Poly [ADP-ribose] polymerase 3
Details
- Name
- Poly [ADP-ribose] polymerase 3
- Synonyms
- 2.4.2.30
- ADP-ribosyltransferase diphtheria toxin-like 3
- ADPRT-3
- ADPRT3
- ADPRTL3
- ARTD3
- IRT1
- NAD(+) ADP-ribosyltransferase 3
- pADPRT-3
- PARP-3
- Poly[ADP-ribose] synthase 3
- Gene Name
- PARP3
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0007738|Poly [ADP-ribose] polymerase 3 MAPKPKPWVQTEGPEKKKGRQAGREEDPFRSTAEALKAIPAEKRIIRVDPTCPLSSNPGT QVYEDYNCTLNQTNIENNNNKFYIIQLLQDSNRFFTCWNHWGRVGEVGQSKINHFTRLED AKKDFEKKFREKTKNNWAERDHFVSHPGKYTLIEVQAEDEAQEAVVKVDRGPVRTVTKRV QPCSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEALEEAL KGPTDGGQSLEELSSHFYTVIPHNFGHSQPPPINSPELLQAKKDMLLVLADIELAQALQA VSEQEKTVEEVPHPLDRDYQLLKCQLQLLDSGAPEYKVIQTYLEQTGSNHRCPTLQHIWK VNQEGEEDRFQAHSKLGNRKLLWHGTNMAVVAAILTSGLRIMPHSGGRVGKGIYFASENS KSAGYVIGMKCGAHHVGYMFLGEVALGREHHINTDNPSLKSPPPGFDSVIARGHTEPDPT QDTELELDGQQVVVPQGQPVPCPEFSSSTFSQSEYLIYQESQCRLRYLLEVHL
- Number of residues
- 533
- Molecular Weight
- 60069.7
- Theoretical pI
- 6.73
- GO Classification
- Functionscatalytic activity / NAD+ ADP-ribosyltransferase activityProcessesDNA repair / double-strand break repair / positive regulation of DNA ligation / protein ADP-ribosylation / protein localization to site of double-strand break / regulation of mitotic spindle organization / telomere maintenanceComponentscentriole / nucleus / site of double-strand break
- General Function
- Nad+ adp-ribosyltransferase activity
- Specific Function
- Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Nucleus
- Gene sequence
>lcl|BSEQ0021378|Poly [ADP-ribose] polymerase 3 (PARP3) ATGTCCCTGCTTTTCTTGGCCATGGCTCCAAAGCCGAAGCCCTGGGTACAGACTGAGGGC CCTGAGAAGAAGAAGGGCCGGCAGGCAGGAAGGGAGGAGGACCCCTTCCGCTCCACCGCT GAGGCCCTCAAGGCCATACCCGCAGAGAAGCGCATAATCCGCGTGGATCCAACATGTCCA CTCAGCAGCAACCCCGGGACCCAGGTGTATGAGGACTACAACTGCACCCTGAACCAGACC AACATCGAGAACAACAACAACAAGTTCTACATCATCCAGCTGCTCCAAGACAGCAACCGC TTCTTCACCTGCTGGAACCGCTGGGGCCGTGTGGGAGAGGTCGGCCAGTCAAAGATCAAC CACTTCACAAGGCTAGAAGATGCAAAGAAGGACTTTGAGAAGAAATTTCGGGAAAAGACC AAGAACAACTGGGCAGAGCGGGACCACTTTGTGTCTCACCCGGGCAAGTACACACTTATC GAAGTACAGGCAGAGGATGAGGCCCAGGAAGCTGTGGTGAAGGTGGACAGAGGCCCAGTG AGGACTGTGACTAAGCGGGTGCAGCCCTGCTCCCTGGACCCAGCCACGCAGAAGCTCATC ACTAACATCTTCAGCAAGGAGATGTTCAAGAACACCATGGCCCTCATGGACCTGGATGTG AAGAAGATGCCCCTGGGAAAGCTGAGCAAGCAACAGATTGCACGGGGTTTCGAGGCCTTG GAGGCGCTGGAGGAGGCCCTGAAAGGCCCCACGGATGGTGGCCAAAGCCTGGAGGAGCTG TCCTCACACTTTTACACCGTCATCCCGCACAACTTCGGCCACAGCCAGCCCCCGCCCATC