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Identification
HMDB Protein ID HMDBP00916
Secondary Accession Numbers
  • 6204
Name Poly [ADP-ribose] polymerase 2
Synonyms
  1. ADPRT-2
  2. NAD(+) ADP-ribosyltransferase 2
  3. PARP-2
  4. Poly[ADP-ribose] synthase 2
  5. hPARP-2
  6. pADPRT-2
  7. ADP-ribosyltransferase diphtheria toxin-like 2
  8. ARTD2
Gene Name PARP2
Protein Type Unknown
Biological Properties
General Function Involved in 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.
Pathways
  • Base excision repair
Reactions
NAD + (ADP-D-ribosyl)(n)-acceptor → Niacinamide + (ADP-D-ribosyl)(n+1)-acceptor details
GO Classification
Biological Process
DNA repair
protein ADP-ribosylation
base-excision repair
Cellular Component
nucleolus
nucleoplasm
Function
catalytic activity
transferase activity
nad+ adp-ribosyltransferase activity
transferase activity, transferring pentosyl groups
transferase activity, transferring glycosyl groups
Molecular Function
NAD+ ADP-ribosyltransferase activity
DNA binding
Process
metabolic process
macromolecule metabolic process
protein amino acid adp-ribosylation
post-translational protein modification
macromolecule modification
protein modification process
Cellular Location
  1. Nucleus
Gene Properties
Chromosome Location 14
Locus 14q11.2-q12
SNPs PARP2
Gene Sequence
>1752 bp
ATGGCGGCGCGGCGGCGACGGAGCACCGGCGGCGGCAGGGCGAGAGCATTAAATGAAAGC
AAAAGAGTTAATAATGGCAACACGGCTCCAGAAGACTCTTCCCCTGCCAAGAAAACTCGT
AGATGCCAGAGACAGGAGTCGAAAAAGATGCCTGTGGCTGGAGGAAAAGCTAATAAGGAC
AGGACAGAAGACAAGCAAGATGGTATGCCAGGAAGGTCATGGGCCAGCAAAAGGGTCTCT
GAATCTGTGAAGGCCTTGCTGTTAAAGGGCAAAGCTCCTGTGGACCCAGAGTGTACAGCC
AAGGTGGGGAAGGCTCATGTGTATTGTGAAGGAAATGATGTCTATGATGTCATGCTAAAT
CAGACCAATCTCCAGTTCAACAACAACAAGTACTATCTGATTCAGCTATTAGAAGATGAT
GCCCAGAGGAACTTCAGTGTTTGGATGAGATGGGGCCGAGTTGGGAAAATGGGACAGCAC
AGCCTGGTGGCTTGTTCAGGCAATCTCAACAAGGCCAAGGAAATCTTTCAGAAGAAATTC
CTTGACAAAACGAAAAACAATTGGGAAGATCGAGAAAAGTTTGAGAAGGTGCCTGGAAAA
TATGATATGCTACAGATGGACTATGCCACCAATACTCAGGATGAAGAGGAAACAAAGAAA
GAGGAATCTCTTAAATCTCCCTTGAAGCCAGAGTCACAGCTAGATCTTCGGGTACAGGAG
TTAATAAAGTTGATCTGTAATGTTCAGGCCATGGAAGAAATGATGATGGAAATGAAGTAT
AATACCAAGAAAGCCCCACTTGGGAAGCTGACAGTGGCACAAATCAAGGCAGGTTACCAG
TCTCTTAAGAAGATTGAGGATTGTATTCGGGCTGGCCAGCATGGACGAGCTCTCATGGAA
GCATGCAATGAATTCTACACCAGGATTCCGCATGACTTTGGACTCCGTACTCCTCCACTA
ATCCGGACACAGAAGGAACTGTCAGAAAAAATACAATTACTAGAGGCTTTGGGAGACATT
GAAATTGCTATTAAGCTGGTGAAAACAGAGCTACAAAGCCCAGAACACCCATTGGACCAA
CACTATAGAAACCTACATTGTGCCTTGCGCCCCCTTGACCATGAAAGTTATGAGTTCAAA
GTGATTTCCCAGTACCTACAATCTACCCATGCTCCCACACACAGCGACTATACCATGACC
TTGCTGGATTTGTTTGAAGTGGAGAAGGATGGTGAGAAAGAAGCCTTCAGAGAGGACCTT
CATAACAGGATGCTTCTATGGCATGGTTCCAGGATGAGTAACTGGGTGGGAATCTTGAGC
CATGGGCTTCGAATTGCCCCACCTGAAGCTCCCATCACAGGTTACATGTTTGGGAAAGGA
ATCTACTTTGCTGACATGTCTTCCAAGAGTGCCAATTACTGCTTTGCCTCTCGCCTAAAG
AATACAGGACTGCTGCTCTTATCAGAGGTAGCTCTAGGTCAGTGTAATGAACTACTAGAG
GCCAATCCTAAGGCCGAAGGATTGCTTCAAGGTAAACATAGCACCAAGGGGCTGGGCAAG
ATGGCTCCCAGTTCTGCCCACTTCGTCACCCTGAATGGGAGTACAGTGCCATTAGGACCA
GCAAGTGACACAGGAATTCTGAATCCAGATGGTTATACCCTCAACTACAATGAATATATT
GTATATAACCCCAACCAGGTCCGTATGCGGTACCTTTTAAAGGTTCAGTTTAATTTCCTT
CAGCTGTGGTGA
Protein Properties
Number of Residues 583
Molecular Weight 64804.695
Theoretical pI 8.676
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Poly [ADP-ribose] polymerase 2
MAARRRRSTGGGRARALNESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKD
RTEDKQDGMPGRSWASKRVSESVKALLLKGKAPVDPECTAKVGKAHVYCEGNDVYDVMLN
QTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKF
LDKTKNNWEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEESLKSPLKPESQLDLRVQE
LIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALME
ACNEFYTRIPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQ
HYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFREDL
HNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLK
NTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTLNGSTVPLGP
ASDTGILNPDGYTLNYNEYIVYNPNQVRMRYLLKVQFNFLQLW
GenBank ID Protein 110825961
UniProtKB/Swiss-Prot ID Q9UGN5
UniProtKB/Swiss-Prot Entry Name PARP2_HUMAN
PDB IDs
GenBank Gene ID NM_005484.3
GeneCard ID PARP2
GenAtlas ID PARP2
HGNC ID HGNC:272
References
General References
  1. 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 ]
  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. 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 ]
  4. 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 ]
  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 ]