NQO2_HUMAN
ID NQO2_HUMAN Reviewed; 231 AA.
AC P16083; B2R492; Q5TD04;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 5.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Ribosyldihydronicotinamide dehydrogenase [quinone];
DE EC=1.10.5.1 {ECO:0000269|PubMed:18579530};
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 gene
RT family. Extensive polymorphism at the NQO2 gene locus on 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; DOI=10.1016/s0021-9258(17)36651-6;
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; PHE-47;
RP 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Deng P.S.-K.,
RA 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 OF PUBMED:9050836.
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 the
RT antimalarial quinolines.";
RL Biochemistry 43:4538-4547(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-197, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Buerckstuemmer T.,
RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
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 [17]
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., Zhang Z.;
RT "Crystal structure of quinone reductase 2 in complex with resveratrol.";
RL Biochemistry 43:11417-11426(2004).
RN [18]
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 prodrug
RT CB1954.";
RL Biochem. Biophys. Res. Commun. 336:332-338(2005).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MELATONIN AND FAD,
RP FUNCTION, SUBUNIT, AND ACTIVITY 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 interaction
RT of melatonin and analogues with quinone reductase 2.";
RL Biochem. J. 413:81-91(2008).
RN [20]
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 [21]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FAD AND
RP 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 as
CC the vitamin K-dependent gamma-carboxylation of glutamate residues in
CC prothrombin synthesis. {ECO:0000269|PubMed:18254726}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone +
CC H(+) = a quinol + beta-nicotinamide D-riboside; Xref=Rhea:RHEA:12364,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15927, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:55458, ChEBI:CHEBI:132124; EC=1.10.5.1;
CC Evidence={ECO:0000269|PubMed:18579530};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- ACTIVITY REGULATION: Inhibited by melatonin, resveratrol and 5-
CC hydroxytryptamine. {ECO:0000269|PubMed:18254726}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28 uM for NRH {ECO:0000269|PubMed:15078100,
CC ECO:0000269|PubMed:9367528};
CC KM=11.6 uM for menadione {ECO:0000269|PubMed:15078100,
CC ECO:0000269|PubMed:9367528};
CC KM=252 uM for NADH {ECO:0000269|PubMed:15078100,
CC ECO:0000269|PubMed:9367528};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15350128,
CC ECO:0000269|PubMed:16129418, ECO:0000269|PubMed:18254726,
CC ECO:0000269|PubMed:19236722}.
CC -!- INTERACTION:
CC P16083; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-358466, EBI-742054;
CC P16083; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-358466, EBI-743105;
CC P16083; Q9H8Y8: GORASP2; NbExp=5; IntAct=EBI-358466, EBI-739467;
CC P16083; Q8IWL3: HSCB; NbExp=4; IntAct=EBI-358466, EBI-1805738;
CC P16083; A1L1C6: LRRC7; NbExp=6; IntAct=EBI-358466, EBI-10171988;
CC P16083; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-358466, EBI-742688;
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 {ECO:0000305}.
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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55107.1; -; Genomic_DNA.
DR EMBL; BC006096; AAH06096.1; -; mRNA.
DR CCDS; CCDS4481.1; -.
DR PIR; A32667; A32667.
DR RefSeq; NP_000895.2; NM_000904.4.
DR RefSeq; NP_001277150.1; NM_001290221.1.
DR RefSeq; NP_001305869.1; NM_001318940.1.
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=2-231.
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 PDB; 4QOD; X-ray; 1.35 A; A/B=1-231.
DR PDB; 4QOE; X-ray; 1.45 A; A/B=1-231.
DR PDB; 4QOF; X-ray; 1.55 A; A/B=1-231.
DR PDB; 4QOG; X-ray; 1.40 A; A/B=1-231.
DR PDB; 4QOH; X-ray; 1.60 A; A/B=1-231.
DR PDB; 4QOI; X-ray; 1.55 A; A/B=1-231.
DR PDB; 4QOJ; X-ray; 1.85 A; A/B=1-231.
DR PDB; 4U7F; X-ray; 1.80 A; A/B=2-231.
DR PDB; 4U7G; X-ray; 1.96 A; A/B=2-231.
DR PDB; 4U7H; X-ray; 1.48 A; A/B=2-231.
DR PDB; 4XDG; X-ray; 1.50 A; A/B=1-231.
DR PDB; 4XDH; X-ray; 1.90 A; A/B=1-231.
DR PDB; 4ZVK; X-ray; 1.87 A; A/B=2-231.
