Full text data of NQO2
NQO2
(NMOR2)
[Confidence: low (only semi-automatic identification from reviews)]
Ribosyldihydronicotinamide dehydrogenase [quinone]; 1.10.99.2 (NRH dehydrogenase [quinone] 2; NRH:quinone oxidoreductase 2; Quinone reductase 2; QR2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ribosyldihydronicotinamide dehydrogenase [quinone]; 1.10.99.2 (NRH dehydrogenase [quinone] 2; NRH:quinone oxidoreductase 2; Quinone reductase 2; QR2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P16083
ID NQO2_HUMAN Reviewed; 231 AA.
AC P16083; B2R492; Q5TD04;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 5.
DT 22-JAN-2014, entry version 150.
DE RecName: Full=Ribosyldihydronicotinamide dehydrogenase [quinone];
DE EC=1.10.99.2;
DE AltName: Full=NRH dehydrogenase [quinone] 2;
DE AltName: Full=NRH:quinone oxidoreductase 2;
DE AltName: Full=Quinone reductase 2;
DE Short=QR2;
GN Name=NQO2; Synonyms=NMOR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-47.
RC TISSUE=Liver;
RX PubMed=1691923; DOI=10.1021/bi00459a034;
RA Jaiswal A.K., Burnett P., Adesnik M., McBride O.W.;
RT "Nucleotide and deduced amino acid sequence of a human cDNA (NQO2)
RT corresponding to a second member of the NAD(P)H:quinone oxidoreductase
RT gene family. Extensive polymorphism at the NQO2 gene locus on
RT chromosome 6.";
RL Biochemistry 29:1899-1906(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-47.
RC TISSUE=Liver;
RX PubMed=8182056;
RA Jaiswal A.K.;
RT "Human NAD(P)H:quinone oxidoreductase 2. Gene structure, activity, and
RT tissue-specific expression.";
RL J. Biol. Chem. 269:14502-14508(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-47.
RA Iida A., Osawa S., Kitamura Y., Kitamoto T., Koyama K., Nakamura Y.;
RT "Human NRH:quinone oxidoreductase 2, complete genomic sequence.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-16; GLY-29;
RP PHE-47; ASP-58 AND ALA-184.
RG NIEHS SNPs program;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-47.
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PHE-47.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-47.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9367528; DOI=10.1006/abbi.1997.0344;
RA Wu K., Knox R., Sun X.Z., Joseph P., Jaiswal A.K., Zhang D.,
RA Deng P.S.-K., Chen S.;
RT "Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a
RT dihydronicotinamide riboside dependent oxidoreductase.";
RL Arch. Biochem. Biophys. 347:221-228(1997).
RN [10]
RP CHARACTERIZATION.
RX PubMed=9050836; DOI=10.1073/pnas.94.5.1669;
RA Zhao Q., Yang X.L., Holtzclaw W.D., Talalay P.;
RT "Unexpected genetic and structural relationships of a long-forgotten
RT flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase).";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1669-1674(1997).
RN [11]
RP ERRATUM.
RA Zhao Q., Yang X.L., Holtzclaw W.D., Talalay P.;
RL Proc. Natl. Acad. Sci. U.S.A. 94:5979-5979(1997).
RN [12]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15078100; DOI=10.1021/bi035923w;
RA Kwiek J.J., Haystead T.A.J., Rudolph J.;
RT "Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by
RT the antimalarial quinolines.";
RL Biochemistry 43:4538-4547(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-197, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=10433694; DOI=10.1021/bi990799v;
RA Foster C.E., Bianchet M.A., Talalay P., Zhao Q., Amzel L.M.;
RT "Crystal structure of human quinone reductase type 2, a
RT metalloflavoprotein.";
RL Biochemistry 38:9881-9886(1999).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH RESVERATROL.
RX PubMed=15350128; DOI=10.1021/bi049162o;
RA Buryanovskyy L., Fu Y., Boyd M., Ma Y., Hsieh T.-C., Wu J.M.,
RA Zhang Z.;
RT "Crystal structure of quinone reductase 2 in complex with
RT resveratrol.";
RL Biochemistry 43:11417-11426(2004).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH CB1954, AND
RP MUTAGENESIS OF ASN-162.
RX PubMed=16129418; DOI=10.1016/j.bbrc.2005.08.081;
RA Fu Y., Buryanovskyy L., Zhang Z.;
RT "Crystal structure of quinone reductase 2 in complex with cancer
RT prodrug CB1954.";
RL Biochem. Biophys. Res. Commun. 336:332-338(2005).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MELATONIN AND
RP FAD, FUNCTION, SUBUNIT, AND ENZYME REGULATION.
RX PubMed=18254726; DOI=10.1042/BJ20071373;
RA Calamini B., Santarsiero B.D., Boutin J.A., Mesecar A.D.;
RT "Kinetic, thermodynamic and X-ray structural insights into the
RT interaction of melatonin and analogues with quinone reductase 2.";
RL Biochem. J. 413:81-91(2008).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH DOPAMINE AND
RP ADRENOCHROME, AND ENZYME ACTIVITY.
RX PubMed=18579530; DOI=10.1074/jbc.M801371200;
RA Fu Y., Buryanovskyy L., Zhang Z.;
RT "Quinone reductase 2 is a catechol quinone reductase.";
RL J. Biol. Chem. 283:23829-23835(2008).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FAD
RP AND IMATINIB.
RX PubMed=19236722; DOI=10.1186/1472-6807-9-7;
RA Winger J.A., Hantschel O., Superti-Furga G., Kuriyan J.;
RT "The structure of the leukemia drug imatinib bound to human quinone
RT reductase 2 (NQO2).";
RL BMC Struct. Biol. 9:7-7(2009).
CC -!- FUNCTION: The enzyme apparently serves as a quinone reductase in
CC connection with conjugation reactions of hydroquinones involved in
CC detoxification pathways as well as in biosynthetic processes such
CC as the vitamin K-dependent gamma-carboxylation of glutamate
CC residues in prothrombin synthesis.
CC -!- CATALYTIC ACTIVITY: 1-(beta-D-ribofuranosyl)-1,4-
CC dihydronicotinamide + a quinone = 1-(beta-D-
CC ribofuranosyl)nicotinamide + a hydroquinone.
CC -!- COFACTOR: Binds 1 zinc ion per subunit.
CC -!- COFACTOR: FAD.
CC -!- ENZYME REGULATION: Inhibited by melatonin, resveratrol and 5-
CC hydroxytryptamine.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28 uM for NRH;
CC KM=11.6 uM for menadione;
CC KM=252 uM for NADH;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Uses dihydronicotinamide riboside (NRH) rather than
CC NAD(P)H as an electron donor.
