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Poly [ADP-ribose] polymerase 1 (PARP-1) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 1) (ARTD1) (NAD( ) ADP-ribosyltransferase 1) (ADPRT 1) (Poly[ADP-ribose] synthase 1)

 PARP1_HUMAN             Reviewed;        1014 AA.
P09874; B1ANJ4; Q8IUZ9;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
30-AUG-2017, entry version 221.
RecName: Full=Poly [ADP-ribose] polymerase 1;
Short=PARP-1;
EC=2.4.2.30 {ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:28190768};
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 1;
Short=ARTD1;
AltName: Full=NAD(+) ADP-ribosyltransferase 1;
Short=ADPRT 1;
AltName: Full=Poly[ADP-ribose] synthase 1;
Name=PARP1; Synonyms=ADPRT, PPOL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=3120710; DOI=10.1016/0006-291X(87)90921-1;
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. 148:617-622(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=2824474;
Kurosaki T., Ushiro H., Mitsuuchi Y., Suzuki S., Matsuda M.,
Matsuda Y., Katunuma N., Kangawa K., Matsuo H., Hirose T., Inayama S.,
Shizuta Y.;
"Primary structure of human poly(ADP-ribose) synthetase as deduced
from cDNA sequence.";
J. Biol. Chem. 262:15990-15997(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-940.
PubMed=2891139; DOI=10.1073/pnas.84.23.8370;
Cherney B.W., McBride O.W., Chen D., Alkhatib H., Bhatia K.,
Hensley P., Smulson M.E.;
"cDNA sequence, protein structure, and chromosomal location of the
human gene for poly(ADP-ribose) polymerase.";
Proc. Natl. Acad. Sci. U.S.A. 84:8370-8374(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2513174; DOI=10.1089/dna.1989.8.575;
Auer B., Nagl U., Herzog H., Schneider R., Schweiger M.;
"Human nuclear NAD+ ADP-ribosyltransferase(polymerizing): organization
of the gene.";
DNA 8:575-580(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-188; ILE-334;
TYR-383; ALA-762 AND ARG-940.
NIEHS SNPs program;
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-762.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
PubMed=2125269; DOI=10.1111/j.1432-1033.1990.tb15647.x;
Yokoyama Y., Kawamoto T., Mitsuuchi Y., Kurosaki T., Toda K.,
Ushiro H., Terashima M., Sumimoto H., Kuribayashi I., Yamamoto Y.,
Maeda T., Ikeda H., Sagara Y., Shizuta Y.;
"Human poly(ADP-ribose) polymerase gene. Cloning of the promoter
region.";
Eur. J. Biochem. 194:521-526(1990).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
PubMed=2108670; DOI=10.1016/0006-291X(90)92082-B;
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. 167:701-710(1990).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
Herzog H., Schneider R., Hirsch-Kauffmann M., Schnitzer D.,
Schweiger M.;
"Human pADPRT is involved in the regulation of its own gene.";
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
[12]
PROTEIN SEQUENCE OF 2-10; 35-47; 66-78; 109-119; 183-197; 209-221;
263-282; 453-467; 487-496; 529-548; 552-564; 572-582; 637-654;
668-695; 748-761; 780-796; 803-816 AND 859-903, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Colon carcinoma, and Ovarian carcinoma;
Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A.,
Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[13]
PROTEIN SEQUENCE OF 166-177 AND 356-367, INTERACTION WITH EEF1A1 AND
TXK, PHOSPHORYLATION BY TXK, SUBCELLULAR LOCATION, AND FUNCTION AS A
TRANSCRIPTION FACTOR.
PubMed=17177976; DOI=10.1111/j.1365-2249.2006.03249.x;
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. 147:164-175(2007).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 381-420 AND 682-710.
PubMed=3121332;
Schneider R., Auer B., Kuhne C., Herzog H., Klocker H.,
Burtscher H.J., Hirsch-Kauffmann M., Wintersberger U., Schweiger M.;
"Isolation of a cDNA clone for human NAD+: protein ADP-
ribosyltransferase.";
Eur. J. Cell Biol. 44:302-307(1987).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 441-1014.
PubMed=3113420; DOI=10.1016/0006-291X(87)90543-2;
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. 146:403-409(1987).
[16]
ERRATUM.
Suzuki H., Uchida K., Shima H., Sato T., Okamoto T., Kimura T.,
Miwa M.;
Biochem. Biophys. Res. Commun. 148:1549-1550(1987).
[17]
ANALYSIS OF ZINC-FINGERS.
PubMed=2109322; DOI=10.1073/pnas.87.8.2990;
Gradwohl G., Menissier-de Murcia J., Molinete M., Simonin F.,
Koken M.H.M., Hoeijmakers J.H.J., de Murcia G.M.;
"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. 87:2990-2994(1990).
[18]
ANALYSIS OF ZINC-FINGERS.
PubMed=2123876;
Ikelima M., Noguchi S., Yamashita R., Ogura T., Sugimura T.,
Gill D.M., 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. 265:21907-21913(1990).
[19]
MUTAGENESIS OF CATALYTIC DOMAIN.
PubMed=2121735;
Simonin F., Menissier-de Murcia J., Poch O., Muller S., Gradwohl G.,
Molinete M., Penning C., Keith G., de Murcia G.M.;
"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. 265:19249-19256(1990).
[20]
NUCLEAR LOCALIZATION SIGNAL.
PubMed=1505517;
Schreiber V., Molinete M., Boeuf H., de Murcia G.M.,
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. 11:3263-3269(1992).
[21]
MUTAGENESIS OF CATALYTIC DOMAIN.
PubMed=9315851; DOI=10.1021/bi971055p;
Rolli V., O'Farrell M., Menissier-de Murcia J., de Murcia G.M.;
"Random mutagenesis of the poly(ADP-ribose) polymerase catalytic
domain reveals amino acids involved in polymer branching.";
Biochemistry 36:12147-12154(1997).
[22]
INTERACTION WITH POLA1, AND SUBCELLULAR LOCATION.
PubMed=9518481; DOI=10.1093/nar/26.8.1891;
Dantzer F., Nasheuer H.P., Vonesch J.L., 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. 26:1891-1898(1998).
[23]
PHOSPHORYLATION.
