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Database: UniProt
Entry: P15559
LinkDB: P15559
Original site: P15559 
ID   NQO1_HUMAN              Reviewed;         274 AA.
AC   P15559; B2R5Y9; B4DNM7; B7ZAD1; Q86UK1;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   02-JUN-2021, entry version 220.
DE   RecName: Full=NAD(P)H dehydrogenase [quinone] 1;
DE            EC=1.6.5.2;
DE   AltName: Full=Azoreductase;
DE   AltName: Full=DT-diaphorase;
DE            Short=DTD;
DE   AltName: Full=Menadione reductase;
DE   AltName: Full=NAD(P)H:quinone oxidoreductase 1;
DE   AltName: Full=Phylloquinone reductase;
DE   AltName: Full=Quinone reductase 1;
DE            Short=QR1;
GN   Name=NQO1; Synonyms=DIA4, NMOR1;
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] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=2843525;
RA   Jaiswal A.K., McBride O.W., Adesnik M., Nebert D.W.;
RT   "Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase. cDNA
RT   sequence and localization of gene to chromosome 16.";
RL   J. Biol. Chem. 263:13572-13578(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=1657151; DOI=10.1021/bi00108a007;
RA   Jaiswal A.K.;
RT   "Human NAD(P)H:quinone oxidoreductase (NQO1) gene structure and induction
RT   by dioxin.";
RL   Biochemistry 30:10647-10653(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-187.
RG   NIEHS SNPs program;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP   SER-187.
RC   TISSUE=Amygdala;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
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   [8]
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   [9]
RP   INTERACTION WITH PDLIM4, AND INDUCTION.
RX   PubMed=21636573; DOI=10.1074/jbc.m111.241554;
RA   Guryanova O.A., Drazba J.A., Frolova E.I., Chumakov P.M.;
RT   "Actin cytoskeleton remodeling by the alternatively spliced isoform of
RT   PDLIM4/RIL protein.";
RL   J. Biol. Chem. 286:26849-26859(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-250 AND LYS-251, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 4-274 IN COMPLEX WITH FAD, AND
RP   SUBUNIT.
RX   PubMed=10543876; DOI=10.1021/jm991060m;
RA   Skelly J.V., Sanderson M.R., Suter D.A., Baumann U., Read M.A.,
RA   Gregory D.S.J., Bennett M., Hobbs S.M., Neidle S.;
RT   "Crystal structure of human DT-diaphorase: a model for interaction with the
RT   cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954).";
RL   J. Med. Chem. 42:4325-4330(1999).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FAD AND DUROQUINONE.
RX   PubMed=10706635; DOI=10.1073/pnas.97.7.3177;
RA   Faig M., Bianchet M.A., Talalay P., Chen S., Winski S., Ross D.,
RA   Amzel L.M.;
RT   "Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases:
RT   species comparison and structural changes with substrate binding and
RT   release.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:3177-3182(2000).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FAD AND THE INHIBITOR
RP   ES936, AND MASS SPECTROMETRY.
RX   PubMed=11735396; DOI=10.1021/bi011324i;
RA   Winski S.L., Faig M., Bianchet M.A., Siegel D., Swann E., Fung K.,
RA   Duncan M.W., Moody C.J., Amzel L.M., Ross D.;
RT   "Characterization of a mechanism-based inhibitor of NAD(P)H:quinone
RT   oxidoreductase 1 by biochemical, X-ray crystallographic, and mass
RT   spectrometric approaches.";
RL   Biochemistry 40:15135-15142(2001).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH FAD AND INHIBITORS,
RP   AND SUBUNIT.
RX   PubMed=11587640; DOI=10.1016/s0969-2126(01)00636-0;
RA   Faig M., Bianchet M.A., Winski S., Hargreaves R., Moody C.J., Hudnott A.R.,
RA   Ross D., Amzel L.M.;
RT   "Structure-based development of anticancer drugs: complexes of
RT   NAD(P)H:quinone oxidoreductase 1 with chemotherapeutic quinones.";
RL   Structure 9:659-667(2001).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR
RP   DICOUMAROL.
RX   PubMed=16700548; DOI=10.1021/bi0600087;
RA   Asher G., Dym O., Tsvetkov P., Adler J., Shaul Y.;
RT   "The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with
RT   its potent inhibitor dicoumarol.";
RL   Biochemistry 45:6372-6378(2006).
