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7,8-dihydro-8-oxoguanine triphosphatase (EC 3.6.1.55) (2-hydroxy-dATP diphosphatase) (EC 3.6.1.56) (8-oxo-dGTPase) (Nucleoside diphosphate-linked moiety X motif 1) (Nudix motif 1)

 8ODP_HUMAN              Reviewed;         197 AA.
P36639; A4D205; Q6LES7; Q6P0Y6; Q7Z7N6; Q8IV95; Q9UBM0; Q9UBM9;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 3.
12-SEP-2018, entry version 179.
RecName: Full=7,8-dihydro-8-oxoguanine triphosphatase;
EC=3.6.1.55 {ECO:0000269|PubMed:10373420, ECO:0000269|PubMed:10608900, ECO:0000269|PubMed:11139615, ECO:0000269|PubMed:11756418, ECO:0000269|PubMed:22556419, ECO:0000269|PubMed:7782328, ECO:0000269|PubMed:8226881};
AltName: Full=2-hydroxy-dATP diphosphatase;
EC=3.6.1.56 {ECO:0000269|PubMed:10373420, ECO:0000269|PubMed:11139615, ECO:0000269|PubMed:11756418, ECO:0000269|PubMed:12857738, ECO:0000269|PubMed:24695224};
AltName: Full=8-oxo-dGTPase;
AltName: Full=Nucleoside diphosphate-linked moiety X motif 1;
Short=Nudix motif 1;
Flags: Precursor;
Name=NUDT1; Synonyms=MTH1 {ECO:0000303|PubMed:7713500};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P18), PARTIAL PROTEIN SEQUENCE,
CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=8226881;
Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H.,
Sekiguchi M.;
"Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-
oxo-dGTP, a mutagenic substrate for DNA synthesis.";
J. Biol. Chem. 268:23524-23530(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=7713500; DOI=10.1006/geno.1994.1657;
Furuichi M., Yoshida M.C., Oda H., Tajiri T., Nakabeppu Y.,
Tsuzuki T., Sekiguchi M.;
"Genomic structure and chromosome location of the human mutT homologue
gene MTH1 encoding 8-oxo-dGTPase for prevention of A:T to C:G
transversion.";
Genomics 24:485-490(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P18), TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND VARIANT MET-124.
PubMed=9211940; DOI=10.1074/jbc.272.28.17843;
Oda H., Nakabeppu Y., Furuichi M., Sekiguchi M.;
"Regulation of expression of the human MTH1 gene encoding 8-oxo-
dGTPase. Alternative splicing of transcription products.";
J. Biol. Chem. 272:17843-17850(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P18/P21/P22/P26), ALTERNATIVE
INITIATION, AND POLYMORPHISM.
PubMed=10536140; DOI=10.1093/nar/27.22.4335;
Oda H., Taketomi A., Maruyama R., Itoh R., Nishioka K., Yakushiji H.,
Suzuki T., Sekiguchi M., Nakabeppu Y.;
"Multi-forms of human MTH1 polypeptides produced by alternative
translation initiation and single nucleotide polymorphism.";
Nucleic Acids Res. 27:4335-4343(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P18).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[8]
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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS P18 AND P22), AND
VARIANT MET-124.
TISSUE=Bone, Lymph, Mammary gland, and Muscle;
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).
[11]
SUBCELLULAR LOCATION (ISOFORM P18), AND CATALYTIC ACTIVITY.
PubMed=7782328; DOI=10.1074/jbc.270.24.14659;
Kang D., Nishida J., Iyama A., Nakabeppu Y., Furuichi M., Fujiwara T.,
Sekiguchi M., Takeshige K.;
"Intracellular localization of 8-oxo-dGTPase in human cells, with
special reference to the role of the enzyme in mitochondria.";
J. Biol. Chem. 270:14659-14665(1995).
[12]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10373420; DOI=10.1074/jbc.274.26.18201;
Fujikawa K., Kamiya H., Yakushiji H., Fujii Y., Nakabeppu Y.,
Kasai H.;
"The oxidized forms of dATP are substrates for the human MutT
homologue, the hMTH1 protein.";
J. Biol. Chem. 274:18201-18205(1999).
[13]
CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-77; GLY-78; VAL-80; GLN-81;
GLY-83; ILE-86; ASP-88; GLY-89; ALA-90; LEU-94; GLN-95; GLU-96; GLU-97
AND SER-98, AND FUNCTION.
PubMed=10608900; DOI=10.1074/jbc.274.53.38251;
Fujii Y., Shimokawa H., Sekiguchi M., Nakabeppu Y.;
"Functional significance of the conserved residues for the 23-residue
module among MTH1 and MutT family proteins.";
J. Biol. Chem. 274:38251-38259(1999).
[14]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11139615; DOI=10.1093/nar/29.2.449;
Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.;
"Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-
ATP.";
Nucleic Acids Res. 29:449-454(2001).
[15]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-68; TRP-158;
ASP-160; LEU-191; ARG-192; GLU-193; VAL-194; ASP-195; THR-196;
VAL-197; 192-ARG--VAL-197; 193-GLU--VAL-197; 194-VAL-VAL-197 AND
195-ASP--VAL-197.
PubMed=11756418; DOI=10.1074/jbc.M110566200;
Sakai Y., Furuichi M., Takahashi M., Mishima M., Iwai S.,
Shirakawa M., Nakabeppu Y.;
"A molecular basis for the selective recognition of 2-hydroxy-dATP and
8-oxo-dGTP by human MTH1.";
J. Biol. Chem. 277:8579-8587(2002).
[16]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION (ISOFORM P18).