PubMed=10467406; DOI=10.1038/sj.onc.1202823;
Ariumi Y., Masutani M., Copeland T.D., 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 18:4616-4625(1999).
[24]
INTERACTION WITH APTX.
PubMed=15044383; DOI=10.1093/hmg/ddh122;
Gueven N., Becherel O.J., Kijas A.W., Chen P., Howe O., Rudolph J.H.,
Gatti R., Date H., Onodera O., Taucher-Scholz G., Lavin M.F.;
"Aprataxin, a novel protein that protects against genotoxic stress.";
Hum. Mol. Genet. 13:1081-1093(2004).
[25]
INTERACTION WITH SRY.
PubMed=16904257; DOI=10.1016/j.mce.2006.06.008;
Li Y., Oh H.J., Lau Y.-F.C.;
"The poly(ADP-ribose) polymerase 1 interacts with Sry and modulates
its biological functions.";
Mol. Cell. Endocrinol. 257:35-46(2006).
[26]
INTERACTION WITH APLF, AND FUNCTION.
PubMed=17396150; DOI=10.1038/sj.emboj.7601663;
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. 26:2094-2103(2007).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[28]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=18172500; DOI=10.1038/nature06420;
Ahel I., Ahel D., Matsusaka T., Clark A.J., Pines J., Boulton S.J.,
West S.C.;
"Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint
proteins.";
Nature 451:81-85(2008).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-368 AND SER-782, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[30]
FUNCTION.
PubMed=19344625; DOI=10.1016/j.bcp.2009.02.025;
Reinemund J., Seidel K., Steckelings U.M., Zaade D., Klare S.,
Rompe F., Katerbaum M., Schacherl J., Li Y., Menk M., Schefe J.H.,
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. 77:1795-1805(2009).
[31]
INTERACTION WITH RNF4.
PubMed=19779455; DOI=10.1038/emboj.2009.279;
Martin N., Schwamborn K., Schreiber V., Werner A., Guillier C.,
Zhang X.D., Bischof O., Seeler J.S., Dejean A.;
"PARP-1 transcriptional activity is regulated by sumoylation upon heat
shock.";
EMBO J. 28:3534-3548(2009).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[33]
FUNCTION, POLY-ADP-RIBOSYLATION, AND INTERACTION WITH CHD1L.
PubMed=19661379; DOI=10.1126/science.1177321;
Ahel D., Horejsi Z., Wiechens N., Polo S.E., Garcia-Wilson E.,
Ahel I., Flynn H., Skehel M., West S.C., Jackson S.P., Owen-Hughes T.,
Boulton S.J.;
"Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin
remodeling enzyme ALC1.";
Science 325:1240-1243(2009).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97; LYS-105; LYS-131;
LYS-600 AND LYS-621, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-782, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[36]
NOMENCLATURE.
PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
"Toward a unified nomenclature for mammalian ADP-
ribosyltransferases.";
Trends Biochem. Sci. 35:208-219(2010).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[38]
INTERACTION WITH PUM3.
PubMed=21266351; DOI=10.1158/0008-5472.CAN-10-1831;
Chang H.Y., Fan C.C., Chu P.C., Hong B.E., Lee H.J., Chang M.S.;
"hPuf-A/KIAA0020 modulates PARP-1 cleavage upon genotoxic stress.";
Cancer Res. 71:1126-1134(2011).
[39]
INTERACTION WITH SNAI1.
PubMed=21577210; DOI=10.1038/onc.2011.153;
Rodriguez M.I., Gonzalez-Flores A., Dantzer F., Collard J.,
de Herreros A.G., Oliver F.J.;
"Poly(ADP-ribose)-dependent regulation of Snail1 protein stability.";
Oncogene 30:4365-4372(2011).
[40]
INTERACTION WITH RNF146, AND SUBCELLULAR LOCATION.
PubMed=21799911; DOI=10.1371/journal.pone.0022595;
Callow M.G., Tran H., Phu L., Lau T., Lee J., Sandoval W.N., Liu P.S.,
Bheddah S., Tao J., Lill J.R., Hongo J.A., Davis D., Kirkpatrick D.S.,
Polakis P., Costa M.;
"Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt
signaling.";
PLoS ONE 6:E22595-E22595(2011).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[42]
INTERACTION WITH ZNF423.
PubMed=22863007; DOI=10.1016/j.cell.2012.06.028;
Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G.,
Wang H., Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G.,
Hong C.J., Hamilton B.A., Cervenka I., Ganji R.S., Bryja V.,
Arts H.H., van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R.,
Husson H., Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L.,
Sayer J.A., Schermer B., Liebau M.C., Benzing T., Le Corre S.,
Drummond I., Janssen S., Allen S.J., Natarajan S., O'Toole J.F.,
Attanasio M., Saunier S., Antignac C., Koenekoop R.K., Ren H.,
Lopez I., Nayir A., Stoetzel C., Dollfus H., Massoudi R.,
Gleeson J.G., Andreoli S.P., Doherty D.G., Lindstrad A., Golzio C.,
Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A., Lewis R.A.,
Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R.,
Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J.,
Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A.,
Hildebrandt F.;
"Exome capture reveals ZNF423 and CEP164 mutations, linking renal
ciliopathies to DNA damage response signaling.";
Cell 150:533-548(2012).
[43]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=22002106; DOI=10.1074/mcp.M111.013680;
Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
"Systematic analysis of protein pools, isoforms, and modifications
affecting turnover and subcellular localization.";
Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
[44]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., 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. 109:12449-12454(2012).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-177; SER-179;
SER-185; SER-274; SER-277; SER-782 AND SER-786, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[46]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PARP9.
PubMed=23230272; DOI=10.1128/MCB.00990-12;
Yan Q., Xu R., Zhu L., Cheng X., Wang Z., Manis J., Shipp M.A.;
"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. 33:845-857(2013).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
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 96:253-262(2014).
[48]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-486; LYS-512 AND LYS-748,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[49]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-203; LYS-486 AND LYS-748,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[50]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-203; LYS-467; LYS-486 AND
LYS-512, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[51]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-512, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[52]
FUNCTION, AND INTERACTION WITH HPF1.