CC -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/nqo2/";
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DR EMBL; J02888; AAA60239.1; -; mRNA.
DR EMBL; AY299456; AAB60642.3; -; Genomic_DNA.
DR EMBL; AB050248; BAB16974.1; -; Genomic_DNA.
DR EMBL; AY855291; AAW29945.1; -; Genomic_DNA.
DR EMBL; AK311746; BAG34689.1; -; mRNA.
DR EMBL; AL133351; CAI23294.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55107.1; -; Genomic_DNA.
DR EMBL; BC006096; AAH06096.1; -; mRNA.
DR PIR; A32667; A32667.
DR RefSeq; NP_000895.2; NM_000904.3.
DR RefSeq; XP_005249204.1; XM_005249147.1.
DR RefSeq; XP_005249205.1; XM_005249148.1.
DR RefSeq; XP_005249206.1; XM_005249149.1.
DR RefSeq; XP_005249207.1; XM_005249150.1.
DR RefSeq; XP_005249208.1; XM_005249151.1.
DR UniGene; Hs.145597; -.
DR UniGene; Hs.533050; -.
DR PDB; 1QR2; X-ray; 2.10 A; A/B=2-231.
DR PDB; 1SG0; X-ray; 1.50 A; A/B=2-231.
DR PDB; 1XI2; X-ray; 1.50 A; A/B=2-231.
DR PDB; 1ZX1; X-ray; 2.16 A; A/B=1-231.
DR PDB; 2BZS; X-ray; 2.00 A; A/B=2-230.
DR PDB; 2QMY; X-ray; 2.50 A; A/B=2-231.
DR PDB; 2QMZ; X-ray; 2.10 A; A/B=2-231.
DR PDB; 2QR2; X-ray; 2.45 A; A/B=2-231.
DR PDB; 2QWX; X-ray; 1.50 A; A/B=1-231.
DR PDB; 2QX4; X-ray; 1.65 A; A/B=2-231.
DR PDB; 2QX6; X-ray; 1.75 A; A/B=2-231.
DR PDB; 2QX8; X-ray; 1.60 A; A/B=2-231.
DR PDB; 2QX9; X-ray; 2.31 A; A/B=2-231.
DR PDB; 3FW1; X-ray; 1.75 A; A=1-231.
DR PDB; 3G5M; X-ray; 1.84 A; A/B=1-231.
DR PDB; 3GAM; X-ray; 1.98 A; A/B=1-231.
DR PDB; 3NFR; X-ray; 1.57 A; A/B=2-231.
DR PDB; 3NHF; X-ray; 2.00 A; A/B=2-231.
DR PDB; 3NHJ; X-ray; 2.33 A; A/B=2-231.
DR PDB; 3NHK; X-ray; 1.96 A; A/B=2-231.
DR PDB; 3NHL; X-ray; 1.57 A; A/B=2-231.
DR PDB; 3NHP; X-ray; 1.70 A; A/B=2-231.
DR PDB; 3NHR; X-ray; 1.80 A; A/B=2-231.
DR PDB; 3NHS; X-ray; 1.78 A; A/B=2-231.
DR PDB; 3NHU; X-ray; 1.90 A; A/B=2-231.
DR PDB; 3NHW; X-ray; 1.65 A; A/B=2-231.
DR PDB; 3NHY; X-ray; 1.90 A; A/B=2-231.
DR PDB; 3O2N; X-ray; 1.60 A; A/B=2-231.
DR PDB; 3O73; X-ray; 2.00 A; A/B=1-231.
DR PDB; 3OVM; X-ray; 2.09 A; A/B=1-231.
DR PDB; 3OWH; X-ray; 2.28 A; A/B=1-231.
DR PDB; 3OWX; X-ray; 1.85 A; A/B=1-231.
DR PDB; 3OX1; X-ray; 2.00 A; A/B=1-231.
DR PDB; 3OX2; X-ray; 2.41 A; A/B=1-231.
DR PDB; 3OX3; X-ray; 1.80 A; A/B=1-231.
DR PDB; 3TE7; X-ray; 1.70 A; A/B=3-230.
DR PDB; 3TEM; X-ray; 1.45 A; A/B=3-230.
DR PDB; 3TZB; X-ray; 2.19 A; A/B/C/D=3-230.
DR PDB; 3UXE; X-ray; 1.50 A; A/B=2-231.
DR PDB; 3UXH; X-ray; 1.53 A; A/B=2-231.
DR PDB; 4FGJ; X-ray; 1.35 A; A/B=1-231.
DR PDB; 4FGK; X-ray; 1.40 A; A/B=1-231.
DR PDB; 4FGL; X-ray; 1.20 A; A/B/C/D=1-231.
DR PDB; 4GQI; X-ray; 1.95 A; A/B=2-231.
DR PDB; 4GR9; X-ray; 2.29 A; A/B=2-231.
DR PDBsum; 1QR2; -.
DR PDBsum; 1SG0; -.
DR PDBsum; 1XI2; -.
DR PDBsum; 1ZX1; -.
DR PDBsum; 2BZS; -.
DR PDBsum; 2QMY; -.
DR PDBsum; 2QMZ; -.
DR PDBsum; 2QR2; -.
DR PDBsum; 2QWX; -.
DR PDBsum; 2QX4; -.
DR PDBsum; 2QX6; -.
DR PDBsum; 2QX8; -.
DR PDBsum; 2QX9; -.
DR PDBsum; 3FW1; -.
DR PDBsum; 3G5M; -.
DR PDBsum; 3GAM; -.
DR PDBsum; 3NFR; -.
DR PDBsum; 3NHF; -.
DR PDBsum; 3NHJ; -.
DR PDBsum; 3NHK; -.
DR PDBsum; 3NHL; -.
DR PDBsum; 3NHP; -.
DR PDBsum; 3NHR; -.
DR PDBsum; 3NHS; -.
DR PDBsum; 3NHU; -.
DR PDBsum; 3NHW; -.
DR PDBsum; 3NHY; -.
DR PDBsum; 3O2N; -.
DR PDBsum; 3O73; -.
DR PDBsum; 3OVM; -.
DR PDBsum; 3OWH; -.
DR PDBsum; 3OWX; -.
DR PDBsum; 3OX1; -.
DR PDBsum; 3OX2; -.
DR PDBsum; 3OX3; -.
DR PDBsum; 3TE7; -.
DR PDBsum; 3TEM; -.
DR PDBsum; 3TZB; -.
DR PDBsum; 3UXE; -.
DR PDBsum; 3UXH; -.
DR PDBsum; 4FGJ; -.
DR PDBsum; 4FGK; -.
DR PDBsum; 4FGL; -.
DR PDBsum; 4GQI; -.
