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Tyrosyl-DNA phosphodiesterase 2

TTRAP, TRAF and TNF receptor-associated protein
This gene encodes a member of a superfamily of divalent cation-dependent phosphodiesterases. The encoded protein associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor associated factors (TRAFs), and inhibits nuclear factor-kappa-B activation. This protein has sequence and structural similarities with APE1 endonuclease, which is involved in both DNA repair and the activation of transcription factors. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Phosphodiesterase, CAN, Ru2, NF-kappaB, THEM2
Papers on TTRAP
TTRAP is a critical factor in grouper immune response to virus infection.
Qin et al., Guangzhou, China. In Fish Shellfish Immunol, Oct 2015
TTRAP (TRAF and TNF receptor-associated protein) is latest identified cytosolic protein that serves as a negative regulator for TNF signaling pathway.
Point mutations of the mTOR-RHEB pathway in renal cell carcinoma.
Sudarshan et al., Birmingham, United States. In Oncotarget, Aug 2015
Interestingly, we found a prominent cluster of hyperactivating mutations in the FAT (FRAP-ATM-TTRAP) domain of mTOR in renal cell carcinoma that led to an increase in both mTORC1 and mTORC2 activities and led to an increased proliferation of cells.
An assessment of gene-by-gene interactions as a tool to unfold missing heritability in dyslexia.
Marino et al., Lecco, Italy. In Hum Genet, Jul 2015
After applying 500,000 permutations and correcting for multiple testing, both methods show that G × G effects between markers within the DYX1C1, KIAA0319/TTRAP, and GRIN2B genes lower the memory letters composite z-score of on average 0.55 standard deviation.
Structural and functional characterization of a novel molluskan ortholog of TRAF and TNF receptor-associated protein from disk abalone (Haliotis discus discus).
Lee et al., Ansan, South Korea. In Fish Shellfish Immunol, 2014
Within the signaling cascade, TNF receptor-associated factor (TRAF) and TNF receptor-associated protein (TTRAP) has been shown to have a crucial role in the modulation of immune signaling in animals.
Tyrosyl-DNA-phosphodiesterases (TDP1 and TDP2).
Marchand et al., Bethesda, United States. In Dna Repair (amst), 2014
Moreover, TDP2 has been involved in signal transduction (under the former names of TTRAP or EAPII).
Proteolytic degradation of topoisomerase II (Top2) enables the processing of Top2·DNA and Top2·RNA covalent complexes by tyrosyl-DNA-phosphodiesterase 2 (TDP2).
Pommier et al., Bethesda, United States. In J Biol Chem, 2014
The Top2 protein-DNA covalent complexes are excised (in part) by tyrosyl-DNA-phosphodiesterase 2 (TDP2/TTRAP/EAP2/VPg unlinkase).
Overexpression of TTRAP inhibits cell growth and induces apoptosis in osteosarcoma cells.
Chen et al., Shanghai, China. In Bmb Rep, 2013
In comparison with wild-type TTRAP, mutations in the 5'-tyrosyl-DNA phosphodiesterase activity of TTRAP, in particular TTRAP(E152A), showed decreased inhibitory activity on cell growth.
Variants in the DYX2 locus are associated with altered brain activation in reading-related brain regions in subjects with reading disability.
Gruen et al., New Haven, United States. In Neuroimage, 2012
Genes on chromosome 6p22, including DCDC2, KIAA0319, and TTRAP, have been identified as RD associated genes.
TDP2 promotes repair of topoisomerase I-mediated DNA damage in the absence of TDP1.
El-Khamisy et al., Brighton, United Kingdom. In Nucleic Acids Res, 2012
Recently, we identified a second tyrosyl DNA phosphodiesterase (TDP2; aka TTRAP/EAPII) that possesses weak 3'-tyrosyl DNA phosphodiesterase (3'-TDP) activity, in vitro.
Biochemical characterization of human tyrosyl-DNA phosphodiesterase 2 (TDP2/TTRAP): a Mg(2+)/Mn(2+)-dependent phosphodiesterase specific for the repair of topoisomerase cleavage complexes.
Pommier et al., Bethesda, United States. In J Biol Chem, 2012
Biochemical characterization of human tyrosyl-DNA phosphodiesterase 2 (TDP2/TTRAP): a Mg(2+)/Mn(2+)-dependent phosphodiesterase specific for the repair of topoisomerase cleavage complexes.
Gene network profiling before and after transplantation in alcoholic cirrhosis liver transplant recipients.
