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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 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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Top mentioned proteins: ADA2, Histone, CAN, N-acetyl-beta-D-glucosaminidase, p53
Papers on ADA3
Subunits of ADA-two-A-containing (ATAC) or Spt-Ada-Gcn5-acetyltrasferase (SAGA) Coactivator Complexes Enhance the Acetyltransferase Activity of GCN5.
Tora et al., Bristol, United Kingdom. In J Biol Chem, Dec 2015
The HAT module of ATAC is composed of GCN5, ADA2a, ADA3, and SGF29, whereas in the SAGA HAT module ADA2b is present instead of ADA2a.
Alteration/Deficiency in Activation 3 (ADA3) Protein, a Cell Cycle Regulator, Associates with the Centromere through CENP-B and Regulates Chromosome Segregation.
Band et al., Omaha, United States. In J Biol Chem, Dec 2015
ADA3 (alteration/deficiency in activation 3) is a conserved component of several transcriptional co-activator and histone acetyltransferase (HAT) complexes.
Chemical cross-linking and mass spectrometry to determine the subunit interaction network in a recombinant human SAGA HAT subcomplex.
Leize-Wagner et al., Strasbourg, France. In Protein Sci, Aug 2015
The identified interlinked peptides suggest a strong network of interaction between GCN5, ADA2B and ADA3 subunits; SGF29 is interacting with GCN5 and ADA3 but not with ADA2B.
Multiple regulatory mechanisms control the expression of the Geobacillus stearothermophilus gene for extracellular xylanase.
Shoham et al., Haifa, Israel. In J Biol Chem, 2014
The xynA gene is located next to an uncharacterized gene, xynX, that has similarity to the NIF3 (Ngg1p interacting factor 3)-like protein family.
High-risk HPV16E6 stimulates hADA3 degradation by enhancing its SUMOylation.
Nag et al., New Delhi, India. In Carcinogenesis, 2014
Recent investigations have identified hADA3, a transcriptional coactivator protein as a target of high-risk HPV16E6.
A functional genomics screen identifies PCAF and ADA3 as regulators of human granzyme B-mediated apoptosis and Bid cleavage.
Trapani et al., Melbourne, Australia. In Cell Death Differ, 2014
Twenty-two shRNAmiRs were identified in the positive-selection screen including two, PCAF and ADA3, whose gene products are known to reside in the same epigenetic regulatory complexes.
C-terminus of the Sgf73 subunit of SAGA and SLIK is important for retention in the larger complex and for heterochromatin boundary function.
Oki et al., Fukui, Japan. In Genes Cells, 2013
Deletion of ada2, ada3 or gcn5 (a HAT module component) caused complete loss of the boundary function of Sgf73.
Identification of transcriptional and phosphatase regulators as interaction partners of human ADA3, a component of histone acetyltransferase complexes.
Topcu et al., Denizli, Turkey. In Biochem J, 2013
To gain a better understanding of ADA3 function, we used a yeast two-hybrid approach to screen a human fetal cDNA library for proteins that interacted with hADA3 (human ADA3).
Cytoplasmic localization of alteration/deficiency in activation 3 (ADA3) predicts poor clinical outcome in breast cancer patients.
Band et al., Omaha, United States. In Breast Cancer Res Treat, 2013
Given previous findings that ADA3 is a critical component of HAT complexes that regulate ER function and evidence that overexpression of other ER coactivators such as SRC-3 is associated with clinical outcomes in breast cancer, the current study was designed to assess the potential significance of ADA3 expression/localization in human breast cancer patients.
Functional characterization and gene expression profiling of Drosophila melanogaster short dADA2b isoform-containing dSAGA complexes.
Boros et al., Szeged, Hungary. In Bmc Genomics, 2012
BACKGROUND: ADA2 proteins, together with ADA3, SGF29 and GCN5 form the acetyltransferase module of GNAT-type histone acetyltransferase complexes.
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.
All-trans retinoic acid affects subcellular localization of a novel BmNIF3l protein: functional deduce and tissue distribution of NIF3l gene from silkworm (Bombyx mori).
Zhang et al., Hangzhou, China. In Arch Insect Biochem Physiol, 2010
The corresponding gene was named BmNIF3l (Bombyx mori NGG1p interacting factor 3-like).
Deletion of host histone acetyltransferases and deacetylases strongly affects Agrobacterium-mediated transformation of Saccharomyces cerevisiae.
Hooykaas et al., Leiden, Netherlands. In Fems Microbiol Lett, 2009
We found that deletion of genes (GCN5, NGG1, YAF9 and EAF7) encoding subunits of the SAGA, SLIK, ADA and NuA4 histone acetyltransferase complexes highly increased the efficiency of AMT, while deletion of genes (HDA2, HDA3 and HST4) encoding subunits of histone deacetylase complexes decreased AMT.
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
The cellular response to protein misfolding in the endoplasmic reticulum.
Kaufman et al., Ann Arbor, United States. In Gene Expr, 1998
Deletion of GCN5, ADA2, and/or ADA3 reduces, and deletion of ADA5 completely abrogates, the transcriptional induction in response to misfolded protein in the ER.
Genetic isolation of ADA2: a potential transcriptional adaptor required for function of certain acidic activation domains.
Guarente et al., Cambridge, United States. In Cell, 1992
We thus identified ADA1, ADA2, and ADA3.
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