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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

NGG1 Ngg1p

ADA3, hADA3, NGG1, NGG1p
Many DNA-binding transcriptional activator proteins enhance the initiation rate of RNA polymerase II-mediated gene transcription by interacting functionally with the general transcription machinery bound at the basal promoter. Adaptor proteins are usually required for this activation, possibly to acetylate and destabilize nucleosomes, thereby relieving chromatin constraints at the promoter. The protein encoded by this gene is a transcriptional activator adaptor and has been found to be part of the PCAF histone acetylase complex. In addition, it associates with the tumor suppressor protein p53 and is required for full activity of p53 and p53-mediated apoptosis. At least four alternatively spliced variants have been found for this gene, but the full-length nature of some variants has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
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Papers on ADA3
Mammalian alteration/deficiency in activation 3 (Ada3) is essential for embryonic development and cell cycle progression.
Band et al., Omaha, United States. In J Biol Chem, 2012
a critical role of Ada3 in embryogenesis and cell cycle progression as an essential component of HAT complex.
Human ADA3 regulates RARalpha transcriptional activity through direct contact between LxxLL motifs and the receptor coactivator pocket.
Chen et al., United States. In Nucleic Acids Res, 2010
hADA3 interacts directly with RARalpha in a hormone-dependent manner and this interaction contributes to RARalpha transactivation
Genes of the ecdysone biosynthesis pathway are regulated by the dATAC histone acetyltransferase complex in Drosophila.
Boros et al., Szeged, Hungary. In Mol Cell Biol, 2010
This study reports the transcriptome analysis of Drosophila melanogaster dAda2a and dAda3 mutants, in which subunits of the ATAC acetyltransferase complex are affected.
HPV16 E6-induced and E6AP-dependent inhibition of the transcriptional coactivator hADA3 in human cervical carcinoma cells.
Xie et al., Hangzhou, China. In Cancer Invest, 2009
oncoprotein E6 inhibits hADA3 in cervical cancer cells and this process is E6AP-dependent.
Ankyrin repeats-containing cofactors interact with ADA3 and modulate its co-activator function.
Chen et al., United States. In Biochem J, 2008
ADA3 is a newly identified target of the ANCO proteins, which may modulate co-activator function in a transcription-factor-specific manner
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