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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
Newly recognized Mendelian disorders with rheumatic manifestations.
New
Goldbach-Mansky et al., Bethesda, United States. In Curr Opin Rheumatol, 20 Aug 2015
Mutations in ADA2, TRNT1 and COPA, AP1S3, and TNFRSF11A cause complex syndromes; loss-of-function mutations in enzymes and molecules are linked to the generation of 'cellular stress' and the release of inflammatory mediators that likely cause the inflammatory disease manifestations.
The role of G22A adenosine deaminase 1 gene polymorphism and the activities of ADA isoenzymes in fertile and infertile men.
New
Tavilani et al., Tabrīz, Iran. In Urology, 09 Aug 2015
In addition, ADA isoenzymes activities (ADA1 and ADA2) were measured using colorimetric method.
Dermatologic Features of ADA2 Deficiency in Cutaneous Polyarteritis Nodosa.
New
Gibson et al., Turku, Finland. In Jama Dermatol, 01 Aug 2015
Importance: Mutations in the CERC1 gene associated with deficiency in the ADA2 protein (DADA2) have been implicated in the pathogenesis of cutaneous polyarteritis nodosa (cPAN) and early-onset vasculopathy.
Unpredictable Chronic Stress Alters Adenosine Metabolism in Zebrafish Brain.
New
Bonan et al., Porto Alegre, Brazil. In Mol Neurobiol, 17 Jul 2015
Additionally, we analyzed ATP metabolism as well as ada1, ada2.1, ada2.2, adaL, and adaasi gene expression in zebrafish brain.
Inhibition of adenosine deaminase (ADA)-mediated metabolism of cordycepin by natural substances.
New
Fujiwara et al., Tokyo, Japan. In Pharmacol Res Perspect, Mar 2015
In this study, ADA1- and ADA2-expressing HEK293 cells were established to determine the major ADA isoform responsible for the deamination of cordycepin.
MicroRNA-146b-3p regulates retinal inflammation by suppressing adenosine deaminase-2 in diabetes.
New
Liou et al., Augusta, United States. In Biomed Res Int, Dec 2014
ADA, including ADA1 and ADA2, exists in all organisms.
Effect of genetic factors on the association between coronary artery disease and PTPN22 polymorphism.
Review
New
Chiariello et al., Roma, Italy. In World J Cardiol, Jul 2014
A highly significant association between PTPN22 and CAD is observed in carriers of ADA2 *2 allele with higher proportion of *T allele carriers in non diabetic subjects with CAD as compared to other group.
Mutant adenosine deaminase 2 in a polyarteritis nodosa vasculopathy.
New
Impact
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.
New
Impact
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.
Adenosine deaminase activity in normal pregnancy and pregnancy associated disorders.
Review
Jain et al., Bhopāl, India. In Arch Physiol Biochem, 2013
Adenosine deaminase (ADA) is an enzyme of purine salvage pathway and has two important isoenzymes ADA1 and ADA2.
CCDC134 interacts with hADA2a and functions as a regulator of hADA2a in acetyltransferase activity, DNA damage-induced apoptosis and cell cycle arrest.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
Impact
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.
GeneRIF
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.
Review
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.
Review
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].
Review
Puczkowski et al., In Pol Merkur Lekarski, 1997
The isoenzymes ADA1 and ADA2 of the enzyme adenosine deaminase (ADA 3.5.4.4) deaminate mainly two nucleotides: adenosine and 2'-deoxyadenosine, molecules with many effects on human cells.
Genetic isolation of ADA2: a potential transcriptional adaptor required for function of certain acidic activation domains.
Impact
Guarente et al., Cambridge, United States. In Cell, 1992
We thus identified ADA1, ADA2, and ADA3.
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