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Werner syndrome ATP-dependent helicase (EC 3.6.4.12) (DNA helicase, RecQ-like type 3) (RecQ3) (Exonuclease WRN) (EC 3.1.-.-) (RecQ protein-like 2)

 WRN_HUMAN               Reviewed;        1432 AA.
Q14191; A1KYY9;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 2.
27-SEP-2017, entry version 200.
RecName: Full=Werner syndrome ATP-dependent helicase;
EC=3.6.4.12 {ECO:0000269|PubMed:16622405};
AltName: Full=DNA helicase, RecQ-like type 3;
Short=RecQ3;
AltName: Full=Exonuclease WRN;
EC=3.1.-.-;
AltName: Full=RecQ protein-like 2;
Name=WRN; Synonyms=RECQ3, RECQL2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-1074.
PubMed=8602509; DOI=10.1126/science.272.5259.258;
Yu C.-E., Oshima J., Fu Y.-H., Wijsman E.M., Hisama F., Alisch R.,
Matthews S., Nakura J., Miki T., Ouais S., Martin G.M., Mulligan J.,
Schellenberg G.D.;
"Positional cloning of the Werner's syndrome gene.";
Science 272:258-262(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-1074.
PubMed=16723399; DOI=10.1073/pnas.0600645103;
Agrelo R., Cheng W.H., Setien F., Ropero S., Espada J., Fraga M.F.,
Herranz M., Paz M.F., Sanchez-Cespedes M., Artiga M.J., Guerrero D.,
Castells A., von Kobbe C., Bohr V.A., Esteller M.;
"Epigenetic inactivation of the premature aging Werner syndrome gene
in human cancer.";
Proc. Natl. Acad. Sci. U.S.A. 103:8822-8827(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-1074.
Paeper B.W., Gayle M., Brady W., Swartz A., Gillett L.A., Alisch R.S.,
Mulligan J., Galas D., Fu Y.-H.;
"Genomic structure of the human Werner's gene and cloning of the mouse
homolog.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-114; LYS-343;
ILE-387; SER-533; CYS-612; PHE-708; CYS-834; SER-912; LEU-1079;
ALA-1133; ILE-1339 AND ARG-1367.
NIEHS SNPs program;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[6]
SUBCELLULAR LOCATION.
PubMed=9618508; DOI=10.1073/pnas.95.12.6887;
Marciniak R.A., Lombard D.B., Johnson F.B., Guarente L.;
"Nucleolar localization of the Werner syndrome protein in human
cells.";
Proc. Natl. Acad. Sci. U.S.A. 95:6887-6892(1998).
[7]
REPEATS.
PubMed=10049920;
Kusano K., Berres M.E., Engels W.R.;
"Evolution of the RECQ family of helicases: a Drosophila homolog,
Dmblm, is similar to the human Bloom syndrome gene.";
Genetics 151:1027-1039(1999).
[8]
POSSIBLE INVOLVEMENT IN CRC.
PubMed=9989816; DOI=10.1038/sj.onc.1202340;
Chughtai S.A., Crundwell M.C., Cruickshank N.R., Affie E.,
Armstrong S., Knowles M.A., Takle L.A., Kuo M., Khan N.,
Phillips S.M., Neoptolemos J.P., Morton D.G.;
"Two novel regions of interstitial deletion on chromosome 8p in
colorectal cancer.";
Oncogene 18:657-665(1999).
[9]
FUNCTION, MUTAGENESIS OF GLU-84, FUNCTION AS AN EXONUCLEASE,
DNA-BINDING, INTERACTION WITH PCNA, AND SUBUNIT.
PubMed=11863428; DOI=10.1021/bi0157161;
Xue Y., Ratcliff G.C., Wang H., Davis-Searles P.R., Gray M.D.,
Erie D.A., Redinbo M.R.;
"A minimal exonuclease domain of WRN forms a hexamer on DNA and
possesses both 3'- 5' exonuclease and 5'-protruding strand
endonuclease activities.";
Biochemistry 41:2901-2912(2002).
[10]
PHOSPHORYLATION.
PubMed=11889123; DOI=10.1074/jbc.M111523200;
Karmakar P., Piotrowski J., Brosh R.M. Jr., Sommers J.A., Miller S.P.,
Cheng W.H., Snowden C.M., Ramsden D.A., Bohr V.A.;
"Werner protein is a target of DNA-dependent protein kinase in vivo
and in vitro, and its catalytic activities are regulated by
phosphorylation.";
J. Biol. Chem. 277:18291-18302(2002).
[11]
INTERACTION WITH EXO1.
PubMed=12704184; DOI=10.1074/jbc.M212798200;
Sharma S., Sommers J.A., Driscoll H.C., Uzdilla L.A., Wilson T.M.,
Brosh R.M. Jr.;
"The exonucleolytic and endonucleolytic cleavage activities of human
exonuclease 1 are stimulated by an interaction with the carboxyl-
terminal region of the Werner syndrome protein.";
J. Biol. Chem. 278:23487-23496(2003).
[12]
INTERACTION WITH SUPV3L1.
PubMed=17961633; DOI=10.1016/j.mad.2007.09.001;
Pereira M., Mason P., Szczesny R.J., Maddukuri L., Dziwura S.,
Jedrzejczak R., Paul E., Wojcik A., Dybczynska L., Tudek B.,
Bartnik E., Klysik J., Bohr V.A., Stepien P.P.;
"Interaction of human SUV3 RNA/DNA helicase with BLM helicase; loss of
the SUV3 gene results in mouse embryonic lethality.";
Mech. Ageing Dev. 128:609-617(2007).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17563354; DOI=10.1073/pnas.0702513104;
Kamath-Loeb A.S., Lan L., Nakajima S., Yasui A., Loeb L.A.;
"Werner syndrome protein interacts functionally with translesion DNA
polymerases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10394-10399(2007).
[14]
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).
[15]
FUNCTION, SUBUNIT, AND DNA-BINDING.
PubMed=18596042; DOI=10.1074/jbc.M803370200;
Compton S.A., Tolun G., Kamath-Loeb A.S., Loeb L.A., Griffith J.D.;
"The Werner syndrome protein binds replication fork and Holliday
junction DNAs as an oligomer.";
J. Biol. Chem. 283:24478-24483(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440 AND SER-467, 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).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19652551; DOI=10.4161/cc.8.17.9410;
Zecevic A., Menard H., Gurel V., Hagan E., DeCaro R., Zhitkovich A.;
"WRN helicase promotes repair of DNA double-strand breaks caused by
aberrant mismatch repair of chromium-DNA adducts.";
Cell Cycle 8:2769-2778(2009).
[19]
FUNCTION.
PubMed=19283071; DOI=10.1371/journal.pone.0004825;
Opresko P.L., Sowd G., Wang H.;
"The Werner syndrome helicase/exonuclease processes mobile D-loops
through branch migration and degradation.";
PLoS ONE 4:E4825-E4825(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426; SER-440; SER-453
AND SER-467, 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).
[21]
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).
[22]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PML.
PubMed=21639834; DOI=10.1134/S000629791105004X;
Liu J., Song Y., Qian J., Liu B., Dong Y., Tian B., Sun Z.;
"Promyelocytic leukemia protein interacts with werner syndrome
helicase and regulates double-strand break repair in gamma-
irradiation-induced DNA damage responses.";
Biochemistry (Mosc.) 76:550-554(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1133, 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).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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).
[25]
POSSIBLE INVOLVEMENT IN CRC.
PubMed=24308539; DOI=10.1186/1755-8794-6-54;
Lee H., Flaherty P., Ji H.P.;
"Systematic genomic identification of colorectal cancer genes
delineating advanced from early clinical stage and metastasis.";
BMC Med. Genomics 6:54-54(2013).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-1133 AND
SER-1400, 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).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-154; LYS-241 AND LYS-252,
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).
[28]
STRUCTURE BY NMR OF 949-1092.
PubMed=16339893; DOI=10.1073/pnas.0509380102;
Hu J.S., Feng H., Zeng W., Lin G.X., Xi X.G.;
"Solution structure of a multifunctional DNA- and protein-binding
motif of human Werner syndrome protein.";
Proc. Natl. Acad. Sci. U.S.A. 102:18379-18384(2005).
[29]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 38-236 IN COMPLEXES WITH
MAGNESIUM; MANGANESE; EUROPIUM AND GMP, PARTIAL PROTEIN SEQUENCE,
IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, COFACTOR,
MUTAGENESIS OF GLU-84; TRP-145 AND TYR-212, AND CHARACTERIZATION OF
VARIANTS ILE-114 AND PRO-172.
PubMed=16622405; DOI=10.1038/nsmb1088;
Perry J.J., Yannone S.M., Holden L.G., Hitomi C., Asaithamby A.,
Han S., Cooper P.K., Chen D.J., Tainer J.A.;
"WRN exonuclease structure and molecular mechanism imply an editing
role in DNA end processing.";
Nat. Struct. Mol. Biol. 13:414-422(2006).
[30]
REVIEW ON VARIANTS.
PubMed=10220139;
DOI=10.1002/(SICI)1098-1004(1999)13:4<271::AID-HUMU2>3.0.CO;2-Q;
Moser M.J., Oshima J., Monnat R.J. Jr.;
"WRN mutations in Werner syndrome.";
Hum. Mutat. 13:271-279(1999).
[31]
STRUCTURE BY NMR OF 1140-1239.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the helicase and RNase D C-terminal domain in
Werner syndrome ATP-dependent helicase.";
Submitted (SEP-2006) to the PDB data bank.
[32]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1142-1242, PARTIAL PROTEIN
SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, AND CIRCULAR DICHROISM.
PubMed=17148451; DOI=10.1074/jbc.M610142200;
Kitano K., Yoshihara N., Hakoshima T.;
"Crystal structure of the HRDC domain of human Werner syndrome
protein, WRN.";
J. Biol. Chem. 282:2717-2728(2007).
[33]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 949-1079 IN COMPLEX WITH
DOUBLE-STRANDED DNA, INTERACTION WITH DNA, AND MUTAGENESIS OF ARG-987;
SER-989; ARG-993; PHE-1037 AND MET-1038.