DR PDBsum; 4GR9; -.
DR DisProt; DP00727; -.
DR ProteinModelPortal; P16083; -.
DR SMR; P16083; 1-231.
DR IntAct; P16083; 7.
DR MINT; MINT-1133243; -.
DR STRING; 9606.ENSP00000337773; -.
DR BindingDB; P16083; -.
DR ChEMBL; CHEMBL3959; -.
DR DrugBank; DB00170; Menadione.
DR DrugBank; DB00157; NADH.
DR PhosphoSite; P16083; -.
DR DMDM; 9911070; -.
DR PaxDb; P16083; -.
DR PRIDE; P16083; -.
DR Ensembl; ENST00000338130; ENSP00000337773; ENSG00000124588.
DR Ensembl; ENST00000380430; ENSP00000369795; ENSG00000124588.
DR Ensembl; ENST00000380455; ENSP00000369822; ENSG00000124588.
DR GeneID; 4835; -.
DR KEGG; hsa:4835; -.
DR UCSC; uc003mus.2; human.
DR CTD; 4835; -.
DR GeneCards; GC06P003006; -.
DR H-InvDB; HIX0018967; -.
DR HGNC; HGNC:7856; NQO2.
DR HPA; HPA021283; -.
DR HPA; HPA021332; -.
DR MIM; 160998; gene.
DR neXtProt; NX_P16083; -.
DR PharmGKB; PA31745; -.
DR eggNOG; COG2249; -.
DR HOGENOM; HOG000149970; -.
DR HOVERGEN; HBG029104; -.
DR InParanoid; P16083; -.
DR KO; K08071; -.
DR OMA; EPKSFNG; -.
DR PhylomeDB; P16083; -.
DR BRENDA; 1.10.99.2; 2681.
DR SABIO-RK; P16083; -.
DR EvolutionaryTrace; P16083; -.
DR GeneWiki; NAD(P)H_dehydrogenase,_quinone_2; -.
DR GenomeRNAi; 4835; -.
DR NextBio; 18630; -.
DR PRO; PR:P16083; -.
DR ArrayExpress; P16083; -.
DR Bgee; P16083; -.
DR CleanEx; HS_NQO2; -.
DR Genevestigator; P16083; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0001512; F:dihydronicotinamide riboside quinone reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron carrier activity; TAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; TAS:ProtInc.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR InterPro; IPR003680; Flavodoxin_fold.
DR Pfam; PF02525; Flavodoxin_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; FAD; Flavoprotein;
KW Metal-binding; Oxidoreductase; Phosphoprotein; Polymorphism;
KW Reference proteome; Zinc.
FT CHAIN 1 231 Ribosyldihydronicotinamide dehydrogenase
FT [quinone].
FT /FTId=PRO_0000071626.
FT NP_BIND 18 21 FAD.
FT NP_BIND 104 107 FAD.
FT NP_BIND 148 151 FAD.
FT REGION 127 129 Substrate binding.
FT METAL 174 174 Zinc.
FT METAL 178 178 Zinc.
FT METAL 223 223 Zinc.
FT BINDING 12 12 FAD.
FT BINDING 156 156 FAD.
FT BINDING 194 194 FAD.
FT BINDING 201 201 FAD.
FT MOD_RES 80 80 Phosphoserine.
FT MOD_RES 197 197 Phosphoserine.
FT VARIANT 16 16 K -> R (in dbSNP:rs28383623).
FT /FTId=VAR_021399.
FT VARIANT 29 29 E -> G (in dbSNP:rs17136117).
FT /FTId=VAR_021400.
FT VARIANT 47 47 L -> F (in dbSNP:rs1143684).
FT /FTId=VAR_021401.
FT VARIANT 58 58 G -> D (in dbSNP:rs17300141).
FT /FTId=VAR_021402.
FT VARIANT 184 184 V -> A (in dbSNP:rs28383651).
FT /FTId=VAR_021403.
FT MUTAGEN 162 162 N->H: Loss of activity toward CB1954, no
FT effect toward menadione.
FT CONFLICT 140 140 G -> C (in Ref. 2; AAB60642).
FT STRAND 5 10
FT HELIX 18 33
FT STRAND 36 41
FT TURN 42 46
FT HELIX 53 55
FT STRAND 63 65
FT HELIX 68 77
FT HELIX 83 94
FT STRAND 96 103
FT STRAND 105 108
FT HELIX 111 120
FT TURN 123 125
FT STRAND 129 132
FT HELIX 133 135
FT TURN 137 140
FT STRAND 142 148
FT TURN 153 156
FT STRAND 160 162
FT HELIX 165 173
FT HELIX 174 178
FT TURN 179 181
FT STRAND 188 190
FT TURN 193 195
FT HELIX 198 212
FT HELIX 213 217
FT HELIX 225 229
SQ SEQUENCE 231 AA; 25919 MW; FE1F4D577517B972 CRC64;
MAGKKVLIVY AHQEPKSFNG SLKNVAVDEL SRQGCTVTVS DLYAMNLEPR ATDKDITGTL
SNPEVFNYGV ETHEAYKQRS LASDITDEQK KVREADLVIF QFPLYWFSVP AILKGWMDRV
LCQGFAFDIP GFYDSGLLQG KLALLSVTTG GTAEMYTKTG VNGDSRYFLW PLQHGTLHFC
GFKVLAPQIS FAPEIASEEE RKGMVAAWSQ RLQTIWKEEP IPCTAHWHFG Q
//
ID NQO2_HUMAN Reviewed; 231 AA.
AC P16083; B2R492; Q5TD04;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 5.
DT 22-JAN-2014, entry version 150.
DE RecName: Full=Ribosyldihydronicotinamide dehydrogenase [quinone];
DE EC=1.10.99.2;
DE AltName: Full=NRH dehydrogenase [quinone] 2;
DE AltName: Full=NRH:quinone oxidoreductase 2;
DE AltName: Full=Quinone reductase 2;
DE Short=QR2;
GN Name=NQO2; Synonyms=NMOR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-47.
RC TISSUE=Liver;
RX PubMed=1691923; DOI=10.1021/bi00459a034;
RA Jaiswal A.K., Burnett P., Adesnik M., McBride O.W.;
RT "Nucleotide and deduced amino acid sequence of a human cDNA (NQO2)
RT corresponding to a second member of the NAD(P)H:quinone oxidoreductase
RT gene family. Extensive polymorphism at the NQO2 gene locus on
RT chromosome 6.";
RL Biochemistry 29:1899-1906(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-47.
RC TISSUE=Liver;
RX PubMed=8182056;
RA Jaiswal A.K.;
RT "Human NAD(P)H:quinone oxidoreductase 2. Gene structure, activity, and
RT tissue-specific expression.";
RL J. Biol. Chem. 269:14502-14508(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-47.
