Poly [ADP-ribose] polymerase 1

Details

Name
Poly [ADP-ribose] polymerase 1
Synonyms
  • 2.4.2.30
  • ADP-ribosyltransferase diphtheria toxin-like 1
  • ADPRT
  • ADPRT 1
  • ARTD1
  • NAD(+) ADP-ribosyltransferase 1
  • PARP-1
  • Poly[ADP-ribose] synthase 1
  • PPOL
Gene Name
PARP1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0016533|Poly [ADP-ribose] polymerase 1
MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKV
GHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKS
NRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQ
LKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKA
QNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSG
QLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPE
TSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLT
GTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSP
WGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLE
HSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNK
LEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPG
TKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAV
SQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRG
GSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIE
REGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADM
VSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSA
NISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW
Number of residues
1014
Molecular Weight
113082.945
Theoretical pI
9.34
GO Classification
Functions
chromatin binding / DNA binding / enzyme binding / identical protein binding / NAD binding / NAD+ ADP-ribosyltransferase activity / poly(A) RNA binding / protein kinase binding / protein N-terminus binding / transcription factor binding / zinc ion binding
Processes
base-excision repair / behavioral response to cocaine / cellular protein metabolic process / cellular response to DNA damage stimulus / cellular response to insulin stimulus / cellular response to oxidative stress / cellular response to superoxide / DNA damage response, detection of DNA damage / DNA repair / double-strand break repair / double-strand break repair via homologous recombination / gene expression / global genome nucleotide-excision repair / macrophage differentiation / mitochondrial DNA metabolic process / mitochondrial DNA repair / mitochondrion organization / negative regulation of transcription from RNA polymerase II promoter / nucleotide-excision repair / nucleotide-excision repair, DNA damage recognition / nucleotide-excision repair, DNA incision / positive regulation of cardiac muscle hypertrophy / positive regulation of SMAD protein import into nucleus / positive regulation of transcription from RNA polymerase II promoter / positive regulation of transcription regulatory region DNA binding / post-translational protein modification / protein ADP-ribosylation / protein autoprocessing / protein modification process / protein poly-ADP-ribosylation / protein sumoylation / regulation of cellular protein localization / regulation of growth rate / regulation of single strand break repair / signal transduction involved in regulation of gene expression / telomere maintenance / transcription from RNA polymerase II promoter / transcription initiation from RNA polymerase II promoter / transcription, DNA-templated / transforming growth factor beta receptor signaling pathway
