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
Functions
catalytic activity / NAD+ ADP-ribosyltransferase activity
Processes
DNA 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 maintenance
Components
centriole / 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
ResourceLink
UniProtKB IDQ9Y6F1
UniProtKB Entry NamePARP3_HUMAN
GenBank Protein ID29788060
GenBank Gene IDY16836
HGNC IDHGNC:273
General References
  1. 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. [PubMed:10329013]
  2. 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. [PubMed:12640039]
  3. 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. [PubMed:16641997]
  4. 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. [PubMed:15489334]
  5. 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. [PubMed:17974005]
  6. 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. [PubMed:16924674]
  7. 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. [PubMed:20106667]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB076772-methyl-3,5,7,8-tetrahydro-4H-thiopyrano[4,3-d]pyrimidin-4-oneexperimentalunknownDetails
DB080584-[3-(1,4-diazepan-1-ylcarbonyl)-4-fluorobenzyl]phthalazin-1(2H)-oneexperimentalunknownDetails
DB08348N~2~,N~2~-DIMETHYL-N~1~-(6-OXO-5,6-DIHYDROPHENANTHRIDIN-2-YL)GLYCINAMIDEexperimentalunknownDetails
DB09074OlaparibapprovedyesinhibitorDetails
DB12332Rucaparibapproved, investigationalyesantagonistDetails