RA Iida A., Osawa S., Kitamura Y., Kitamoto T., Koyama K., Nakamura Y.;
RT "Human NRH:quinone oxidoreductase 2, complete genomic sequence.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-16; GLY-29;
RP PHE-47; ASP-58 AND ALA-184.
RG NIEHS SNPs program;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-47.
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PHE-47.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-47.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9367528; DOI=10.1006/abbi.1997.0344;
RA Wu K., Knox R., Sun X.Z., Joseph P., Jaiswal A.K., Zhang D.,
RA Deng P.S.-K., Chen S.;
RT "Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a
RT dihydronicotinamide riboside dependent oxidoreductase.";
RL Arch. Biochem. Biophys. 347:221-228(1997).
RN [10]
RP CHARACTERIZATION.
RX PubMed=9050836; DOI=10.1073/pnas.94.5.1669;
RA Zhao Q., Yang X.L., Holtzclaw W.D., Talalay P.;
RT "Unexpected genetic and structural relationships of a long-forgotten
RT flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase).";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1669-1674(1997).
RN [11]
RP ERRATUM.
RA Zhao Q., Yang X.L., Holtzclaw W.D., Talalay P.;
RL Proc. Natl. Acad. Sci. U.S.A. 94:5979-5979(1997).
RN [12]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15078100; DOI=10.1021/bi035923w;
RA Kwiek J.J., Haystead T.A.J., Rudolph J.;
RT "Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by
RT the antimalarial quinolines.";
RL Biochemistry 43:4538-4547(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-197, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=10433694; DOI=10.1021/bi990799v;
RA Foster C.E., Bianchet M.A., Talalay P., Zhao Q., Amzel L.M.;
RT "Crystal structure of human quinone reductase type 2, a
RT metalloflavoprotein.";
RL Biochemistry 38:9881-9886(1999).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH RESVERATROL.
RX PubMed=15350128; DOI=10.1021/bi049162o;
RA Buryanovskyy L., Fu Y., Boyd M., Ma Y., Hsieh T.-C., Wu J.M.,
RA Zhang Z.;
RT "Crystal structure of quinone reductase 2 in complex with
RT resveratrol.";
RL Biochemistry 43:11417-11426(2004).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH CB1954, AND
RP MUTAGENESIS OF ASN-162.
RX PubMed=16129418; DOI=10.1016/j.bbrc.2005.08.081;
RA Fu Y., Buryanovskyy L., Zhang Z.;
RT "Crystal structure of quinone reductase 2 in complex with cancer
RT prodrug CB1954.";
RL Biochem. Biophys. Res. Commun. 336:332-338(2005).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MELATONIN AND
RP FAD, FUNCTION, SUBUNIT, AND ENZYME REGULATION.
RX PubMed=18254726; DOI=10.1042/BJ20071373;
RA Calamini B., Santarsiero B.D., Boutin J.A., Mesecar A.D.;
RT "Kinetic, thermodynamic and X-ray structural insights into the
RT interaction of melatonin and analogues with quinone reductase 2.";
RL Biochem. J. 413:81-91(2008).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH DOPAMINE AND
RP ADRENOCHROME, AND ENZYME ACTIVITY.
RX PubMed=18579530; DOI=10.1074/jbc.M801371200;
RA Fu Y., Buryanovskyy L., Zhang Z.;
RT "Quinone reductase 2 is a catechol quinone reductase.";
RL J. Biol. Chem. 283:23829-23835(2008).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FAD
RP AND IMATINIB.
RX PubMed=19236722; DOI=10.1186/1472-6807-9-7;
RA Winger J.A., Hantschel O., Superti-Furga G., Kuriyan J.;
RT "The structure of the leukemia drug imatinib bound to human quinone
RT reductase 2 (NQO2).";
RL BMC Struct. Biol. 9:7-7(2009).
CC -!- FUNCTION: The enzyme apparently serves as a quinone reductase in
CC connection with conjugation reactions of hydroquinones involved in
CC detoxification pathways as well as in biosynthetic processes such
CC as the vitamin K-dependent gamma-carboxylation of glutamate
CC residues in prothrombin synthesis.
CC -!- CATALYTIC ACTIVITY: 1-(beta-D-ribofuranosyl)-1,4-
CC dihydronicotinamide + a quinone = 1-(beta-D-
CC ribofuranosyl)nicotinamide + a hydroquinone.
CC -!- COFACTOR: Binds 1 zinc ion per subunit.
CC -!- COFACTOR: FAD.
CC -!- ENZYME REGULATION: Inhibited by melatonin, resveratrol and 5-
CC hydroxytryptamine.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28 uM for NRH;
CC KM=11.6 uM for menadione;
CC KM=252 uM for NADH;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Uses dihydronicotinamide riboside (NRH) rather than
CC NAD(P)H as an electron donor.
CC -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/nqo2/";
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DR EMBL; J02888; AAA60239.1; -; mRNA.
DR EMBL; AY299456; AAB60642.3; -; Genomic_DNA.
DR EMBL; AB050248; BAB16974.1; -; Genomic_DNA.
DR EMBL; AY855291; AAW29945.1; -; Genomic_DNA.
DR EMBL; AK311746; BAG34689.1; -; mRNA.
DR EMBL; AL133351; CAI23294.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55107.1; -; Genomic_DNA.
DR EMBL; BC006096; AAH06096.1; -; mRNA.
DR PIR; A32667; A32667.
DR RefSeq; NP_000895.2; NM_000904.3.
DR RefSeq; XP_005249204.1; XM_005249147.1.
DR RefSeq; XP_005249205.1; XM_005249148.1.
DR RefSeq; XP_005249206.1; XM_005249149.1.
DR RefSeq; XP_005249207.1; XM_005249150.1.
DR RefSeq; XP_005249208.1; XM_005249151.1.
DR UniGene; Hs.145597; -.
DR UniGene; Hs.533050; -.
DR PDB; 1QR2; X-ray; 2.10 A; A/B=2-231.
DR PDB; 1SG0; X-ray; 1.50 A; A/B=2-231.
DR PDB; 1XI2; X-ray; 1.50 A; A/B=2-231.
DR PDB; 1ZX1; X-ray; 2.16 A; A/B=1-231.
DR PDB; 2BZS; X-ray; 2.00 A; A/B=2-230.
DR PDB; 2QMY; X-ray; 2.50 A; A/B=2-231.
DR PDB; 2QMZ; X-ray; 2.10 A; A/B=2-231.
DR PDB; 2QR2; X-ray; 2.45 A; A/B=2-231.
DR PDB; 2QWX; X-ray; 1.50 A; A/B=1-231.
DR PDB; 2QX4; X-ray; 1.65 A; A/B=2-231.
DR PDB; 2QX6; X-ray; 1.75 A; A/B=2-231.
DR PDB; 2QX8; X-ray; 1.60 A; A/B=2-231.
DR PDB; 2QX9; X-ray; 2.31 A; A/B=2-231.
DR PDB; 3FW1; X-ray; 1.75 A; A=1-231.
DR PDB; 3G5M; X-ray; 1.84 A; A/B=1-231.
DR PDB; 3GAM; X-ray; 1.98 A; A/B=1-231.
DR PDB; 3NFR; X-ray; 1.57 A; A/B=2-231.
DR PDB; 3NHF; X-ray; 2.00 A; A/B=2-231.
DR PDB; 3NHJ; X-ray; 2.33 A; A/B=2-231.
DR PDB; 3NHK; X-ray; 1.96 A; A/B=2-231.
DR PDB; 3NHL; X-ray; 1.57 A; A/B=2-231.
DR PDB; 3NHP; X-ray; 1.70 A; A/B=2-231.
DR PDB; 3NHR; X-ray; 1.80 A; A/B=2-231.
DR PDB; 3NHS; X-ray; 1.78 A; A/B=2-231.
DR PDB; 3NHU; X-ray; 1.90 A; A/B=2-231.
DR PDB; 3NHW; X-ray; 1.65 A; A/B=2-231.
DR PDB; 3NHY; X-ray; 1.90 A; A/B=2-231.
DR PDB; 3O2N; X-ray; 1.60 A; A/B=2-231.
DR PDB; 3O73; X-ray; 2.00 A; A/B=1-231.
DR PDB; 3OVM; X-ray; 2.09 A; A/B=1-231.
DR PDB; 3OWH; X-ray; 2.28 A; A/B=1-231.
DR PDB; 3OWX; X-ray; 1.85 A; A/B=1-231.
DR PDB; 3OX1; X-ray; 2.00 A; A/B=1-231.
DR PDB; 3OX2; X-ray; 2.41 A; A/B=1-231.
DR PDB; 3OX3; X-ray; 1.80 A; A/B=1-231.
DR PDB; 3TE7; X-ray; 1.70 A; A/B=3-230.
DR PDB; 3TEM; X-ray; 1.45 A; A/B=3-230.
DR PDB; 3TZB; X-ray; 2.19 A; A/B/C/D=3-230.
DR PDB; 3UXE; X-ray; 1.50 A; A/B=2-231.
DR PDB; 3UXH; X-ray; 1.53 A; A/B=2-231.
DR PDB; 4FGJ; X-ray; 1.35 A; A/B=1-231.
DR PDB; 4FGK; X-ray; 1.40 A; A/B=1-231.
DR PDB; 4FGL; X-ray; 1.20 A; A/B/C/D=1-231.
DR PDB; 4GQI; X-ray; 1.95 A; A/B=2-231.
DR PDB; 4GR9; X-ray; 2.29 A; A/B=2-231.
DR PDBsum; 1QR2; -.
DR PDBsum; 1SG0; -.
DR PDBsum; 1XI2; -.
DR PDBsum; 1ZX1; -.
DR PDBsum; 2BZS; -.
DR PDBsum; 2QMY; -.
DR PDBsum; 2QMZ; -.
DR PDBsum; 2QR2; -.
DR PDBsum; 2QWX; -.
DR PDBsum; 2QX4; -.
DR PDBsum; 2QX6; -.
DR PDBsum; 2QX8; -.
DR PDBsum; 2QX9; -.
DR PDBsum; 3FW1; -.
DR PDBsum; 3G5M; -.
DR PDBsum; 3GAM; -.
DR PDBsum; 3NFR; -.
DR PDBsum; 3NHF; -.
DR PDBsum; 3NHJ; -.
DR PDBsum; 3NHK; -.
DR PDBsum; 3NHL; -.
DR PDBsum; 3NHP; -.
DR PDBsum; 3NHR; -.
DR PDBsum; 3NHS; -.
DR PDBsum; 3NHU; -.
DR PDBsum; 3NHW; -.
DR PDBsum; 3NHY; -.
DR PDBsum; 3O2N; -.
DR PDBsum; 3O73; -.
DR PDBsum; 3OVM; -.
DR PDBsum; 3OWH; -.
DR PDBsum; 3OWX; -.
DR PDBsum; 3OX1; -.
DR PDBsum; 3OX2; -.
DR PDBsum; 3OX3; -.
DR PDBsum; 3TE7; -.
DR PDBsum; 3TEM; -.
DR PDBsum; 3TZB; -.
DR PDBsum; 3UXE; -.
DR PDBsum; 3UXH; -.
DR PDBsum; 4FGJ; -.
DR PDBsum; 4FGK; -.
DR PDBsum; 4FGL; -.
DR PDBsum; 4GQI; -.
DR PDBsum; 4GR9; -.
DR DisProt; DP00727; -.
DR ProteinModelPortal; P16083; -.
DR SMR; P16083; 1-231.
DR IntAct; P16083; 7.
DR MINT; MINT-1133243; -.
DR STRING; 9606.ENSP00000337773; -.
DR BindingDB; P16083; -.
DR ChEMBL; CHEMBL3959; -.
DR DrugBank; DB00170; Menadione.
DR DrugBank; DB00157; NADH.
DR PhosphoSite; P16083; -.
DR DMDM; 9911070; -.
DR PaxDb; P16083; -.
DR PRIDE; P16083; -.
DR Ensembl; ENST00000338130; ENSP00000337773; ENSG00000124588.
DR Ensembl; ENST00000380430; ENSP00000369795; ENSG00000124588.
DR Ensembl; ENST00000380455; ENSP00000369822; ENSG00000124588.
DR GeneID; 4835; -.
DR KEGG; hsa:4835; -.
DR UCSC; uc003mus.2; human.
DR CTD; 4835; -.
DR GeneCards; GC06P003006; -.
DR H-InvDB; HIX0018967; -.
DR HGNC; HGNC:7856; NQO2.
DR HPA; HPA021283; -.
DR HPA; HPA021332; -.
DR MIM; 160998; gene.
DR neXtProt; NX_P16083; -.
DR PharmGKB; PA31745; -.
DR eggNOG; COG2249; -.
DR HOGENOM; HOG000149970; -.
DR HOVERGEN; HBG029104; -.
DR InParanoid; P16083; -.
DR KO; K08071; -.
DR OMA; EPKSFNG; -.
DR PhylomeDB; P16083; -.
DR BRENDA; 1.10.99.2; 2681.
DR SABIO-RK; P16083; -.
DR EvolutionaryTrace; P16083; -.
