@prefix this: . @prefix sub: . @prefix beldoc: . @prefix rdfs: . @prefix rdf: . @prefix xsd: . @prefix dct: . @prefix dce: . @prefix pav: . @prefix np: . @prefix belv: . @prefix prov: . @prefix schem: . @prefix go: . @prefix Protein: . @prefix hgnc: . @prefix geneProductOf: . @prefix hasAgent: . @prefix species: . @prefix occursIn: . @prefix pubmed: . @prefix orcid: . sub:Head { this: np:hasAssertion sub:assertion; np:hasProvenance sub:provenance; np:hasPublicationInfo sub:pubinfo; a np:Nanopublication . } sub:assertion { sub:_1 hasAgent: sub:_2; a go:0016301 . sub:_2 geneProductOf: hgnc:19341; a Protein: . sub:_3 occursIn: species:9606; rdf:object sub:_1; rdf:predicate belv:increases; rdf:subject schem:Calcium; a rdf:Statement . sub:assertion rdfs:label "a(SCHEM:Calcium) -> kin(p(HGNC:CAMK1D))" . } sub:provenance { beldoc: dce:description "Approximately 61,000 statements."; dce:rights "Copyright (c) 2011-2012, Selventa. All rights reserved."; dce:title "BEL Framework Large Corpus Document"; pav:authoredBy sub:_5; pav:version "1.4" . sub:_4 prov:value "CKLiK kinase activity was dependent on Ca(++) and calmodulin as analyzed by in vitro phosphorylation of cyclic adenosine monophosphate responsive element modulator (CREM). these results demonstrate that CKLiK is regulated by Ca ++ /calmodulin and that active CKLiK can directly phosphorylate CREM and activate CREB, enhancing its transactivation capacity."; prov:wasQuotedFrom pubmed:11050006 . sub:_5 rdfs:label "Selventa" . sub:assertion prov:hadPrimarySource pubmed:11050006; prov:wasDerivedFrom beldoc:, sub:_4 . } sub:pubinfo { this: dct:created "2014-07-03T14:29:52.859+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }