PARP2

From Wikipedia, the free encyclopedia

Poly (ADP-ribose) polymerase family, member 2

PDB rendering based on 1gs0.

Available structures: 1gs0

Identifiers

Symbol(s)

PARP2; ADPRT2; ADPRTL2; ADPRTL3; PARP-2; pADPRT-2

External IDs

OMIM: 607725 MGI: 1341112 HomoloGene: 4004

Gene ontology
Molecular Function:	• DNA binding • NAD+ ADP-ribosyltransferase activity • protein binding • transferase activity, transferring glycosyl groups
Cellular Component:	• nucleus
Biological Process:	• base-excision repair • protein amino acid ADP-ribosylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001042618 (mRNA)
NP_001036083 (protein)

NM_009632 (mRNA)
NP_033762 (protein)

Location

Chr 14: 19.88 - 19.9 Mb

Chr 14: 49.73 - 49.74 Mb

Pubmed search

[1]

[2]

Poly (ADP-ribose) polymerase family, member 2, also known as PARP2, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: PARP2 poly (ADP-ribose) polymerase family, member 2.

[edit] Further reading

Bashford CL, Chance B, Lloyd D, Poole RK (1981). "Oscillations of redox states in synchronously dividing cultures of Acanthamoeba castellanii and Schizosaccharomyces pombe.". Biophys. J. 29 (1): 1-11. PMID 7260241.
Johansson M (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.
Berghammer H, Ebner M, Marksteiner R, Auer B (1999). "pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans.". FEBS Lett. 449 (2-3): 259-63. PMID 10338144.
Amé JC, Rolli V, Schreiber V, et al. (1999). "PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase.". J. Biol. Chem. 274 (25): 17860-8. PMID 10364231.
Still IH, Vince P, Cowell JK (2000). "Identification of a novel gene (ADPRTL1) encoding a potential Poly(ADP-ribosyl)transferase protein.". Genomics 62 (3): 533-6. doi:10.1006/geno.1999.6024. PMID 10644454.
Schreiber V, Amé JC, Dollé P, et al. (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. 277 (25): 23028-36. doi:10.1074/jbc.M202390200. PMID 11948190.
Saxena A, Wong LH, Kalitsis P, et al. (2003). "Poly(ADP-ribose) polymerase 2 localizes to mammalian active centromeres and interacts with PARP-1, Cenpa, Cenpb and Bub3, but not Cenpc.". Hum. Mol. Genet. 11 (19): 2319-29. PMID 12217960.
Malanga M, Althaus FR (2004). "Poly(ADP-ribose) reactivates stalled DNA topoisomerase I and Induces DNA strand break resealing.". J. Biol. Chem. 279 (7): 5244-8. doi:10.1074/jbc.C300437200. PMID 14699148.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55-65. doi:10.1101/gr.4039406. PMID 16344560.
Maeda Y, Hunter TC, Loudy DE, et al. (2006). "PARP-2 interacts with TTF-1 and regulates expression of surfactant protein-B.". J. Biol. Chem. 281 (14): 9600-6. doi:10.1074/jbc.M510435200. PMID 16461352.
Chevanne M, Calia C, Zampieri M, et al. (2007). "Oxidative DNA damage repair and parp 1 and parp 2 expression in Epstein-Barr virus-immortalized B lymphocyte cells from young subjects, old subjects, and centenarians.". Rejuvenation Res 10 (2): 191-204. doi:10.1089/rej.2006.0514. PMID 17518695.