PubMed=27067600; DOI=10.1016/j.molcel.2016.03.008;
Gibbs-Seymour I., Fontana P., Rack J.G., Ahel I.;
"HPF1/C4orf27 is a PARP-1-interacting protein that regulates PARP-1
ADP-ribosylation activity.";
Mol. Cell 62:432-442(2016).
[53]
FUNCTION.
PubMed=27257257; DOI=10.1126/science.aad9335;
Wright R.H., Lioutas A., Le Dily F., Soronellas D., Pohl A., Bonet J.,
Nacht A.S., Samino S., Font-Mateu J., Vicent G.P., Wierer M.,
Trabado M.A., Schelhorn C., Carolis C., Macias M.J., Yanes O.,
Oliva B., Beato M.;
"ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for
chromatin remodeling.";
Science 352:1221-1225(2016).
[54]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH HPF1, ADP-RIBOSYLATION
AT SER-499; SER-507 AND SER-519, AND MUTAGENESIS OF SER-499; SER-507
AND SER-519.
PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003;
Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I.,
Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.;
"Serine ADP-ribosylation depends on HPF1.";
Mol. Cell 0:0-0(2017).
[55]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-192; LYS-203; LYS-249;
LYS-467; LYS-486; LYS-512; LYS-528 AND LYS-748, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[56]
STRUCTURE BY NMR OF 1-93 AND 385-643.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the first ZF-PARP domain, of the BRCT domain
and of the WGR domain of human poly(ADP-ribose)polymerase-1.";
Submitted (APR-2007) to the PDB data bank.
[57]
VARIANT [LARGE SCALE ANALYSIS] VAL-488.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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 (PubMed:17177976, PubMed:18172500,
PubMed:19344625, PubMed:19661379, PubMed:23230272). Mediates the
poly(ADP-ribosyl)ation of APLF and CHFR (PubMed:17396150).
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 (PubMed:17177976). Required
for PARP9 and DTX3L recruitment to DNA damage sites
(PubMed:23230272). PARP1-dependent PARP9-DTX3L-mediated
ubiquitination promotes the rapid and specific recruitment of
53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites
(PubMed:23230272). Mediates serine ADP-ribosylation of target
proteins following interaction with HPF1; HPF1 conferring serine
specificity (PubMed:28190768). Mediates the poly(ADP-ribosyl)ation
of histones in a HPF1-dependent manner (PubMed:27067600). Involved
in the synthesis of ATP in the nucleus, together with NMNAT1, PARG
and NUDT5 (PubMed:27257257). Nuclear ATP generation is required
for extensive chromatin remodeling events that are energy-
consuming (PubMed:27257257). {ECO:0000269|PubMed:17177976,
ECO:0000269|PubMed:17396150, ECO:0000269|PubMed:18172500,
ECO:0000269|PubMed:19344625, ECO:0000269|PubMed:19661379,
ECO:0000269|PubMed:23230272, ECO:0000269|PubMed:27067600,
ECO:0000269|PubMed:27257257, ECO:0000269|PubMed:28190768}.
-!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
{ECO:0000255|PROSITE-ProRule:PRU00397,
ECO:0000269|PubMed:18172500, ECO:0000269|PubMed:28190768}.
-!- SUBUNIT: Component of a base excision repair (BER) complex,
containing at least XRCC1, PARP2, POLB and LRIG3. Homo- and
heterodimer with PARP2. Interacts with APTX (PubMed:15044383).
Interacts with PARP3. Interacts with SRY (PubMed:16904257). The
SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts
with TIAM2 (By similarity). Interacts (when poly-ADP-ribosylated)
with CHD1L (PubMed:19661379). Interacts with the DNA polymerase
alpha catalytic subunit POLA1; this interaction functions as part
of the control of replication fork progression (PubMed:9518481).
Interacts with EEF1A1 and TXK (PubMed:17177976). Interacts with
RNF4 (PubMed:19779455). Interacts with RNF146 (PubMed:21799911).
Interacts with ZNF423 (PubMed:22863007). Interacts with SNAI1 (via
zinc fingers); the interaction requires SNAI1 to be poly-ADP-
ribosylated and non-phosphorylated (active) by GSK3B
(PubMed:21577210). Interacts (when poly-ADP-ribosylated) with
PARP9 (PubMed:23230272). Interacts with NR4A3; activates PARP1 by
improving acetylation of PARP1 and suppressing the interaction
between PARP1 and SIRT1 (By similarity). Interacts (via catalytic
domain) with PUM3; the interaction inhibits the poly(ADP-
ribosyl)ation activity of PARP1 and the degradation of PARP1 by
CASP3 following genotoxic stress (PubMed:21266351). Interacts (via
the PARP catalytic domain) with HPF1 (PubMed:27067600,
PubMed:28190768). {ECO:0000250|UniProtKB:P27008,
ECO:0000269|PubMed:15044383, ECO:0000269|PubMed:16904257,
ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:17396150,
ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:19779455,
ECO:0000269|PubMed:21266351, ECO:0000269|PubMed:21577210,
ECO:0000269|PubMed:21799911, ECO:0000269|PubMed:22863007,
ECO:0000269|PubMed:23230272, ECO:0000269|PubMed:27067600,
ECO:0000269|PubMed:28190768, ECO:0000269|PubMed:9518481}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-355676, EBI-355676;
Q8IW19:APLF; NbExp=3; IntAct=EBI-355676, EBI-1256044;
Q7Z2E3:APTX; NbExp=8; IntAct=EBI-355676, EBI-847814;
P49715:CEBPA; NbExp=2; IntAct=EBI-355676, EBI-1172054;
P26358:DNMT1; NbExp=6; IntAct=EBI-355676, EBI-719459;
Q01094:E2F1; NbExp=2; IntAct=EBI-355676, EBI-448924;
P11308:ERG; NbExp=7; IntAct=EBI-355676, EBI-79704;
Q13007:IL24; NbExp=2; IntAct=EBI-355676, EBI-3915542;
Q9Y530:OARD1; NbExp=5; IntAct=EBI-355676, EBI-8502288;
Q8N2W9:PIAS4; NbExp=5; IntAct=EBI-355676, EBI-473160;
O95863:SNAI1; NbExp=10; IntAct=EBI-355676, EBI-1045459;
Q02085:Snai1 (xeno); NbExp=3; IntAct=EBI-355676, EBI-6049807;
P63165:SUMO1; NbExp=2; IntAct=EBI-355676, EBI-80140;
P04637:TP53; NbExp=3; IntAct=EBI-355676, EBI-366083;
P0CG48:UBC; NbExp=2; IntAct=EBI-355676, EBI-3390054;
Q14191:WRN; NbExp=8; IntAct=EBI-355676, EBI-368417;
P18887:XRCC1; NbExp=6; IntAct=EBI-355676, EBI-947466;
Q2M1K9:ZNF423; NbExp=2; IntAct=EBI-355676, EBI-950016;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17177976,
ECO:0000269|PubMed:21799911, ECO:0000269|PubMed:23230272}.
