@prefix dcterms: . @prefix this: . @prefix sub: . @prefix beldoc: . @prefix rdfs: . @prefix rdf: . @prefix xsd: . @prefix dce: . @prefix pav: . @prefix np: . @prefix belv: . @prefix prov: . @prefix obo: . @prefix Protein: . @prefix hgnc: . @prefix geneProductOf: . @prefix hasPart: . @prefix ProteinComplex: . @prefix go: . @prefix hasAgent: . @prefix species: . @prefix occursIn: . @prefix do: . @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 hasPart: sub:_2, sub:_3; a ProteinComplex: . sub:_2 geneProductOf: hgnc:9052; a Protein: . sub:_3 geneProductOf: hgnc:9053; a Protein: . sub:_4 geneProductOf: hgnc:9071; a Protein: . sub:_5 hasAgent: sub:_6; a go:0003824 . sub:_6 geneProductOf: hgnc:9052; a Protein: . sub:_7 rdf:object sub:_5; rdf:predicate belv:increases; rdf:subject sub:_4; a rdf:Statement . sub:_8 occursIn: do:1936, obo:CLO_0008947, obo:CL_0000192, obo:UBERON_0001135, species:9606; rdf:object sub:_7; rdf:predicate belv:increases; rdf:subject sub:_1; a rdf:Statement . sub:assertion rdfs:label "complex(p(HGNC:PLAU),p(HGNC:PLAUR)) -> (p(HGNC:PLG) -> cat(p(HGNC:PLAU)))", "p(HGNC:PLG) -> cat(p(HGNC:PLAU))" . } 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:_10; pav:version "20131211" . sub:_10 rdfs:label "Selventa" . sub:_9 prov:value "The single-chain urokinase (scuPA) secreted by cells has a low enzymatic activity which increases ~300-fold after the proteolytic cleavage of the Lys158-Ile159 bond [32] that results in uPA conversion into the two-chain form consisting of two polypeptide chains joined via the Cys148-Cys279 disulfide bond. The N-terminal A-chain includes the GFD and kringle domain; the B-chain contains the proteolytic domain. Plasmin is the most efficient activator of scuPA, although the other enzymes (kallikrein, trypsin, blood coagulation factor XIIa, and cathepsin in tumor cells [32]) could potentially compensate for any loss of plasmin function. In addition to spatial control of extracellular proteolysis, the urokinase receptor is involved in the activation and inactivation of urokinase. The binding of the secreted single-chain urokinase to the uPAR makes it more sensitive to proteolytic activation by plasmin than the free urokinase [35]."; prov:wasQuotedFrom pubmed:11841347 . sub:assertion prov:hadPrimarySource pubmed:11841347; prov:wasDerivedFrom beldoc:, sub:_9 . } sub:pubinfo { this: dcterms:created "2014-07-03T14:31:46.927+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }