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 04-NOV-2026, entry version 241. 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. 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 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 IN COMPLEX WITH CB1954, AND 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 IN COMPLEX WITH MELATONIN AND FAD, FUNCTION, SUBUNIT, RP 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 IN COMPLEXES WITH DOPAMINE AND ADRENOCHROME, AND RP 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 IN COMPLEX WITH ZINC IONS; FAD 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 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(+) = beta-nicotinamide D-riboside + a quinol; 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_000904.6. DR RefSeq; NP_001277150.1; NM_001290221.2. DR RefSeq; NP_001305869.1; NM_001318940.2. 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 PDB; 7O4D; X-ray; 2.25 A; A/B=1-231. DR AlphaFoldDB; P16083; -. DR SMR; P16083; -. DR BioGRID; 110898; 32. DR CORUM; P16083; -. DR DIP; DIP-39704N; -. DR FunCoup; P16083; 127. DR IntAct; P16083; 22. DR NDEx; IQUERY-CP-NQO2; 1 NDEx IQuery Curated Pathway. 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; DB18950; Caricotamide. 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 jPOST; P16083; -. DR MassIVE; P16083; -. DR PaxDb; 9606-ENSP00000369822; -. DR PeptideAtlas; P16083; -. DR ProteomicsDB; 53285; -. DR Pumba; P16083; -. DR Antibodypedia; 9328; 614 antibodies from 38 providers. DR DNASU; 4835; -. DR Ensembl; ENST00000338130.7; ENSP00000337773.2; ENSG00000124588.23. DR Ensembl; ENST00000380430.6; ENSP00000369795.1; ENSG00000124588.23. DR Ensembl; ENST00000380455.11; ENSP00000369822.4; ENSG00000124588.23. DR Ensembl; ENST00000892207.1; ENSP00000562266.1; ENSG00000124588.23. DR Ensembl; ENST00000892208.1; ENSP00000562267.1; ENSG00000124588.23. DR Ensembl; ENST00000892209.1; ENSP00000562268.1; ENSG00000124588.23. DR Ensembl; ENST00000892210.1; ENSP00000562269.1; ENSG00000124588.23. DR Ensembl; ENST00000892212.1; ENSP00000562271.1; ENSG00000124588.23. DR Ensembl; ENST00000892214.1; ENSP00000562273.1; ENSG00000124588.23. DR Ensembl; ENST00000892215.1; ENSP00000562274.1; ENSG00000124588.23. DR Ensembl; ENST00000892216.1; ENSP00000562275.1; ENSG00000124588.23. DR Ensembl; ENST00000892217.1; ENSP00000562276.1; ENSG00000124588.23. DR Ensembl; ENST00000892219.1; ENSP00000562278.1; ENSG00000124588.23. DR Ensembl; ENST00000892220.1; ENSP00000562279.1; ENSG00000124588.23. DR Ensembl; ENST00000892222.1; ENSP00000562281.1; ENSG00000124588.23. DR Ensembl; ENST00000892223.1; ENSP00000562282.1; ENSG00000124588.23. DR Ensembl; ENST00000892224.1; ENSP00000562283.1; ENSG00000124588.23. DR Ensembl; ENST00000892225.1; ENSP00000562284.1; ENSG00000124588.23. DR Ensembl; ENST00000892227.1; ENSP00000562286.1; ENSG00000124588.23. DR Ensembl; ENST00000892228.1; ENSP00000562287.1; ENSG00000124588.23. DR Ensembl; ENST00000892231.1; ENSP00000562290.1; ENSG00000124588.23. DR Ensembl; ENST00000892232.1; ENSP00000562291.1; ENSG00000124588.23. DR Ensembl; ENST00000892234.1; ENSP00000562293.1; ENSG00000124588.23. DR Ensembl; ENST00000892235.1; ENSP00000562294.1; ENSG00000124588.23. DR Ensembl; ENST00000892239.1; ENSP00000562298.1; ENSG00000124588.23. DR Ensembl; ENST00000892240.1; ENSP00000562299.1; ENSG00000124588.23. DR Ensembl; ENST00000929208.1; ENSP00000599267.1; ENSG00000124588.23. DR