PubMed=12857738; DOI=10.1074/jbc.M306201200;
Yoshimura D., Sakumi K., Ohno M., Sakai Y., Furuichi M., Iwai S.,
Nakabeppu Y.;
"An oxidized purine nucleoside triphosphatase, MTH1, suppresses cell
death caused by oxidative stress.";
J. Biol. Chem. 278:37965-37973(2003).
[17]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORM P26),
ALTERNATIVE SPLICING, AND CHARACTERIZATION OF VARIANT MET-124.
PubMed=16607562; DOI=10.1007/s00109-006-0053-5;
Sakai Y., Oda H., Yoshimura D., Furuichi M., Kang D., Iwai S.,
Hara T., Nakabeppu Y.;
"The GT to GC single nucleotide polymorphism at the beginning of an
alternative exon 2C of human MTH1 gene confers an amino terminal
extension that functions as a mitochondrial targeting signal.";
J. Mol. Med. 84:660-670(2006).
[18]
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).
[19]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=22556419; DOI=10.1074/jbc.M112.363010;
Takagi Y., Setoyama D., Ito R., Kamiya H., Yamagata Y., Sekiguchi M.;
"Human MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine
and deoxyguanosine diphosphates: comparison with MTH1 and MTH2.";
J. Biol. Chem. 287:21541-21549(2012).
[20]
STRUCTURE BY NMR OF 42-197, SUBUNIT, COFACTOR, AND SUBSTRATE BINDING
SITE.
PubMed=15133035; DOI=10.1074/jbc.M402393200;
Mishima M., Sakai Y., Itoh N., Kamiya H., Furuichi M., Takahashi M.,
Yamagata Y., Iwai S., Nakabeppu Y., Shirakawa M.;
"Structure of human MTH1, a Nudix family hydrolase that selectively
degrades oxidized purine nucleoside triphosphates.";
J. Biol. Chem. 279:33806-33815(2004).
[21]
CRYSTALLIZATION, AND PRELIMINARY X-RAY CRYSTALLOGRAPHY (1.95
ANGSTROMS).
PubMed=17142918; DOI=10.1107/S1744309106049529;
Nakamura T., Kitaguchi Y., Miyazawa M., Kamiya H., Toma S.,
Ikemizu S., Shirakawa M., Nakabeppu Y., Yamagata Y.;
"Crystallization and preliminary X-ray analysis of human MTH1
complexed with two oxidized nucleotides, 8-oxo-dGMP and 2-oxo-dATP.";
Acta Crystallogr. F 62:1283-1285(2006).
[22] {ECO:0000244|PDB:3ZR0, ECO:0000244|PDB:3ZR1}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 42-197 IN COMPLEX WITH
8-OXO-DGMP, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=21787772; DOI=10.1016/j.febslet.2011.07.017;
Svensson L.M., Jemth A.S., Desroses M., Loseva O., Helleday T.,
Hogbom M., Stenmark P.;
"Crystal structure of human MTH1 and the 8-oxo-dGMP product complex.";
FEBS Lett. 585:2617-2621(2011).
[23]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 42-197.
Structural genomics consortium (SGC);
Tresaugues L., Siponen M.I., Arrowsmith C.H., Berglund H., Bountra C.,
Collins R., Edwards A.M., Ekblad T., Flodin S., Flores A.,
Graslund S., Hammarstrom M., Johansson I., Karlberg T., Kol S.,
Kotenyova T., Kouznetsova E., Moche M., Nyman T., Persson C.,
Schuler H., Schutz P., Thorsell A.G., Van Der Berg S., Wahlberg E.,
Weigelt J., Welin M., Nordlund P.;
"Crystal Structure of Human 8-oxo-dGTPase (MTH1).";
Submitted (JAN-2011) to the PDB data bank.
[24] {ECO:0000244|PDB:4N1T, ECO:0000244|PDB:4N1U}
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 42-196 IN COMPLEX WITH
SYNTHETIC INHIBITORS, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
GLU-97.
PubMed=24695224; DOI=10.1038/nature13181;
Gad H., Koolmeister T., Jemth A.S., Eshtad S., Jacques S.A.,
Strom C.E., Svensson L.M., Schultz N., Lundback T., Einarsdottir B.O.,
Saleh A., Gokturk C., Baranczewski P., Svensson R., Berntsson R.P.,
Gustafsson R., Stromberg K., Sanjiv K., Jacques-Cordonnier M.C.,
Desroses M., Gustavsson A.L., Olofsson R., Johansson F., Homan E.J.,
Loseva O., Brautigam L., Johansson L., Hoglund A., Hagenkort A.,
Pham T., Altun M., Gaugaz F.Z., Vikingsson S., Evers B.,
Henriksson M., Vallin K.S., Wallner O.A., Hammarstrom L.G., Wiita E.,
Almlof I., Kalderen C., Axelsson H., Djureinovic T., Puigvert J.C.,
Haggblad M., Jeppsson F., Martens U., Lundin C., Lundgren B.,
Granelli I., Jensen A.J., Artursson P., Nilsson J.A., Stenmark P.,
Scobie M., Berglund U.W., Helleday T.;
"MTH1 inhibition eradicates cancer by preventing sanitation of the
dNTP pool.";
Nature 508:215-221(2014).