RN   [17]
RP   VARIANT SER-187.
RX   PubMed=1737339;
RA   Traver R.D., Horikoshi T., Danenberg K.D., Stadlbauer T.H., Danenberg P.V.,
RA   Ross D., Gibson N.W.;
RT   "NAD(P)H:quinone oxidoreductase gene expression in human colon carcinoma
RT   cells: characterization of a mutation which modulates DT-diaphorase
RT   activity and mitomycin sensitivity.";
RL   Cancer Res. 52:797-802(1992).
RN   [18]
RP   VARIANT SER-187.
RX   PubMed=10447260;
RX   DOI=10.1002/(sici)1098-1004(1999)14:1<67::aid-humu8>3.0.co;2-5;
RA   Kristiansen O.P., Larsen Z.M., Johannesen J., Nerup J., Mandrup-Poulsen T.,
RA   Pociot F.;
RT   "No linkage of P187S polymorphism in NAD(P)H: quinone oxidoreductase
RT   (NQO1/DIA4) and type 1 diabetes in the Danish population.";
RL   Hum. Mutat. 14:67-70(1999).
CC   -!- FUNCTION: The enzyme apparently serves as a quinone reductase in
CC       connection with conjugation reactions of hydroquinons 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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC         Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC         Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- ACTIVITY REGULATION: Inhibited by dicoumarol.
CC   -!- SUBUNIT: Homodimer (PubMed:10543876, PubMed:10706635, PubMed:11735396,
CC       PubMed:11587640, PubMed:16700548). Interacts with PDLIM4 isoform 2;
CC       this interaction stabilizes PDLIM4 isoform 2 in response to oxidative
CC       stress and protects it from ubiquitin-independent degradation by the
CC       core 20S proteasome (PubMed:21636573). {ECO:0000269|PubMed:10543876,
CC       ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11587640,
CC       ECO:0000269|PubMed:11735396, ECO:0000269|PubMed:16700548,
CC       ECO:0000269|PubMed:21636573}.
CC   -!- INTERACTION:
CC       P15559; P07902: GALT; NbExp=3; IntAct=EBI-3989435, EBI-750827;
CC       P15559; Q9UK53: ING1; NbExp=3; IntAct=EBI-3989435, EBI-399198;
CC       P15559; P15559: NQO1; NbExp=5; IntAct=EBI-3989435, EBI-3989435;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P15559-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P15559-2; Sequence=VSP_042716;
CC       Name=3;
CC         IsoId=P15559-3; Sequence=VSP_044446;
CC   -!- INDUCTION: By dioxin (PubMed:1657151). By oxidative stress
CC       (PubMed:21636573). {ECO:0000269|PubMed:1657151,
CC       ECO:0000269|PubMed:21636573}.
CC   -!- MASS SPECTROMETRY: Mass=30864; Mass_error=6; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11735396};
CC   -!- POLYMORPHISM: The Ser-187 polymorphism may be linked to susceptibility
CC       to forms of cancers.
CC   -!- MISCELLANEOUS: Quinone reductase accepts electrons from both NADH and
CC       NADPH with equal efficiency.
CC   -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/NQO1ID375.html";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/nqo1/";
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DR   EMBL; J03934; AAA59940.1; -; mRNA.
DR   EMBL; M81600; AAB60701.1; -; Genomic_DNA.
DR   EMBL; M81596; AAB60701.1; JOINED; Genomic_DNA.
DR   EMBL; M81597; AAB60701.1; JOINED; Genomic_DNA.
DR   EMBL; M81598; AAB60701.1; JOINED; Genomic_DNA.
DR   EMBL; M81599; AAB60701.1; JOINED; Genomic_DNA.
DR   EMBL; AY281093; AAP20940.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK297979; BAG60289.1; -; mRNA.
DR   EMBL; AK312368; BAG35286.1; -; mRNA.
DR   EMBL; AK316246; BAH14617.1; -; mRNA.
DR   EMBL; AC092115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471092; EAW83283.1; -; Genomic_DNA.
DR   EMBL; CH471092; EAW83284.1; -; Genomic_DNA.
DR   EMBL; BC007659; AAH07659.1; -; mRNA.
DR   CCDS; CCDS10883.1; -. [P15559-1]
DR   CCDS; CCDS32471.1; -. [P15559-3]
DR   CCDS; CCDS32472.1; -. [P15559-2]
DR   PIR; A41135; A30879.