Ensembl; ENST00000929212.1; ENSP00000599271.1; ENSG00000124588.23. DR Ensembl; ENST00000929213.1; ENSP00000599272.1; ENSG00000124588.23. DR Ensembl; ENST00000929214.1; ENSP00000599273.1; ENSG00000124588.23. DR Ensembl; ENST00000929216.1; ENSP00000599275.1; ENSG00000124588.23. DR Ensembl; ENST00000929217.1; ENSP00000599276.1; ENSG00000124588.23. DR Ensembl; ENST00000929227.1; ENSP00000599286.1; ENSG00000124588.23. DR Ensembl; ENST00000929228.1; ENSP00000599287.1; ENSG00000124588.23. DR Ensembl; ENST00000952437.1; ENSP00000622496.1; ENSG00000124588.23. DR Ensembl; ENST00000952438.1; ENSP00000622497.1; ENSG00000124588.23. DR Ensembl; ENST00000952439.1; ENSP00000622498.1; ENSG00000124588.23. DR Ensembl; ENST00000952440.1; ENSP00000622499.1; ENSG00000124588.23. DR Ensembl; ENST00000952441.1; ENSP00000622500.1; ENSG00000124588.23. DR Ensembl; ENST00000952442.1; ENSP00000622501.1; ENSG00000124588.23. DR Ensembl; ENST00000952443.1; ENSP00000622502.1; ENSG00000124588.23. DR Ensembl; ENST00000952445.1; ENSP00000622504.1; ENSG00000124588.23. DR Ensembl; ENST00000952446.1; ENSP00000622505.1; ENSG00000124588.23. DR Ensembl; ENST00000952447.1; ENSP00000622506.1; ENSG00000124588.23. DR Ensembl; ENST00000952448.1; ENSP00000622507.1; ENSG00000124588.23. DR Ensembl; ENST00000952449.1; ENSP00000622508.1; ENSG00000124588.23. DR Ensembl; ENST00000952451.1; ENSP00000622510.1; ENSG00000124588.23. DR Ensembl; ENST00000952453.1; ENSP00000622512.1; ENSG00000124588.23. DR Ensembl; ENST00000952456.1; ENSP00000622515.1; ENSG00000124588.23. DR Ensembl; ENST00000952457.1; ENSP00000622516.1; ENSG00000124588.23. 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 AGR; HGNC:7856; -. DR ClinPGx; PA31745; -. 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 OpenTargets; ENSG00000124588; -. DR VEuPathDB; HostDB:ENSG00000124588; -. DR eggNOG; ENOG502QWY5; Eukaryota. DR GeneTree; ENSGT00940000156563; -. DR HOGENOM; CLU_058643_2_0_1; -. DR InParanoid; P16083; -. DR OMA; ADHIAMK; -. DR OrthoDB; 26889at2759; -. DR PAN-GO; P16083; 2 GO annotations based on evolutionary models. DR PhylomeDB; P16083; -. 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 Agora; ENSG00000124588; -. DR BioGRID-ORCS; 4835; 8 hits in 1159 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 196 other cell types or tissues. DR ExpressionAtlas; P16083; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:CAFA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. 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 FunFam; 3.40.50.360:FF:000030; ribosyldihydronicotinamide dehydrogenase [quinone]; 1. DR Gene3D; 3.40.50.360; -; 1. DR InterPro; IPR003680; Flavodoxin_fold. DR InterPro; IPR029039; Flavoprotein-like_sf. DR InterPro; IPR051545; NAD(P)H_dehydrogenase_qn. DR PANTHER; PTHR10204; NAD P H OXIDOREDUCTASE-RELATED; 1. DR PANTHER; PTHR10204:SF33; RIBOSYLDIHYDRONICOTINAMIDE DEHYDROGENASE [QUINONE]; 1. DR Pfam; PF02525; Flavodoxin_2; 1. DR SUPFAM; SSF52218; Flavoproteins; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; FAD; Flavoprotein; Metal-binding; Oxidoreductase; KW Phosphoprotein; Proteomics identification; 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 124..126 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..172 FT /evidence="ECO:0007829|PDB:4FGL" FT HELIX 173..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 215..217 FT /evidence="ECO:0007829|PDB:4FGL" FT HELIX 218..221 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 //