Protein: Poly [ADP-ribose] polymerase 2 (PARP-2) (hPARP-2) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 2) (ARTD2) (DNA ADP-ribosyltransferase PARP2) (EC 2.4.2.-) (NAD(+) ADP-ribosyltransferase 2) (ADPRT-2) (Poly[ADP-ribose] synthase 2) (pADPRT-2) (Protein poly-ADP-ribosyltransferase PARP2) (EC 2.4.2.-) (Q9UGN5)
Organism: Homo sapiens (Human)
Function: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. Mediates glutamate, aspartate or serine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1. Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP2 active site. PARP2 initiates the repair of double-strand DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks. HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP2 in order to limit the length of poly-ADP-ribose chains. Specifically mediates formation of branched poly-ADP-ribosylation. Branched poly-ADP-ribose chains are specifically recognized by some factors, such as APLF. In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex.
Subcellular location: Nucleus {ECO:0000269|PubMed:10364231, ECO:0000269|PubMed:26704974}. Chromosome {ECO:0000269|PubMed:26704974, ECO:0000269|PubMed:30104678, ECO:0000269|PubMed:30321391, ECO:0000269|PubMed:32939087, ECO:0000269|PubMed:33141820, ECO:0000269|PubMed:35349716}. Note=Recruited to DNA damage sites in a PARP1-dependent process: recognizes and binds poly-ADP-ribose chains produced by PARP1 at DNA damage sites via its N-terminus, leading to its recruitment. {ECO:0000269|PubMed:26704974, ECO:0000269|PubMed:30104678, ECO:0000269|PubMed:30321391, ECO:0000269|PubMed:32939087, ECO:0000269|PubMed:33141820, ECO:0000269|PubMed:35349716}.
Interaction partners:
- Histone PARylation factor 1
- DNA polymerase beta
- DNA repair protein XRCC1
- DNA ligase 3
- Poly
- Poly [ADP-ribose] polymerase 1
- Histone H2B type 1-J
- Histone H2A type 1-C
- X-ray repair cross-complementing protein 6
- Caspase-3
Sequence:
MAARRRRSTGGGRARALNESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKDRTEDKQDGMPGRSWASKRVSESVKALLLKGKAPVDPECTAKVGKAHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEESLKSPLKPESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALMEACNEFYTRIPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFREDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTLNGSTVPLGPASDTGILNPDGYTLNYNEYIVYNPNQVRMRYLLKVQFNFLQLW