3.6.1.70	physiological function	3'-phosphate RNA ligase RtcB3 caps DNA and RNA 5'-PO4 ends to form GppDNA and GppRNA products, respectively. GppDNA formed by RtcB3 can be decapped to pDNA by the DNA repair enzyme aprataxin	-, 740627	
3.6.1.70	physiological function	aprataxin interacts with the repair proteins XRCC1, PARP-1 and p53 and colocalizes with XRCC1 along charged particle tracks on chromatin	740518	
3.6.1.70	physiological function	aprataxin is directly involved in DNA single-strand-break repair	740277	
3.6.1.70	physiological function	APTX interacts with X-ray repair cross-complementing group XRCC1, which has an essential role in single-strand DNA break repair. The 20 N-terminal amino acids of the forkhead-associated FHA-domain of APTX are important for its interaction with the C-terminal region (residues 492–574) of XRCC1. Poly(ADP–ribose) polymerase PARP-1 is also co-immunoprecipitated with APTX	739976	
3.6.1.70	physiological function	APTX suppresses DNA-ligase 1-catalyzed ligation of 8oxoG-containing DNA. In presence of APTX, the catalytic commitment of DNA ligase 1 to erroneous ligation is reduced by 70 and 90%, respectively, for the 8oxoG:A and 8oxoG:C substrates	754827	
3.6.1.70	physiological function	deletion of the Saccharomyces cerevisiae Hnt3 gene, which encodes the aprataxin homolog, in combination with known DNA repair genes. While Hnt3 single mutants are not sensitive to DNA damaging agents, loss of Hnt3 causes synergistic sensitivity to H2O2 in backgrounds that accumulate strand breaks with blocked termini, including lack of Apn1, Apn2, Tpp1 and Ntg1, Ntg2, Ogg1. Loss of HNT3 in Rad27 mutant cells, which are deficient in long-patch base excision repair, results in synergistic sensitivity to H2O2 and methylmethane sulfonate. Loss of Hnt3 also increases the sister chromatid exchange frequency. Hnt3 deletion partially rescues H2O2 sensitivity in recombination-deficient mutant Rad51 and mutant Rad52 cells	740352	
3.6.1.70	physiological function	depletion of aprataxin in human SHSY5Y neuroblastoma cells and primary skeletal muscle myoblasts results in mitochondrial dysfunction, revealed by reduced citrate synthase activity and mtDNA copy number. mtDNA, not nuclear DNA, has higher levels of background DNA damage on aprataxin knockdown	755241	
3.6.1.70	physiological function	interaction between aprataxin and nucleolin occurs through their respective N-terminal regions. In cells from patients with ataxia with oculomotor apraxia type 1, AOA1, lacking aprataxin, the stability of nucleolin is significantly reduced. Down-regulation of nucleolin by RNA interference does not affect aprataxin protein levels but abolishes its nucleolar localization	740519	
3.6.1.70	physiological function	poly-ADP ribose polymerase PARP-1 is required in the recruitment of aprataxin to sites of DNA breaks. Inhibition of PARP activity does not affect aprataxin activity in vitro, it retards its recruitment to sites of DNA damage in vivo	703960	
3.6.1.70	physiological function	the long-form but not the short-form aprataxin interacts with x-ray repair cross-complementing group XRCC1. Aprataxin and XRCC1 may constitute a multiprotein complex and are involved in single-strand DNA break repair	739862