gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 02 Oct 2014.

Transcriptional adaptor 2A

ADA2, Ada2p
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. Several alternatively spliced transcript variants encoding different isoforms of this gene have been described, but the full-length nature of some of these variants has not been determined. [provided by RefSeq, Oct 2009] (from NCBI)
Top mentioned proteins: ADA1, Histone, CAN, ADA3, ACID
Papers on ADA2
Mutant adenosine deaminase 2 in a polyarteritis nodosa vasculopathy.
Levy-Lahad et al., Aş Şanamayn, Syria. In N Engl J Med, Apr 2014
RESULTS: In all the families, vasculitis was caused by recessive mutations in CECR1, the gene encoding adenosine deaminase 2 (ADA2).
Early-onset stroke and vasculopathy associated with mutations in ADA2.
Aksentijevich et al., Aş Şanamayn, Syria. In N Engl J Med, Apr 2014
RESULTS: All nine patients carried recessively inherited mutations in CECR1 (cat eye syndrome chromosome region, candidate 1), encoding adenosine deaminase 2 (ADA2), that were predicted to be deleterious; these mutations were rare or absent in healthy controls.
Coronary artery disease. A study of three polymorphic sites of adenosine deaminase gene.
Gloria-Bottini et al., In Acta Cardiol, Feb 2014
The recent observation of an association between ADA, genetic polymorphism and coronary artery disease (CAD) prompted us to study the possible relevance of three intragenic polymorphic sites of the ADA gene (ADA1, ADA2 and ADA6).
Lysine acetyltransferase GCN5b interacts with AP2 factors and is required for Toxoplasma gondii proliferation.
Sullivan et al., New York City, United States. In Plos Pathog, Jan 2014
Proteomics studies revealed that GCN5b interacts with AP2-domain proteins, apicomplexan plant-like transcription factors, as well as a "core complex" that includes the co-activator ADA2-A, TFIID subunits, LEO1 polymerase-associated factor (Paf1) subunit, and RRM proteins.
Evaluating pleural ADA, ADA2, IFN-γ and IGRA for diagnosing tuberculous pleurisy.
Lee et al., Taipei, Taiwan. In J Infect, Oct 2013
Performances of pleural adenosine deaminase (ADA), ADA2, interferon-gamma (IFN-γ), and interferon-gamma release assays (IGRA) as diagnostic tools for TB pleurisy were evaluated.
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, Sep 2013
Deletion of ada2, ada3 or gcn5 (a HAT module component) caused complete loss of the boundary function of Sgf73.
Potential roles of adenosine deaminase-2 in diabetic retinopathy.
Liou et al., Augusta, United States. In Biochem Biophys Res Commun, Aug 2013
In the vertebrates but not rodents, a macrophage-associated ADA2 is identified.
Adenosine deaminase activity in normal pregnancy and pregnancy associated disorders.
Jain et al., Bhopāl, India. In Arch Physiol Biochem, May 2013
Adenosine deaminase (ADA) is an enzyme of purine salvage pathway and has two important isoenzymes ADA1 and ADA2.
Diagnostic value of serum adenosine deaminase activity in HIV infected patients of Kurdish population.
Hoseini et al., Sanandaj, Iran. In Clin Lab, 2012
Blood CD4+ cell count was recorded and serum total ADA, and ADA1 and ADA2 isoenzyme activities were determined.
CCDC134 interacts with hADA2a and functions as a regulator of hADA2a in acetyltransferase activity, DNA damage-induced apoptosis and cell cycle arrest.
Qiu et al., Beijing, China. In Histochem Cell Biol, 2012
CCDC134 increased the PCAF-dependent K320 acetylation of p53 and p53 protein stability in the presence of hADA2a overexpression.
The SAGA subunit Ada2 functions in transcriptional silencing.
Pillus et al., San Diego, United States. In Mol Cell Biol, 2009
Ada2, likely in the context of SAGA, is positioned at chromosomal termini to participate in both transcriptional repression and activation in response to nutrient signaling.
A conserved central region of yeast Ada2 regulates the histone acetyltransferase activity of Gcn5 and interacts with phospholipids.
Brandl et al., London, Canada. In J Mol Biol, 2009
Indicative of Ada2 affecting Gcn5 function, Ada2 mutation resulted in a decrease in Gcn5-mediated histone acetylation in vitro to a level approximately 40% that with wild-type Ada2.
hADA2a and hADA3 are required for acetylation, transcriptional activity and proliferative effects of beta-catenin.
Brachmann et al., Irvine, United States. In Cancer Biol Ther, 2008
hADA2a and hADA3 as crucial cofactors of beta-catenin that are likely involved in the assembly of transactivation-competent beta-catenin complexes at Wnt target genes.
SAGA interacting factors confine sub-diffusion of transcribed genes to the nuclear envelope.
Nehrbass et al., Paris, France. In Nature, 2006
This confinement was mediated by Sus1 and Ada2, members of the SAGA histone acetyltransferase complex, and Sac3, a messenger RNA export factor, physically linking the activated GAL genes to the nuclear-pore-complex component Nup1.
Roles for Gcn5p and Ada2p in transcription and nucleotide excision repair at the Saccharomyces cerevisiae MET16 gene.
Waters et al., Oviedo, Spain. In Nucleic Acids Res, 2005
Ada2p regulates transcription and DNA repair at the MET16 gene.
The use of adenosine deaminase and adenosine deaminase isoenzymes in the diagnosis of tuberculous pleuritis.
Jiménez Castro et al., Madrid, Spain. In Curr Opin Pulm Med, 2000
Adenosine deaminase expresses the sum of two isoenzymes (ADA1 and ADA2).
The cellular response to protein misfolding in the endoplasmic reticulum.
Kaufman et al., Ann Arbor, United States. In Gene Expr, 1998
A yeast transcriptional coactivator complex, Gcn5p/Ada, which is composed of Gcn5p, Ada2p, Ada3p, and Ada5p, was identified that interacts with Ire1p and Hac1p.
[Adenosine deaminase: isoenzymes ADA1 and ADA2].
Puczkowski et al., In Pol Merkur Lekarski, 1997
The isoenzymes ADA1 and ADA2 of the enzyme adenosine deaminase (ADA deaminate mainly two nucleotides: adenosine and 2'-deoxyadenosine, molecules with many effects on human cells.
[Adenosine deaminase].
Kurata, In Nihon Rinsho, 1995
Two ADA isozymes are known as ADA1 and ADA2.
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.
share on facebooktweetadd +1mail to friends