Protein: Protein mono-ADP-ribosyltransferase PARP3 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 3) (ARTD3) (DNA ADP-ribosyltransferase PARP3) (EC 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) (Q9Y6F1)
Organism: Homo sapiens (Human)
Function: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins and plays a key role in the response to DNA damage. Mediates mono-ADP-ribosylation of glutamate, aspartate or lysine residues on target proteins. In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation. 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 histone H2B, XRCC5 and XRCC6. ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Involved in single-strand break repair by catalyzing mono-ADP-ribosylation of histone H2B on 'Glu-2' (H2BE2ADPr) of nucleosomes containing nicked DNA. Cooperates with the XRCC5-XRCC6 (Ku80-Ku70) heterodimer to limit end-resection thereby promoting accurate NHEJ. Suppresses G-quadruplex (G4) structures in response to DNA damage. Associates with a number of DNA repair factors and is involved in the response to exogenous and endogenous DNA strand breaks. Together with APLF, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ). May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Acts as a negative regulator of immunoglobulin class switch recombination, probably by controlling the level of AICDA /AID on the chromatin (By similarity). In addition to proteins, also able to ADP-ribosylate DNA: mediates DNA mono-ADP-ribosylation of DNA strand break termini via covalent addition of a single ADP-ribose moiety to a 5'- or 3'-terminal phosphate residues in DNA containing multiple strand breaks.
Subcellular location: Nucleus {ECO:0000269|PubMed:16924674}. Chromosome {ECO:0000269|PubMed:21270334, ECO:0000269|PubMed:27530147, ECO:0000269|PubMed:28447610}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10329013}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:10329013}. Note=Almost exclusively localized in the nucleus and appears in numerous small foci and a small number of larger foci whereas a centrosomal location has not been detected (PubMed:16924674). In response to DNA damage, localizes to sites of double-strand break (PubMed:21270334, PubMed:28447610). Also localizes to single-strand breaks (PubMed:27530147). Preferentially localized to the daughter centriole (PubMed:10329013). {ECO:0000269|PubMed:10329013, ECO:0000269|PubMed:16924674, ECO:0000269|PubMed:21270334, ECO:0000269|PubMed:27530147, ECO:0000269|PubMed:28447610}.
Interaction partners:
- Caspase-3
- Caspase-9
- Caspase-7
- Granzyme B
- Aprataxin and PNK-like factor
- Poly
- Protein mono-ADP-ribosyltransferase PARP16
- Protein mono-ADP-ribosyltransferase PARP10
- X-ray repair cross-complementing protein 6
- Protein mono-ADP-ribosyltransferase PARP15
Sequence:
MAPKPKPWVQTEGPEKKKGRQAGREEDPFRSTAEALKAIPAEKRIIRVDPTCPLSSNPGTQVYEDYNCTLNQTNIENNNNKFYIIQLLQDSNRFFTCWNRWGRVGEVGQSKINHFTRLEDAKKDFEKKFREKTKNNWAERDHFVSHPGKYTLIEVQAEDEAQEAVVKVDRGPVRTVTKRVQPCSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEALEEALKGPTDGGQSLEELSSHFYTVIPHNFGHSQPPPINSPELLQAKKDMLLVLADIELAQALQAVSEQEKTVEEVPHPLDRDYQLLKCQLQLLDSGAPEYKVIQTYLEQTGSNHRCPTLQHIWKVNQEGEEDRFQAHSKLGNRKLLWHGTNMAVVAAILTSGLRIMPHSGGRVGKGIYFASENSKSAGYVIGMKCGAHHVGYMFLGEVALGREHHINTDNPSLKSPPPGFDSVIARGHTEPDPTQDTELELDGQQVVVPQGQPVPCPEFSSSTFSQSEYLIYQESQCRLRYLLEVHL