|Other Names||Tyrosyl-DNA phosphodiesterase 2, Tyr-DNA phosphodiesterase 2, hTDP2, 314-, 5'-tyrosyl-DNA phosphodiesterase, 5'-Tyr-DNA phosphodiesterase, ETS1-associated protein 2, ETS1-associated protein II, EAPII, TRAF and TNF receptor-associated protein, Tyrosyl-RNA phosphodiesterase, VPg unlinkase, TDP2, EAP2, TTRAP|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. Hydrolyzes 5'- phosphoglycolates on protruding 5' ends on DNA double-strand breaks (DSBs) due to DNA damage by radiation and free radicals. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation. Has preference for single-stranded DNA or duplex DNA with a 4 base pair overhang as substrate. Has also 3'- tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. Constitutes the major if not only 5'- tyrosyl-DNA phosphodiesterase in cells. Also acts as a 5'-tyrosyl- RNA phosphodiesterase following picornavirus infection: its activity is hijacked by picornavirus and acts by specifically cleaving the protein-RNA covalent linkage generated during the viral genomic RNA replication steps of a picornavirus infection, without impairing the integrity of viral RNA. Also acts as an adapter by participating in the specific activation of MAP3K7/TAK1 in response to TGF-beta: associates with components of the TGF- beta receptor-TRAF6-TAK1 signaling module and promotes their ubiquitination dependent complex formation. Involved in non- canonical TGF-beta induced signaling routes. May also act as a negative regulator of ETS1 and may inhibit NF-kappa-B activation. Acts as a regulator of ribosome biogenesis following stress.|
|Cellular Location||Nucleus. Nucleus, PML body. Nucleus, nucleolus. Cytoplasm. Note=Localizes to nucleolar cavities following stress; localization to nucleolus is dependent on PML protein. In case of infection by picornavirus, relocalizes to cytoplasmic sites distinct from those containing viral proteins associated with RNA replication or encapsidation|
|Tissue Location||Widely expressed.|
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This gene encodes a member of a superfamily of divalentcation-dependent phosphodiesterases. The encoded protein associateswith CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptorassociated factors (TRAFs), and inhibits nuclear factor-kappa-Bactivation. This protein has sequence and structural similaritieswith APE1 endonuclease, which is involved in both DNA repair andthe activation of transcription factors.
Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)Wang, B.Y., et al. Mol. Biol. Rep. 37(6):2809-2816(2010)Iijima, M., et al. Neurology 73(17):1348-1352(2009)Cortes Ledesma, F., et al. Nature 461(7264):674-678(2009)Zhang, J.Q., et al. Biochem. Biophys. Res. Commun. 387(2):256-260(2009)
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