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
- FunctionsDNA binding / NAD+ ADP-ribosyltransferase activityProcessesbase-excision repair / DNA repair / extrinsic apoptotic signaling pathway / protein ADP-ribosylationComponentsnucleolus / 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
Resource Link UniProtKB ID Q9UGN5 UniProtKB Entry Name PARP2_HUMAN GenBank Protein ID 6688130 GenBank Gene ID AJ236912 HGNC ID HGNC:272 - General References
- 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. [Article]
- 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]
- 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. [Article]
- 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. [Article]
- 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. [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]
- 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. [Article]
- 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. [Article]
- 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. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB07232 Veliparib investigational unknown Details DB09074 Olaparib approved yes inhibitor Details DB12332 Rucaparib approved, investigational yes inhibitor Details DB11793 Niraparib approved, investigational yes inhibitor Details DB11760 Talazoparib approved, investigational yes inhibitor Details