Matches in DBpedia 2015-10 for { <http://dbpedia.org/resource/CAPN10> ?p ?o }
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- CAPN10 abstract "Calpain-10 is a protein that in humans is encoded by the CAPN10 gene.Calpains are ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. The typical calpain proteins are heterodimers consisting of an invariant small subunit and variable large subunits. The large catalytic subunit has four domains: domain I, the N-terminal regulatory domain that is processed upon calpain activation; domain II, the protease domain; domain III, a linker domain of unknown function; and domain IV, the calmodulin-like calcium-binding domain. The heterodimer interface is predominantly found between domain IV and the small subunit, which is also a calmodulin-like calcium-binding domain. This gene encodes a large subunit. It is an atypical calpain in that it lacks the calmodulin-like calcium-binding domain and instead has a divergent C-terminal domain. It therefore cannot heterodimerize with the small subunit. It is similar in organization to calpains 5 and 6. This gene is associated with type 2 or non-insulin-dependent diabetes mellitus (NIDDM) and located within the NIDDM1 region. Multiple alternative transcript variants encoding different isoforms have been described for this gene.".
- CAPN10 entrezgene "11132".
- CAPN10 wikiPageExternalLink merops.cgi?id=C02.018.
- CAPN10 wikiPageID "14133932".
- CAPN10 wikiPageLength "10686".
- CAPN10 wikiPageOutDegree "4".
- CAPN10 wikiPageRevisionID "673170124".
- CAPN10 wikiPageWikiLink Calpain.
- CAPN10 wikiPageWikiLink Gene.
- CAPN10 wikiPageWikiLink MEROPS.
- CAPN10 wikiPageWikiLink Protein.
- CAPN10 wikiPageWikiLinkText "CAPN10".
- CAPN10 hasPhotoCollection CAPN10.
- CAPN10 requireManualInspection "no".
- CAPN10 summaryText "Calpains are ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. The typical calpain proteins are heterodimers consisting of an invariant small subunit and variable large subunits. The large catalytic subunit has four domains: domain I, the N-terminal regulatory domain that is processed upon calpain activation; domain II, the protease domain; domain III, a linker domain of unknown function; and domain IV, the calmodulin-like calcium-binding domain. The heterodimer interface is predominantly found between domain IV and the small subunit, which is also a calmodulin-like calcium-binding domain. This gene encodes a large subunit. It is an atypical calpain in that it lacks the calmodulin-like calcium-binding domain and instead has a divergent C-terminal domain. It therefore cannot heterodimerize with the small subunit. It is similar in organization to calpains 5 and 6. This gene is associated with type 2 or non-insulin-dependent diabetes mellitus and located within the NIDDM1 region. Multiple alternative transcript variants encoding different isoforms have been described for this gene.".
- CAPN10 updateCitations "yes".
- CAPN10 updatePage "yes".
- CAPN10 updateProteinBox "yes".
- CAPN10 updateSummary "yes".
- CAPN10 wikiPageUsesTemplate Template:Cysteine_proteases.
- CAPN10 wikiPageUsesTemplate Template:Gene-2-stub.
- CAPN10 wikiPageUsesTemplate Template:PBB.
- CAPN10 wikiPageUsesTemplate Template:PBB_Controls.
- CAPN10 wikiPageUsesTemplate Template:PBB_Further_reading.
- CAPN10 wikiPageUsesTemplate Template:PBB_Summary.
- CAPN10 wikiPageUsesTemplate Template:Refbegin.
- CAPN10 wikiPageUsesTemplate Template:Refend.
- CAPN10 wikiPageUsesTemplate Template:Reflist.
- CAPN10 hypernym Protein.
- CAPN10 type Biomolecule.
- CAPN10 type Protein.
- CAPN10 type Thing.
- CAPN10 type Q206229.
- CAPN10 type Q8054.
- CAPN10 comment "Calpain-10 is a protein that in humans is encoded by the CAPN10 gene.Calpains are ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. The typical calpain proteins are heterodimers consisting of an invariant small subunit and variable large subunits.".
- CAPN10 label "CAPN10".
- CAPN10 sameAs m.03cvmwn.
- CAPN10 sameAs Q5008747.
- CAPN10 sameAs Q5008747.
- CAPN10 wasDerivedFrom CAPN10?oldid=673170124.
- CAPN10 isPrimaryTopicOf CAPN10.