Nucleus, nucleolus {ECO:0000269|PubMed:9518481}. Note=Localizes at
sites of DNA damage. {ECO:0000269|PubMed:23230272}.
-!- PTM: Phosphorylated by PRKDC and TXK.
{ECO:0000269|PubMed:10467406, ECO:0000269|PubMed:17177976}.
-!- PTM: Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates
the recruitment of CHD1L to DNA damage sites (PubMed:19661379).
ADP-ribosylated on serine by autocatalysis; serine ADP-
ribosylation takes place following interaction with HPF1
(PubMed:28190768). {ECO:0000269|PubMed:19661379,
ECO:0000269|PubMed:28190768}.
-!- PTM: S-nitrosylated, leading to inhibit transcription regulation
activity. {ECO:0000250|UniProtKB:P11103}.
-!- 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.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/adprt/";
-----------------------------------------------------------------------
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EMBL; M18112; AAA60137.1; -; mRNA.
EMBL; J03473; AAB59447.1; -; mRNA.
EMBL; M32721; AAA60155.1; -; mRNA.
EMBL; M29786; AAA51663.1; -; Genomic_DNA.
EMBL; M29545; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29766; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29767; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29768; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29769; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29770; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29771; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29772; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29773; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29774; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29775; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29776; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29777; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29778; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29779; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29780; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29781; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29783; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29784; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29785; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29544; AAA51663.1; JOINED; Genomic_DNA.
EMBL; M29782; AAA51663.1; JOINED; Genomic_DNA.
EMBL; AF524947; AAM75364.1; -; Genomic_DNA.
EMBL; AL359704; CAH70215.1; -; Genomic_DNA.
EMBL; AL359742; CAH70215.1; JOINED; Genomic_DNA.
EMBL; AL359742; CAI12102.1; -; Genomic_DNA.
EMBL; AL359704; CAI12102.1; JOINED; Genomic_DNA.
EMBL; CH471098; EAW69783.1; -; Genomic_DNA.
EMBL; BC037545; AAH37545.1; -; mRNA.
EMBL; X56140; CAA39606.1; -; Genomic_DNA.
EMBL; X56141; CAA39606.1; JOINED; Genomic_DNA.
EMBL; X16674; CAA34663.1; -; Genomic_DNA.
EMBL; M60436; AAA60000.1; -; Genomic_DNA.
EMBL; M17081; AAA51599.1; ALT_SEQ; mRNA.
CCDS; CCDS1554.1; -.
PIR; A29725; A29725.
RefSeq; NP_001609.2; NM_001618.3.
UniGene; Hs.177766; -.
PDB; 1UK0; X-ray; 3.00 A; A/B=662-1011.
PDB; 1UK1; X-ray; 3.00 A; A/B=662-1011.
PDB; 1WOK; X-ray; 3.00 A; A/B/C/D=662-1011.
PDB; 2COK; NMR; -; A=387-486.
PDB; 2CR9; NMR; -; A=518-643.
PDB; 2CS2; NMR; -; A=103-223.
PDB; 2DMJ; NMR; -; A=1-93.
PDB; 2JVN; NMR; -; A=233-358.
PDB; 2L30; NMR; -; A=1-108.
PDB; 2L31; NMR; -; A=103-214.
PDB; 2N8A; NMR; -; A=1-214.
PDB; 2RCW; X-ray; 2.80 A; A=662-1011.
PDB; 2RD6; X-ray; 2.30 A; A=662-1011.
PDB; 2RIQ; X-ray; 1.70 A; A=216-366.
PDB; 3GJW; X-ray; 2.30 A; A=662-1011.
PDB; 3GN7; X-ray; 2.50 A; A=662-1011.
PDB; 3L3L; X-ray; 2.50 A; A=662-1011.
PDB; 3L3M; X-ray; 2.50 A; A=662-1011.
PDB; 3OD8; X-ray; 2.40 A; A/B/C/D/E/F/G/H=2-96.
PDB; 3ODA; X-ray; 2.64 A; A/B/C/D/E/F/G/H=2-96.
PDB; 3ODC; X-ray; 2.80 A; A/B=105-206.
PDB; 3ODE; X-ray; 2.95 A; A/B=105-206.
PDB; 4AV1; X-ray; 3.10 A; A/B/C/D=5-202.
PDB; 4DQY; X-ray; 3.25 A; A/D=1-96, B/E=216-366, C/F=518-1014.
PDB; 4GV7; X-ray; 2.89 A; A/B/C/D=662-1011.
PDB; 4HHY; X-ray; 2.36 A; A/B/C/D=660-1011.
PDB; 4HHZ; X-ray; 2.72 A; A/B/C/D=660-1011.
PDB; 4L6S; X-ray; 2.20 A; A/B=662-1011.
PDB; 4OPX; X-ray; 3.31 A; A/D=1-97, A/D=207-366, C/F=518-1014.
PDB; 4OQA; X-ray; 3.65 A; A/D=1-97, A/D=207-366, C/F=518-1014.
PDB; 4OQB; X-ray; 3.36 A; A/D=1-97, A/D=207-366, C/F=518-1014.
PDB; 4PJT; X-ray; 2.35 A; A/B/C/D=662-1011.
PDB; 4R5W; X-ray; 2.84 A; A/B=662-1011.
PDB; 4R6E; X-ray; 2.20 A; A/B/C/D=662-1011.
PDB; 4RV6; X-ray; 3.19 A; A/B/C/D=662-1011.
PDB; 4UND; X-ray; 2.20 A; A/B=662-1011.