Components
membrane / mitochondrion / nuclear chromosome, telomeric region / nuclear envelope / nucleolus / nucleoplasm / nucleus / protein complex / transcription factor complex
General Function
Zinc ion binding
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. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Nucleus
Gene sequence
>lcl|BSEQ0016534|Poly [ADP-ribose] polymerase 1 (PARP1)
ATGGCGGAGTCTTCGGATAAGCTCTATCGAGTCGAGTACGCCAAGAGCGGGCGCGCCTCT
TGCAAGAAATGCAGCGAGAGCATCCCCAAGGACTCGCTCCGGATGGCCATCATGGTGCAG
TCGCCCATGTTTGATGGAAAAGTCCCACACTGGTACCACTTCTCCTGCTTCTGGAAGGTG
GGCCACTCCATCCGGCACCCTGACGTTGAGGTGGATGGGTTCTCTGAGCTTCGGTGGGAT
GACCAGCAGAAAGTCAAGAAGACAGCGGAAGCTGGAGGAGTGACAGGCAAAGGCCAGGAT
GGAATTGGTAGCAAGGCAGAGAAGACTCTGGGTGACTTTGCAGCAGAGTATGCCAAGTCC
AACAGAAGTACGTGCAAGGGGTGTATGGAGAAGATAGAAAAGGGCCAGGTGCGCCTGTCC
AAGAAGATGGTGGACCCGGAGAAGCCACAGCTAGGCATGATTGACCGCTGGTACCATCCA
GGCTGCTTTGTCAAGAACAGGGAGGAGCTGGGTTTCCGGCCCGAGTACAGTGCGAGTCAG
CTCAAGGGCTTCAGCCTCCTTGCTACAGAGGATAAAGAAGCCCTGAAGAAGCAGCTCCCA
GGAGTCAAGAGTGAAGGAAAGAGAAAAGGCGATGAGGTGGATGGAGTGGATGAAGTGGCG
AAGAAGAAATCTAAAAAAGAAAAAGACAAGGATAGTAAGCTTGAAAAAGCCCTAAAGGCT
CAGAACGACCTGATCTGGAACATCAAGGACGAGCTAAAGAAAGTGTGTTCAACTAATGAC
CTGAAGGAGCTACTCATCTTCAACAAGCAGCAAGTGCCTTCTGGGGAGTCGGCGATCTTG
GACCGAGTAGCTGATGGCATGGTGTTCGGTGCCCTCCTTCCCTGCGAGGAATGCTCGGGT
CAGCTGGTCTTCAAGAGCGATGCCTATTACTGCACTGGGGACGTCACTGCCTGGACCAAG
TGTATGGTCAAGACACAGACACCCAACCGGAAGGAGTGGGTAACCCCAAAGGAATTCCGA
GAAATCTCTTACCTCAAGAAATTGAAGGTTAAAAAACAGGACCGTATATTCCCCCCAGAA
ACCAGCGCCTCCGTGGCGGCCACGCCTCCGCCCTCCACAGCCTCGGCTCCTGCTGCTGTG
AACTCCTCTGCTTCAGCAGATAAGCCATTATCCAACATGAAGATCCTGACTCTCGGGAAG
CTGTCCCGGAACAAGGATGAAGTGAAGGCCATGATTGAGAAACTCGGGGGGAAGTTGACG
GGGACGGCCAACAAGGCTTCCCTGTGCATCAGCACCAAAAAGGAGGTGGAAAAGATGAAT
AAGAAGATGGAGGAAGTAAAGGAAGCCAACATCCGAGTTGTGTCTGAGGACTTCCTCCAG
GACGTCTCCGCCTCCACCAAGAGCCTTCAGGAGTTGTTCTTAGCGCACATCTTGTCCCCT
TGGGGGGCAGAGGTGAAGGCAGAGCCTGTTGAAGTTGTGGCCCCAAGAGGGAAGTCAGGG
GCTGCGCTCTCCAAAAAAAGCAAGGGCCAGGTCAAGGAGGAAGGTATCAACAAATCTGAA
AAGAGAATGAAATTAACTCTTAAAGGAGGAGCAGCTGTGGATCCTGATTCTGGACTGGAA
CACTCTGCGCATGTCCTGGAGAAAGGTGGGAAGGTCTTCAGTGCCACCCTTGGCCTGGTG
GACATCGTTAAAGGAACCAACTCCTACTACAAGCTGCAGCTTCTGGAGGACGACAAGGAA
AACAGGTATTGGATATTCAGGTCCTGGGGCCGTGTGGGTACGGTGATCGGTAGCAACAAA
CTGGAACAGATGCCGTCCAAGGAGGATGCCATTGAGCACTTCATGAAATTATATGAAGAA
AAAACCGGGAACGCTTGGCACTCCAAAAATTTCACGAAGTATCCCAAAAAGTTCTACCCC
CTGGAGATTGACTATGGCCAGGATGAAGAGGCAGTGAAGAAGCTGACAGTAAATCCTGGC
ACCAAGTCCAAGCTCCCCAAGCCAGTTCAGGACCTCATCAAGATGATCTTTGATGTGGAA
AGTATGAAGAAAGCCATGGTGGAGTATGAGATCGACCTTCAGAAGATGCCCTTGGGGAAG
