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DESCRIBE <http://purl.uniprot.org/SHA-384/3992C3687DDE406615F342B20B7E505804E84C71AF3E951205D953D81065783577942C4972D6F3B21DB84F1CBE271D23>
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http://purl.uniprot.org/SHA-384/3992C3687DDE406615F342B20B7E505804E84C71AF3E951205D953D81065783577942C4972D6F3B21DB84F1CBE271D23
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/3992C3687DDE406615F342B20B7E505804E84C71AF3E951205D953D81065783577942C4972D6F3B21DB84F1CBE271D23
http://www.w3.org/2000/01/rdf-schema#comment
"mutations associated with hPGK1 deficiency lead to increased aggregation and proteolysis rates in vitro and inside cells due to protein thermodynamic destabilization"
xsd:string
http://purl.uniprot.org/uniprot/#_180C3D4A85CE92A912EA1997C3560B450B8BFE15641736FB9939CE124C9E3E9308384A28D5BAC2ECCEF1FAABCF9A57CB
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/3992C3687DDE406615F342B20B7E505804E84C71AF3E951205D953D81065783577942C4972D6F3B21DB84F1CBE271D23
http://purl.uniprot.org/uniprot/B4DWQ3
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/3992C3687DDE406615F342B20B7E505804E84C71AF3E951205D953D81065783577942C4972D6F3B21DB84F1CBE271D23
http://purl.uniprot.org/uniprot/#_B4DWQ3-mappedCitation-24838780
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/3992C3687DDE406615F342B20B7E505804E84C71AF3E951205D953D81065783577942C4972D6F3B21DB84F1CBE271D23