PubMed=20159463; DOI=10.1016/j.str.2009.12.011;
Kitano K., Kim S.Y., Hakoshima T.;
"Structural basis for DNA strand separation by the unconventional
winged-helix domain of RecQ helicase WRN.";
Structure 18:177-187(2010).
[34]
VARIANT ARG-1367.
PubMed=9021029;
DOI=10.1002/(SICI)1096-8628(19970211)68:4<494::AID-AJMG30>3.0.CO;2-L;
Ye L., Miki T., Nakura J., Oshima J., Kamino K., Rakugi H.,
Ikegami H., Higaki J., Edland S.D., Martin G.M., Ogihara T.;
"Association of a polymorphic variant of the Werner helicase gene with
myocardial infarction in a Japanese population.";
Am. J. Med. Genet. 68:494-498(1997).
[35]
ERRATUM.
Ye L., Miki T., Nakura J., Oshima J., Kamino K., Rakugi H.,
Ikegami H., Higaki J., Edland S.D., Martin G.M., Ogihara T.;
Am. J. Med. Genet. 70:103-103(1997).
[36]
VARIANTS ILE-387 AND PHE-1074.
PubMed=9450180;
Meisslitzer C., Ruppitsch W., Weirich-Schwaiger H., Weirich H.G.,
Jabkowsky J., Klein G., Schweiger M., Hirsch-Kauffmann M.;
"Werner syndrome: characterization of mutations in the WRN gene in an
affected family.";
Eur. J. Hum. Genet. 5:364-370(1997).
[37]
VARIANT ILE-387.
PubMed=10206685;
DOI=10.1002/(SICI)1098-1004(1998)11:5<413::AID-HUMU18>3.0.CO;2-C;
Vidal V., Bay J.-O., Champomier F., Grancho M., Beauville L.,
Glowaczower C., Lemery D., Ferrara M., Bignon Y.-J.;
"The 1396del A mutation and a missense mutation or a rare polymorphism
of the WRN gene detected in a French Werner family with a severe
phenotype and a case of an unusual vulvar cancer.";
Hum. Mutat. 11:413-414(1998).
[38]
VARIANTS ALA-324 AND ARG-1367.
PubMed=10069711;
DOI=10.1002/(SICI)1096-8628(19990219)82:5<399::AID-AJMG8>3.3.CO;2-I;
Castro E., Ogburn C.E., Hunt K.E., Tilvis R., Louhija J.,
Penttinen R., Erkkola R., Panduro A., Riestra R., Piussan C.,
Deeb S.S., Wang L., Edland S.D., Martin G.M., Oshima J.;
"Polymorphisms at the Werner locus: I. Newly identified polymorphisms,
ethnic variability of 1367Cys/Arg, and its stability in a population
of Finnish centenarians.";
Am. J. Med. Genet. 82:399-403(1999).
[39]
VARIANTS ARG-32; ILE-114; PRO-172; LYS-240; TRP-383; ILE-387; LEU-724;
PHE-1074; GLU-1269 AND ARG-1367.
PubMed=11161804; DOI=10.1006/geno.2000.6405;
Passarino G., Shen P., Van Kirk J.B., Lin A.A., De Benedictis G.,
Cavalli-Sforza L.L., Oefner P.J., Underhill P.A.;
"The Werner syndrome gene and global sequence variation.";
Genomics 71:118-122(2001).
[40]
VARIANTS WRN ASN-125 AND GLU-135.
PubMed=16673358; DOI=10.1002/humu.20337;
Huang S., Lee L., Hanson N.B., Lenaerts C., Hoehn H., Poot M.,
Rubin C.D., Chen D.-F., Yang C.-C., Juch H., Dorn T., Spiegel R.,
Oral E.A., Abid M., Battisti C., Lucci-Cordisco E., Neri G.,
Steed E.H., Kidd A., Isley W., Showalter D., Vittone J.L.,
Konstantinow A., Ring J., Meyer P., Wenger S.L., Herbay A.V.,
Wollina U., Schuelke M., Huizenga C.R., Leistritz D.F., Martin G.M.,
Mian I.S., Oshima J.;
"The spectrum of WRN mutations in Werner syndrome patients.";
Hum. Mutat. 27:558-567(2006).
[41]
VARIANT [LARGE SCALE ANALYSIS] VAL-92.
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).
[42]
VARIANT [LARGE SCALE ANALYSIS] LEU-1141.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
-!- FUNCTION: Multifunctional enzyme that has both magnesium and ATP-
dependent DNA-helicase activity and 3'->5' exonuclease activity
towards double-stranded DNA with a 5'-overhang. Has no nuclease
activity towards single-stranded DNA or blunt-ended double-
stranded DNA. Binds preferentially to DNA substrates containing
alternate secondary structures, such as replication forks and
Holliday junctions. May play an important role in the dissociation
of joint DNA molecules that can arise as products of homologous
recombination, at stalled replication forks or during DNA repair.
Alleviates stalling of DNA polymerases at the site of DNA lesions.
Important for genomic integrity. Plays a role in the formation of
DNA replication focal centers; stably associates with foci
elements generating binding sites for RP-A (By similarity). Plays
a role in double-strand break repair after gamma-irradiation.
