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DESCRIBE <http://purl.uniprot.org/SHA-384/640ADA7371F6EF285E192F2BE79A2B01B589ED8B8F53239E817C49A5EB55DC0788D884A06E8F5D314A17EF797C08A6C1>
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http://purl.uniprot.org/SHA-384/640ADA7371F6EF285E192F2BE79A2B01B589ED8B8F53239E817C49A5EB55DC0788D884A06E8F5D314A17EF797C08A6C1
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/640ADA7371F6EF285E192F2BE79A2B01B589ED8B8F53239E817C49A5EB55DC0788D884A06E8F5D314A17EF797C08A6C1
http://www.w3.org/2000/01/rdf-schema#comment
"Data suggest that TYMS exhibits a ligand-binding site in dimer interface suggesting that cavity in dimer interface serves as an allosteric site to regulate conformational switching between active and inactive states of the enzyme."
xsd:string
http://purl.uniprot.org/uniprot/#_87D7D0E92B3F2035D7F41B1E9D5E41A22AA3A1F84A329A2AFA6DAF53BCC2584788C24CFC14BA4CB20E46CDF953632701
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/640ADA7371F6EF285E192F2BE79A2B01B589ED8B8F53239E817C49A5EB55DC0788D884A06E8F5D314A17EF797C08A6C1
http://purl.uniprot.org/uniprot/P04818
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/640ADA7371F6EF285E192F2BE79A2B01B589ED8B8F53239E817C49A5EB55DC0788D884A06E8F5D314A17EF797C08A6C1
http://purl.uniprot.org/uniprot/#_P04818-mappedCitation-28634233
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/640ADA7371F6EF285E192F2BE79A2B01B589ED8B8F53239E817C49A5EB55DC0788D884A06E8F5D314A17EF797C08A6C1