[25] {ECO:0000244|PDB:4C9W, ECO:0000244|PDB:4C9X}
X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 42-197 IN COMPLEX WITH
SYNTHETIC INHIBITORS, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=24695225; DOI=10.1038/NATURE13194;
Huber K.V., Salah E., Radic B., Gridling M., Elkins J.M., Stukalov A.,
Jemth A.S., Gokturk C., Sanjiv K., Stromberg K., Pham T.,
Berglund U.W., Colinge J., Bennett K.L., Loizou J.I., Helleday T.,
Knapp S., Superti-Furga G.;
"Stereospecific targeting of MTH1 by (S)-crizotinib as an anticancer
strategy.";
Nature 508:222-227(2014).
[26] {ECO:0000244|PDB:5FSI, ECO:0000244|PDB:5FSK, ECO:0000244|PDB:5FSL, ECO:0000244|PDB:5FSM, ECO:0000244|PDB:5FSN, ECO:0000244|PDB:5FSO}
X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 42-197 IN COMPLEX WITH
8-OXO-GTP; 8-OXO-ATP AND SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, AND
FUNCTION.
PubMed=26999531; DOI=10.1371/journal.pone.0151154;
Nissink J.W., Bista M., Breed J., Carter N., Embrey K., Read J.,
Winter-Holt J.J.;
"MTH1 Substrate Recognition--An Example of Specific Promiscuity.";
PLoS ONE 11:e0151154-e0151154(2016).
[27] {ECO:0000244|PDB:5NHY}
X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 42-197, AND FUNCTION.
PubMed=28679043; DOI=10.1021/acschembio.7b00370;
Ellermann M., Eheim A., Rahm F., Viklund J., Guenther J.,
Andersson M., Ericsson U., Forsblom R., Ginman T., Lindstrom J.,
Silvander C., Tresaugues L., Giese A., Bunse S., Neuhaus R.,
Weiske J., Quanz M., Glasauer A., Nowak-Reppel K., Bader B.,
Irlbacher H., Meyer H., Queisser N., Bauser M., Haegebarth A.,
Gorjanacz M.;
"Novel Class of Potent and Cellularly Active Inhibitors Devalidates
MTH1 as Broad-Spectrum Cancer Target.";
ACS Chem. Biol. 12:1986-1992(2017).
[28] {ECO:0000244|PDB:5GHI, ECO:0000244|PDB:5GHJ, ECO:0000244|PDB:5GHM, ECO:0000244|PDB:5GHN, ECO:0000244|PDB:5GHO, ECO:0000244|PDB:5GHP, ECO:0000244|PDB:5GHQ, ECO:0000244|PDB:5WS7}
X-RAY CRYSTALLOGRAPHY (1.00 ANGSTROMS) OF 42-197 IN COMPLEXES WITH
8-OXO-GTP AND 2-OXO-ATP, CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS
OF ASP-161.
PubMed=28035004; DOI=10.1074/jbc.M116.749713;
Waz S., Nakamura T., Hirata K., Koga-Ogawa Y., Chirifu M., Arimori T.,
Tamada T., Ikemizu S., Nakabeppu Y., Yamagata Y.;
"Structural and Kinetic Studies of the Human Nudix Hydrolase MTH1
Reveal the Mechanism for Its Broad Substrate Specificity.";
J. Biol. Chem. 292:2785-2794(2017).
[29]
VARIANT MET-124.
PubMed=15516784; DOI=10.1507/endocrj.51.493;
Miyako K., Kohno H., Ihara K., Kuromaru R., Matsuura N., Hara T.;
"Association study of human MTH1 gene polymorphisms with type 1
diabetes mellitus.";
Endocr. J. 51:493-498(2004).
[30]
VARIANT MET-124.
PubMed=16774934; DOI=10.1093/carcin/bgl095;
Kohno T., Sakiyama T., Kunitoh H., Goto K., Nishiwaki Y., Saito D.,
Hirose H., Eguchi T., Yanagitani N., Saito R., Sasaki-Matsumura R.,
Mimaki S., Toyama K., Yamamoto S., Kuchiba A., Sobue T., Ohta T.,
Ohki M., Yokota J.;
"Association of polymorphisms in the MTH1 gene with small cell lung
carcinoma risk.";
Carcinogenesis 27:2448-2454(2006).
-!- FUNCTION: Antimutagenic (PubMed:8226881, PubMed:7713500,
PubMed:10608900). Plays a redundant role in sanitizing oxidized
nucleotide pools, such as 8-oxo-dGTP pools (PubMed:28679043). Acts
as a sanitizing enzyme for oxidized nucleotide pools, thus
suppressing cell dysfunction and death induced by oxidative stress
(PubMed:12857738, PubMed:24695224, PubMed:24695225). Hydrolyzes 8-
oxo-dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing
misincorporation of oxidized purine nucleoside triphosphates into
DNA and subsequently preventing A:T to C:G and G:C to T:A
transversions (PubMed:8226881, PubMed:10373420, PubMed:10608900,
PubMed:11756418, PubMed:12857738, PubMed:16607562,
PubMed:24695224, PubMed:24695225, PubMed:26999531,
PubMed:28035004). Able to hydrolyze also the corresponding
ribonucleotides, 2-OH-ATP, 8-oxo-GTP and 8-oxo-ATP
(PubMed:10373420, PubMed:11139615). Does not play a role in U8
snoRNA decapping activity. Binds U8 snoRNA (By similarity).
{ECO:0000250|UniProtKB:P53368, ECO:0000269|PubMed:10373420,
ECO:0000269|PubMed:10608900, ECO:0000269|PubMed:11139615,
ECO:0000269|PubMed:11756418, ECO:0000269|PubMed:12857738,
ECO:0000269|PubMed:16607562, ECO:0000269|PubMed:22556419,
ECO:0000269|PubMed:24695224, ECO:0000269|PubMed:24695225,
ECO:0000269|PubMed:26999531, ECO:0000269|PubMed:28035004,
ECO:0000269|PubMed:28679043, ECO:0000269|PubMed:7713500,
ECO:0000269|PubMed:8226881}.
