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PARP1 |
Protein FULL name:
poly [ADP-ribose] polymerase 1 [Homo sapiens].
PARP1 (Homo sapiens) is product of expression of PARP1 gene.
PARP1 is involved in:
BER in Homo sapiens
Keywords:
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.
CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
SUBUNIT: Component of a base excision repair (BER) complex, containing at least XRCC1, PARP2, POLB and LIG3. Homo- and heterodimer with PARP2. Interacts with PARP3, APTX and SRY. The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with TIAM2 and ZNF423 (By similarity). Interacts (when poly-ADP- ribosylated) with CHD1L. Interacts with the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression.
INTERACTION: Self; NbExp=1; IntAct=EBI-355676, EBI-355676; Q7Z2E3:APTX; NbExp=1; IntAct=EBI-355676, EBI-847814; P49715:CEBPA; NbExp=1; IntAct=EBI-355676, EBI-1172054; Q01094:E2F1; NbExp=2; IntAct=EBI-355676, EBI-448924; P04637:TP53; NbExp=1; IntAct=EBI-355676, EBI-366083; Q14191:WRN; NbExp=2; IntAct=EBI-355676, EBI-368417;
SUBCELLULAR LOCATION: Nucleus.
PTM: Phosphorylated by PRKDC. Phosphorylated upon DNA damage, probably by ATM or ATR.
PTM: Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites.
MISCELLANEOUS: The ADP-D-ribosyl group of NAD(+) is transferred to an acceptor carboxyl group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.
SIMILARITY: Contains 1 BRCT domain.
SIMILARITY: Contains 1 PARP alpha-helical domain.
SIMILARITY: Contains 1 PARP catalytic domain.
SIMILARITY: Contains 2 PARP-type zinc fingers.
WEB RESOURCE: Name=NIEHS-SNPs; [LINK]
| NCBI GenPept GI number(s): |
156523968 |
| Species: | Homo sapiens |
Links to other databases:
| Database | ID | Link |
| Uniprot | P09874 |
P09874 |
| PFAM: | - |
P09874 (Link - using uniprot id) |
| InterPro: | - |
P09874 (Link - using uniprot id) |
| CATH: | None | |
| SCOP: | None | |
| PDB: | - | - |
Protein sequence:
|
MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPH WYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQD GIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQ LGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLP GVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKD ELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSG QLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKV KKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGK LSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEAN IRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSG AALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGG KVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNK LEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEE AVKKLTVNPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGK LSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPP LLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTD IKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKP FKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADM VSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKG LGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLK YLLKLKFNFKTSLW |
PARP1 (Homo sapiens) is able to recognize following damages:
PARP1 (Homo sapiens) belongs to following protein families:
References:
| Title | Authors | Journal |
| Molecular cloning of cDNA for human poly(ADP-ribose) polymerase and expression of its gene during HL-60 cell differentiation. | Suzuki H, Uchida K, Shima H, Sato T, Okamoto T, Kimura T, Miwa M | Biochem Biophys Res Commun July 31, 1987 |
| Nucleotide sequence of a full-length cDNA for human fibroblast poly(ADP-ribose) polymerase. | Uchida K, Morita T, Sato T, Ogura T, Yamashita R, Noguchi S, Suzuki H, Nyunoya H, Miwa M, Sugimura T | Biochem Biophys Res Commun Oct. 1, 1987 |
| Isolation of a cDNA clone for human NAD+: protein ADP-ribosyltransferase. | Schneider R, Auer B, Kuhne C, Herzog H, Klocker H, Burtscher HJ, Hirsch-Kauffmann M, Wintersberger U, Schweiger M | Eur J Cell Biol Oct. 1, 1987 |
| Primary structure of human poly(ADP-ribose) synthetase as deduced from cDNA sequence. | Kurosaki T, Ushiro H, Mitsuuchi Y, Suzuki S, Matsuda M, Matsuda Y, Katunuma N, Kangawa K, Matsuo H, Hirose T, et al. | J Biol Chem Nov. 25, 1987 |
| cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase. | Cherney BW, McBride OW, Chen DF, Alkhatib H, Bhatia K, Hensley P, Smulson ME | Proc Natl Acad Sci U S A Dec. 1, 1987 |
