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DESCRIBE <http://purl.uniprot.org/SHA-384/181337EE0EE939850989A3AB78D76D30FCEE87E2408526BF94D61282016854E8ADC2E1050DFBF65613109070B6D7D517>
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http://purl.uniprot.org/SHA-384/181337EE0EE939850989A3AB78D76D30FCEE87E2408526BF94D61282016854E8ADC2E1050DFBF65613109070B6D7D517
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/181337EE0EE939850989A3AB78D76D30FCEE87E2408526BF94D61282016854E8ADC2E1050DFBF65613109070B6D7D517
http://www.w3.org/2000/01/rdf-schema#comment
"The data suggest that LULL1 oligomerizes to engage and transiently disassemble torsinA oligomers and is thereby positioned to transduce cytoplasmic signals to the inner nuclear membrane through torsinA."
xsd:string
http://purl.uniprot.org/uniprot/#_2F9E3C4727491166859D77F8CF1294EB46A0025549023389389961FD902385418C1B583FA4018D927A8AD861EA307A49
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/181337EE0EE939850989A3AB78D76D30FCEE87E2408526BF94D61282016854E8ADC2E1050DFBF65613109070B6D7D517
http://purl.uniprot.org/uniprot/Q8BYU6
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/181337EE0EE939850989A3AB78D76D30FCEE87E2408526BF94D61282016854E8ADC2E1050DFBF65613109070B6D7D517
http://purl.uniprot.org/uniprot/#_Q8BYU6-mappedCitation-26092934
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/181337EE0EE939850989A3AB78D76D30FCEE87E2408526BF94D61282016854E8ADC2E1050DFBF65613109070B6D7D517