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DESCRIBE <http://purl.uniprot.org/SHA-384/66AE4914877349E9EAD934EC595C2777B41931580A5FCA74BC9C13FC9E7517DD4FE494A1194A515A2177216FF394D3FB>
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http://purl.uniprot.org/SHA-384/66AE4914877349E9EAD934EC595C2777B41931580A5FCA74BC9C13FC9E7517DD4FE494A1194A515A2177216FF394D3FB
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/66AE4914877349E9EAD934EC595C2777B41931580A5FCA74BC9C13FC9E7517DD4FE494A1194A515A2177216FF394D3FB
http://www.w3.org/2000/01/rdf-schema#comment
"Using a series of engineered protein substrates which are similar in size yet differ in secondary structure we demonstrate that thermal stability is a key factor that significantly affects UCH-L3 hydrolysis."
xsd:string
http://purl.uniprot.org/uniprot/#_A900CE28F8524947C1B2C92F7A4BCB2CF06695E02CA50F6A0A6701323EA72AADF8D3D07E5DCE73742C1B785992A5AEDC
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/66AE4914877349E9EAD934EC595C2777B41931580A5FCA74BC9C13FC9E7517DD4FE494A1194A515A2177216FF394D3FB
http://purl.uniprot.org/uniprot/P15374
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/66AE4914877349E9EAD934EC595C2777B41931580A5FCA74BC9C13FC9E7517DD4FE494A1194A515A2177216FF394D3FB
http://purl.uniprot.org/uniprot/#_P15374-mappedCitation-25369561
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/66AE4914877349E9EAD934EC595C2777B41931580A5FCA74BC9C13FC9E7517DD4FE494A1194A515A2177216FF394D3FB