DR GeneWiki; NAD(P)H_dehydrogenase,_quinone_2; -.
DR GenomeRNAi; 4835; -.
DR NextBio; 18630; -.
DR PRO; PR:P16083; -.
DR ArrayExpress; P16083; -.
DR Bgee; P16083; -.
DR CleanEx; HS_NQO2; -.
DR Genevestigator; P16083; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0001512; F:dihydronicotinamide riboside quinone reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron carrier activity; TAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; TAS:ProtInc.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR InterPro; IPR003680; Flavodoxin_fold.
DR Pfam; PF02525; Flavodoxin_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; FAD; Flavoprotein;
KW Metal-binding; Oxidoreductase; Phosphoprotein; Polymorphism;
KW Reference proteome; Zinc.
FT CHAIN 1 231 Ribosyldihydronicotinamide dehydrogenase
FT [quinone].
FT /FTId=PRO_0000071626.
FT NP_BIND 18 21 FAD.
FT NP_BIND 104 107 FAD.
FT NP_BIND 148 151 FAD.
FT REGION 127 129 Substrate binding.
FT METAL 174 174 Zinc.
FT METAL 178 178 Zinc.
FT METAL 223 223 Zinc.
FT BINDING 12 12 FAD.
FT BINDING 156 156 FAD.
FT BINDING 194 194 FAD.
FT BINDING 201 201 FAD.
FT MOD_RES 80 80 Phosphoserine.
FT MOD_RES 197 197 Phosphoserine.
FT VARIANT 16 16 K -> R (in dbSNP:rs28383623).
FT /FTId=VAR_021399.
FT VARIANT 29 29 E -> G (in dbSNP:rs17136117).
FT /FTId=VAR_021400.
FT VARIANT 47 47 L -> F (in dbSNP:rs1143684).
FT /FTId=VAR_021401.
FT VARIANT 58 58 G -> D (in dbSNP:rs17300141).
FT /FTId=VAR_021402.
FT VARIANT 184 184 V -> A (in dbSNP:rs28383651).
FT /FTId=VAR_021403.
FT MUTAGEN 162 162 N->H: Loss of activity toward CB1954, no
FT effect toward menadione.
FT CONFLICT 140 140 G -> C (in Ref. 2; AAB60642).
FT STRAND 5 10
FT HELIX 18 33
FT STRAND 36 41
FT TURN 42 46
FT HELIX 53 55
FT STRAND 63 65
FT HELIX 68 77
FT HELIX 83 94
FT STRAND 96 103
FT STRAND 105 108
FT HELIX 111 120
FT TURN 123 125
FT STRAND 129 132
FT HELIX 133 135
FT TURN 137 140
FT STRAND 142 148
FT TURN 153 156
FT STRAND 160 162
FT HELIX 165 173
FT HELIX 174 178
FT TURN 179 181
FT STRAND 188 190
FT TURN 193 195
FT HELIX 198 212
FT HELIX 213 217
FT HELIX 225 229
SQ SEQUENCE 231 AA; 25919 MW; FE1F4D577517B972 CRC64;
MAGKKVLIVY AHQEPKSFNG SLKNVAVDEL SRQGCTVTVS DLYAMNLEPR ATDKDITGTL
SNPEVFNYGV ETHEAYKQRS LASDITDEQK KVREADLVIF QFPLYWFSVP AILKGWMDRV
LCQGFAFDIP GFYDSGLLQG KLALLSVTTG GTAEMYTKTG VNGDSRYFLW PLQHGTLHFC
GFKVLAPQIS FAPEIASEEE RKGMVAAWSQ RLQTIWKEEP IPCTAHWHFG Q
//
MIM
160998
*RECORD*
*FIELD* NO
160998
*FIELD* TI
*160998 NAD(P)H DEHYDROGENASE, QUINONE 2; NQO2
;;NAD(P)H:MENADIONE OXIDOREDUCTASE 1, DIOXIN-INDUCIBLE 2; NMOR2
read more*FIELD* TX
DESCRIPTION
NQO2 (EC 1.10.99.2) is a flavoprotein that catalyzes the 2-electron
reduction of various quinones, redox dyes, and the vitamin K menadione.
NQO2 predominantly uses dihydronicotinamide riboside (NRH) as the
electron donor (summary by Wu et al., 1997).
CLONING
Jaiswal et al. (1988) described a cDNA that encodes a dioxin-inducible
cytosolic form of human NAD(P)H:quinone oxidoreductase (NQO1; 125860).
Jaiswal et al. (1990) cloned a cDNA clone that encodes a second form of
this oxidoreductase, NQO2. It was isolated by screening a human liver
cDNA library by hybridization with an NQO1 cDNA probe. The deduced
231-amino acid NQO2 protein has a calculated molecular mass of 25.95 kD
and shares 49% similarity with the liver cytosolic NQO1 protein.
Using Northern blot analysis, Jaiswal (1994) detected variable
expression of a single 1.2-kb NQO2 transcript in several human tissues,
with highest expression in skeletal muscle, and little to no expression
in pancreas and placenta.
Gaikwad et al. (2009) stated that NQO2 is ubiquitously expressed.
GENE FUNCTION
By in vitro assay of human NQO2 expressed in transfected COS-1 cells,
Jaiswal (1994) showed that NQO2 catalyzed nitroreduction of an antitumor
analog of nitrophenylaziridine. However, unlike NQO1, NQO2 could not
efficiently reduce DCIP (2,6-dichlorophenolindophenol) and menadione.
Wu et al. (1997) found that NQO2, like NQO1, functioned as a dimer with
1 FAD prosthetic group per 26-kD subunit. NRH was an efficient electron
donor for NQO2-mediated 2-electron reduction of menadione and DCIP;
however, NADH was a poor electron donor. NQO2 did not reduce 1-electron
acceptors, such as potassium ferricyanide. NQO2 also catalyzed a
4-electron reduction of methyl red and a cytotoxic compound, CB 1954
(5-(aziridine-1-yl)-2,4-dinitrobenzamide). NQO2 was resistant to typical
inhibitors of NQO1 and was sensitive to a different group of flavone
inhibitors, including quercetin, a competitive inhibitor of NRH.
Estrogens are metabolized to reactive catechol estrogen quinones, and
these quinones can depurinate DNA, leading to cancer-causing mutations.
Using mass spectrometry, Gaikwad et al. (2009) showed that NQO2 could
bind estrone-3,4-quinone (E1-3,4-Q) and estradiol-3,4-quinone
(E2-3,4-Q). Preliminary kinetic studies revealed that NQO2 was faster in
reducing and deactivating the estrogen quinones than NQO1. The reduction
of E1-3,4-Q and E2-3,4-Q by NQO2 was confirmed by ultraviolet and liquid
chromatography-tandem mass spectrometry assays. Both estrogens and
melatonin bound NQO2, but melatonin did not affect estrogen quinone
reduction by NQO2.