DR PDB; 4ZVL; X-ray; 1.90 A; A/B=2-231.
DR PDB; 4ZVM; X-ray; 1.97 A; A/B=2-231.
DR PDB; 4ZVN; X-ray; 1.87 A; A/B=2-231.
DR PDB; 5BUC; X-ray; 1.87 A; A/B=2-231.
DR PDB; 5LBT; X-ray; 1.75 A; A/B=1-231.
DR PDB; 5LBU; X-ray; 1.65 A; A/B=1-231.
DR PDB; 5LBW; X-ray; 1.90 A; A/B=1-231.
DR PDB; 5LBY; X-ray; 1.40 A; A/B=1-231.
DR PDB; 5LBZ; X-ray; 1.40 A; A/B=1-231.
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 PDBsum; 4QOD; -.
DR PDBsum; 4QOE; -.
DR PDBsum; 4QOF; -.
DR PDBsum; 4QOG; -.
DR PDBsum; 4QOH; -.
DR PDBsum; 4QOI; -.
DR PDBsum; 4QOJ; -.
DR PDBsum; 4U7F; -.
DR PDBsum; 4U7G; -.
DR PDBsum; 4U7H; -.
DR PDBsum; 4XDG; -.
DR PDBsum; 4XDH; -.
DR PDBsum; 4ZVK; -.
DR PDBsum; 4ZVL; -.
DR PDBsum; 4ZVM; -.
DR PDBsum; 4ZVN; -.
DR PDBsum; 5BUC; -.
DR PDBsum; 5LBT; -.
DR PDBsum; 5LBU; -.
DR PDBsum; 5LBW; -.
DR PDBsum; 5LBY; -.
DR PDBsum; 5LBZ; -.
DR AlphaFoldDB; P16083; -.
DR SMR; P16083; -.
DR BioGRID; 110898; 20.
DR CORUM; P16083; -.
DR DIP; DIP-39704N; -.
DR IntAct; P16083; 16.
DR MINT; P16083; -.
DR STRING; 9606.ENSP00000369822; -.
DR BindingDB; P16083; -.
DR ChEMBL; CHEMBL3959; -.
DR DrugBank; DB07339; (3S)-3-hydroxy-1-methyl-2,3-dihydro-1H-indole-5,6-dione.
DR DrugBank; DB03541; 10-Propargyl-5,8-Dideazafolic Acid.
DR DrugBank; DB08228; 5,8-dimethoxy-1,4-dimethylquinolin-2(1H)-one.
DR DrugBank; DB08744; Casimiroin.
DR DrugBank; DB06695; Dabigatran etexilate.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB01065; Melatonin.
DR DrugBank; DB00170; Menadione.
DR DrugBank; DB08190; N-[2-(2-iodo-5-methoxy-1H-indol-3-yl)ethyl]acetamide.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB01087; Primaquine.
DR DrugBank; DB04216; Quercetin.
DR DrugBank; DB02709; Resveratrol.
DR DrugBank; DB04253; Tretazicar.
DR DrugCentral; P16083; -.
DR iPTMnet; P16083; -.
DR PhosphoSitePlus; P16083; -.
DR BioMuta; NQO2; -.
DR DMDM; 317373581; -.
DR EPD; P16083; -.
DR jPOST; P16083; -.
DR MassIVE; P16083; -.
DR MaxQB; P16083; -.
DR PaxDb; P16083; -.
DR PeptideAtlas; P16083; -.
DR PRIDE; P16083; -.
DR ProteomicsDB; 53285; -.
DR Antibodypedia; 9328; 555 antibodies from 34 providers.
DR DNASU; 4835; -.
DR Ensembl; ENST00000338130.7; ENSP00000337773.2; ENSG00000124588.22.
DR Ensembl; ENST00000380430.6; ENSP00000369795.1; ENSG00000124588.22.
DR Ensembl; ENST00000380455.11; ENSP00000369822.4; ENSG00000124588.22.
DR GeneID; 4835; -.
DR KEGG; hsa:4835; -.
DR MANE-Select; ENST00000380455.11; ENSP00000369822.4; NM_000904.6; NP_000895.2.
DR UCSC; uc003mus.3; human.
DR CTD; 4835; -.
DR DisGeNET; 4835; -.
DR GeneCards; NQO2; -.
DR HGNC; HGNC:7856; NQO2.
DR HPA; ENSG00000124588; Low tissue specificity.
DR MalaCards; NQO2; -.
DR MIM; 160998; gene.
DR neXtProt; NX_P16083; -.
DR OpenTargets; ENSG00000124588; -.
DR PharmGKB; PA31745; -.
DR VEuPathDB; HostDB:ENSG00000124588; -.
DR eggNOG; ENOG502QWY5; Eukaryota.
DR GeneTree; ENSGT00940000156563; -.
DR HOGENOM; CLU_058643_2_0_1; -.
DR InParanoid; P16083; -.
DR OMA; LFPIHHG; -.
DR OrthoDB; 1394543at2759; -.
DR PhylomeDB; P16083; -.
DR TreeFam; TF300296; -.
DR BRENDA; 1.10.5.1; 2681.
DR PathwayCommons; P16083; -.
DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR SABIO-RK; P16083; -.
DR SignaLink; P16083; -.
DR BioGRID-ORCS; 4835; 8 hits in 1081 CRISPR screens.
DR ChiTaRS; NQO2; human.
DR EvolutionaryTrace; P16083; -.
DR GeneWiki; NAD(P)H_dehydrogenase,_quinone_2; -.
DR GenomeRNAi; 4835; -.
DR Pharos; P16083; Tchem.
DR PRO; PR:P16083; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P16083; protein.
DR Bgee; ENSG00000124588; Expressed in left adrenal gland and 194 other tissues.
DR ExpressionAtlas; P16083; baseline and differential.
DR Genevisible; P16083; HS.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0031404; F:chloride ion binding; IDA:CAFA.
DR GO; GO:0001512; F:dihydronicotinamide riboside quinone reductase activity; IDA:CAFA.
DR GO; GO:0009055; F:electron transfer activity; IDA:CAFA.
DR GO; GO:0071949; F:FAD binding; IDA:CAFA.
DR GO; GO:1904408; F:melatonin binding; IDA:CAFA.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:CAFA.
DR GO; GO:0016661; F:oxidoreductase activity, acting on other nitrogenous compounds as donors; IDA:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:CAFA.
DR GO; GO:1905594; F:resveratrol binding; IDA:CAFA.
DR GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
DR GO; GO:1901662; P:quinone catabolic process; IDA:CAFA.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR003680; Flavodoxin_fold.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR Pfam; PF02525; Flavodoxin_2; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; Metal-binding; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..231
FT /note="Ribosyldihydronicotinamide dehydrogenase [quinone]"
FT /id="PRO_0000071626"
FT BINDING 12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18254726,
FT ECO:0000269|PubMed:19236722"
FT BINDING 18..21
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18254726,
FT ECO:0000269|PubMed:19236722"
FT BINDING 104..107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18254726,
FT ECO:0000269|PubMed:19236722"
FT BINDING 127..129
FT /ligand="substrate"
FT BINDING 148..151
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18254726,
FT ECO:0000269|PubMed:19236722"
FT BINDING 156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18254726,
FT ECO:0000269|PubMed:19236722"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 194
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18254726,
FT ECO:0000269|PubMed:19236722"
FT BINDING 201
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:18254726,
FT ECO:0000269|PubMed:19236722"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT VARIANT 16
FT /note="K -> R (in dbSNP:rs28383623)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_021399"
FT VARIANT 29
FT /note="E -> G (in dbSNP:rs17136117)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_021400"
FT VARIANT 47
FT /note="L -> F (in dbSNP:rs1143684)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1691923,
FT ECO:0000269|PubMed:8182056, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.7"
FT /id="VAR_021401"
FT VARIANT 58
FT /note="G -> D (in dbSNP:rs17300141)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_021402"
FT VARIANT 184
FT /note="V -> A (in dbSNP:rs28383651)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_021403"
FT MUTAGEN 162
FT /note="N->H: Loss of activity toward CB1954, no effect
FT toward menadione."
FT /evidence="ECO:0000269|PubMed:16129418"
FT CONFLICT 140
FT /note="G -> C (in Ref. 2; AAB60642)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:4FGL"
FT HELIX 18..33
FT /evidence="ECO:0007829|PDB:4FGL"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:4FGL"
FT TURN 42..46
FT /evidence="ECO:0007829|PDB:4FGL"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:4FGL"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4FGL"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:4FGL"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:4FGL"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:4FGL"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:3O2N"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:4FGL"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:4FGL"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:3NHF"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:4FGL"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:4FGL"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:4FGL"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:4FGL"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:1SG0"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:4FGL"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:4FGL"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:4FGL"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4FGL"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:4FGL"
FT HELIX 198..212
FT /evidence="ECO:0007829|PDB:4FGL"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:4FGL"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:4FGL"
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