CTGAGCAAAAGGCAGATCCAGGCCGCATACTCCATCCTCAGTGAGGTCCAGCAGGCGGTG
TCTCAGGGCAGCAGCGACTCTCAGATCCTGGATCTCTCAAATCGCTTTTACACCCTGATC
CCCCACGACTTTGGGATGAAGAAGCCTCCGCTCCTGAACAATGCAGACAGTGTGCAGGCC
AAGGTGGAAATGCTTGACAACCTGCTGGACATCGAGGTGGCCTACAGTCTGCTCAGGGGA
GGGTCTGATGATAGCAGCAAGGATCCCATCGATGTCAACTATGAGAAGCTCAAAACTGAC
ATTAAGGTGGTTGACAGAGATTCTGAAGAAGCCGAGATCATCAGGAAGTATGTTAAGAAC
ACTCATGCAACCACACACAATGCGTATGACTTGGAAGTCATCGATATCTTTAAGATAGAG
CGTGAAGGCGAATGCCAGCGTTACAAGCCCTTTAAGCAGCTTCATAACCGAAGATTGCTG
TGGCACGGGTCCAGGACCACCAACTTTGCTGGGATCCTGTCCCAGGGTCTTCGGATAGCC
CCGCCTGAAGCGCCCGTGACAGGCTACATGTTTGGTAAAGGGATCTATTTCGCTGACATG
GTCTCCAAGAGTGCCAACTACTGCCATACGTCTCAGGGAGACCCAATAGGCTTAATCCTG
TTGGGAGAAGTTGCCCTTGGAAACATGTATGAACTGAAGCACGCTTCACATATCAGCAAG
TTACCCAAGGGCAAGCACAGTGTCAAAGGTTTGGGCAAAACTACCCCTGATCCTTCAGCT
AACATTAGTCTGGATGGTGTAGACGTTCCTCTTGGGACCGGGATTTCATCTGGTGTGAAT
GACACCTCTCTACTATATAACGAGTACATTGTCTATGATATTGCTCAGGTAAATCTGAAG
TATCTGCTGAAACTGAAATTCAATTTTAAGACCTCCCTGTGGTAA
Chromosome Location
1
Locus
1q41-q42
External Identifiers
ResourceLink
UniProtKB IDP09874
UniProtKB Entry NamePARP1_HUMAN
GenBank Protein ID1017423
GenBank Gene IDX16674
GenAtlas IDPARP1
HGNC IDHGNC:270
General References
  1. Uchida K, Morita T, Sato T, Ogura T, Yamashita R, Noguchi S, Suzuki H, Nyunoya H, Miwa M, Sugimura T: Nucleotide sequence of a full-length cDNA for human fibroblast poly(ADP-ribose) polymerase. Biochem Biophys Res Commun. 1987 Oct 29;148(2):617-22. [PubMed:3120710]
  2. Kurosaki T, Ushiro H, Mitsuuchi Y, Suzuki S, Matsuda M, Matsuda Y, Katunuma N, Kangawa K, Matsuo H, Hirose T, et al.: Primary structure of human poly(ADP-ribose) synthetase as deduced from cDNA sequence. J Biol Chem. 1987 Nov 25;262(33):15990-7. [PubMed:2824474]
  3. Cherney BW, McBride OW, Chen DF, Alkhatib H, Bhatia K, Hensley P, Smulson ME: cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase. Proc Natl Acad Sci U S A. 1987 Dec;84(23):8370-4. [PubMed:2891139]
  4. Auer B, Nagl U, Herzog H, Schneider R, Schweiger M: Human nuclear NAD+ ADP-ribosyltransferase(polymerizing): organization of the gene. DNA. 1989 Oct;8(8):575-80. [PubMed:2513174]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414]
  6. 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]
  7. Yokoyama Y, Kawamoto T, Mitsuuchi Y, Kurosaki T, Toda K, Ushiro H, Terashima M, Sumimoto H, Kuribayashi I, Yamamoto Y, et al.: Human poly(ADP-ribose) polymerase gene. Cloning of the promoter region. Eur J Biochem. 1990 Dec 12;194(2):521-6. [PubMed:2125269]
  8. Ogura T, Nyunoya H, Takahashi-Masutani M, Miwa M, Sugimura T, Esumi H: Characterization of a putative promoter region of the human poly(ADP-ribose) polymerase gene: structural similarity to that of the DNA polymerase beta gene. Biochem Biophys Res Commun. 1990 Mar 16;167(2):701-10. [PubMed:2108670]
  9. Maruyama T, Nara K, Yoshikawa H, Suzuki N: Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha and regulates interferon-gamma gene transcription in Th1 cells. Clin Exp Immunol. 2007 Jan;147(1):164-75. [PubMed:17177976]
