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DESCRIBE <http://purl.uniprot.org/SHA-384/AE6CF30CEE678B7592E27D4870DA37FCE35C53762F95E53871BEF3A60A31801267673C70B0CA44E4B82939941E7B9590>
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http://purl.uniprot.org/SHA-384/AE6CF30CEE678B7592E27D4870DA37FCE35C53762F95E53871BEF3A60A31801267673C70B0CA44E4B82939941E7B9590
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/AE6CF30CEE678B7592E27D4870DA37FCE35C53762F95E53871BEF3A60A31801267673C70B0CA44E4B82939941E7B9590
http://www.w3.org/2000/01/rdf-schema#comment
"Mutation of the Sil1 residues involved in binding the Bip ATPase domain compromise the binding affinity of Sil1 to Bip and these Sil1 mutants also abolish the ability to stimulate the ATPase activity of Bip."
xsd:string
http://purl.uniprot.org/uniprot/#_FF0BF8B590A968C542241190642560F0572B52F3B97AF91A8EE063A187B46131B1226D7A6499C7C42769A9EE1B8D6A10
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/AE6CF30CEE678B7592E27D4870DA37FCE35C53762F95E53871BEF3A60A31801267673C70B0CA44E4B82939941E7B9590
http://purl.uniprot.org/uniprot/Q08199
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/AE6CF30CEE678B7592E27D4870DA37FCE35C53762F95E53871BEF3A60A31801267673C70B0CA44E4B82939941E7B9590
http://purl.uniprot.org/uniprot/#_Q08199-mappedCitation-21675960
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/AE6CF30CEE678B7592E27D4870DA37FCE35C53762F95E53871BEF3A60A31801267673C70B0CA44E4B82939941E7B9590