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.-) (NAD(+) ADP-ribosyltransferase 3) (ADPRT-3) (Poly [ADP-ribose] polymerase 3) (PARP-3) (Poly[ADP-ribose] synthase 3) (pADPRT-3) (Q3ULW8)
Organism: Mus musculus (Mouse)
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 (By similarity). In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (By similarity). 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 (By similarity). ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (By similarity). Involved in single-strand break repair by catalyzing mono-ADP-ribosylation of histone H2B on 'Glu-2' (H2BE2ADPr) of nucleosomes containing nicked DNA (By similarity). Cooperates with the XRCC5-XRCC6 (Ku80-Ku70) heterodimer to limit end-resection thereby promoting accurate NHEJ (By similarity). Suppresses G-quadruplex (G4) structures in response to DNA damage (By similarity). 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) (By similarity). May link the DNA damage surveillance network to the mitotic fidelity checkpoint (By similarity). Acts as a negative regulator of immunoglobulin class switch recombination, probably by controlling the level of AICDA /AID on the chromatin. 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 (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y6F1}. Chromosome {ECO:0000250|UniProtKB:Q9Y6F1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y6F1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9Y6F1}. 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. In response to DNA damage, localizes to sites of double-strand break. Also localizes to single-strand breaks. Preferentially localized to the daughter centriole. {ECO:0000250|UniProtKB:Q9Y6F1}.
Interaction partners:
- Caspase-3
- Caspase-7
- Caspase-9
- Aprataxin and PNK-like factor
- Granzyme B
- X-ray repair cross-complementing protein 6
- Poly
- Histone PARylation factor 1
- Protein mono-ADP-ribosyltransferase PARP16
- Protein mono-ADP-ribosyltransferase PARP10
Sequence:
MAPKRKASVQTEGSKKRRQGTEEEDSFRSTAEALRAAPADNRVIRVDPSCPFSRNPGIQVHEDYDCTLNQTNIGNNNNKFYIIQLLEEGSRFFCWNRWGRVGEVGQSKMNHFTCLEDAKKDFKKKFWEKTKNKWEERDRFVAQPNKYTLIEVQGEAESQEAVVKALSPQVYSGPVRTVVKPCSLDPATQNLITNIFSKEMFKNAMTLMNLDVKKMPLGKLTKQQIARGFEALEALEEAMKNPTGDGQSLEELSSCFYTVIPHNFGRSRPPPINSPDVLQAKKDMLLVLADIELAQTLQAAPGEEEEKVEEVPHPLDRDYQLLRCQLQLLDSGESEYKAIQTYLKQTGNSYRCPDLRHVWKVNREGEGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRIMPHSGGRVGKGIYFASENSKSAGYVTTMHCGGHQVGYMFLGEVALGKEHHITIDDPSLKSPPSGFDSVIARGQTEPDPAQDIELELDGQPVVVPQGPPVQCPSFKSSSFSQSEYLIYKESQCRLRYLLEIHL