{ECO:0000250, ECO:0000269|PubMed:11863428,
ECO:0000269|PubMed:17563354, ECO:0000269|PubMed:18596042,
ECO:0000269|PubMed:19283071, ECO:0000269|PubMed:19652551,
ECO:0000269|PubMed:21639834}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:16622405}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:16622405};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:16622405};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:16622405};
Note=Binds 2 magnesium ions per subunit. Has high activity with
manganese and zinc ions (in vitro). {ECO:0000269|PubMed:16622405};
-!- SUBUNIT: Monomer, and homooligomer. May exist as homodimer,
homotrimer, homotetramer and/or homohexamer. Homotetramer, or
homohexamer, when bound to DNA. Interacts via its N-terminal
domain with WRNIP1 (By similarity). Interacts with EXO1, PCNA and
SUPV3L1. Interacts with PML (isoform PML-4). {ECO:0000250,
ECO:0000269|PubMed:11863428, ECO:0000269|PubMed:12704184,
ECO:0000269|PubMed:17961633, ECO:0000269|PubMed:18596042,
ECO:0000269|PubMed:20159463, ECO:0000269|PubMed:21639834}.
-!- INTERACTION:
P54132:BLM; NbExp=9; IntAct=EBI-368417, EBI-621372;
P39748:FEN1; NbExp=9; IntAct=EBI-368417, EBI-707816;
P16104:H2AFX; NbExp=6; IntAct=EBI-368417, EBI-494830;
P09874:PARP1; NbExp=8; IntAct=EBI-368417, EBI-355676;
P43351:RAD52; NbExp=9; IntAct=EBI-368417, EBI-706448;
P27694:RPA1; NbExp=9; IntAct=EBI-368417, EBI-621389;
Q96EB6:SIRT1; NbExp=9; IntAct=EBI-368417, EBI-1802965;
Q15554:TERF2; NbExp=8; IntAct=EBI-368417, EBI-706637;
P04637:TP53; NbExp=5; IntAct=EBI-368417, EBI-366083;
P12956:XRCC6; NbExp=8; IntAct=EBI-368417, EBI-353208;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:9618508}. Nucleus
{ECO:0000269|PubMed:17563354, ECO:0000269|PubMed:19652551}.
Nucleus, nucleoplasm {ECO:0000269|PubMed:21639834}. Note=Gamma-
irradiation leads to its translocation from nucleoli to
nucleoplasm and PML regulates the irradiation-induced WRN
relocation. {ECO:0000269|PubMed:21639834}.
-!- PTM: Phosphorylated by PRKDC. {ECO:0000269|PubMed:11889123}.
-!- DISEASE: Werner syndrome (WRN) [MIM:277700]: A rare autosomal
recessive progeroid syndrome characterized by the premature onset
of multiple age-related disorders, including atherosclerosis,
cancer, non-insulin-dependent diabetes mellitus, ocular cataracts
and osteoporosis. The major cause of death, at a median age of 47,
is myocardial infarction. {ECO:0000269|PubMed:16673358}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease
characterized by malignant lesions arising from the inner wall of
the large intestine (the colon) and the rectum. Genetic
alterations are often associated with progression from
premalignant lesion (adenoma) to invasive adenocarcinoma. Risk
factors for cancer of the colon and rectum include colon polyps,
long-standing ulcerative colitis, and genetic family history.
{ECO:0000305|PubMed:24308539, ECO:0000305|PubMed:9989816}.
Note=The disease may be caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=WRN; Note=WRN mutation db (Warner disease);
URL="http://www.pathology.washington.edu/werner/ws_wrn.html";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/WRNID284.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/wrn/";
-----------------------------------------------------------------------
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EMBL; L76937; AAC41981.1; -; Genomic_DNA.
EMBL; AY818673; AAX21098.1; -; mRNA.
EMBL; AF091214; AAC63361.1; -; mRNA.
EMBL; AF181897; AAF06162.1; -; Genomic_DNA.
EMBL; AF181896; AAF06162.1; JOINED; Genomic_DNA.
EMBL; AY442327; AAR05448.1; -; Genomic_DNA.
EMBL; AC084736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS6082.1; -.
RefSeq; NP_000544.2; NM_000553.4.
UniGene; Hs.632050; -.
PDB; 2AXL; NMR; -; A=949-1092.
PDB; 2DGZ; NMR; -; A=1140-1239.
PDB; 2E1E; X-ray; 2.30 A; A=1142-1242.
PDB; 2E1F; X-ray; 2.00 A; A=1142-1242.
PDB; 2FBT; X-ray; 2.05 A; A=38-236.
PDB; 2FBV; X-ray; 2.40 A; A=38-236.
PDB; 2FBX; X-ray; 2.20 A; A=38-236.
PDB; 2FBY; X-ray; 2.00 A; A=38-236.
PDB; 2FC0; X-ray; 2.00 A; A=38-236.
PDB; 3AAF; X-ray; 1.90 A; A/B=949-1079.
PDBsum; 2AXL; -.
PDBsum; 2DGZ; -.
PDBsum; 2E1E; -.
PDBsum; 2E1F; -.
PDBsum; 2FBT; -.
PDBsum; 2FBV; -.
PDBsum; 2FBX; -.
PDBsum; 2FBY; -.
PDBsum; 2FC0; -.