DR   RefSeq; NP_000894.1; NM_000903.2. [P15559-1]
DR   RefSeq; NP_001020604.1; NM_001025433.1. [P15559-2]
DR   RefSeq; NP_001020605.1; NM_001025434.1. [P15559-3]
DR   PDB; 1D4A; X-ray; 1.70 A; A/B/C/D=2-274.
DR   PDB; 1DXO; X-ray; 2.50 A; A/B/C/D=2-274.
DR   PDB; 1GG5; X-ray; 2.50 A; A/B/C/D=2-274.
DR   PDB; 1H66; X-ray; 2.00 A; A/B/C/D=3-274.
DR   PDB; 1H69; X-ray; 1.86 A; A/B/C/D=3-274.
DR   PDB; 1KBO; X-ray; 2.30 A; A/B/C/D=2-274.
DR   PDB; 1KBQ; X-ray; 1.80 A; A/B/C/D=2-274.
DR   PDB; 1QBG; X-ray; 2.30 A; A/B/C/D=4-274.
DR   PDB; 2F1O; X-ray; 2.75 A; A/B/C/D/E/F/G/H=2-274.
DR   PDB; 3JSX; X-ray; 2.45 A; A/B/C/D/E/F/G/H=2-274.
DR   PDB; 4CET; X-ray; 2.20 A; A=1-274.
DR   PDB; 4CF6; X-ray; 2.69 A; A/B=1-274.
DR   PDB; 5A4K; X-ray; 2.09 A; A/B/C/D=1-274.
DR   PDB; 5EA2; X-ray; 2.01 A; A/C/E/G=1-273.
DR   PDB; 5EAI; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-274.
DR   PDB; 5FUQ; X-ray; 2.04 A; A/B=1-274.
DR   PDB; 6FY4; X-ray; 2.76 A; A/B/C/D=1-274.
DR   PDB; 6LLC; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=2-274.
DR   PDBsum; 1D4A; -.
DR   PDBsum; 1DXO; -.
DR   PDBsum; 1GG5; -.
DR   PDBsum; 1H66; -.
DR   PDBsum; 1H69; -.
DR   PDBsum; 1KBO; -.
DR   PDBsum; 1KBQ; -.
DR   PDBsum; 1QBG; -.
DR   PDBsum; 2F1O; -.
DR   PDBsum; 3JSX; -.
DR   PDBsum; 4CET; -.
DR   PDBsum; 4CF6; -.
DR   PDBsum; 5A4K; -.
DR   PDBsum; 5EA2; -.
DR   PDBsum; 5EAI; -.
DR   PDBsum; 5FUQ; -.
DR   PDBsum; 6FY4; -.
DR   PDBsum; 6LLC; -.
DR   SMR; P15559; -.
DR   BioGRID; 108072; 56.
DR   DIP; DIP-24210N; -.
DR   IntAct; P15559; 8.
DR   MINT; P15559; -.
DR   STRING; 9606.ENSP00000319788; -.
DR   BindingDB; P15559; -.
DR   ChEMBL; CHEMBL3623; -.
DR   DrugBank; DB07385; 3-(HYDROXYMETHYL)-1-METHYL-5-(2-METHYLAZIRIDIN-1-YL)-2-PHENYL-1H-INDOLE-4,7-DIONE.
DR   DrugBank; DB02395; 3-Hydroxymethyl-5-Aziridinyl-1methyl-2-[1h-Indole-4,7-Dione]-Propanol.
DR   DrugBank; DB03626; 5-Methoxy-1,2-Dimethyl-3-(Phenoxymethyl)Indole-4,7-Dione.
DR   DrugBank; DB14001; alpha-Tocopherol succinate.
DR   DrugBank; DB04392; Bishydroxy[2h-1-Benzopyran-2-One,1,2-Benzopyrone].
DR   DrugBank; DB09061; Cannabidiol.
DR   DrugBank; DB00958; Carboplatin.
DR   DrugBank; DB02633; Cibacron Blue.
DR   DrugBank; DB00515; Cisplatin.
DR   DrugBank; DB14002; D-alpha-Tocopherol acetate.
DR   DrugBank; DB00266; Dicoumarol.
DR   DrugBank; DB00997; Doxorubicin.
DR   DrugBank; DB01927; Duroquinone.
