Poly [ADP-ribose] polymerase 2

Details

Name
Poly [ADP-ribose] polymerase 2
Synonyms
  • 2.4.2.30
  • ADP-ribosyltransferase diphtheria toxin-like 2
  • ADPRT-2
  • ADPRT2
  • ADPRTL2
  • ARTD2
  • NAD(+) ADP-ribosyltransferase 2
  • pADPRT-2
  • PARP-2
  • Poly[ADP-ribose] synthase 2
Gene Name
PARP2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0007286|Poly [ADP-ribose] polymerase 2
MAARRRRSTGGGRARALNESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKD
RTEDKQDGMPGRSWASKRVSESVKALLLKGKAPVDPECTAKVGKAHVYCEGNDVYDVMLN
QTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKF
LDKTKNNWEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEESLKSPLKPESQLDLRVQE
LIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALME
ACNEFYTRIPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQ
HYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFREDL
HNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLK
NTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTLNGSTVPLGP
ASDTGILNPDGYTLNYNEYIVYNPNQVRMRYLLKVQFNFLQLW
Number of residues
583
Molecular Weight
66205.31
Theoretical pI
9.22
GO Classification
Functions
DNA binding / NAD+ ADP-ribosyltransferase activity
Processes
base-excision repair / DNA repair / extrinsic apoptotic signaling pathway / protein ADP-ribosylation
Components
nucleolus / nucleoplasm / nucleus
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Nucleus
Gene sequence
>lcl|BSEQ0012648|Poly [ADP-ribose] polymerase 2 (PARP2)
ATGGCGGCGCGGCGGCGACGGAGCACCGGCGGCGGCAGGGCGAGAGCATTAAATGAAAGC
AAAAGAGTTAATAATGGCAACACGGCTCCAGAAGACTCTTCCCCTGCCAAGAAAACTCGT
AGATGCCAGAGACAGGAGTCGAAAAAGATGCCTGTGGCTGGAGGAAAAGCTAATAAGGAC
AGGACAGAAGACAAGCAAGATGAATCTGTGAAGGCCTTGCTGTTAAAGGGCAAAGCTCCT
GTGGACCCAGAGTGTACAGCCAAGGTGGGGAAGGCTCATGTGTATTGTGAAGGAAATGAT
GTCTATGATGTCATGCTAAATCAGACCAATCTCCAGTTCAACAACAACAAGTACTATCTG
ATTCAGCTATTAGAAGATGATGCCCAGAGGAACTTCAGTGTTTGGATGAGATGGGGCCGA
GTTGGGAAAATGGGACAGCACAGCCTGGTGGCTTGTTCAGGCAATCTCAACAAGGCCAAG
GAAATCTTTCAGAAGAAATTCCTTGACAAAACGAAAAACAATTGGGAAGATCGAGAAAAG
TTTGAGAAGGTGCCTGGAAAATATGATATGCTACAGATGGACTATGCCACCAATACTCAG
GATGAAGAGGAAACAAAGAAAGAGGAATCTCTTAAATCTCCCTTGAAGCCAGAGTCACAG
CTAGATCTTCGGGTACAGGAGTTAATAAAGTTGATCTGTAATGTTCAGGCCATGGAAGAA
ATGATGATGGAAATGAAGTATAATACCAAGAAAGCCCCACTTGGGAAGCTGACAGTGGCA
CAAATCAAGGCAGGTTACCAGTCTCTTAAGAAGATTGAGGATTGTATTCGGGCTGGCCAG
CATGGACGAGCTCTCATGGAAGCATGCAATGAATTCTACACCAGGATTCCGCATGACTTT
GGACTCCGTACTCCTCCACTAATCCGGACACAGAAGGAACTGTCAGAAAAAATACAATTA
CTAGAGGCTTTGGGAGACATTGAAATTGCTATTAAGCTGGTGAAAACAGAGCTACAAAGC
CCAGAACACCCATTGGACCAACACTATAGAAACCTACATTGTGCCTTGCGCCCCCTTGAC
CATGAAAGTTATGAGTTCAAAGTGATTTCCCAGTACCTACAATCTACCCATGCTCCCACA
CACAGCGACTATACCATGACCTTGCTGGATTTGTTTGAAGTGGAGAAGGATGGTGAGAAA
GAAGCCTTCAGAGAGGACCTTCATAACAGGATGCTTCTATGGCATGGTTCCAGGATGAGT
AACTGGGTGGGAATCTTGAGCCATGGGCTTCGAATTGCCCCACCTGAAGCTCCCATCACA
GGTTACATGTTTGGGAAAGGAATCTACTTTGCTGACATGTCTTCCAAGAGTGCCAATTAC
TGCTTTGCCTCTCGCCTAAAGAATACAGGACTGCTGCTCTTATCAGAGGTAGCTCTAGGT
CAGTGTAATGAACTACTAGAGGCCAATCCTAAGGCCGAAGGATTGCTTCAAGGTAAACAT
AGCACCAAGGGGCTGGGCAAGATGGCTCCCAGTTCTGCCCACTTCGTCACCCTGAATGGG
AGTACAGTGCCATTAGGACCAGCAAGTGACACAGGAATTCTGAATCCAGATGGTTATACC
CTCAACTACAATGAATATATTGTATATAACCCCAACCAGGTCCGTATGCGGTACCTTTTA
AAGGTTCAGTTTAATTTCCTTCAGCTGTGGTGA
Chromosome Location
14
Locus
14q11.2-q12
External Identifiers
ResourceLink
UniProtKB IDQ9UGN5
UniProtKB Entry NamePARP2_HUMAN
GenBank Protein ID6688130
GenBank Gene IDAJ236912
HGNC IDHGNC:272
General References
  1. Ame JC, Rolli V, Schreiber V, Niedergang C, Apiou F, Decker P, Muller S, Hoger T, Menissier-de Murcia J, de Murcia G: PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase. J Biol Chem. 1999 Jun 18;274(25):17860-8. [PubMed:10364231]
  2. 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]
  3. Berghammer H, Ebner M, Marksteiner R, Auer B: pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans. FEBS Lett. 1999 Apr 23;449(2-3):259-63. [PubMed:10338144]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039]
  5. Schreiber V, Ame JC, Dolle P, Schultz I, Rinaldi B, Fraulob V, Menissier-de Murcia J, de Murcia G: 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. 2002 Jun 21;277(25):23028-36. Epub 2002 Apr 10. [PubMed:11948190]
  6. 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]
  7. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [PubMed:21269460]
  8. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. [PubMed:21406692]
  9. Karlberg T, Hammarstrom M, Schutz P, Svensson L, Schuler H: Crystal structure of the catalytic domain of human PARP2 in complex with PARP inhibitor ABT-888. Biochemistry. 2010 Feb 16;49(6):1056-8. doi: 10.1021/bi902079y. [PubMed:20092359]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB07232VeliparibinvestigationalunknownDetails
DB09074OlaparibapprovedyesinhibitorDetails
DB12332Rucaparibapproved, investigationalyesantagonistDetails
DB11793Niraparibapproved, investigationalyesantagonistDetails
DB11760Talazoparibapproved, investigationalyesinhibitorDetails