PDBsum; 3AAF; -.
DisProt; DP00443; -.
ProteinModelPortal; Q14191; -.
SMR; Q14191; -.
BioGrid; 113323; 50.
CORUM; Q14191; -.
DIP; DIP-31380N; -.
ELM; Q14191; -.
IntAct; Q14191; 26.
MINT; MINT-95856; -.
STRING; 9606.ENSP00000298139; -.
BindingDB; Q14191; -.
ChEMBL; CHEMBL2146312; -.
iPTMnet; Q14191; -.
PhosphoSitePlus; Q14191; -.
BioMuta; WRN; -.
DMDM; 322510082; -.
EPD; Q14191; -.
MaxQB; Q14191; -.
PaxDb; Q14191; -.
PeptideAtlas; Q14191; -.
PRIDE; Q14191; -.
Ensembl; ENST00000298139; ENSP00000298139; ENSG00000165392.
GeneID; 7486; -.
KEGG; hsa:7486; -.
UCSC; uc003xio.5; human.
CTD; 7486; -.
DisGeNET; 7486; -.
EuPathDB; HostDB:ENSG00000165392.9; -.
GeneCards; WRN; -.
GeneReviews; WRN; -.
H-InvDB; HIX0007441; -.
HGNC; HGNC:12791; WRN.
HPA; HPA028661; -.
MalaCards; WRN; -.
MIM; 114500; phenotype.
MIM; 277700; phenotype.
MIM; 604611; gene.
neXtProt; NX_Q14191; -.
OpenTargets; ENSG00000165392; -.
Orphanet; 902; Werner syndrome.
PharmGKB; PA367; -.
eggNOG; KOG0351; Eukaryota.
eggNOG; KOG4373; Eukaryota.
eggNOG; COG0514; LUCA.
GeneTree; ENSGT00550000074520; -.
HOGENOM; HOG000146447; -.
HOVERGEN; HBG000325; -.
InParanoid; Q14191; -.
KO; K10900; -.
OMA; SHFEDKQ; -.
OrthoDB; EOG091G0B07; -.
PhylomeDB; Q14191; -.
TreeFam; TF312852; -.
BRENDA; 3.6.4.12; 2681.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
SIGNOR; Q14191; -.
ChiTaRS; WRN; human.
EvolutionaryTrace; Q14191; -.
GeneWiki; Werner_syndrome_ATP-dependent_helicase; -.
GenomeRNAi; 7486; -.
PRO; PR:Q14191; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000165392; -.
CleanEx; HS_WRN; -.
Genevisible; Q14191; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005657; C:replication fork; ISS:BHF-UCL.
GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:UniProtKB.
GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
GO; GO:0070337; F:3'-flap-structured DNA binding; IDA:BHF-UCL.
GO; GO:1905773; F:8-hydroxy-2'-deoxyguanosine DNA binding; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IBA:GO_Central.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; IDA:UniProtKB.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0000405; F:bubble DNA binding; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003678; F:DNA helicase activity; IDA:BHF-UCL.
GO; GO:0004527; F:exonuclease activity; IDA:MGI.
GO; GO:0061749; F:forked DNA-dependent helicase activity; IDA:BHF-UCL.
GO; GO:0000400; F:four-way junction DNA binding; IDA:BHF-UCL.
GO; GO:0009378; F:four-way junction helicase activity; IDA:UniProtKB.
GO; GO:0051880; F:G-quadruplex DNA binding; IDA:UniProtKB.
GO; GO:0004386; F:helicase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0061821; F:telomeric D-loop binding; IDA:BHF-UCL.
GO; GO:0061849; F:telomeric G-quadruplex DNA binding; IC:BHF-UCL.
GO; GO:0000403; F:Y-form DNA binding; IDA:UniProtKB.
GO; GO:0007568; P:aging; NAS:UniProtKB.
GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0007569; P:cell aging; IMP:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0071480; P:cellular response to gamma radiation; IDA:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; IDA:MGI.
GO; GO:0032508; P:DNA duplex unwinding; IDA:BHF-UCL.
GO; GO:0006259; P:DNA metabolic process; IDA:UniProtKB.
GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
GO; GO:0000731; P:DNA synthesis involved in DNA repair; IDA:UniProtKB.
GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
GO; GO:0044806; P:G-quadruplex DNA unwinding; IDA:BHF-UCL.
GO; GO:0010259; P:multicellular organism aging; IMP:UniProtKB.
GO; GO:0032066; P:nucleolus to nucleoplasm transport; IDA:MGI.
GO; GO:0051345; P:positive regulation of hydrolase activity; IDA:UniProtKB.
GO; GO:0098530; P:positive regulation of strand invasion; IDA:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; IGI:MGI.
GO; GO:0040009; P:regulation of growth rate; IEA:Ensembl.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0031297; P:replication fork processing; IDA:UniProtKB.
GO; GO:0001302; P:replicative cell aging; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
GO; GO:0010225; P:response to UV-C; IDA:UniProtKB.
GO; GO:0000732; P:strand displacement; TAS:Reactome.
GO; GO:0090656; P:t-circle formation; TAS:BHF-UCL.
GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB.