-!- CATALYTIC ACTIVITY: 8-oxo-dGTP + H(2)O = 8-oxo-dGMP + diphosphate.
{ECO:0000269|PubMed:10373420, ECO:0000269|PubMed:10608900,
ECO:0000269|PubMed:11139615, ECO:0000269|PubMed:11756418,
ECO:0000269|PubMed:12857738, ECO:0000269|PubMed:16607562,
ECO:0000269|PubMed:21787772, ECO:0000269|PubMed:22556419,
ECO:0000269|PubMed:24695224, ECO:0000269|PubMed:24695225,
ECO:0000269|PubMed:26999531, ECO:0000269|PubMed:28035004,
ECO:0000269|PubMed:7782328, ECO:0000269|PubMed:8226881}.
-!- CATALYTIC ACTIVITY: 2-hydroxy-dATP + H(2)O = 2-hydroxy-dAMP +
diphosphate. {ECO:0000269|PubMed:10373420,
ECO:0000269|PubMed:11139615, ECO:0000269|PubMed:11756418,
ECO:0000269|PubMed:12857738, ECO:0000269|PubMed:16607562,
ECO:0000269|PubMed:24695224, ECO:0000269|PubMed:24695225,
ECO:0000269|PubMed:26999531, ECO:0000269|PubMed:28035004}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000305|PubMed:15133035};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000305|PubMed:15133035};
-!- ACTIVITY REGULATION: 2-hydroxy-dATPase activity is inhibited by 2-
OH-dADP, 8-OH-dGDP and 8-OH-dGTP. 8-OH-dGTPase activity is
inhibited by 8-OH-dGDP, 2-OH-dADP and 2-OH-dATP.
{ECO:0000269|PubMed:10373420}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=8.3 uM for 2-hydroxy-dATP (at 30 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:11139615};
KM=5.7 uM for 2-hydroxy-dATP (at 30 degrees Celsius and pH 7.2)
{ECO:0000269|PubMed:11139615};
KM=4.3 uM for 2-hydroxy-rATP (at 30 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:11139615};
KM=13.9 uM for 8-hydroxy-dATP (at 30 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:11139615};
KM=51.0 uM for 8-hydroxy-rATP (at 30 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:11139615};
KM=15.2 uM for 8-hydroxy-dGTP (at 30 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:11139615};
KM=12.8 uM for 8-hydroxy-dGTP (at 30 degrees Celsius and pH 7.2)
{ECO:0000269|PubMed:11139615};
KM=13.2 uM for 8-hydroxy-dGTP (at 22 degrees Celsius and pH 7.5)
{ECO:0000269|PubMed:21787772};
KM=55.0 uM for 8-hydroxy-rGTP (at 30 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:11139615};
KM=258 uM for dGTP (at 30 degrees Celsius and pH 8.0)
{ECO:0000269|PubMed:11139615};
Note=The kinetic constants are determined for the recombinant
enzyme expressed in E.coli. 2-hydroxy-rATP shows the best
catalytic efficiency.;
pH dependence:
Optimum pH is 7.8-8.2 with 8-hydroxy-dGTP as substrate, and 8.0-
8.5 with 2-hydroxy-dATP as substrate.
{ECO:0000269|PubMed:10373420, ECO:0000269|PubMed:11139615,
ECO:0000269|PubMed:21787772};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15133035,
ECO:0000269|PubMed:21787772}.
-!- INTERACTION:
V9HWA0:HEL-S-5; NbExp=3; IntAct=EBI-1048967, EBI-10207332;
-!- SUBCELLULAR LOCATION: Isoform p18: Cytoplasm, cytosol
{ECO:0000269|PubMed:12857738, ECO:0000269|PubMed:16607562,
ECO:0000269|PubMed:7782328}. Mitochondrion matrix
{ECO:0000269|PubMed:7782328, ECO:0000305|PubMed:12857738,
ECO:0000305|PubMed:16607562}. Nucleus
{ECO:0000269|PubMed:12857738, ECO:0000269|PubMed:7782328}.
Note=Mostly present in cytosol (PubMed:7782328). A minor
proportion is mitochondrial (PubMed:7782328). A very small amount
of the protein is associated with nuclei (PubMed:7782328). Variant
Met-124 has decreased efficiency in translocation to mitochondria
(PubMed:16607562). {ECO:0000269|PubMed:16607562,
ECO:0000269|PubMed:7782328}.
-!- SUBCELLULAR LOCATION: Isoform p26: Mitochondrion matrix
{ECO:0000269|PubMed:16607562}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=4;
Name=p26;
IsoId=P36639-1; Sequence=Displayed;
Note=Derived from a B-type mRNA with a polymorphic alteration
(GU-->GC) at the beginning of exon 2c that converts an in-frame
UGA to CGA yielding another in-frame AUG further upstream.;
Name=p22;
IsoId=P36639-2; Sequence=VSP_018812;
Name=p21;
IsoId=P36639-3; Sequence=VSP_018813;
Name=p18;
IsoId=P36639-4; Sequence=VSP_018814;
-!- TISSUE SPECIFICITY: Widely expressed with highest expression in
thymus, testis, embryo and proliferating blood lymphocytes.
{ECO:0000269|PubMed:9211940}.