  10. Schneider R, Auer B, Kuhne C, Herzog H, Klocker H, Burtscher HJ, Hirsch-Kauffmann M, Wintersberger U, Schweiger M: Isolation of a cDNA clone for human NAD+: protein ADP-ribosyltransferase. Eur J Cell Biol. 1987 Oct;44(2):302-7. [PubMed:3121332]
  11. Suzuki H, Uchida K, Shima H, Sato T, Okamoto T, Kimura T, Miwa M: Molecular cloning of cDNA for human poly(ADP-ribose) polymerase and expression of its gene during HL-60 cell differentiation. Biochem Biophys Res Commun. 1987 Jul 31;146(2):403-9. [PubMed:3113420]
  12. Gradwohl G, Menissier de Murcia JM, Molinete M, Simonin F, Koken M, Hoeijmakers JH, de Murcia G: The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA. Proc Natl Acad Sci U S A. 1990 Apr;87(8):2990-4. [PubMed:2109322]
  13. Ikejima M, Noguchi S, Yamashita R, Ogura T, Sugimura T, Gill DM, Miwa M: The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA. J Biol Chem. 1990 Dec 15;265(35):21907-13. [PubMed:2123876]
  14. Simonin F, Menissier-de Murcia J, Poch O, Muller S, Gradwohl G, Molinete M, Penning C, Keith G, de Murcia G: Expression and site-directed mutagenesis of the catalytic domain of human poly(ADP-ribose)polymerase in Escherichia coli. Lysine 893 is critical for activity. J Biol Chem. 1990 Nov 5;265(31):19249-56. [PubMed:2121735]
  15. Schreiber V, Molinete M, Boeuf H, de Murcia G, Menissier-de Murcia J: The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity. EMBO J. 1992 Sep;11(9):3263-9. [PubMed:1505517]
  16. Rolli V, O'Farrell M, Menissier-de Murcia J, de Murcia G: Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching. Biochemistry. 1997 Oct 7;36(40):12147-54. [PubMed:9315851]
  17. Dantzer F, Nasheuer HP, Vonesch JL, de Murcia G, Menissier-de Murcia J: Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication. Nucleic Acids Res. 1998 Apr 15;26(8):1891-8. [PubMed:9518481]
  18. Ariumi Y, Masutani M, Copeland TD, Mimori T, Sugimura T, Shimotohno K, Ueda K, Hatanaka M, Noda M: Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent protein kinase in vitro. Oncogene. 1999 Aug 12;18(32):4616-25. [PubMed:10467406]
  19. Gueven N, Becherel OJ, Kijas AW, Chen P, Howe O, Rudolph JH, Gatti R, Date H, Onodera O, Taucher-Scholz G, Lavin MF: Aprataxin, a novel protein that protects against genotoxic stress. Hum Mol Genet. 2004 May 15;13(10):1081-93. Epub 2004 Mar 25. [PubMed:15044383]
  20. Li Y, Oh HJ, Lau YF: The poly(ADP-ribose) polymerase 1 interacts with Sry and modulates its biological functions. Mol Cell Endocrinol. 2006 Sep 26;257-258:35-46. Epub 2006 Aug 9. [PubMed:16904257]
  21. Kanno S, Kuzuoka H, Sasao S, Hong Z, Lan L, Nakajima S, Yasui A: A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses. EMBO J. 2007 Apr 18;26(8):2094-103. Epub 2007 Mar 29. [PubMed:17396150]
  22. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed:17525332]