DR   DrugBank; DB02400; ES-936.
DR   DrugBank; DB03147; Flavin adenine dinucleotide.
DR   DrugBank; DB00170; Menadione.
DR   DrugBank; DB00526; Oxaliplatin.
DR   DrugBank; DB00252; Phenytoin.
DR   DrugBank; DB04090; RH-1.
DR   DrugBank; DB00163; Vitamin E.
DR   DrugCentral; P15559; -.
DR   iPTMnet; P15559; -.
DR   MetOSite; P15559; -.
DR   PhosphoSitePlus; P15559; -.
DR   SwissPalm; P15559; -.
DR   BioMuta; NQO1; -.
DR   DMDM; 118607; -.
DR   EPD; P15559; -.
DR   jPOST; P15559; -.
DR   MassIVE; P15559; -.
DR   MaxQB; P15559; -.
DR   PaxDb; P15559; -.
DR   PeptideAtlas; P15559; -.
DR   PRIDE; P15559; -.
DR   ProteomicsDB; 12688; -. [P15559-2]
DR   ProteomicsDB; 53187; -. [P15559-1]
DR   ProteomicsDB; 53188; -. [P15559-2]
DR   TopDownProteomics; P15559-1; -. [P15559-1]
DR   Antibodypedia; 1549; 803 antibodies.
DR   DNASU; 1728; -.
DR   Ensembl; ENST00000320623; ENSP00000319788; ENSG00000181019. [P15559-1]
DR   Ensembl; ENST00000379046; ENSP00000368334; ENSG00000181019. [P15559-3]
DR   Ensembl; ENST00000379047; ENSP00000368335; ENSG00000181019. [P15559-2]
DR   GeneID; 1728; -.
DR   KEGG; hsa:1728; -.
DR   UCSC; uc002exp.5; human. [P15559-1]
DR   CTD; 1728; -.
DR   DisGeNET; 1728; -.
DR   GeneCards; NQO1; -.
DR   HGNC; HGNC:2874; NQO1.
DR   HPA; ENSG00000181019; Tissue enhanced (stomach).
DR   MIM; 125860; gene.
DR   neXtProt; NX_P15559; -.
DR   OpenTargets; ENSG00000181019; -.
DR   PharmGKB; PA31744; -.
DR   VEuPathDB; HostDB:ENSG00000181019.12; -.
DR   eggNOG; ENOG502QQMI; Eukaryota.
DR   GeneTree; ENSGT00940000159150; -.
DR   InParanoid; P15559; -.
DR   OMA; WFERVLV; -.
DR   OrthoDB; 1394543at2759; -.
DR   PhylomeDB; P15559; -.
DR   TreeFam; TF300296; -.
DR   BioCyc; MetaCyc:HS11566-MONOMER; -.
DR   BRENDA; 1.6.5.2; 2681.
DR   PathwayCommons; P15559; -.
DR   Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR   SABIO-RK; P15559; -.
DR   SIGNOR; P15559; -.
DR   BioGRID-ORCS; 1728; 9 hits in 995 CRISPR screens.
DR   ChiTaRS; NQO1; human.
DR   EvolutionaryTrace; P15559; -.
DR   GeneWiki; NAD(P)H_dehydrogenase_(quinone_1); -.
DR   GenomeRNAi; 1728; -.
DR   Pharos; P15559; Tchem.
DR   PRO; PR:P15559; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P15559; protein.
DR   Bgee; ENSG00000181019; Expressed in stomach and 231 other tissues.
DR   ExpressionAtlas; P15559; baseline and differential.
DR   Genevisible; P15559; HS.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005829; C:cytosol; IDA:CAFA.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; TAS:ProtInc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IBA:GO_Central.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR   GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:Ensembl.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0045454; P:cell redox homeostasis; IEP:UniProtKB.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0071248; P:cellular response to metal ion; IEA:Ensembl.
DR   GO; GO:0006116; P:NADH oxidation; IEA:Ensembl.
DR   GO; GO:0070995; P:NADPH oxidation; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; IEA:Ensembl.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; TAS:ProtInc.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR   GO; GO:0043279; P:response to alkaloid; IEA:Ensembl.
DR   GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR   GO; GO:0009743; P:response to carbohydrate; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:1905395; P:response to flavonoid; IEA:Ensembl.