-!- DEVELOPMENTAL STAGE: In peripheral blood lymphocytes, expressed at
much higher levels in proliferating cells than in resting cells.
{ECO:0000269|PubMed:9211940}.
-!- PTM: The N-terminus is blocked.
-!- POLYMORPHISM: A polymorphism between Met-1 and Met-19 removes a
stop codon before the initiation codon for isoform p22 and gives
rise to the production of isoform p26. The allele frequency of
isoform p26 is about 20%. {ECO:0000269|PubMed:10536140}.
-!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
-!- CAUTION: The role in cancer cell survival is under debate. Was
originally considered to play a role as a sanitizing enzyme for
oxidized nucleotide pools, and thus important for the survival of
cancer cells (PubMed:24695224, PubMed:24695225). A later study
indicates that NUDT1 plays a redundant role in eliminating
oxidized nucleotides and that it is not essential for cancer cell
proliferation and survival (PubMed:28679043).
{ECO:0000269|PubMed:24695224, ECO:0000269|PubMed:24695225,
ECO:0000269|PubMed:28679043}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/nudt1/";
-----------------------------------------------------------------------
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EMBL; D16581; BAA04013.1; -; mRNA.
EMBL; D38594; BAA07601.1; -; Genomic_DNA.
EMBL; AB025233; BAA83791.1; -; mRNA.
EMBL; AB025234; BAA83792.1; -; mRNA.
EMBL; AB025235; BAA83793.1; -; mRNA.
EMBL; AB025236; BAA83794.1; -; mRNA.
EMBL; AB025237; BAA83795.1; -; mRNA.
EMBL; AB025238; BAA83796.1; -; mRNA.
EMBL; AB025239; BAA83797.1; -; mRNA.
EMBL; AB025240; BAA83798.1; -; mRNA.
EMBL; AB025241; BAA83799.1; -; mRNA.
EMBL; AB025242; BAA83800.1; -; mRNA.
EMBL; DQ230907; ABB02181.1; -; Genomic_DNA.
EMBL; CH236953; EAL23948.1; -; Genomic_DNA.
EMBL; CH236953; EAL23949.1; -; Genomic_DNA.
EMBL; CR407655; CAG28583.1; -; mRNA.
EMBL; CH471144; EAW87225.1; -; Genomic_DNA.
EMBL; CH471144; EAW87227.1; -; Genomic_DNA.
EMBL; AC004971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC014618; AAH14618.1; -; mRNA.
EMBL; BC040144; AAH40144.2; -; mRNA.
EMBL; BC051375; AAH51375.2; -; mRNA.
EMBL; BC065367; AAH65367.1; -; mRNA.
CCDS; CCDS5329.1; -. [P36639-2]
CCDS; CCDS5330.1; -. [P36639-4]
RefSeq; NP_002443.3; NM_002452.3. [P36639-4]
RefSeq; NP_945186.1; NM_198948.1. [P36639-4]
RefSeq; NP_945187.1; NM_198949.1. [P36639-2]
RefSeq; NP_945188.1; NM_198950.1. [P36639-4]
RefSeq; NP_945190.1; NM_198952.1. [P36639-2]
RefSeq; NP_945191.1; NM_198953.1. [P36639-4]
RefSeq; NP_945192.1; NM_198954.1. [P36639-2]
UniGene; Hs.534331; -.
PDB; 1IRY; NMR; -; A=42-197.
PDB; 3Q93; X-ray; 1.80 A; A/B=42-197.
PDB; 3WHW; X-ray; 2.70 A; A/B=42-197.
PDB; 3ZR0; X-ray; 1.80 A; A/B=42-197.
PDB; 3ZR1; X-ray; 1.90 A; A/B=42-197.
PDB; 4C9W; X-ray; 1.65 A; A=42-197.
PDB; 4C9X; X-ray; 1.20 A; A=42-197.
PDB; 4N1T; X-ray; 1.60 A; A=42-197.
PDB; 4N1U; X-ray; 1.60 A; A/B=42-196.
PDB; 5ANS; X-ray; 1.60 A; A=42-197.
PDB; 5ANT; X-ray; 2.00 A; A/B/C=42-197.
PDB; 5ANU; X-ray; 1.80 A; A=42-197.
PDB; 5ANV; X-ray; 1.16 A; A=42-197.
PDB; 5ANW; X-ray; 1.37 A; A=42-197.
PDB; 5FSI; X-ray; 1.63 A; A=42-197.
PDB; 5FSK; X-ray; 1.56 A; A=42-197.
PDB; 5FSL; X-ray; 1.24 A; A=42-197.
PDB; 5FSM; X-ray; 1.67 A; A=42-197.
PDB; 5FSN; X-ray; 1.69 A; A=42-197.
PDB; 5FSO; X-ray; 1.67 A; A=42-197.
PDB; 5GHI; X-ray; 1.21 A; A/B=42-197.
PDB; 5GHJ; X-ray; 1.20 A; A/B=42-197.
PDB; 5GHM; X-ray; 1.50 A; A/B=42-197.
PDB; 5GHN; X-ray; 1.39 A; A/B=42-197.
PDB; 5GHO; X-ray; 1.19 A; A/B=42-197.
PDB; 5GHP; X-ray; 1.19 A; A/B=42-197.
PDB; 5GHQ; X-ray; 1.18 A; A/B=42-197.
PDB; 5NGR; X-ray; 2.20 A; A/B=42-197.
PDB; 5NGS; X-ray; 1.85 A; A/B=42-197.
PDB; 5NGT; X-ray; 1.54 A; A=42-197.
