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:_6 ;
    pav:version "1.4" .
  sub:_5 prov:value "Because these residues are required for enhanced MEF2C activity in monocytic cells, we tested whether MyoD activation of Gal4-MEF2C required the same amino acids. The combined mutation of both Thr293 and Thr300 to alanine (T293;300A) did not affect the basal activity of Gal4-MEF2C (Figure 3b, compare columns 3 and 5), but did enhance the activity of Gal4-MEF2C when MyoD+E12 were co-expressed (Figure 3b, compare columns 4 and 6). In contrast, mutation of Ser387 to alanine (S387A) decreased the basal activity of Gal4-MEF2C and completely eliminated its activation by co-transfected MyoD+E12 (Figure 3b, columns 7,8). Importantly, activation of the p38 kinase pathway did stimulate the function of the S387A Gal4-MEF2C mutant (data not shown; see also [25,27]), indicating that this mutation does not simply inactivate the protein. Therefore, MyoD activation of the MEF2C TAD requires Ser387, but neither Thr293 nor Thr300, of MEF2C." ;
    prov:wasQuotedFrom pubmed:10322110 .
  sub:_6 rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:10322110 ;
    prov:wasDerivedFrom beldoc: , sub:_5 .
}