AATTCCCCTGAGCTTCTGCAGGCCAAGAAGGACATGCTGCTGGTGCTGGCGGACATCGAG CTGGCCCAGGCCCTGCAGGCAGTCTCTGAGCAGGAGAAGACGGTGGAGGAGGTGCCACAC CCCCTGGACCGAGACTACCAGCTTCTCAAGTGCCAGCTGCAGCTGCTAGACTCTGGAGCA CCTGAGTACAAGGTGATACAGACCTACTTAGAACAGACTGGCAGCAACCACAGGTGCCCT ACACTTCAACACATCTGGAAAGTAAACCAAGAAGGGGAGGAAGACAGATTCCAGGCCCAC TCCAAACTGGGTAATCGGAAGCTGCTGTGGCATGGCACCAACATGGCCGTGGTGGCCGCC ATCCTCACTAGTGGGCTCCGCATCATGCCACATTCTGGTGGGCGTGTTGGCAAGGGCATC TACTTTGCCTCAGAGAACAGCAAGTCAGCTGGATATGTTATTGGCATGAAGTGTGGGGCC CACCATGTCGGCTACATGTTCCTGGGTGAGGTGGCCCTGGGCAGAGAGCACCATATCAAC ACGGACAACCCCAGCTTGAAGAGCCCACCTCCTGGCTTCGACAGTGTCATTGCCCGAGGC CACACCGAGCCTGATCCGACCCAGGACACTGAGTTGGAGCTGGATGGCCAGCAAGTGGTG GTGCCCCAGGGCCAGCCTGTGCCCTGCCCAGAGTTCAGCAGCTCCACATTCTCCCAGAGC GAGTACCTCATCTACCAGGAGAGCCAGTGTCGCCTGCGCTACCTGCTGGAGGTCCACCTC TGA
- Chromosome Location
- 3
- Locus
- 3p21.31-p21.1
- External Identifiers
Resource Link UniProtKB ID Q9Y6F1 UniProtKB Entry Name PARP3_HUMAN GenBank Protein ID 29788060 GenBank Gene ID Y16836 HGNC ID HGNC:273 - General References
- Johansson M: A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues. Genomics. 1999 May 1;57(3):442-5. [Article]
- Augustin A, Spenlehauer C, Dumond H, Menissier-De Murcia J, Piel M, Schmit AC, Apiou F, Vonesch JL, Kock M, Bornens M, De Murcia G: PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression. J Cell Sci. 2003 Apr 15;116(Pt 8):1551-62. [Article]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [Article]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [Article]
- Rouleau M, McDonald D, Gagne P, Ouellet ME, Droit A, Hunter JM, Dutertre S, Prigent C, Hendzel MJ, Poirier GG: PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery. J Cell Biochem. 2007 Feb 1;100(2):385-401. [Article]
- Hottiger MO, Hassa PO, Luscher B, Schuler H, Koch-Nolte F: Toward a unified nomenclature for mammalian ADP-ribosyltransferases. Trends Biochem Sci. 2010 Apr;35(4):208-19. doi: 10.1016/j.tibs.2009.12.003. Epub 2010 Jan 26. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB07677 2-methyl-3,5,7,8-tetrahydro-4H-thiopyrano[4,3-d]pyrimidin-4-one experimental unknown Details DB08058 4-[3-(1,4-diazepan-1-ylcarbonyl)-4-fluorobenzyl]phthalazin-1(2H)-one experimental unknown Details DB08348 N~2~,N~2~-DIMETHYL-N~1~-(6-OXO-5,6-DIHYDROPHENANTHRIDIN-2-YL)GLYCINAMIDE experimental unknown Details DB09074 Olaparib approved yes inhibitor Details DB12332 Rucaparib approved, investigational yes inhibitor Details