PDB; 5NHY; X-ray; 1.72 A; A/B=42-197.
PDB; 5WS7; X-ray; 1.00 A; A/B=42-197.
PDB; 6F1X; X-ray; 1.90 A; A/B=42-197.
PDB; 6F20; X-ray; 2.00 A; A/B=42-197.
PDB; 6F22; X-ray; 1.55 A; A/B=42-197.
PDB; 6F23; X-ray; 1.84 A; A/B=42-197.
PDBsum; 1IRY; -.
PDBsum; 3Q93; -.
PDBsum; 3WHW; -.
PDBsum; 3ZR0; -.
PDBsum; 3ZR1; -.
PDBsum; 4C9W; -.
PDBsum; 4C9X; -.
PDBsum; 4N1T; -.
PDBsum; 4N1U; -.
PDBsum; 5ANS; -.
PDBsum; 5ANT; -.
PDBsum; 5ANU; -.
PDBsum; 5ANV; -.
PDBsum; 5ANW; -.
PDBsum; 5FSI; -.
PDBsum; 5FSK; -.
PDBsum; 5FSL; -.
PDBsum; 5FSM; -.
PDBsum; 5FSN; -.
PDBsum; 5FSO; -.
PDBsum; 5GHI; -.
PDBsum; 5GHJ; -.
PDBsum; 5GHM; -.
PDBsum; 5GHN; -.
PDBsum; 5GHO; -.
PDBsum; 5GHP; -.
PDBsum; 5GHQ; -.
PDBsum; 5NGR; -.
PDBsum; 5NGS; -.
PDBsum; 5NGT; -.
PDBsum; 5NHY; -.
PDBsum; 5WS7; -.
PDBsum; 6F1X; -.
PDBsum; 6F20; -.
PDBsum; 6F22; -.
PDBsum; 6F23; -.
ProteinModelPortal; P36639; -.
SMR; P36639; -.
BioGrid; 110621; 14.
IntAct; P36639; 9.
STRING; 9606.ENSP00000339503; -.
BindingDB; P36639; -.
ChEMBL; CHEMBL3708265; -.
iPTMnet; P36639; -.
PhosphoSitePlus; P36639; -.
DMDM; 254763430; -.
EPD; P36639; -.
MaxQB; P36639; -.
PaxDb; P36639; -.
PeptideAtlas; P36639; -.
PRIDE; P36639; -.
ProteomicsDB; 55217; -.
ProteomicsDB; 55218; -. [P36639-2]
ProteomicsDB; 55219; -. [P36639-3]
ProteomicsDB; 55220; -. [P36639-4]
TopDownProteomics; P36639-4; -. [P36639-4]
DNASU; 4521; -.
Ensembl; ENST00000339737; ENSP00000343439; ENSG00000106268. [P36639-4]
Ensembl; ENST00000343985; ENSP00000339503; ENSG00000106268. [P36639-2]
Ensembl; ENST00000356714; ENSP00000349148; ENSG00000106268. [P36639-4]
Ensembl; ENST00000397046; ENSP00000380239; ENSG00000106268. [P36639-4]
Ensembl; ENST00000397048; ENSP00000380241; ENSG00000106268. [P36639-2]
Ensembl; ENST00000397049; ENSP00000380242; ENSG00000106268. [P36639-4]
GeneID; 4521; -.
KEGG; hsa:4521; -.
UCSC; uc003slr.1; human. [P36639-1]
CTD; 4521; -.
DisGeNET; 4521; -.
EuPathDB; HostDB:ENSG00000106268.15; -.
GeneCards; NUDT1; -.
HGNC; HGNC:8048; NUDT1.
HPA; HPA012636; -.
MIM; 600312; gene.
neXtProt; NX_P36639; -.
OpenTargets; ENSG00000106268; -.
PharmGKB; PA31830; -.
eggNOG; ENOG410IXIA; Eukaryota.
eggNOG; COG0494; LUCA.
GeneTree; ENSGT00390000000341; -.
HOGENOM; HOG000261970; -.
HOVERGEN; HBG000032; -.
InParanoid; P36639; -.
KO; K17816; -.
OMA; GAGKWNG; -.
OrthoDB; EOG091G0O4Y; -.
PhylomeDB; P36639; -.
TreeFam; TF106348; -.
BioCyc; MetaCyc:HS02879-MONOMER; -.
BRENDA; 3.6.1.55; 2681.
BRENDA; 3.6.1.56; 2681.
Reactome; R-HSA-2393930; Phosphate bond hydrolysis by NUDT proteins.
SABIO-RK; P36639; -.
EvolutionaryTrace; P36639; -.
GeneWiki; NUDT1; -.
GenomeRNAi; 4521; -.
PRO; PR:P36639; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106268; Expressed in 175 organ(s), highest expression level in right testis.
CleanEx; HS_NUDT1; -.
ExpressionAtlas; P36639; baseline and differential.
Genevisible; P36639; HS.
GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0044714; F:2-hydroxy-(deoxy)adenosine-triphosphate pyrophosphatase activity; EXP:Reactome.
GO; GO:0044713; F:2-hydroxy-adenosine triphosphate pyrophosphatase activity; EXP:Reactome.
GO; GO:0035539; F:8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity; IDA:UniProtKB.
GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IDA:UniProtKB.
GO; GO:0047693; F:ATP diphosphatase activity; IDA:UniProtKB.
GO; GO:0036219; F:GTP diphosphatase activity; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0046061; P:dATP catabolic process; IDA:UniProtKB.
GO; GO:0006203; P:dGTP catabolic process; IDA:UniProtKB.