DR   GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR   GO; GO:1904880; P:response to hydrogen sulfide; IEA:Ensembl.
DR   GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR   GO; GO:1904844; P:response to L-glutamine; IEA:Ensembl.
DR   GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:UniProtKB.
DR   GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR   GO; GO:1904772; P:response to tetrachloromethane; IEA:Ensembl.
DR   GO; GO:0009636; P:response to toxic substance; TAS:ProtInc.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; TAS:ProtInc.
DR   GO; GO:0006805; P:xenobiotic metabolic process; TAS:ProtInc.
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; Alternative splicing; Cytoplasm; FAD; Flavoprotein;
KW   Isopeptide bond; NAD; NADP; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..274
FT                   /note="NAD(P)H dehydrogenase [quinone] 1"
FT                   /id="PRO_0000071622"
FT   NP_BIND         18..19
FT                   /note="FAD"
FT                   /evidence="ECO:0000269|PubMed:10543876,
FT                   ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396"
FT   NP_BIND         104..107
FT                   /note="FAD"
FT                   /evidence="ECO:0000269|PubMed:10543876,
FT                   ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396"
FT   NP_BIND         148..151
FT                   /note="FAD"
FT                   /evidence="ECO:0000269|PubMed:10543876,
FT                   ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396"
FT   REGION          126..128
FT                   /note="Substrate binding"
FT   BINDING         12
FT                   /note="FAD"
FT                   /evidence="ECO:0000269|PubMed:10543876,
FT                   ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396"
FT   BINDING         67
FT                   /note="FAD"
FT                   /evidence="ECO:0000269|PubMed:10543876,
FT                   ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396"
FT   BINDING         156
FT                   /note="FAD"
FT                   /evidence="ECO:0000269|PubMed:10543876,
FT                   ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396"
FT   BINDING         201
FT                   /note="FAD"
FT                   /evidence="ECO:0000269|PubMed:10543876,
FT                   ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        250
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        251
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         102..139
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044446"
FT   VAR_SEQ         140..173
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042716"
FT   VARIANT         139
FT                   /note="R -> W (in dbSNP:rs1131341)"
FT                   /id="VAR_016170"
FT   VARIANT         187
FT                   /note="P -> S (lack of activity; dbSNP:rs1800566)"
FT                   /evidence="ECO:0000269|PubMed:10447260,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:1737339,
FT                   ECO:0000269|Ref.3"
FT                   /id="VAR_008384"
FT   VARIANT         269
FT                   /note="Q -> H (in dbSNP:rs34447156)"
FT                   /id="VAR_050220"
FT   CONFLICT        252
FT                   /note="F -> S (in Ref. 4; BAG60289)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..10
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   STRAND          15..17
FT                   /evidence="ECO:0007829|PDB:1QBG"
FT   HELIX           18..32
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   STRAND          36..41
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   TURN            42..46
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:5EA2"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:5EA2"
FT   HELIX           68..78
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   HELIX           83..94
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   STRAND          96..103
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   STRAND          106..108
FT                   /evidence="ECO:0007829|PDB:4CET"
FT   HELIX           111..120
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   HELIX           129..131
FT                   /evidence="ECO:0007829|PDB:1H69"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   TURN            137..140
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   STRAND          142..148
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   HELIX           154..156
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:1H69"
FT   HELIX           165..173
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   TURN            174..177
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   HELIX           178..180
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   STRAND          188..190
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   HELIX           193..195
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   HELIX           198..212
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   HELIX           213..217
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   HELIX           226..228
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   HELIX           233..235
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:1H69"
FT   HELIX           241..248
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   STRAND          254..256
FT                   /evidence="ECO:0007829|PDB:1D4A"
FT   TURN            266..270
FT                   /evidence="ECO:0007829|PDB:1D4A"
SQ   SEQUENCE   274 AA;  30868 MW;  A4010462AD00F3FE CRC64;
     MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES DLYAMNFNPI ISRKDITGKL
     KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF QFPLQWFGVP AILKGWFERV
     FIGEFAYTYA AMYDKGPFRS KKAVLSITTG GSGSMYSLQG IHGDMNVILW PIQSGILHFC
     GFQVLEPQLT YSIGHTPADA RIQILEGWKK RLENIWDETP LYFAPSSLFD LNFQAGFLMK
     KEVQDEEKNK KFGLSVGHHL GKSIPTDNQI KARK
//
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