PDB; 4UXB; X-ray; 3.22 A; A/B=662-1011.
PDB; 4XHU; X-ray; 2.09 A; A/C=661-1014.
PDB; 4ZZZ; X-ray; 1.90 A; A/B=655-1014.
PDB; 5A00; X-ray; 2.75 A; A=655-1014.
PDB; 5DS3; X-ray; 2.60 A; A=788-1012.
PDB; 5HA9; X-ray; 4.01 A; A/B=662-1011.
PDB; 5KPN; X-ray; 2.30 A; A/B=662-1011.
PDB; 5KPO; X-ray; 2.65 A; A/B=662-1011.
PDB; 5KPP; X-ray; 2.33 A; A/B=662-1011.
PDB; 5KPQ; X-ray; 2.55 A; A/B=662-1011.
PDB; 5WRQ; X-ray; 2.65 A; A/B=662-1011.
PDB; 5WRY; X-ray; 2.30 A; A/B=662-1011.
PDB; 5WRZ; X-ray; 2.20 A; A/B=662-1011.
PDB; 5WS0; X-ray; 2.60 A; A/B=662-1011.
PDB; 5WS1; X-ray; 1.90 A; A/B=662-1011.
PDB; 5WTC; X-ray; 2.20 A; A/B=662-1011.
PDBsum; 1UK0; -.
PDBsum; 1UK1; -.
PDBsum; 1WOK; -.
PDBsum; 2COK; -.
PDBsum; 2CR9; -.
PDBsum; 2CS2; -.
PDBsum; 2DMJ; -.
PDBsum; 2JVN; -.
PDBsum; 2L30; -.
PDBsum; 2L31; -.
PDBsum; 2N8A; -.
PDBsum; 2RCW; -.
PDBsum; 2RD6; -.
PDBsum; 2RIQ; -.
PDBsum; 3GJW; -.
PDBsum; 3GN7; -.
PDBsum; 3L3L; -.
PDBsum; 3L3M; -.
PDBsum; 3OD8; -.
PDBsum; 3ODA; -.
PDBsum; 3ODC; -.
PDBsum; 3ODE; -.
PDBsum; 4AV1; -.
PDBsum; 4DQY; -.
PDBsum; 4GV7; -.
PDBsum; 4HHY; -.
PDBsum; 4HHZ; -.
PDBsum; 4L6S; -.
PDBsum; 4OPX; -.
PDBsum; 4OQA; -.
PDBsum; 4OQB; -.
PDBsum; 4PJT; -.
PDBsum; 4R5W; -.
PDBsum; 4R6E; -.
PDBsum; 4RV6; -.
PDBsum; 4UND; -.
PDBsum; 4UXB; -.
PDBsum; 4XHU; -.
PDBsum; 4ZZZ; -.
PDBsum; 5A00; -.
PDBsum; 5DS3; -.
PDBsum; 5HA9; -.
PDBsum; 5KPN; -.
PDBsum; 5KPO; -.
PDBsum; 5KPP; -.
PDBsum; 5KPQ; -.
PDBsum; 5WRQ; -.
PDBsum; 5WRY; -.
PDBsum; 5WRZ; -.
PDBsum; 5WS0; -.
PDBsum; 5WS1; -.
PDBsum; 5WTC; -.
ProteinModelPortal; P09874; -.
SMR; P09874; -.
BioGrid; 106652; 267.
DIP; DIP-38N; -.
ELM; P09874; -.
IntAct; P09874; 96.
MINT; MINT-104344; -.
STRING; 9606.ENSP00000355759; -.
BindingDB; P09874; -.
ChEMBL; CHEMBL3105; -.
DrugBank; DB04010; 2-(3'-Methoxyphenyl) Benzimidazole-4-Carboxamide.
DrugBank; DB03509; 2-(4-Chlorophenyl)-5-Quinoxalinecarboxamide.
DrugBank; DB03073; 3-Methoxybenzamide.
DrugBank; DB02498; Carba-Nicotinamide-Adenine-Dinucleotide.
DrugBank; DB02701; Nicotinamide.
DrugBank; DB02690; NU1025.
DrugBank; DB09074; Olaparib.
DrugBank; DB12332; Rucaparib.
DrugBank; DB07330; trans-4-(7-carbamoyl-1H-benzimidazol-2-yl)-1-propylpiperidinium.
DrugBank; DB07232; Veliparib.
GuidetoPHARMACOLOGY; 2771; -.
iPTMnet; P09874; -.
PhosphoSitePlus; P09874; -.
SwissPalm; P09874; -.
BioMuta; PARP1; -.
DMDM; 130781; -.
SWISS-2DPAGE; P09874; -.
EPD; P09874; -.
MaxQB; P09874; -.
PaxDb; P09874; -.
PeptideAtlas; P09874; -.
PRIDE; P09874; -.
DNASU; 142; -.
Ensembl; ENST00000366794; ENSP00000355759; ENSG00000143799.
GeneID; 142; -.
KEGG; hsa:142; -.
UCSC; uc001hqd.5; human.
CTD; 142; -.
DisGeNET; 142; -.
GeneCards; PARP1; -.
H-InvDB; HIX0023551; -.
HGNC; HGNC:270; PARP1.
HPA; CAB000147; -.
HPA; CAB003839; -.
HPA; CAB003840; -.
HPA; CAB075726; -.
HPA; CAB075727; -.
HPA; HPA045168; -.
MIM; 173870; gene.
neXtProt; NX_P09874; -.
OpenTargets; ENSG00000143799; -.
PharmGKB; PA32; -.
eggNOG; KOG1037; Eukaryota.
eggNOG; ENOG410XP18; LUCA.
GeneTree; ENSGT00390000017341; -.
HOGENOM; HOG000030402; -.
HOVERGEN; HBG053513; -.
InParanoid; P09874; -.
KO; K10798; -.
OMA; WNHASCI; -.
OrthoDB; EOG091G13H1; -.
PhylomeDB; P09874; -.
TreeFam; TF316616; -.
BRENDA; 2.4.2.30; 2681.
Reactome; R-HSA-110362; POLB-Dependent Long Patch Base Excision Repair.
Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-5685939; HDR through MMEJ (alt-NHEJ).
Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-HSA-5696400; Dual Incision in GG-NER.