GO; GO:0042262; P:DNA protection; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IC:UniProtKB.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0034656; P:nucleobase-containing small molecule catabolic process; TAS:Reactome.
GO; GO:0006195; P:purine nucleotide catabolic process; IDA:UniProtKB.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc.
InterPro; IPR020476; Nudix_hydrolase.
InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
InterPro; IPR020084; NUDIX_hydrolase_CS.
InterPro; IPR000086; NUDIX_hydrolase_dom.
InterPro; IPR003563; OxG-triPHTase.
Pfam; PF00293; NUDIX; 1.
PRINTS; PR01403; 8OXTPHPHTASE.
PRINTS; PR00502; NUDIXFAMILY.
SUPFAM; SSF55811; SSF55811; 1.
PROSITE; PS51462; NUDIX; 1.
PROSITE; PS00893; NUDIX_BOX; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Complete proteome; Cytoplasm;
Direct protein sequencing; Hydrolase; Magnesium; Metal-binding;
Mitochondrion; Nucleus; Polymorphism; Reference proteome; RNA-binding;
Transit peptide.
TRANSIT 1 18 Mitochondrion. {ECO:0000255}.
CHAIN 19 197 7,8-dihydro-8-oxoguanine triphosphatase.
/FTId=PRO_0000019944.
DOMAIN 44 173 Nudix hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00794}.
REGION 76 79 Substrate binding. {ECO:0000244|PDB:5FSK,
ECO:0000269|PubMed:26999531}.
REGION 158 161 Substrate binding. {ECO:0000244|PDB:3ZR0,
ECO:0000244|PDB:5FSI,
ECO:0000244|PDB:5FSK,
ECO:0000244|PDB:5GHI,
ECO:0000244|PDB:5GHM,
ECO:0000244|PDB:5GHO,
ECO:0000269|PubMed:21787772,
ECO:0000269|PubMed:26999531}.
MOTIF 78 99 Nudix box. {ECO:0000255|PROSITE-
ProRule:PRU00794}.
METAL 78 78 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
METAL 93 93 Magnesium. {ECO:0000250}.
METAL 96 96 Magnesium. {ECO:0000250}.
METAL 97 97 Magnesium. {ECO:0000250}.
BINDING 49 49 Substrate; via carbonyl oxygen.
{ECO:0000244|PDB:3ZR0,
ECO:0000244|PDB:5FSI,
ECO:0000244|PDB:5GHI,
ECO:0000269|PubMed:21787772,
ECO:0000269|PubMed:26999531}.
BINDING 64 64 Substrate. {ECO:0000244|PDB:3ZR0,
ECO:0000244|PDB:5GHI,
ECO:0000269|PubMed:21787772,
ECO:0000269|PubMed:26999531}.
BINDING 74 74 Substrate. {ECO:0000244|PDB:3ZR0,
ECO:0000244|PDB:5FSI,
ECO:0000244|PDB:5GHI,
ECO:0000244|PDB:5GHM,
ECO:0000244|PDB:5GHO,
ECO:0000269|PubMed:21787772,
ECO:0000269|PubMed:26999531}.
SITE 68 68 Important for 2-OH-dATPase and 8-oxo-
dGTPase activities.
{ECO:0000269|PubMed:11756418}.
SITE 158 158 Essential for 2-OH-dATPase and 8-oxo-
dGTPase activities.
{ECO:0000269|PubMed:11756418}.
SITE 160 160 Essential for 2-OH-dATPase activity and
important for 8-oxo-dGTPase activity.
{ECO:0000269|PubMed:11756418}.
VAR_SEQ 1 41 Missing (in isoform p18).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8226881,
ECO:0000303|PubMed:9211940,
ECO:0000303|Ref.7}.
/FTId=VSP_018814.
VAR_SEQ 1 26 Missing (in isoform p21). {ECO:0000305}.
/FTId=VSP_018813.
VAR_SEQ 1 18 Missing (in isoform p22).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_018812.
VARIANT 77 77 G -> W (in dbSNP:rs11547459).
/FTId=VAR_068715.
VARIANT 124 124 V -> M (associated with type I diabetes
in Japanese female population; may be
associated with an increased risk for
small cell lung carcinoma (SCLC);
decreased efficiency of translocation to
mitochondria; dbSNP:rs4866).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15516784,
ECO:0000269|PubMed:16607562,
ECO:0000269|PubMed:16774934,
ECO:0000269|PubMed:9211940}.
/FTId=VAR_013757.
MUTAGEN 68 68 F->A: Reduces 2-OH-dATPase and 8-oxo-
dGTPase activities.
{ECO:0000269|PubMed:11756418}.
MUTAGEN 77 77 G->R: Reduces activity by 97%.
{ECO:0000269|PubMed:10608900}.
MUTAGEN 78 78 G->F: Loss of activity.
{ECO:0000269|PubMed:10608900}.
MUTAGEN 80 80 V->E: Loss of activity.
{ECO:0000269|PubMed:10608900}.
MUTAGEN 81 81 Q->P: Reduces activity by 97%.
{ECO:0000269|PubMed:10608900}.
MUTAGEN 83 83 G->I: Reduces activity by 60%.
{ECO:0000269|PubMed:10608900}.
MUTAGEN 86 86 I->K: Loss of activity.
{ECO:0000269|PubMed:10608900}.
MUTAGEN 88 88 D->P: Loss of activity.
{ECO:0000269|PubMed:10608900}.
MUTAGEN 89 89 G->M: Loss of activity.
{ECO:0000269|PubMed:10608900}.