  23. Ahel I, Ahel D, Matsusaka T, Clark AJ, Pines J, Boulton SJ, West SC: Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins. Nature. 2008 Jan 3;451(7174):81-5. doi: 10.1038/nature06420. [PubMed:18172500]
  24. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648]
  25. Reinemund J, Seidel K, Steckelings UM, Zaade D, Klare S, Rompe F, Katerbaum M, Schacherl J, Li Y, Menk M, Schefe JH, Goldin-Lang P, Szabo C, Olah G, Unger T, Funke-Kaiser H: Poly(ADP-ribose) polymerase-1 (PARP-1) transcriptionally regulates angiotensin AT2 receptor (AT2R) and AT2R binding protein (ATBP) genes. Biochem Pharmacol. 2009 Jun 15;77(12):1795-805. doi: 10.1016/j.bcp.2009.02.025. Epub 2009 Mar 19. [PubMed:19344625]
  26. Martin N, Schwamborn K, Schreiber V, Werner A, Guillier C, Zhang XD, Bischof O, Seeler JS, Dejean A: PARP-1 transcriptional activity is regulated by sumoylation upon heat shock. EMBO J. 2009 Nov 18;28(22):3534-48. doi: 10.1038/emboj.2009.279. Epub 2009 Sep 24. [PubMed:19779455]
  27. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332]
  28. Ahel D, Horejsi Z, Wiechens N, Polo SE, Garcia-Wilson E, Ahel I, Flynn H, Skehel M, West SC, Jackson SP, Owen-Hughes T, Boulton SJ: Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1. Science. 2009 Sep 4;325(5945):1240-3. doi: 10.1126/science.1177321. Epub 2009 Aug 6. [PubMed:19661379]
  29. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861]
  30. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [PubMed:20068231]
  31. 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]
  32. 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]
  33. Chang HY, Fan CC, Chu PC, Hong BE, Lee HJ, Chang MS: hPuf-A/KIAA0020 modulates PARP-1 cleavage upon genotoxic stress. Cancer Res. 2011 Feb 1;71(3):1126-34. doi: 10.1158/0008-5472.CAN-10-1831. Epub 2011 Jan 25. [PubMed:21266351]
  34. Rodriguez MI, Gonzalez-Flores A, Dantzer F, Collard J, de Herreros AG, Oliver FJ: Poly(ADP-ribose)-dependent regulation of Snail1 protein stability. Oncogene. 2011 Oct 20;30(42):4365-72. doi: 10.1038/onc.2011.153. Epub 2011 May 16. [PubMed:21577210]
  35. Callow MG, Tran H, Phu L, Lau T, Lee J, Sandoval WN, Liu PS, Bheddah S, Tao J, Lill JR, Hongo JA, Davis D, Kirkpatrick DS, Polakis P, Costa M: Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt signaling. PLoS One. 2011;6(7):e22595. doi: 10.1371/journal.pone.0022595. Epub 2011 Jul 25. [PubMed:21799911]
  36. 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]
  37. Chaki M, Airik R, Ghosh AK, Giles RH, Chen R, Slaats GG, Wang H, Hurd TW, Zhou W, Cluckey A, Gee HY, Ramaswami G, Hong CJ, Hamilton BA, Cervenka I, Ganji RS, Bryja V, Arts HH, van Reeuwijk J, Oud MM, Letteboer SJ, Roepman R, Husson H, Ibraghimov-Beskrovnaya O, Yasunaga T, Walz G, Eley L, Sayer JA, Schermer B, Liebau MC, Benzing T, Le Corre S, Drummond I, Janssen S, Allen SJ, Natarajan S, O'Toole JF, Attanasio M, Saunier S, Antignac C, Koenekoop RK, Ren H, Lopez I, Nayir A, Stoetzel C, Dollfus H, Massoudi R, Gleeson JG, Andreoli