GENE STRUCTURE
By Southern blot analysis, Jaiswal et al. (1990) demonstrated the
presence of a single human NQO2 gene spanning approximately 14 to 17 kb.
Jaiswal (1994) determined that the NQO2 gene contains 7 exons and spans
20 kb. The first exon is noncoding. The promoter region contains a
modified TATA box, 2 CCAAT boxes, 4 SP1 (189906)-binding sites, a single
antioxidant response element (ARE), and 3 xenobiotic response elements
(XREs).
MAPPING
By study of rodent/human somatic cell hybrids, Jaiswal et al. (1990)
mapped the NQO2 gene to chromosome 6pter-q12. By fluorescence in situ
hybridization, Jaiswal et al. (1999) narrowed the mapping of NQO2 to
chromosome 6p25.
MOLECULAR GENETICS
In a hospital-based study of 893 Chinese breast cancer patients and 711
Chinese cancer-free controls, Yu et al. (2009) genotyped 11
polymorphisms of the NQO2 gene, which encodes NRH:quinone
oxidoreductase-2 and has enzymatic activity on estrogen-derived quinones
and is able to stabilize p53 (TP53; 191170). The authors identified
significant association between the incidence of breast cancer and a
29-bp insertion/deletion polymorphism (29-bp I/D; p = 0.0027; OR, 0.76)
and the dbSNP rs2071002 SNP (+237A-C; p = 0.0031; OR, 0.80), both of
which are within the NQO2 promoter region. The findings were replicated
in a second Chinese population of 403 familial/early-onset breast cancer
patients and 1,039 controls. Decreased risk was associated with the D
allele of 29 bp-I/D and the +237C allele of dbSNP rs2071002. The
susceptibility variants within NQO2 were notably associated with breast
carcinomas with wildtype p53. The 29-bp insertion allele introduced a
transcriptional repressor Sp3 binding sites, and the authors
demonstrated that the 237A allele of dbSNP rs2071002 abolished a
transcriptional activator Sp1 binding site. Real-time PCR assay showed
that normal breast tissues harboring protective genotypes expressed
significantly higher levels of NQO2 mRNA than those in normal breast
tissues harboring risk genotypes. Yu et al. (2009) suggested that NQO2
is a susceptibility gene for breast carcinogenesis.
*FIELD* RF
1. Gaikwad, N. W.; Yang, L.; Rogan, E. G.; Cavalieri, E. L.: Evidence
for NQO2-mediated reduction of the carcinnogenic estrogen ortho-quinones. Free
Radical Biol. Med. 46: 253-262, 2009.
2. Jaiswal, A. K.: Human NAD(P)H:quinone oxidoreductase-2: gene structure,
activity, and tissue-specific expression. J. Biol. Chem. 20: 14502-14508,
1994.
3. Jaiswal, A. K.; Bell, D. W.; Radjendirane, V.; Testa, J. R.: Localization
of human NQO1 gene to chromosome 16q22 and NQO2-6p25 and associated
polymorphisms. Pharmacogenetics 9: 413-418, 1999.
4. Jaiswal, A. K.; Burnett, P.; Adesnik, M.; McBride, O. W.: Nucleotide
and deduced amino acid sequence of a human cDNA (NQO2) corresponding
to a second member of the NAD(P)H:quinone oxidoreductase gene family:
extensive polymorphism at the NQO2 gene locus on chromosome 6. (Abstract) Biochemistry 29:
1899-1906, 1990.
5. Jaiswal, A. K.; McBride, O. W.; Adesnik, M.; Nebert, D. W.: Human
dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase: cDNA
sequence and localization of gene to chromosome 16. J. Biol. Chem. 263:
13572-13578, 1988.
6. Wu, K.; Knot, R.; Sun, X. Z.; Joseph, P.; Jaiswal, A. K.; Zhang,
D.; Deng, P. S.-K.; Chen, S.: Catalytic properties of NAD(P)H:Quinone
oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent
oxidoreductase. Arch. Biochem. Biphys. 347: 221-228, 1997.
7. Yu, K.-D.; Di, G.-H.; Yuan, W.-T.; Fan, L.; Wu, J.; Hu, Z.; Shen,
Z.-Z.; Zheng, Y.; Huang, W.; Shao, Z.-M.: Functional polymorphisms,
altered gene expression and genetic association link NRH:quinone oxidoreductase
2 to breast cancer with wild-type p53. Hum. Molec. Genet. 18: 2502-2517,
2009.
*FIELD* CN
Patricia A. Hartz - updated: 4/15/2010
George E. Tiller - updated: 3/30/2010
Victor A. McKusick - updated: 11/1/1999
*FIELD* CD
Victor A. McKusick: 9/17/1991
*FIELD* ED
mgross: 04/16/2010
terry: 4/15/2010
wwang: 4/6/2010
terry: 3/30/2010
carol: 11/10/1999
terry: 11/1/1999
dkim: 7/24/1998
alopez: 6/22/1998
supermim: 3/16/1992
carol: 9/17/1991
*RECORD*
*FIELD* NO
160998
*FIELD* TI
*160998 NAD(P)H DEHYDROGENASE, QUINONE 2; NQO2
;;NAD(P)H:MENADIONE OXIDOREDUCTASE 1, DIOXIN-INDUCIBLE 2; NMOR2
read more*FIELD* TX
DESCRIPTION
NQO2 (EC 1.10.99.2) is a flavoprotein that catalyzes the 2-electron
reduction of various quinones, redox dyes, and the vitamin K menadione.
NQO2 predominantly uses dihydronicotinamide riboside (NRH) as the
electron donor (summary by Wu et al., 1997).
CLONING
Jaiswal et al. (1988) described a cDNA that encodes a dioxin-inducible
cytosolic form of human NAD(P)H:quinone oxidoreductase (NQO1; 125860).
Jaiswal et al. (1990) cloned a cDNA clone that encodes a second form of
this oxidoreductase, NQO2. It was isolated by screening a human liver
cDNA library by hybridization with an NQO1 cDNA probe. The deduced
231-amino acid NQO2 protein has a calculated molecular mass of 25.95 kD
and shares 49% similarity with the liver cytosolic NQO1 protein.
Using Northern blot analysis, Jaiswal (1994) detected variable
expression of a single 1.2-kb NQO2 transcript in several human tissues,
with highest expression in skeletal muscle, and little to no expression
in pancreas and placenta.
Gaikwad et al. (2009) stated that NQO2 is ubiquitously expressed.
