2.3.1.32	K1358A	site directed mutagenesis of lysine 1358 of the p300 acetyltransferase domain reveals that inhibitor binds via a hydrogen bond to this lysine residue in the wild-type, in the mutant no binding leads to total loss of acetyltransferase activity	704529	
2.3.1.32	L254P	esa1 mutant (reduced histone H4 acetylation) at 36°C (restrictive temperature) is sensitive to 6-azauracil (inhibitor impeding elongation by lowering nucleotide pools) but shows little effect at 30°C (permissive temperature), gene length dependent defects in transcription	705700	
2.3.1.32	additional information	double mutant esa1/gcn5 at 36°C is very sensitive to 6-azauracil (inhibitor impeding elongation by lowering nucleotide pools) and shows littler but still strong effect at 30°C (permissive temperature), gene length dependent defects in transcription	705700	
2.3.1.32	additional information	gcn5 deletion mutant (reduced H3 acetylation) at 36°C (restrictive temperature) is very sensitive to 6-azauracil (inhibitor impeding elongation by lowering nucleotide pools) but shows less effect at 30°C (permissive temperature), gene length dependent defects in transcription	705700	
2.3.1.32	additional information	in human embryonic kidney 293 cells, overexpression of cyclic adenosine monophosphate response element-binding binding protein, CBP, or p300, but not p300/CBP-associated factor, increases mineralocorticoid receptor acetylation and decreases expression of mineralocorticoid receptor target genes	735974	
2.3.1.32	additional information	Lysine 158 and 287 in the RIP140 (receptor-interacting protein 140) are targets for acetylation by p300 acetyltransferase as shown by site directed mutagenesis of these residues, lysine 158 and 287 replaced by glutamine (mimicking acetylation) turn the RIP140 repressive in the absence of p300, while the alanine replacements (preventing acetylation) prevents responsiveness to p300, the double mutants show stronger effects in the same directions, while lysine 111 and 311 seem not to be targets for the p300 acetyltransferase. Mitogen-activated protein kinase (MAPK) target mutants that mimic (T202E/T207E) or abolish (T202A/T207A) threonine phosphorylation of RIP140 enhance or reduce the stimulation of p300 acetyltransferase, respectively, extracellular-signal-related kinase 2 (Erk2) is identified as the responsible MAPK in this pathway	703138