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http://purl.uniprot.org/SHA-384/ECAB7D2F63FA121E9E052E6C9FC37C3673F179F1BD53E777A416ABC6D0515D059B50D431A99B4B2171A200C61B3EEDAEhttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/ECAB7D2F63FA121E9E052E6C9FC37C3673F179F1BD53E777A416ABC6D0515D059B50D431A99B4B2171A200C61B3EEDAEhttp://www.w3.org/2000/01/rdf-schema#comment"the catalytic activity of Pop2 deadenylase is important for Pumilio RD activity. Further we show that the Pumilio RDs directly bind to the CNOT complex. We also report that the decapping enzyme Dcp2 participates in repression by the N-terminus of Pumilio. These results support a model wherein Pumilio utilizes CNOT deadenylase and decapping complexes to accelerate destruction of target mRNAs."xsd:string
http://purl.uniprot.org/uniprot/#_A581AF471F5533DBE266A7978C49BF2394375974E07B7BDEADA4752D7C2595B904270DA45B9A72F4F6CE57C4304BAB5Ahttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/ECAB7D2F63FA121E9E052E6C9FC37C3673F179F1BD53E777A416ABC6D0515D059B50D431A99B4B2171A200C61B3EEDAE
http://purl.uniprot.org/uniprot/Q5U127http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/ECAB7D2F63FA121E9E052E6C9FC37C3673F179F1BD53E777A416ABC6D0515D059B50D431A99B4B2171A200C61B3EEDAE
http://purl.uniprot.org/uniprot/#_Q5U127-mappedCitation-31863588http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/ECAB7D2F63FA121E9E052E6C9FC37C3673F179F1BD53E777A416ABC6D0515D059B50D431A99B4B2171A200C61B3EEDAE