| Synonyms |
ADP-ribosyltransferase diphtheria toxin-like 3, ARTD3, DNA ADP-ribosyltransferase PARP3, 2.4.2.-, IRT1, NAD(+) ADP-ribosyltransferase 3, ADPRT-3, Poly [ADP-ribose] polymerase 3, PARP-3, hPARP-3, Poly[ADP-ribose] synthase 3, pADPRT-3 | ADPRT3, ADPRTL3 |
| Function |
Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins and plays a key role in the response to DNA damage (PubMed:16924674, PubMed:20064938, PubMed:21211721, PubMed:21270334, PubMed:25043379, PubMed:24598253). Mediates mono-ADP-ribosylation of glutamate, aspartate or lysine residues on target proteins (PubMed:20064938, PubMed:25043379). In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (PubMed:25043379). Associates with a number of DNA repair factors and is involved in the response to exogenous and endogenous DNA strand breaks (PubMed:16924674, PubMed:21211721, PubMed:21270334). Together with APLF, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ) (PubMed:21211721). Cooperates with the XRRC6-XRCC5 (Ku70-Ku80) heterodimer to limit end-resection thereby promoting accurate NHEJ (PubMed:24598253). Involved in DNA repair by mediating mono-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism, such as XRRC5 and XRCC6 (PubMed:16924674, PubMed:24598253). ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (PubMed:16924674, PubMed:21211721, PubMed:21270334). May link the DNA damage surveillance network to the mitotic fidelity checkpoint (PubMed:16924674). In addition to proteins, also able to ADP-ribosylate DNA |
3.0
PARP3
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chemical inhibition