PARP3

Poly (ADP-ribose) polymerase family, member 3
PDB rendering based on 2pa9.
Available structures PDB 2EOC, 3C49, 3C4H, 3CE0, 3FHB
Identifiers
Symbols	PARP3; ADPRT3; ADPRTL2; ADPRTL3; IRT1; PADPRT-3
External IDs	OMIM: 607726 MGI: 1891258 HomoloGene: 4005 GeneCards: PARP3 Gene
EC number	2.4.2.30
Gene Ontology Molecular function • catalytic activity • NAD+ ADP-ribosyltransferase activity • protein binding • transferase activity, transferring glycosyl groups Cellular component • nucleus • cytoplasm • centriole • microtubule organizing center • cytoskeleton Biological process • DNA repair • protein ADP-ribosylation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10039	235587
Ensembl	ENSG00000041880	ENSMUSG00000023249
UniProt	Q9Y6F1	n/a
RefSeq (mRNA)	NM_001003931.2	NM_145619.2
RefSeq (protein)	NP_001003931.2	NP_663594.2
Location (UCSC)	Chr 3: 51.98 – 51.98 Mb	Chr 9: 106.37 – 106.38 Mb
PubMed search	[1]	[2]

Poly [ADP-ribose] polymerase 3 is an enzyme that in humans is encoded by the PARP3 gene.^[1][2]

The protein encoded by this gene belongs to the PARP family. These enzymes modify nuclear proteins by poly-ADP-ribosylation, which is required for DNA repair, regulation of apoptosis, and maintenance of genomic stability. This gene encodes the poly(ADP-ribosyl)transferase 3, which is preferentially localized to the daughter centriole throughout the cell cycle. Alternatively spliced transcript variants encoding different isoforms have been identified.^[2]

References

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. ^ ^{a b} "Entrez Gene: PARP3 poly (ADP-ribose) polymerase family, member 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10039. 

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. Bibcode 1980BpJ....29....1B. doi:10.1016/S0006-3495(80)85114-9. PMC 1328658. PMID 7260241. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1328658. 
• Borggrefe T, Wabl M, Akhmedov AT, Jessberger R (1998). "A B-cell-specific DNA recombination complex.". J. Biol. Chem. 273 (27): 17025–35. doi:10.1074/jbc.273.27.17025. PMID 9642267. 
• 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. doi:10.1016/S0014-5793(99)00448-2. PMID 10338144. 
• 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. 
• Dias Neto E, Correa RG, Verjovski-Almeida S, et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags.". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16267. 
• Glowacki G, Braren R, Cetkovic-Cvrlje M, et al. (2001). "Structure, chromosomal localization, and expression of the gene for mouse ecto-mono(ADP-ribosyl)transferase ART5.". Gene 275 (2): 267–77. doi:10.1016/S0378-1119(01)00608-4. PMID 11587854. 
• Wistow G, Bernstein SL, Wyatt MK, et al. (2002). "Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants.". Mol. Vis. 8: 205–20. PMID 12107410. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Augustin A, Spenlehauer C, Dumond H, et al. (2004). "PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression.". J. Cell. Sci. 116 (Pt 8): 1551–62. doi:10.1242/jcs.00341. PMID 12640039. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
• Rouleau M, McDonald D, Gagné P, et al. (2007). "PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery.". J. Cell. Biochem. 100 (2): 385–401. doi:10.1002/jcb.21051. PMID 16924674. 
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.