GO; GO:0061820; P:telomeric D-loop disassembly; IDA:BHF-UCL.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR002562; 3'-5'_exonuclease_dom.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR029491; Helicase_HTH.
InterPro; IPR010997; HRDC-like.
InterPro; IPR002121; HRDC_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR032284; RecQ_Zn-bd.
InterPro; IPR012337; RNaseH-like_dom.
InterPro; IPR018982; RQC_domain.
InterPro; IPR011991; WHTH_DNA-bd_dom.
Pfam; PF00270; DEAD; 1.
Pfam; PF01612; DNA_pol_A_exo1; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF00570; HRDC; 1.
Pfam; PF14493; HTH_40; 1.
Pfam; PF16124; RecQ_Zn_bind; 1.
Pfam; PF09382; RQC; 1.
SMART; SM00474; 35EXOc; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00341; HRDC; 1.
SMART; SM00956; RQC; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF47819; SSF47819; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF53098; SSF53098; 1.
TIGRFAMs; TIGR00614; recQ_fam; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50967; HRDC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome;
Direct protein sequencing; Disease mutation; DNA damage; DNA repair;
DNA-binding; Exonuclease; Helicase; Hydrolase; Isopeptide bond;
Magnesium; Metal-binding; Multifunctional enzyme; Nuclease;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Ubl conjugation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 1432 Werner syndrome ATP-dependent helicase.
/FTId=PRO_0000205045.
DOMAIN 60 228 3'-5' exonuclease.
REPEAT 424 450 1. {ECO:0000269|PubMed:10049920}.
REPEAT 451 477 2. {ECO:0000269|PubMed:10049920}.
DOMAIN 558 724 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 749 899 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 1150 1229 HRDC. {ECO:0000255|PROSITE-
ProRule:PRU00328}.
NP_BIND 571 578 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 2 277 Interaction with WRNIP1. {ECO:0000250}.
REGION 424 477 2 X 27 AA tandem repeats of H-L-S-P-N-D-
N-E-N-D-T-S-Y-V-I-E-S-D-E-D-L-E-M-E-M-L-
K.
REGION 987 993 Interaction with DNA.
{ECO:0000269|PubMed:20159463}.
MOTIF 668 671 DEAH box.
COMPBIAS 507 510 Poly-Glu.
METAL 82 82 Magnesium 1; catalytic.
{ECO:0000244|PDB:2FBV,
ECO:0000244|PDB:2FBX,
ECO:0000244|PDB:2FC0,
ECO:0000269|PubMed:16622405}.
METAL 82 82 Magnesium 2; catalytic.
{ECO:0000244|PDB:2FBV,
ECO:0000244|PDB:2FBX,
ECO:0000244|PDB:2FC0,
ECO:0000269|PubMed:16622405}.
METAL 84 84 Magnesium 1; catalytic.
{ECO:0000244|PDB:2FBV,
ECO:0000244|PDB:2FBX,
ECO:0000244|PDB:2FC0,
ECO:0000269|PubMed:16622405}.
METAL 216 216 Magnesium 1; catalytic.
{ECO:0000244|PDB:2FBV,
ECO:0000244|PDB:2FBX,
ECO:0000244|PDB:2FC0,
ECO:0000269|PubMed:16622405}.
SITE 145 145 Interaction with DNA. {ECO:0000305}.
SITE 1037 1037 Interaction with DNA.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 426 426 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 440 440 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 453 453 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1133 1133 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1400 1400 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 154 154 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 241 241 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 252 252 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 32 32 K -> R (in dbSNP:rs34477820).
{ECO:0000269|PubMed:11161804}.
/FTId=VAR_017453.
VARIANT 92 92 G -> V (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036318.
VARIANT 114 114 V -> I (polymorphism; no effect on
exonuclease activity; dbSNP:rs2230009).
{ECO:0000269|PubMed:11161804,
ECO:0000269|PubMed:16622405,
ECO:0000269|Ref.4}.
/FTId=VAR_017454.
VARIANT 125 125 K -> N (in WRN; dbSNP:rs387906337).
{ECO:0000269|PubMed:16673358}.
/FTId=VAR_026588.
VARIANT 135 135 K -> E (in WRN; dbSNP:rs267607008).
{ECO:0000269|PubMed:16673358}.
/FTId=VAR_026589.
VARIANT 172 172 T -> P (polymorphism; no effect on
exonuclease activity; dbSNP:rs367991517).
{ECO:0000269|PubMed:11161804,
ECO:0000269|PubMed:16622405}.
/FTId=VAR_017455.
VARIANT 240 240 N -> K (in dbSNP:rs148229804).
{ECO:0000269|PubMed:11161804}.
/FTId=VAR_017456.
VARIANT 324 324 T -> A (in dbSNP:rs1800390).
{ECO:0000269|PubMed:10069711}.
/FTId=VAR_006904.
VARIANT 329 329 Q -> R (in dbSNP:rs4987237).
/FTId=VAR_020450.
VARIANT 343 343 E -> K (in dbSNP:rs11574222).
{ECO:0000269|Ref.4}.
/FTId=VAR_018941.
VARIANT 383 383 L -> F (in dbSNP:rs4987238).
/FTId=VAR_020451.
VARIANT 383 383 L -> W. {ECO:0000269|PubMed:11161804}.
