PARP2

Poly [ADP-ribose] polymerase 2 is an enzyme that in humans is encoded by the PARP2 gene.[5][6][7] It is one of the PARP family of enzymes.

PARP2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPARP2, ADPRT2, ADPRTL2, ADPRTL3, ARTD2, PARP-2, pADPRT-2, poly(ADP-ribose) polymerase 2
External IDsOMIM: 607725 MGI: 1341112 HomoloGene: 4004 GeneCards: PARP2
Gene location (Human)
Chr.Chromosome 14 (human)[1]
Band14q11.2Start20,343,582 bp[1]
End20,357,905 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

10038

11546

Ensembl

ENSG00000129484

ENSMUSG00000036023

UniProt

Q9UGN5

O88554

RefSeq (mRNA)

NM_001042618
NM_005484

NM_009632

RefSeq (protein)

NP_001036083
NP_005475

NP_033762

Location (UCSC)Chr 14: 20.34 – 20.36 MbChr 14: 50.81 – 50.82 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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.[7]

In the plant species Arabidopsis thaliana, PARP2 plays more significant roles than PARP1 in protective responses to DNA damage and bacterial pathogenesis.[8] The plant PARP2 carries N-terminal SAP DNA binding motifs rather than the Zn-finger DNA binding motifs of plant and animal PARP1 proteins.[8]

PARP inhibitor drugs

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

Interactions

PARP2 has been shown to interact with XRCC1.[9]

References

  1. GRCh38: Ensembl release 89: ENSG00000129484 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000036023 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Johansson M (May 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.
  6. Yélamos J, Schreiber V, Dantzer F (April 2008). "Toward specific functions of poly(ADP-ribose) polymerase-2". Trends in Molecular Medicine. 14 (4): 169–78. doi:10.1016/j.molmed.2008.02.003. PMID 18353725.
  7. "Entrez Gene: PARP2 poly (ADP-ribose) polymerase family, member 2".
  8. Song J, Keppler BD, Wise RR, Bent AF (May 2015). "PARP2 Is the Predominant Poly(ADP-Ribose) Polymerase in Arabidopsis DNA Damage and Immune Responses". PLoS Genetics. 11 (5): e1005200. doi:10.1371/journal.pgen.1005200. PMC 4423837. PMID 25950582.
  9. Schreiber V, Amé JC, Dollé P, Schultz I, Rinaldi B, Fraulob V, Ménissier-de Murcia J, de Murcia G (June 2002). "Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1". The Journal of Biological Chemistry. 277 (25): 23028–36. doi:10.1074/jbc.M202390200. PMID 11948190.

Further reading

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