Ferron et al., Granada, Spain. In Transplant Proc, 2012
Selected genes up-regulated before transplantation were: TNFRSF9 (tumor necrosis factor [TNF] receptor superfamily, member 9); IL2RB (interleukin-2 receptor beta); BCL2L2 (BCL2-like 2); NOX5 (NADPH) oxidase, EF-hand calcium binding domain 5); PEX5 (peroxisomal biogenesis factor 5); PPARG (peroxisome proliferator-activated receptor gamma); NIBP (IKK2 binding protein); NKIRAS2 (NFKappaBeta inhibitor interacting Ras-like 2); IL4 (interleukin-4); IL-4R (interleukin 4 receptor); ADH1A (alcohol dehydrogenase 1A, class 1); ALDH1L1 (aldehyde dehydrogenase 1 family, member L1); MPO (myeloperoxidase); NPPA (natriuretic peptide precursor A); BCL2A1 (BCL2-related protein A1); GADD45A (growth arrest and DNA-damage-inducible alpha); TEGT (Bax inhibitor 1); PIK3CA (phosphoinositide-3-kinase, catalytic, alpha polypeptide); IFNGR2 (interferon gamma receptor 2); JAK2 (Janus Kinase 2); FAS (Fas, TNF receptor superfamily, member 6); TANK (TRAF family member-associated NFKB activator); TTRAP (TRAF and TNF receptor-associated protein); and ANXA5 (annexin A5).
The PML nuclear bodies-associated protein TTRAP regulates ribosome biogenesis in nucleolar cavities upon proteasome inhibition.
Gustincich et al., Trieste, Italy. In Cell Death Differ, 2012
findings suggest a previously unidentified function for TTRAP and nucleolar cavities in ribosome biogenesis under stress.
Genetic variants of FOXP2 and KIAA0319/TTRAP/THEM2 locus are associated with altered brain activation in distinct language-related regions.
Dehaene et al., Gif-sur-Yvette, France. In J Neurosci, 2012
both FOXP2 and KIAA0319/TTRAP/THEM2 genes play an important role in human language development, but probably through different cerebral pathways.
Parkinson's disease DJ-1 L166P alters rRNA biogenesis by exclusion of TTRAP from the nucleolus and sequestration into cytoplasmic aggregates via TRAF6.
Zucchelli et al., Trieste, Italy. In Plos One, 2011
Upon proteasome impairment L166P activates the JNK/p38 MAPK apoptotic pathway by its interaction with TRAF and TNF Receptor Associated Protein (TTRAP).
Pleiotropic functions of EAPII/TTRAP/TDP2: cancer development, chemoresistance and beyond.
Li et al., Atlanta, United States. In Cell Cycle, 2011
EAPII (also called TTRAP, TDP2), a protein identified a decade ago, has recently been shown to function as an oncogenic factor.
Few Smad proteins and many Smad-interacting proteins yield multiple functions and action modes in TGFβ/BMP signaling in vivo.
Huylebroeck et al., Leuven, Belgium. In Cytokine Growth Factor Rev, 2011
In this survey, we selected appropriate examples on the BMP-Smads, with emphasis on Smad1 and Smad5, and on a number of SIPs, i.e. the CPSF subunit Smicl, Ttrap (Tdp2) and Sip1 (Zeb2, Zfhx1b) from our own research carried out in three different vertebrate models.
Oncogenic role of EAPII in lung cancer development and its activation of the MAPK-ERK pathway.
Li et al., Atlanta, United States. In Oncogene, 2011
EAPII is an oncogenic factor and the activation of MAPK-ERK signaling pathway by EAPII may contribute to lung cancer development.
TDP2/TTRAP is the major 5'-tyrosyl DNA phosphodiesterase activity in vertebrate cells and is critical for cellular resistance to topoisomerase II-induced DNA damage.
Caldecott et al., Brighton, United Kingdom. In J Biol Chem, 2011
an important mechanism for resistance to Top2-induced chromosome breakage and the possibility that TDP2 is a significant factor in cancer development and treatment
A human 5'-tyrosyl DNA phosphodiesterase that repairs topoisomerase-mediated DNA damage.
Caldecott et al., Brighton, United Kingdom. In Nature, 2009
TTRAP is the first human 5'-tyrosyl DNA phosphodiesterase to be identified, and we suggest that this enzyme is denoted tyrosyl DNA phosphodiesterase-2 (TDP2).
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