GENE FUNCTION
By in vitro assay of human NQO2 expressed in transfected COS-1 cells,
Jaiswal (1994) showed that NQO2 catalyzed nitroreduction of an antitumor
analog of nitrophenylaziridine. However, unlike NQO1, NQO2 could not
efficiently reduce DCIP (2,6-dichlorophenolindophenol) and menadione.
Wu et al. (1997) found that NQO2, like NQO1, functioned as a dimer with
1 FAD prosthetic group per 26-kD subunit. NRH was an efficient electron
donor for NQO2-mediated 2-electron reduction of menadione and DCIP;
however, NADH was a poor electron donor. NQO2 did not reduce 1-electron
acceptors, such as potassium ferricyanide. NQO2 also catalyzed a
4-electron reduction of methyl red and a cytotoxic compound, CB 1954
(5-(aziridine-1-yl)-2,4-dinitrobenzamide). NQO2 was resistant to typical
inhibitors of NQO1 and was sensitive to a different group of flavone
inhibitors, including quercetin, a competitive inhibitor of NRH.
Estrogens are metabolized to reactive catechol estrogen quinones, and
these quinones can depurinate DNA, leading to cancer-causing mutations.
Using mass spectrometry, Gaikwad et al. (2009) showed that NQO2 could
bind estrone-3,4-quinone (E1-3,4-Q) and estradiol-3,4-quinone
(E2-3,4-Q). Preliminary kinetic studies revealed that NQO2 was faster in
reducing and deactivating the estrogen quinones than NQO1. The reduction
of E1-3,4-Q and E2-3,4-Q by NQO2 was confirmed by ultraviolet and liquid
chromatography-tandem mass spectrometry assays. Both estrogens and
melatonin bound NQO2, but melatonin did not affect estrogen quinone
reduction by NQO2.
GENE STRUCTURE
By Southern blot analysis, Jaiswal et al. (1990) demonstrated the
presence of a single human NQO2 gene spanning approximately 14 to 17 kb.
Jaiswal (1994) determined that the NQO2 gene contains 7 exons and spans
20 kb. The first exon is noncoding. The promoter region contains a
modified TATA box, 2 CCAAT boxes, 4 SP1 (189906)-binding sites, a single
antioxidant response element (ARE), and 3 xenobiotic response elements
(XREs).
MAPPING
By study of rodent/human somatic cell hybrids, Jaiswal et al. (1990)
mapped the NQO2 gene to chromosome 6pter-q12. By fluorescence in situ
hybridization, Jaiswal et al. (1999) narrowed the mapping of NQO2 to
chromosome 6p25.
MOLECULAR GENETICS
In a hospital-based study of 893 Chinese breast cancer patients and 711
Chinese cancer-free controls, Yu et al. (2009) genotyped 11
polymorphisms of the NQO2 gene, which encodes NRH:quinone
oxidoreductase-2 and has enzymatic activity on estrogen-derived quinones
and is able to stabilize p53 (TP53; 191170). The authors identified
significant association between the incidence of breast cancer and a
29-bp insertion/deletion polymorphism (29-bp I/D; p = 0.0027; OR, 0.76)
and the dbSNP rs2071002 SNP (+237A-C; p = 0.0031; OR, 0.80), both of
which are within the NQO2 promoter region. The findings were replicated
in a second Chinese population of 403 familial/early-onset breast cancer
patients and 1,039 controls. Decreased risk was associated with the D
allele of 29 bp-I/D and the +237C allele of dbSNP rs2071002. The
susceptibility variants within NQO2 were notably associated with breast
carcinomas with wildtype p53. The 29-bp insertion allele introduced a
transcriptional repressor Sp3 binding sites, and the authors
demonstrated that the 237A allele of dbSNP rs2071002 abolished a
transcriptional activator Sp1 binding site. Real-time PCR assay showed
that normal breast tissues harboring protective genotypes expressed
significantly higher levels of NQO2 mRNA than those in normal breast
tissues harboring risk genotypes. Yu et al. (2009) suggested that NQO2
is a susceptibility gene for breast carcinogenesis.
*FIELD* RF
1. Gaikwad, N. W.; Yang, L.; Rogan, E. G.; Cavalieri, E. L.: Evidence
for NQO2-mediated reduction of the carcinnogenic estrogen ortho-quinones. Free
Radical Biol. Med. 46: 253-262, 2009.
2. Jaiswal, A. K.: Human NAD(P)H:quinone oxidoreductase-2: gene structure,
activity, and tissue-specific expression. J. Biol. Chem. 20: 14502-14508,
1994.
3. Jaiswal, A. K.; Bell, D. W.; Radjendirane, V.; Testa, J. R.: Localization
of human NQO1 gene to chromosome 16q22 and NQO2-6p25 and associated
polymorphisms. Pharmacogenetics 9: 413-418, 1999.
4. Jaiswal, A. K.; Burnett, P.; Adesnik, M.; McBride, O. W.: Nucleotide
and deduced amino acid sequence of a human cDNA (NQO2) corresponding
to a second member of the NAD(P)H:quinone oxidoreductase gene family:
extensive polymorphism at the NQO2 gene locus on chromosome 6. (Abstract) Biochemistry 29:
1899-1906, 1990.
5. Jaiswal, A. K.; McBride, O. W.; Adesnik, M.; Nebert, D. W.: Human
dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase: cDNA
sequence and localization of gene to chromosome 16. J. Biol. Chem. 263:
13572-13578, 1988.
6. Wu, K.; Knot, R.; Sun, X. Z.; Joseph, P.; Jaiswal, A. K.; Zhang,
D.; Deng, P. S.-K.; Chen, S.: Catalytic properties of NAD(P)H:Quinone
oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent
oxidoreductase. Arch. Biochem. Biphys. 347: 221-228, 1997.
7. Yu, K.-D.; Di, G.-H.; Yuan, W.-T.; Fan, L.; Wu, J.; Hu, Z.; Shen,
Z.-Z.; Zheng, Y.; Huang, W.; Shao, Z.-M.: Functional polymorphisms,
altered gene expression and genetic association link NRH:quinone oxidoreductase
2 to breast cancer with wild-type p53. Hum. Molec. Genet. 18: 2502-2517,
2009.
*FIELD* CN
Patricia A. Hartz - updated: 4/15/2010
George E. Tiller - updated: 3/30/2010
Victor A. McKusick - updated: 11/1/1999
*FIELD* CD
Victor A. McKusick: 9/17/1991
*FIELD* ED
mgross: 04/16/2010
terry: 4/15/2010
wwang: 4/6/2010
terry: 3/30/2010
carol: 11/10/1999
terry: 11/1/1999
dkim: 7/24/1998
alopez: 6/22/1998
supermim: 3/16/1992
carol: 9/17/1991