SignaLink; P09874; -.
SIGNOR; P09874; -.
ChiTaRS; PARP1; human.
EvolutionaryTrace; P09874; -.
GeneWiki; PARP1; -.
GenomeRNAi; 142; -.
PMAP-CutDB; P09874; -.
PRO; PR:P09874; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143799; -.
CleanEx; HS_PARP1; -.
ExpressionAtlas; P09874; baseline and differential.
Genevisible; P09874; HS.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:CAFA.
GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
GO; GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0003910; F:DNA ligase (ATP) activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IEA:Ensembl.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051287; F:NAD binding; IEA:Ensembl.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:UniProtKB.
GO; GO:1990404; F:protein ADP-ribosylase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0070412; F:R-SMAD binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; IDA:UniProtKB.
GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:BHF-UCL.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:MGI.
GO; GO:0071294; P:cellular response to zinc ion; IEA:Ensembl.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; IEA:Ensembl.
GO; GO:0051103; P:DNA ligation involved in DNA repair; IBA:GO_Central.
GO; GO:0006281; P:DNA repair; TAS:UniProtKB.
GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; TAS:Reactome.
GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
GO; GO:0030225; P:macrophage differentiation; TAS:UniProtKB.
GO; GO:0032042; P:mitochondrial DNA metabolic process; IMP:MGI.
GO; GO:0043504; P:mitochondrial DNA repair; IMP:MGI.
GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
GO; GO:2001170; P:negative regulation of ATP biosynthetic process; IMP:ParkinsonsUK-UCL.
GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; ISS:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; TAS:Reactome.
GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; TAS:Reactome.
GO; GO:0033683; P:nucleotide-excision repair, DNA incision; TAS:Reactome.
GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; TAS:Reactome.
GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome.
GO; GO:0006293; P:nucleotide-excision repair, preincision complex stabilization; TAS:Reactome.
GO; GO:0018312; P:peptidyl-serine ADP-ribosylation; IDA:UniProtKB.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS:UniProtKB.
GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IEA:Ensembl.
GO; GO:1904762; P:positive regulation of myofibroblast differentiation; IEA:Ensembl.
GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
GO; GO:0060391; P:positive regulation of SMAD protein import into nucleus; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IEA:Ensembl.
GO; GO:0006471; P:protein ADP-ribosylation; IDA:UniProtKB.
GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl.
GO; GO:0036211; P:protein modification process; IMP:MGI.
GO; GO:0070212; P:protein poly-ADP-ribosylation; IDA:UniProtKB.
GO; GO:0050790; P:regulation of catalytic activity; IDA:BHF-UCL.
GO; GO:1903827; P:regulation of cellular protein localization; IMP:MGI.
GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
GO; GO:1903376; P:regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0010990; P:regulation of SMAD protein complex assembly; IEA:Ensembl.
GO; GO:1904044; P:response to aldosterone; IEA:Ensembl.
GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
GO; GO:0000723; P:telomere maintenance; TAS:BHF-UCL.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
CDD; cd00027; BRCT; 1.
Gene3D; 1.20.142.10; -; 1.
Gene3D; 2.20.140.10; -; 1.
Gene3D; 3.30.1740.10; -; 2.
Gene3D; 3.40.50.10190; -; 1.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR012982; PADR1.
InterPro; IPR008288; PARP.
InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
InterPro; IPR008893; WGR_domain.
InterPro; IPR001510; Znf_PARP.
Pfam; PF00533; BRCT; 1.
Pfam; PF08063; PADR1; 1.
Pfam; PF00644; PARP; 1.
Pfam; PF02877; PARP_reg; 1.
Pfam; PF05406; WGR; 1.
Pfam; PF00645; zf-PARP; 2.
PIRSF; PIRSF000489; NAD_ADPRT; 1.
SMART; SM00292; BRCT; 1.
SMART; SM01335; PADR1; 1.
SMART; SM00773; WGR; 1.
SMART; SM01336; zf-PARP; 2.
SUPFAM; SSF142921; SSF142921; 1.
SUPFAM; SSF47587; SSF47587; 1.
SUPFAM; SSF52113; SSF52113; 1.
PROSITE; PS50172; BRCT; 1.
PROSITE; PS51060; PARP_ALPHA_HD; 1.
PROSITE; PS51059; PARP_CATALYTIC; 1.
PROSITE; PS00347; PARP_ZN_FINGER_1; 2.
PROSITE; PS50064; PARP_ZN_FINGER_2; 2.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Complete proteome;
Direct protein sequencing; DNA damage; DNA repair; DNA-binding;
Glycosyltransferase; Isopeptide bond; Metal-binding; NAD; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation; Transferase; Ubl conjugation;
Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.12}.
CHAIN 2 1014 Poly [ADP-ribose] polymerase 1.
/FTId=PRO_0000211320.
DOMAIN 385 476 BRCT. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 662 779 PARP alpha-helical. {ECO:0000255|PROSITE-
ProRule:PRU00398}.
DOMAIN 788 1014 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
DNA_BIND 2 372
ZN_FING 9 93 PARP-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00264}.
ZN_FING 113 203 PARP-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00264}.
REGION 373 524 Automodification domain.
MOTIF 207 209 Nuclear localization signal.
{ECO:0000269|PubMed:1505517}.
MOTIF 221 226 Nuclear localization signal.
{ECO:0000269|PubMed:1505517}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.12}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 97 97 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 105 105 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 131 131 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:23186163}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 277 277 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 364 364 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 368 368 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 407 407 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 413 413 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 435 435 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 437 437 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 444 444 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 445 445 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 448 448 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 456 456 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 471 471 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 484 484 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 488 488 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 491 491 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 499 499 ADP-ribosylserine.
{ECO:0000269|PubMed:28190768}.
MOD_RES 507 507 ADP-ribosylserine.
{ECO:0000269|PubMed:28190768}.
MOD_RES 513 513 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 514 514 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 519 519 ADP-ribosylserine.
{ECO:0000269|PubMed:28190768}.
MOD_RES 520 520 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 600 600 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 621 621 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 782 782 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 786 786 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 192 192 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 203 203 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 203 203 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 249 249 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 467 467 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 486 486 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 486 486 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 512 512 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 528 528 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 748 748 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 748 748 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VARIANT 54 54 F -> L (in dbSNP:rs3738708).
