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http://purl.uniprot.org/SHA-384/2D689324C4C0B03C458241572722399F47A913092F0CC77121B37E87C68D86B20763F3164F984318ACBE726360CAADC2http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/2D689324C4C0B03C458241572722399F47A913092F0CC77121B37E87C68D86B20763F3164F984318ACBE726360CAADC2http://www.w3.org/2000/01/rdf-schema#comment"The authors show that phosphorylation of two different HAC1 splicing intermediates is required for their degradation by the 5'-->3' exonuclease Xrn1 to enact opposing effects on the UPR. We also found that ligated but 2'-phosphorylated HAC1 mRNA is cleaved yielding a decay intermediate with both 5'- and 2'-phosphates at its 5'-end that inhibit 5'-->3' decay and suggesting that Ire1 degrades incompletely processed HAC1."xsd:string
http://purl.uniprot.org/uniprot/#_3282DF3B673F2F7414D23BFA590352BEB3C71BD7FAE32EE7541092AE6250DBA304E735D851994C080E84F1FC88569B8Ahttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/2D689324C4C0B03C458241572722399F47A913092F0CC77121B37E87C68D86B20763F3164F984318ACBE726360CAADC2
http://purl.uniprot.org/uniprot/P41546http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/2D689324C4C0B03C458241572722399F47A913092F0CC77121B37E87C68D86B20763F3164F984318ACBE726360CAADC2
http://purl.uniprot.org/uniprot/#_P41546-mappedCitation-30874502http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/2D689324C4C0B03C458241572722399F47A913092F0CC77121B37E87C68D86B20763F3164F984318ACBE726360CAADC2