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 "1.4" .
  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 .
}