SP, Doherty DG, Lindstrad A, Golzio C, Katsanis N, Pape L, Abboud EB, Al-Rajhi AA, Lewis RA, Omran H, Lee EY, Wang S, Sekiguchi JM, Saunders R, Johnson CA, Garner E, Vanselow K, Andersen JS, Shlomai J, Nurnberg G, Nurnberg P, Levy S, Smogorzewska A, Otto EA, Hildebrandt F: Exome capture reveals ZNF423 and CEP164 mutations, linking renal ciliopathies to DNA damage response signaling. Cell. 2012 Aug 3;150(3):533-48. doi: 10.1016/j.cell.2012.06.028. [PubMed:22863007]
  38. Ahmad Y, Boisvert FM, Lundberg E, Uhlen M, Lamond AI: Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization. Mol Cell Proteomics. 2012 Mar;11(3):M111.013680. doi: 10.1074/mcp.M111.013680. Epub 2011 Oct 16. [PubMed:22002106]
  39. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [PubMed:22814378]
  40. Yan Q, Xu R, Zhu L, Cheng X, Wang Z, Manis J, Shipp MA: BAL1 and its partner E3 ligase, BBAP, link Poly(ADP-ribose) activation, ubiquitylation, and double-strand DNA repair independent of ATM, MDC1, and RNF8. Mol Cell Biol. 2013 Feb;33(4):845-57. doi: 10.1128/MCB.00990-12. Epub 2012 Dec 10. [PubMed:23230272]
  41. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569]
  42. Hendriks IA, D'Souza RC, Yang B, Verlaan-de Vries M, Mann M, Vertegaal AC: Uncovering global SUMOylation signaling networks in a site-specific manner. Nat Struct Mol Biol. 2014 Oct;21(10):927-36. doi: 10.1038/nsmb.2890. Epub 2014 Sep 14. [PubMed:25218447]
  43. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed:16959974]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02498Carba-Nicotinamide-Adenine-DinucleotideexperimentalunknownDetails
DB030722-{3-[4-(4-Fluorophenyl)-3,6-Dihydro-1(2h)-Pyridinyl]Propyl}-8-Methyl-4(3h)-QuinazolinoneexperimentalunknownDetails
DB030733-MethoxybenzamideexperimentalunknownDetails
DB035092-(4-Chlorophenyl)-5-QuinoxalinecarboxamideexperimentalunknownDetails
DB037223,4-Dihydro-5-Methyl-IsoquinolinoneexperimentalunknownDetails
DB02701Nicotinamideapproved, investigationalunknownbinderDetails
DB13877IniparibinvestigationalunknownDetails
DB070966-AMINO-BENZO[DE]ISOQUINOLINE-1,3-DIONEexperimentalunknownDetails
DB07232VeliparibinvestigationalunknownDetails
DB07330trans-4-(7-carbamoyl-1H-benzimidazol-2-yl)-1-propylpiperidiniumexperimentalunknownDetails
DB040102-(3'-Methoxyphenyl) Benzimidazole-4-CarboxamideexperimentalunknownDetails
DB077875-FLUORO-1-[4-(4-PHENYL-3,6-DIHYDROPYRIDIN-1(2H)-YL)BUTYL]QUINAZOLINE-2,4(1H,3H)-DIONEexperimentalunknownDetails
DB02690NU1025experimentalunknownDetails
DB09074OlaparibapprovedyesinhibitorDetails
DB12332Rucaparibapproved, investigationalyesantagonistDetails
DB11793Niraparibapproved, investigationalyesantagonistDetails
DB00277TheophyllineapprovedunknownDetails
DB01593Zincapproved, investigationalunknownDetails
DB14487Zinc acetateapproved, investigationalunknownDetails
DB14533Zinc chlorideapproved, investigationalunknownDetails
DB11760Talazoparibapproved, investigationalyesinhibitorDetails