/FTId=VAR_017457.
VARIANT 387 387 M -> I (in dbSNP:rs1800391).
{ECO:0000269|PubMed:10206685,
ECO:0000269|PubMed:11161804,
ECO:0000269|PubMed:9450180,
ECO:0000269|Ref.4}.
/FTId=VAR_006905.
VARIANT 533 533 N -> S (in dbSNP:rs11574240).
{ECO:0000269|Ref.4}.
/FTId=VAR_018942.
VARIANT 612 612 S -> C (in dbSNP:rs11574250).
{ECO:0000269|Ref.4}.
/FTId=VAR_018943.
VARIANT 708 708 S -> F (in dbSNP:rs11574289).
{ECO:0000269|Ref.4}.
/FTId=VAR_018944.
VARIANT 711 711 R -> W (in dbSNP:rs34560788).
/FTId=VAR_057124.
VARIANT 724 724 Q -> L. {ECO:0000269|PubMed:11161804}.
/FTId=VAR_017458.
VARIANT 834 834 R -> C (in dbSNP:rs3087425).
{ECO:0000269|Ref.4}.
/FTId=VAR_014913.
VARIANT 912 912 I -> S (in dbSNP:rs11574323).
{ECO:0000269|Ref.4}.
/FTId=VAR_018945.
VARIANT 1074 1074 L -> F (in dbSNP:rs1801195).
{ECO:0000269|PubMed:11161804,
ECO:0000269|PubMed:16723399,
ECO:0000269|PubMed:8602509,
ECO:0000269|PubMed:9450180,
ECO:0000269|Ref.3}.
/FTId=VAR_007903.
VARIANT 1079 1079 S -> L (in dbSNP:rs3087414).
{ECO:0000269|Ref.4}.
/FTId=VAR_014914.
VARIANT 1133 1133 S -> A (in dbSNP:rs11574358).
{ECO:0000269|Ref.4}.
/FTId=VAR_018946.
VARIANT 1141 1141 S -> L (in dbSNP:rs139323683).
{ECO:0000269|PubMed:18987736}.
/FTId=VAR_054162.
VARIANT 1269 1269 K -> E (in dbSNP:rs746648510).
{ECO:0000269|PubMed:11161804}.
/FTId=VAR_017459.
VARIANT 1339 1339 V -> I (in dbSNP:rs11574395).
{ECO:0000269|Ref.4}.
/FTId=VAR_018947.
VARIANT 1367 1367 C -> R (polymorphism associated with a
higher risk of myocardial infarction;
dbSNP:rs1346044).
{ECO:0000269|PubMed:10069711,
ECO:0000269|PubMed:11161804,
ECO:0000269|PubMed:9021029,
ECO:0000269|Ref.4}.
/FTId=VAR_006906.
MUTAGEN 84 84 E->A: Abolishes exonuclease activity.
{ECO:0000269|PubMed:11863428,
ECO:0000269|PubMed:16622405}.
MUTAGEN 88 88 L->A: No effect on exonuclease activity.
MUTAGEN 145 145 W->A: Reduces exonuclease activity.
{ECO:0000269|PubMed:16622405}.
MUTAGEN 212 212 Y->F: Strongly reduces exonuclease
activity. {ECO:0000269|PubMed:16622405}.
MUTAGEN 987 987 R->A: Reduces affinity for DNA about 8-
fold. Loss of DNA binding; when
associated with A-993.
{ECO:0000269|PubMed:20159463}.
MUTAGEN 989 989 S->A: Reduces affinity for DNA about 4-
fold. {ECO:0000269|PubMed:20159463}.
MUTAGEN 993 993 R->A: Reduces affinity for DNA about 20-
fold. Loss of DNA binding; when
associated with A-987.
{ECO:0000269|PubMed:20159463}.
MUTAGEN 993 993 R->E: Loss of DNA binding.
{ECO:0000269|PubMed:20159463}.
MUTAGEN 1037 1037 F->A: Reduces affinity for DNA about 8-
fold. {ECO:0000269|PubMed:20159463}.
MUTAGEN 1038 1038 M->A: Reduces affinity for DNA about 4-
fold. {ECO:0000269|PubMed:20159463}.
HELIX 39 41 {ECO:0000244|PDB:2FBY}.
STRAND 51 56 {ECO:0000244|PDB:2FBY}.
HELIX 59 72 {ECO:0000244|PDB:2FBY}.
STRAND 78 84 {ECO:0000244|PDB:2FBY}.
STRAND 99 105 {ECO:0000244|PDB:2FBY}.
STRAND 108 112 {ECO:0000244|PDB:2FBY}.
HELIX 114 116 {ECO:0000244|PDB:2FBY}.
STRAND 117 119 {ECO:0000244|PDB:2FBY}.
HELIX 122 128 {ECO:0000244|PDB:2FBY}.
STRAND 133 139 {ECO:0000244|PDB:2FBY}.
HELIX 140 151 {ECO:0000244|PDB:2FBY}.
STRAND 157 160 {ECO:0000244|PDB:2FBY}.
HELIX 161 169 {ECO:0000244|PDB:2FBY}.
HELIX 177 185 {ECO:0000244|PDB:2FBY}.