MUTAGEN 90 90 A->P: Loss of activity.
{ECO:0000269|PubMed:10608900}.
MUTAGEN 94 94 L->P: Loss of activity.
{ECO:0000269|PubMed:10608900}.
MUTAGEN 95 95 Q->P: Loss of activity.
{ECO:0000269|PubMed:10608900}.
MUTAGEN 96 96 E->G: Loss of activity.
{ECO:0000269|PubMed:10608900}.
MUTAGEN 97 97 E->A: Loss of ability to prevent DNA
damage. Expected to cause loss of enzyme
activity. {ECO:0000269|PubMed:24695224}.
MUTAGEN 97 97 E->Y: Loss of activity.
{ECO:0000269|PubMed:10608900}.
MUTAGEN 98 98 S->R: Loss of activity.
{ECO:0000269|PubMed:10608900}.
MUTAGEN 158 158 W->A: Greatly reduces or abolishes 2-OH-
dATPase and 8-oxo-dGTPase activities.
{ECO:0000269|PubMed:11756418}.
MUTAGEN 158 158 W->Y: Enhances 2-OH-dATPase activity and
greatly reduces 8-oxo-dGTPase activity.
{ECO:0000269|PubMed:11756418}.
MUTAGEN 160 160 D->A,N: Loss of 2-OH-dATPase activity,
reduces 8-oxo-dGTPase activity.
{ECO:0000269|PubMed:11756418}.
MUTAGEN 161 161 D->A,N: Mildly decreased 2-OH-dATPase
activity, nearly abolishes 8-oxo-dGTPase
activity. {ECO:0000269|PubMed:28035004}.
MUTAGEN 191 191 L->A: Reduces 2-OH-dATPase and 8-oxo-
dGTPase activities and increases
thermolability.
{ECO:0000269|PubMed:11756418}.
MUTAGEN 192 197 Missing: Almost abolishes 2-OH-dATPase
and 8-oxo-dGTPase activities and
increases thermolability.
{ECO:0000269|PubMed:11756418}.
MUTAGEN 192 192 R->A: Reduces 2-OH-dATPase and 8-oxo-
dGTPase activities and increases
thermolability.
{ECO:0000269|PubMed:11756418}.
MUTAGEN 193 197 Missing: Greatly reduces 2-OH-dATPase and
8-oxo-dGTPase activities and increases
thermolability.
{ECO:0000269|PubMed:11756418}.
MUTAGEN 193 193 E->A: Reduces 2-OH-dATPase and 8-oxo-
dGTPase activities and increases
thermolability.
{ECO:0000269|PubMed:11756418}.
MUTAGEN 194 197 Missing: Reduces 2-OH-dATPase and 8-oxo-
dGTPase activities and increases
thermolability.
{ECO:0000269|PubMed:11756418}.
MUTAGEN 194 194 V->A: Reduces 2-OH-dATPase and 8-oxo-
dGTPase activities and increases
thermolability.
{ECO:0000269|PubMed:11756418}.
MUTAGEN 195 197 Missing: Slightly enhances 2-OH-dATPase
and 8-oxo-dGTPase activities and
increases thermolability.
{ECO:0000269|PubMed:11756418}.
MUTAGEN 195 195 D->A: Enhances 2-OH-dATPase and 8-oxo-
dGTPase activities and increases
thermolability.
{ECO:0000269|PubMed:11756418}.
MUTAGEN 196 196 T->A: Reduces 2-OH-dATPase and 8-oxo-
dGTPase activities and increases
thermolability.
{ECO:0000269|PubMed:11756418}.
MUTAGEN 197 197 V->A: Slightly reduces 2-OH-dATPase and
8-oxo-dGTPase activities and increases
thermolability.
{ECO:0000269|PubMed:11756418}.
STRAND 45 54 {ECO:0000244|PDB:5WS7}.
STRAND 56 64 {ECO:0000244|PDB:5WS7}.
TURN 68 71 {ECO:0000244|PDB:5WS7}.
STRAND 72 74 {ECO:0000244|PDB:5ANV}.
STRAND 76 79 {ECO:0000244|PDB:5ANV}.
HELIX 86 98 {ECO:0000244|PDB:5WS7}.
STRAND 101 103 {ECO:0000244|PDB:5ANV}.
STRAND 105 115 {ECO:0000244|PDB:5WS7}.
STRAND 120 131 {ECO:0000244|PDB:5WS7}.
STRAND 132 134 {ECO:0000244|PDB:5ANV}.
STRAND 140 148 {ECO:0000244|PDB:5WS7}.
HELIX 149 151 {ECO:0000244|PDB:4C9X}.
HELIX 154 156 {ECO:0000244|PDB:5WS7}.
HELIX 161 169 {ECO:0000244|PDB:5WS7}.
STRAND 173 181 {ECO:0000244|PDB:5WS7}.
TURN 182 184 {ECO:0000244|PDB:5WS7}.
STRAND 185 195 {ECO:0000244|PDB:5WS7}.
SEQUENCE 197 AA; 22520 MW; 82AFF5E1CE287957 CRC64;
MYWSNQITRR LGERVQGFMS GISPQQMGEP EGSWSGKNPG TMGASRLYTL VLVLQPQRVL
LGMKKRGFGA GRWNGFGGKV QEGETIEDGA RRELQEESGL TVDALHKVGQ IVFEFVGEPE
LMDVHVFCTD SIQGTPVESD EMRPCWFQLD QIPFKDMWPD DSYWFPLLLQ KKKFHGYFKF
QGQDTILDYT LREVDTV


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