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Poly (ADP-ribose) polymerase 2
Protein PARP2 PDB 1gs0.png
PDB rendering based on 1gs0.
Available structures
PDB Ortholog search: PDBe, RCSB
External IDs OMIM607725 MGI1341112 HomoloGene4004 IUPHAR: 2772 ChEMBL: 5366 GeneCards: PARP2 Gene
EC number
RNA expression pattern
PBB GE PARP2 214086 s at tn.png
PBB GE PARP2 204752 x at tn.png
PBB GE PARP2 215773 x at tn.png
More reference expression data
Species Human Mouse
Entrez 10038 11546
Ensembl ENSG00000129484 ENSMUSG00000036023
UniProt Q9UGN5 O88554
RefSeq (mRNA) NM_001042618 NM_009632
RefSeq (protein) NP_001036083 NP_033762
Location (UCSC) Chr 14:
20.34 – 20.36 Mb
Chr 14:
50.81 – 50.82 Mb
PubMed search [1] [2]

Poly [ADP-ribose] polymerase 2 is an enzyme that in humans is encoded by the PARP2 gene.[1][2][3]


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]


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 journal = J. Biol. Chem." 277 (25). United States: 23028–36. doi:10.1074/jbc.M202390200. ISSN 0021-9258. PMID 11948190. 

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