PARP2

PARP2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3KCZ, 3KJD, 4PJV, 4TVJ, 4ZZX, 4ZZY, 5DSY, 5D5K
Identifiers
Aliases	PARP2, ADPRT2, ADPRTL2, ADPRTL3, ARTD2, PARP-2, pADPRT-2, poly(ADP-ribose) polymerase 2
External IDs	OMIM: 607725 MGI: 1341112 HomoloGene: 4004 GeneCards: PARP2
Gene location (Human)
Chr.	Chromosome 14 (human)
End	20,357,904 bp
Gene location (Mouse)
Chr.	Chromosome 14 (mouse)
End	51,058,758 bp
RNA expression pattern
	Top expressed in
	cerebellar hemisphere; ; Brodmann area 9; ; ganglionic eminence; ; prefrontal cortex; ; cerebellar vermis; ; anterior pituitary; ; tibial nerve; ; cingulate gyrus; ; middle temporal gyrus; ; nucleus accumbens;
	Top expressed in
	otic placode; ; primitive streak; ; spermatocyte; ; saccule; ; morula; ; abdominal wall; ; spleen; ; thymus; ; blood; ; vas deferens;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	transferase activity; DNA binding; protein binding; DNA ligase (ATP) activity; glycosyltransferase activity; NAD+ ADP-ribosyltransferase activity; protein ADP-ribosylase activity; NAD DNA ADP-ribosyltransferase activity;
Cellular component	cytoplasm; nucleolus; nucleus; nucleoplasm;
Biological process	DNA ligation involved in DNA repair; lagging strand elongation; protein ADP-ribosylation; DNA repair; extrinsic apoptotic signaling pathway; base-excision repair; peptidyl-serine ADP-ribosylation; positive regulation of cell growth involved in cardiac muscle cell development; negative regulation of neuron death; double-strand break repair; protein poly-ADP-ribosylation; DNA ADP-ribosylation; cellular response to DNA damage stimulus;
	Sources:Amigo / QuickGO
Orthologs
	10038
	11546
	ENSG00000129484
	ENSMUSG00000036023
	Q9UGN5
	O88554
	NM_001042618; NM_005484
	NM_009632
	NP_001036083; NP_005475
	NP_033762
	Wikidata
View/Edit Human	View/Edit Mouse

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.

Function edit

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 edit

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

Interactions edit

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

PARP2 also interacts with HPF1.^[10]^[11]^[12]

PARP2 binds to and bridges blunt DNA ends.^[12]^[13]^[14]

References edit

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000129484 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000036023 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ ^a ^b "Entrez Gene: PARP2 poly (ADP-ribose) polymerase family, member 2".
^ ^a ^b 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.
^ 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.
^ Gibbs-Seymour I, Fontana P, Rack JG, Ahel I (5 May 2016). "HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity". Molecular Cell. 62 (3): 432–442. doi:10.1016/j.molcel.2016.03.008. PMC 4858568. PMID 27067600.
^ Suskiewicz MJ, Zobel F, Ogden TE, Fontana P, Ariza A, Yang JC, Zhu K, Bracken L, Hawthorne WJ, Ahel D, Neuhaus D, Ahel I (March 2020). "HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation". Nature. 579 (7800): 598–602. Bibcode:2020Natur.579..598S. doi:10.1038/s41586-020-2013-6. PMC 7104379. PMID 32028527.
^ ^a ^b Gaullier G, Roberts G, Muthurajan UM, Bowerman S, Rudolph J, Mahadevan J, Jha A, Rae PS, Luger K (3 November 2020). "Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1". PLOS ONE. 15 (11): e0240932. Bibcode:2020PLoSO..1540932G. doi:10.1371/journal.pone.0240932. PMC 7608914. PMID 33141820.
^ Obaji E, Haikarainen T, Lehtiö L (14 December 2018). "Structural basis for DNA break recognition by ARTD2/PARP2". Nucleic Acids Research. 46 (22): 12154–12165. doi:10.1093/nar/gky927. PMC 6294510. PMID 30321391.
^ Bilokapic S, Suskiewicz MJ, Ahel I, Halic M (September 2020). "Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin". Nature. 585 (7826): 609–613. Bibcode:2020Natur.585..609B. doi:10.1038/s41586-020-2725-7. PMC 7529888. PMID 32939087.

External links edit

PARP2 human gene location in the UCSC Genome Browser.
PARP2 human gene details in the UCSC Genome Browser.

This article on a gene on human chromosome 14 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000129484 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid10329013-5] 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.

[pmid18353725-6] 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.

[entrez-7] "Entrez Gene: PARP2 poly (ADP-ribose) polymerase family, member 2".

[Song2015-8] 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.

[pmid11948190-9] 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.

[pmid27067600-10] Gibbs-Seymour I, Fontana P, Rack JG, Ahel I (5 May 2016). "HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity". Molecular Cell. 62 (3): 432–442. doi:10.1016/j.molcel.2016.03.008. PMC 4858568. PMID 27067600.

[pmid32028527-11] Suskiewicz MJ, Zobel F, Ogden TE, Fontana P, Ariza A, Yang JC, Zhu K, Bracken L, Hawthorne WJ, Ahel D, Neuhaus D, Ahel I (March 2020). "HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation". Nature. 579 (7800): 598–602. Bibcode:2020Natur.579..598S. doi:10.1038/s41586-020-2013-6. PMC 7104379. PMID 32028527.

[pmid33141820-12] Gaullier G, Roberts G, Muthurajan UM, Bowerman S, Rudolph J, Mahadevan J, Jha A, Rae PS, Luger K (3 November 2020). "Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1". PLOS ONE. 15 (11): e0240932. Bibcode:2020PLoSO..1540932G. doi:10.1371/journal.pone.0240932. PMC 7608914. PMID 33141820.

[pmid30321391-13] Obaji E, Haikarainen T, Lehtiö L (14 December 2018). "Structural basis for DNA break recognition by ARTD2/PARP2". Nucleic Acids Research. 46 (22): 12154–12165. doi:10.1093/nar/gky927. PMC 6294510. PMID 30321391.

[pmid32939087-14] Bilokapic S, Suskiewicz MJ, Ahel I, Halic M (September 2020). "Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin". Nature. 585 (7826): 609–613. Bibcode:2020Natur.585..609B. doi:10.1038/s41586-020-2725-7. PMC 7529888. PMID 32939087.

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