HELIX 193 196 {ECO:0000244|PDB:2FBY}.
STRAND 202 204 {ECO:0000244|PDB:2FBY}.
HELIX 207 228 {ECO:0000244|PDB:2FBY}.
STRAND 955 958 {ECO:0000244|PDB:2AXL}.
HELIX 960 972 {ECO:0000244|PDB:3AAF}.
TURN 973 975 {ECO:0000244|PDB:3AAF}.
HELIX 980 986 {ECO:0000244|PDB:3AAF}.
HELIX 996 1000 {ECO:0000244|PDB:3AAF}.
TURN 1002 1009 {ECO:0000244|PDB:3AAF}.
HELIX 1012 1024 {ECO:0000244|PDB:3AAF}.
STRAND 1027 1032 {ECO:0000244|PDB:3AAF}.
TURN 1036 1038 {ECO:0000244|PDB:2AXL}.
STRAND 1039 1043 {ECO:0000244|PDB:3AAF}.
HELIX 1045 1054 {ECO:0000244|PDB:3AAF}.
STRAND 1062 1064 {ECO:0000244|PDB:2AXL}.
HELIX 1147 1171 {ECO:0000244|PDB:2E1F}.
HELIX 1175 1178 {ECO:0000244|PDB:2E1F}.
HELIX 1181 1190 {ECO:0000244|PDB:2E1F}.
HELIX 1195 1198 {ECO:0000244|PDB:2E1F}.
STRAND 1201 1203 {ECO:0000244|PDB:2DGZ}.
HELIX 1206 1211 {ECO:0000244|PDB:2E1F}.
HELIX 1213 1225 {ECO:0000244|PDB:2E1F}.
SEQUENCE 1432 AA; 162461 MW; 63F10D19E90AA461 CRC64;
MSEKKLETTA QQRKCPEWMN VQNKRCAVEE RKACVRKSVF EDDLPFLEFT GSIVYSYDAS
DCSFLSEDIS MSLSDGDVVG FDMEWPPLYN RGKLGKVALI QLCVSESKCY LFHVSSMSVF
PQGLKMLLEN KAVKKAGVGI EGDQWKLLRD FDIKLKNFVE LTDVANKKLK CTETWSLNSL
VKHLLGKQLL KDKSIRCSNW SKFPLTEDQK LYAATDAYAG FIIYRNLEIL DDTVQRFAIN
KEEEILLSDM NKQLTSISEE VMDLAKHLPH AFSKLENPRR VSILLKDISE NLYSLRRMII
GSTNIETELR PSNNLNLLSF EDSTTGGVQQ KQIREHEVLI HVEDETWDPT LDHLAKHDGE
DVLGNKVERK EDGFEDGVED NKLKENMERA CLMSLDITEH ELQILEQQSQ EEYLSDIAYK
STEHLSPNDN ENDTSYVIES DEDLEMEMLK HLSPNDNEND TSYVIESDED LEMEMLKSLE
NLNSGTVEPT HSKCLKMERN LGLPTKEEEE DDENEANEGE EDDDKDFLWP APNEEQVTCL
KMYFGHSSFK PVQWKVIHSV LEERRDNVAV MATGYGKSLC FQYPPVYVGK IGLVISPLIS
LMEDQVLQLK MSNIPACFLG SAQSENVLTD IKLGKYRIVY VTPEYCSGNM GLLQQLEADI
GITLIAVDEA HCISEWGHDF RDSFRKLGSL KTALPMVPIV ALTATASSSI REDIVRCLNL
RNPQITCTGF DRPNLYLEVR RKTGNILQDL QPFLVKTSSH WEFEGPTIIY CPSRKMTQQV
TGELRKLNLS CGTYHAGMSF STRKDIHHRF VRDEIQCVIA TIAFGMGINK ADIRQVIHYG
APKDMESYYQ EIGRAGRDGL QSSCHVLWAP ADINLNRHLL TEIRNEKFRL YKLKMMAKME
KYLHSSRCRR QIILSHFEDK QVQKASLGIM GTEKCCDNCR SRLDHCYSMD DSEDTSWDFG
PQAFKLLSAV DILGEKFGIG LPILFLRGSN SQRLADQYRR HSLFGTGKDQ TESWWKAFSR
QLITEGFLVE VSRYNKFMKI CALTKKGRNW LHKANTESQS LILQANEELC PKKLLLPSSK
TVSSGTKEHC YNQVPVELST EKKSNLEKLY SYKPCDKISS GSNISKKSIM VQSPEKAYSS
SQPVISAQEQ ETQIVLYGKL VEARQKHANK MDVPPAILAT NKILVDMAKM RPTTVENVKR
IDGVSEGKAA MLAPLLEVIK HFCQTNSVQT DLFSSTKPQE EQKTSLVAKN KICTLSQSMA
ITYSLFQEKK MPLKSIAESR ILPLMTIGMH LSQAVKAGCP LDLERAGLTP EVQKIIADVI
RNPPVNSDMS KISLIRMLVP ENIDTYLIHM AIEILKHGPD SGLQPSCDVN KRRCFPGSEE
ICSSSKRSKE EVGINTETSS AERKRRLPVW FAKGSDTSKK LMDKTKRGGL FS


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