| Human nuclear NAD+ ADP-ribosyltransferase(polymerizing): organization of the gene. | Auer B, Nagl U, Herzog H, Schneider R, Schweiger M | DNA Oct. 1, 1989 |
| Characterization of a putative promoter region of the human poly(ADP-ribose) polymerase gene: structural similarity to that of the DNA polymerase beta gene. | Ogura T, Nyunoya H, Takahashi-Masutani M, Miwa M, Sugimura T, Esumi H | Biochem Biophys Res Commun March 16, 1990 |
| The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA. | Gradwohl G, Menissier de Murcia JM, Molinete M, Simonin F, Koken M, Hoeijmakers JH, de Murcia G | Proc Natl Acad Sci U S A April 1, 1990 |
| Expression and site-directed mutagenesis of the catalytic domain of human poly(ADP-ribose)polymerase in Escherichia coli. Lysine 893 is critical for activity. | Simonin F, Menissier-de Murcia J, Poch O, Muller S, Gradwohl G, Molinete M, Penning C, Keith G, de Murcia G | J Biol Chem Nov. 5, 1990 |
| Human poly(ADP-ribose) polymerase gene. Cloning of the promoter region. | Yokoyama Y, Kawamoto T, Mitsuuchi Y, Kurosaki T, Toda K, Ushiro H, Terashima M, Sumimoto H, Kuribayashi I, Yamamoto Y, et al. | Eur J Biochem Dec. 12, 1990 |
| 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. | Ikejima M, Noguchi S, Yamashita R, Ogura T, Sugimura T, Gill DM, Miwa M | J Biol Chem Dec. 15, 1990 |
| The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity. | Schreiber V, Molinete M, Boeuf H, de Murcia G, Menissier-de Murcia J | EMBO J Sept. 1, 1992 |
| Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching. | Rolli V, O'Farrell M, Menissier-de Murcia J, de Murcia G | Biochemistry Oct. 7, 1997 |
| Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication. | Dantzer F, Nasheuer HP, Vonesch JL, de Murcia G, Menissier-de Murcia J | Nucleic Acids Res April 15, 1998 |
| Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent protein kinase in vitro. | Ariumi Y, Masutani M, Copeland TD, Mimori T, Sugimura T, Shimotohno K, Ueda K, Hatanaka M, Noda M | Oncogene Aug. 12, 1999 |
| Aprataxin, a novel protein that protects against genotoxic stress. | Gueven N, Becherel OJ, Kijas AW, Chen P, Howe O, Rudolph JH, Gatti R, Date H, Onodera O, Taucher-Scholz G, Lavin MF | Hum Mol Genet May 15, 2004 |
| The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). | 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 | Genome Res Oct. 1, 2004 |
| The DNA sequence and biological annotation of human chromosome 1. | 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 | Nature May 18, 2006 |
| The poly(ADP-ribose) polymerase 1 interacts with Sry and modulates its biological functions. | Li Y, Oh HJ, Lau YF | Mol Cell Endocrinol Sept. 26, 2006 |
| The consensus coding sequences of human breast and colorectal cancers. | 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 | Science Oct. 13, 2006 |
| A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses. | Kanno S, Kuzuoka H, Sasao S, Hong Z, Lan L, Nakajima S, Yasui A | EMBO J April 18, 2007 |
| ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. | 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 | Science May 25, 2007 |
| Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins. | Ahel I, Ahel D, Matsusaka T, Clark AJ, Pines J, Boulton SJ, West SC | Nature Feb. 3, 2008 |
| A quantitative atlas of mitotic phosphorylation. | Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP | Proc Natl Acad Sci U S A Aug. 5, 2008 |
| Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. | Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK | Sci Signal Jan. 1, 2009 |
| Poly(ADP-ribose) polymerase-1 (PARP-1) transcriptionally regulates angiotensin AT2 receptor (AT2R) and AT2R binding protein (ATBP) genes. | 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 | Biochem Pharmacol June 15, 2009 |
| Lysine acetylation targets protein complexes and co-regulates major cellular functions. | Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M | Science Aug. 14, 2009 |
| Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1. | 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 | Science Sept. 4, 2009 |
| PARP-1 transcriptional activity is regulated by sumoylation upon heat shock. | Martin N, Schwamborn K, Schreiber V, Werner A, Guillier C, Zhang XD, Bischof O, Seeler JS, Dejean A | EMBO J Nov. 18, 2009 |
Last modification of this entry: Oct. 14, 2010.
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