/FTId=VAR_050460.
VARIANT 188 188 A -> T (in dbSNP:rs1805409).
{ECO:0000269|Ref.5}.
/FTId=VAR_014714.
VARIANT 334 334 V -> I (in dbSNP:rs3219057).
{ECO:0000269|Ref.5}.
/FTId=VAR_019171.
VARIANT 377 377 P -> S (in dbSNP:rs2230484).
/FTId=VAR_050461.
VARIANT 383 383 S -> Y (in dbSNP:rs3219062).
{ECO:0000269|Ref.5}.
/FTId=VAR_019172.
VARIANT 488 488 E -> V (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035852.
VARIANT 762 762 V -> A (in dbSNP:rs1136410).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.5}.
/FTId=VAR_014715.
VARIANT 940 940 K -> R (in dbSNP:rs3219145).
{ECO:0000269|PubMed:2891139,
ECO:0000269|Ref.5}.
/FTId=VAR_019173.
MUTAGEN 499 499 S->A: Abolishes automodification on
serine following interaction with HPF1;
when associated with A-507 and A-519.
{ECO:0000269|PubMed:28190768}.
MUTAGEN 507 507 S->A: Abolishes automodification on
serine following interaction with HPF1;
when associated with A-499 and A-519.
{ECO:0000269|PubMed:28190768}.
MUTAGEN 519 519 S->A: Abolishes automodification on
serine following interaction with HPF1;
when associated with A-499 and A-507.
{ECO:0000269|PubMed:28190768}.
MUTAGEN 797 797 L->P: 1.5% of wild-type activity.
MUTAGEN 868 868 N->S: 4% of wild-type activity.
MUTAGEN 890 890 M->V: <0.5% of wild-type activity.
MUTAGEN 893 893 K->I: Abolishes enzymatic activity.
MUTAGEN 897 897 F->S: 10% of wild-type activity.
MUTAGEN 899 899 D->N: 0.6% of wild-type activity.
MUTAGEN 908 908 C->R: <0.5% of wild-type activity.
MUTAGEN 926 926 L->F: 1.5% of wild-type activity.
MUTAGEN 986 986 Y->H: 14% of wild-type activity and
increased branching 15-fold.
MUTAGEN 988 988 E->K: 1.25% of wild-type activity; only
monomers are added.
MUTAGEN 1003 1003 L->P: 1.5% of wild-type activity.
CONFLICT 17 17 G -> E (in Ref. 2; AAB59447).
{ECO:0000305}.
CONFLICT 70 70 E -> Q (in Ref. 1; AAA60137).
{ECO:0000305}.
CONFLICT 212 212 E -> K (in Ref. 2; AAB59447).
{ECO:0000305}.
CONFLICT 613 613 H -> Q (in Ref. 3; AAA60155).
{ECO:0000305}.
CONFLICT 827 827 N -> S (in Ref. 3; AAA60155).
{ECO:0000305}.
CONFLICT 908 908 C -> Y (in Ref. 3; AAA60155).
{ECO:0000305}.
CONFLICT 980 980 N -> I (in Ref. 3; AAA60155).
{ECO:0000305}.
TURN 2 5 {ECO:0000244|PDB:2L30}.
STRAND 8 13 {ECO:0000244|PDB:3OD8}.
STRAND 15 17 {ECO:0000244|PDB:3OD8}.
TURN 22 24 {ECO:0000244|PDB:3OD8}.
STRAND 25 27 {ECO:0000244|PDB:2L30}.
STRAND 32 40 {ECO:0000244|PDB:3OD8}.
STRAND 42 53 {ECO:0000244|PDB:3OD8}.
HELIX 54 59 {ECO:0000244|PDB:3OD8}.
HELIX 67 70 {ECO:0000244|PDB:3OD8}.
HELIX 74 76 {ECO:0000244|PDB:3OD8}.
HELIX 79 90 {ECO:0000244|PDB:3OD8}.
STRAND 102 105 {ECO:0000244|PDB:2N8A}.
STRAND 113 117 {ECO:0000244|PDB:3ODC}.
STRAND 119 121 {ECO:0000244|PDB:3ODC}.
TURN 126 128 {ECO:0000244|PDB:3ODC}.
STRAND 137 145 {ECO:0000244|PDB:3ODC}.
STRAND 148 158 {ECO:0000244|PDB:3ODC}.
HELIX 160 165 {ECO:0000244|PDB:3ODC}.
HELIX 167 170 {ECO:0000244|PDB:3ODC}.
TURN 174 176 {ECO:0000244|PDB:3ODC}.
HELIX 177 180 {ECO:0000244|PDB:3ODC}.
HELIX 184 186 {ECO:0000244|PDB:3ODC}.
HELIX 189 198 {ECO:0000244|PDB:3ODC}.
TURN 204 206 {ECO:0000244|PDB:2L31}.
STRAND 209 211 {ECO:0000244|PDB:2N8A}.
HELIX 226 255 {ECO:0000244|PDB:2RIQ}.
HELIX 258 267 {ECO:0000244|PDB:2RIQ}.
TURN 273 275 {ECO:0000244|PDB:2JVN}.
HELIX 276 289 {ECO:0000244|PDB:2RIQ}.
TURN 296 298 {ECO:0000244|PDB:2RIQ}.
STRAND 302 305 {ECO:0000244|PDB:2RIQ}.
STRAND 308 311 {ECO:0000244|PDB:2RIQ}.
STRAND 314 316 {ECO:0000244|PDB:2RIQ}.
STRAND 324 327 {ECO:0000244|PDB:2RIQ}.
HELIX 337 340 {ECO:0000244|PDB:2RIQ}.
HELIX 342 347 {ECO:0000244|PDB:2RIQ}.
STRAND 389 392 {ECO:0000244|PDB:2COK}.
STRAND 394 397 {ECO:0000244|PDB:2COK}.
HELIX 405 414 {ECO:0000244|PDB:2COK}.
STRAND 418 421 {ECO:0000244|PDB:2COK}.
STRAND 427 430 {ECO:0000244|PDB:2COK}.
HELIX 433 438 {ECO:0000244|PDB:2COK}.
