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Protein PARP2 PDB 1gs0.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases PARP2, ADPRT2, ADPRTL2, ADPRTL3, ARTD2, PARP-2, pADPRT-2, poly(ADP-ribose) polymerase 2
External IDs MGI: 1341112 HomoloGene: 4004 GeneCards: 10038
RNA expression pattern
PBB GE PARP2 204752 x at tn.png

PBB GE PARP2 214086 s at tn.png

PBB GE PARP2 215773 x at tn.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 14: 20.34 – 20.36 Mb Chr 14: 50.81 – 50.82 Mb
PubMed search [1] [2]
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Poly [ADP-ribose] polymerase 2 is an enzyme that in humans is encoded by the PARP2 gene.[1][2][3] It is one of the PARP family of enzymes.


This gene encodes poly(ADP-ribosyl)transferase-like 2 protein, which contains a catalytic domain and is capable of catalyzing a poly(ADP-ribosyl)ation reaction. This protein has a catalytic domain which is homologous to that of poly (ADP-ribosyl) transferase, but lacks an N-terminal DNA binding domain which activates the C-terminal catalytic domain of poly (ADP-ribosyl) transferase. The basic residues within the N-terminal region of this protein may bear potential DNA-binding properties, and may be involved in the nuclear and/or nucleolar targeting of the protein. Two alternatively spliced transcript variants encoding distinct isoforms have been found.[3]

PARP inhibitor drugs[edit]

Some PARP inhibitor anti-cancer drugs (primarily aimed at PARP1) also inhibit PARP2, eg. niraparib.


PARP2 has been shown to interact with XRCC1.[4]


  1. ^ Johansson M (Aug 1999). "A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues". Genomics 57 (3): 442–5. doi:10.1006/geno.1999.5799. PMID 10329013. 
  2. ^ Yélamos J, Schreiber V, Dantzer F (Apr 2008). "Toward specific functions of poly(ADP-ribose) polymerase-2". Trends Mol Med 14 (4): 169–78. doi:10.1016/j.molmed.2008.02.003. PMID 18353725. 
  3. ^ a b "Entrez Gene: PARP2 poly (ADP-ribose) polymerase family, member 2". 
  4. ^ Schreiber V, Amé JC, Dollé P, Schultz I, Rinaldi B, Fraulob V, Ménissier-de Murcia J, de Murcia G (Jun 2002). "Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1". J. Biol. Chem. (United States) 277 (25): 23028–36. doi:10.1074/jbc.M202390200. ISSN 0021-9258. PMID 11948190. 

Further reading[edit]

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