@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 Protein: .
@prefix hgnc: .
@prefix geneProductOf: .
@prefix hasPart: .
@prefix ProteinComplex: .
@prefix go: .
@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 hasPart: sub:_2, sub:_3;
a ProteinComplex: .
sub:_2 geneProductOf: hgnc:7668;
a Protein: .
sub:_3 geneProductOf: hgnc:3467;
a Protein: .
sub:_4 hasAgent: sub:_5;
a go:0042789 .
sub:_5 geneProductOf: hgnc:3467;
a Protein: .
sub:_6 occursIn: species:9606;
rdf:object sub:_4;
rdf:predicate belv:directlyIncreases;
rdf:subject sub:_1;
a rdf:Statement .
sub:assertion rdfs:label "complex(p(HGNC:NCOA1),p(HGNC:ESR1)) => tscript(p(HGNC:ESR1))" .
}
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:_8;
pav:version "20131211" .
sub:_7 prov:value "In this study, we show that a p160 coactivator contributes to the ligand- independent ER activation of a target gene in a cellular model in which ER, coactivator, and target gene are endogenous. Using transfected cells, we further show that the full-length ER can interact physically and functionally with all three p160/SRCs and CBP in the absence of ligand in vivo and that mutation of Ser104/106/118 to Ala residues in ER affects these interactions. In addition, mutation of these residues affects ER coactivation by a subset of coactivators in the presence of E2, albeit to a lesser extent than in the absence of hormone. Further analysis reveals that mutations of both Ser104/106 and Ser118 decrease ligand-independent SRC-1 coactivation of ER activity by two mechanisms. First, there is a seemingly indirect effect on SRC-1 recruitment that, surprisingly, requires other receptor domains in addition to A/B, which is consistent with our finding that SRC-1 enhancement of the ligand- independent interaction between the A/B and DEF regions is regulated by the Ser104/106/118 phosphorylation sites. Secondly, we observe an effect on SRC-1 coactivation of the A/B domain that does not depend on the remainder of the molecule. further show that the full-length ER can interact physically and functionally with all three p160/SRCs and CBP in the absence of ligand in vivo";
prov:wasQuotedFrom pubmed:12714702 .
sub:_8 rdfs:label "Selventa" .
sub:assertion prov:hadPrimarySource pubmed:12714702;
prov:wasDerivedFrom beldoc:, sub:_7 .
}
sub:pubinfo {
this: dcterms:created "2014-07-03T14:32:01.532+02:00"^^xsd:dateTime;
pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 .
}