HELIX 441 448 {ECO:0000244|PDB:2COK}.
HELIX 457 463 {ECO:0000244|PDB:2COK}.
HELIX 469 475 {ECO:0000244|PDB:2COK}.
HELIX 535 537 {ECO:0000244|PDB:4DQY}.
TURN 540 542 {ECO:0000244|PDB:4DQY}.
STRAND 543 545 {ECO:0000244|PDB:2CR9}.
STRAND 551 560 {ECO:0000244|PDB:4DQY}.
TURN 562 564 {ECO:0000244|PDB:4DQY}.
STRAND 567 573 {ECO:0000244|PDB:4DQY}.
TURN 578 581 {ECO:0000244|PDB:2CR9}.
STRAND 585 591 {ECO:0000244|PDB:4DQY}.
STRAND 597 602 {ECO:0000244|PDB:4DQY}.
HELIX 608 622 {ECO:0000244|PDB:4DQY}.
STRAND 639 641 {ECO:0000244|PDB:4DQY}.
HELIX 667 676 {ECO:0000244|PDB:4ZZZ}.
HELIX 679 688 {ECO:0000244|PDB:4ZZZ}.
TURN 693 695 {ECO:0000244|PDB:4ZZZ}.
HELIX 698 700 {ECO:0000244|PDB:4ZZZ}.
HELIX 703 721 {ECO:0000244|PDB:4ZZZ}.
HELIX 726 739 {ECO:0000244|PDB:4ZZZ}.
STRAND 745 747 {ECO:0000244|PDB:3GJW}.
STRAND 752 754 {ECO:0000244|PDB:1UK0}.
HELIX 755 779 {ECO:0000244|PDB:4ZZZ}.
STRAND 785 787 {ECO:0000244|PDB:4R6E}.
HELIX 789 795 {ECO:0000244|PDB:4ZZZ}.
TURN 796 798 {ECO:0000244|PDB:4GV7}.
STRAND 799 803 {ECO:0000244|PDB:4ZZZ}.
STRAND 806 808 {ECO:0000244|PDB:2RCW}.
HELIX 809 820 {ECO:0000244|PDB:4ZZZ}.
HELIX 824 826 {ECO:0000244|PDB:5WS1}.
STRAND 829 841 {ECO:0000244|PDB:4ZZZ}.
HELIX 844 848 {ECO:0000244|PDB:4ZZZ}.
HELIX 849 853 {ECO:0000244|PDB:4ZZZ}.
STRAND 857 864 {ECO:0000244|PDB:4ZZZ}.
HELIX 866 868 {ECO:0000244|PDB:4ZZZ}.
HELIX 869 875 {ECO:0000244|PDB:4ZZZ}.
STRAND 882 884 {ECO:0000244|PDB:1WOK}.
HELIX 886 888 {ECO:0000244|PDB:4ZZZ}.
STRAND 889 891 {ECO:0000244|PDB:1WOK}.
STRAND 893 900 {ECO:0000244|PDB:4ZZZ}.
HELIX 901 905 {ECO:0000244|PDB:4ZZZ}.
HELIX 906 908 {ECO:0000244|PDB:4ZZZ}.
STRAND 912 914 {ECO:0000244|PDB:4R6E}.
STRAND 916 925 {ECO:0000244|PDB:4ZZZ}.
STRAND 928 934 {ECO:0000244|PDB:4ZZZ}.
STRAND 947 950 {ECO:0000244|PDB:4ZZZ}.
STRAND 952 956 {ECO:0000244|PDB:4ZZZ}.
HELIX 958 960 {ECO:0000244|PDB:5WS1}.
STRAND 962 964 {ECO:0000244|PDB:4ZZZ}.
STRAND 967 969 {ECO:0000244|PDB:4ZZZ}.
STRAND 974 976 {ECO:0000244|PDB:4ZZZ}.
STRAND 983 986 {ECO:0000244|PDB:4ZZZ}.
STRAND 988 993 {ECO:0000244|PDB:4ZZZ}.
HELIX 994 996 {ECO:0000244|PDB:4ZZZ}.
STRAND 997 1009 {ECO:0000244|PDB:4ZZZ}.
SEQUENCE 1014 AA; 113084 MW; 6A5FC01EB91C046B CRC64;
MAESSDKLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV
GHSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVTGKGQD GIGSKAEKTL GDFAAEYAKS
NRSTCKGCME KIEKGQVRLS KKMVDPEKPQ LGMIDRWYHP GCFVKNREEL GFRPEYSASQ
LKGFSLLATE DKEALKKQLP GVKSEGKRKG DEVDGVDEVA KKKSKKEKDK DSKLEKALKA
QNDLIWNIKD ELKKVCSTND LKELLIFNKQ QVPSGESAIL DRVADGMVFG ALLPCEECSG
QLVFKSDAYY CTGDVTAWTK CMVKTQTPNR KEWVTPKEFR EISYLKKLKV KKQDRIFPPE
TSASVAATPP PSTASAPAAV NSSASADKPL SNMKILTLGK LSRNKDEVKA MIEKLGGKLT
GTANKASLCI STKKEVEKMN KKMEEVKEAN IRVVSEDFLQ DVSASTKSLQ ELFLAHILSP
WGAEVKAEPV EVVAPRGKSG AALSKKSKGQ VKEEGINKSE KRMKLTLKGG AAVDPDSGLE
HSAHVLEKGG KVFSATLGLV DIVKGTNSYY KLQLLEDDKE NRYWIFRSWG RVGTVIGSNK
LEQMPSKEDA IEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE AVKKLTVNPG
TKSKLPKPVQ DLIKMIFDVE SMKKAMVEYE IDLQKMPLGK LSKRQIQAAY SILSEVQQAV
SQGSSDSQIL DLSNRFYTLI PHDFGMKKPP LLNNADSVQA KVEMLDNLLD IEVAYSLLRG
GSDDSSKDPI DVNYEKLKTD IKVVDRDSEE AEIIRKYVKN THATTHNAYD LEVIDIFKIE
REGECQRYKP FKQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM
VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG LGKTTPDPSA
NISLDGVDVP LGTGISSGVN DTSLLYNEYI VYDIAQVNLK YLLKLKFNFK TSLW


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