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DESCRIBE <http://purl.uniprot.org/SHA-384/9D92C03A71F6450E299DC4CA339FE5919FC2F83DEF7B02C1DEF923B488AA34C0963F0BA23C2E46F60A574DB3C79638E6>
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http://purl.uniprot.org/SHA-384/9D92C03A71F6450E299DC4CA339FE5919FC2F83DEF7B02C1DEF923B488AA34C0963F0BA23C2E46F60A574DB3C79638E6
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/9D92C03A71F6450E299DC4CA339FE5919FC2F83DEF7B02C1DEF923B488AA34C0963F0BA23C2E46F60A574DB3C79638E6
http://www.w3.org/2000/01/rdf-schema#comment
"These findings indicate that glycosylation of DMP1 is a key posttranslational modification process during development and that DMP1-PG functions as an indispensable proteoglycan in osteogenesis."
xsd:string
http://purl.uniprot.org/uniprot/#_16D9CD892B41B6529D5058DBF5F40EE0A00E40EF0FE8D6FC00CA86967624BDC1087C01B8670AA175747C7AA47FF6BEF2
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/9D92C03A71F6450E299DC4CA339FE5919FC2F83DEF7B02C1DEF923B488AA34C0963F0BA23C2E46F60A574DB3C79638E6
http://purl.uniprot.org/uniprot/O55188
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/9D92C03A71F6450E299DC4CA339FE5919FC2F83DEF7B02C1DEF923B488AA34C0963F0BA23C2E46F60A574DB3C79638E6
http://purl.uniprot.org/uniprot/#_O55188-mappedCitation-26634432
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/9D92C03A71F6450E299DC4CA339FE5919FC2F83DEF7B02C1DEF923B488AA34C0963F0BA23C2E46F60A574DB3C79638E6