABD42435E72E1148BCDAA8D8C240748930681A9E481851E3699AAF48766C826D15A9126C1
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/C1AACAC1371AC774AFFE8082137953BA88D446C8D8B9B11E2BF75A4A774DE9ACA3F16312FEE6FBD1113EC4FEE1A95457
http://purl.uniprot.org/uniprot/Q2VP91
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/C1AACAC1371AC774AFFE8082137953BA88D446C8D8B9B11E2BF75A4A774DE9ACA3F16312FEE6FBD1113EC4FEE1A95457
http://purl.uniprot.org/uniprot/#_Q2VP91-mappedCitation-25352621
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/C1AACAC1371AC774AFFE8082137953BA88D446C8D8B9B11E2BF75A4A774DE9ACA3F16312FEE6FBD1113EC4FEE1A95457