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DESCRIBE <http://purl.uniprot.org/SHA-384/A0B1B9FFDB69C870DC02FCE0E72DA67B2A3C4A19370D4E09E37B2C692CE8A0EBF667C9C168A30858B3DD7EE5AE672C38>
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http://purl.uniprot.org/SHA-384/A0B1B9FFDB69C870DC02FCE0E72DA67B2A3C4A19370D4E09E37B2C692CE8A0EBF667C9C168A30858B3DD7EE5AE672C38
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/A0B1B9FFDB69C870DC02FCE0E72DA67B2A3C4A19370D4E09E37B2C692CE8A0EBF667C9C168A30858B3DD7EE5AE672C38
http://www.w3.org/2000/01/rdf-schema#comment
"collagen type I alpha 1(COL1A1) messenger RNA remained unchanged in fibroblasts plated on fibroblast derived-extracellular matrix and excess COL1A1 polypeptide chains were degraded by the combined action of matrix metalloproteinases"
xsd:string
http://purl.uniprot.org/uniprot/#_33CE8FDAF51F4BCE7F4E7854B3F9C17C9AE1A8E229E071D963007601B8A0091564C66454635FCD295B8F291703476EF0
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/A0B1B9FFDB69C870DC02FCE0E72DA67B2A3C4A19370D4E09E37B2C692CE8A0EBF667C9C168A30858B3DD7EE5AE672C38
http://purl.uniprot.org/uniprot/Q9UMA6
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/A0B1B9FFDB69C870DC02FCE0E72DA67B2A3C4A19370D4E09E37B2C692CE8A0EBF667C9C168A30858B3DD7EE5AE672C38
http://purl.uniprot.org/uniprot/#_Q9UMA6-mappedCitation-24637022
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/A0B1B9FFDB69C870DC02FCE0E72DA67B2A3C4A19370D4E09E37B2C692CE8A0EBF667C9C168A30858B3DD7EE5AE672C38