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Protein

Ribosyldihydronicotinamide dehydrogenase [quinone]

Gene

NQO2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.1 Publication

Miscellaneous

Uses dihydronicotinamide riboside (NRH) rather than NAD(P)H as an electron donor.

Catalytic activityi

1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(beta-D-ribofuranosyl)nicotinamide + a quinol.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Zn2+Note: Binds 1 zinc ion per subunit.
  • FAD

Enzyme regulationi

Inhibited by melatonin, resveratrol and 5-hydroxytryptamine.1 Publication

Kineticsi

  1. KM=28 µM for NRH2 Publications
  2. KM=11.6 µM for menadione2 Publications
  3. KM=252 µM for NADH2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei12FAD2 Publications1
    Binding sitei156FAD2 Publications1
    Metal bindingi174Zinc1
    Metal bindingi178Zinc1
    Binding sitei194FAD2 Publications1
    Binding sitei201FAD2 Publications1
    Metal bindingi223Zinc1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi18 – 21FAD2 Publications4
    Nucleotide bindingi104 – 107FAD2 Publications4
    Nucleotide bindingi148 – 151FAD2 Publications4

    GO - Molecular functioni

    • chloride ion binding Source: CAFA
    • dihydronicotinamide riboside quinone reductase activity Source: CAFA
    • electron transfer activity Source: CAFA
    • FAD binding Source: CAFA
    • melatonin binding Source: CAFA
    • oxidoreductase activity Source: CAFA
    • oxidoreductase activity, acting on other nitrogenous compounds as donors Source: CAFA
    • protein homodimerization activity Source: CAFA
    • resveratrol binding Source: CAFA
    • zinc ion binding Source: CAFA

    GO - Biological processi

    • oxidation-reduction process Source: CAFA
    • xenobiotic metabolic process Source: Reactome

    Keywordsi

    Molecular functionOxidoreductase
    LigandFAD, Flavoprotein, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi1.10.99.2 2681
    ReactomeiR-HSA-211945 Phase I - Functionalization of compounds
    SABIO-RKiP16083

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosyldihydronicotinamide dehydrogenase [quinone] (EC:1.10.5.11 Publication)
    Alternative name(s):
    NRH dehydrogenase [quinone] 2
    NRH:quinone oxidoreductase 2
    Quinone reductase 2
    Short name:
    QR2
    Gene namesi
    Name:NQO2
    Synonyms:NMOR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 6

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000124588.19
    HGNCiHGNC:7856 NQO2
    MIMi160998 gene
    neXtProtiNX_P16083

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi162N → H: Loss of activity toward CB1954, no effect toward menadione. 1 Publication1

    Organism-specific databases

    DisGeNETi4835
    MalaCardsiNQO2
    OpenTargetsiENSG00000124588
    PharmGKBiPA31745

    Chemistry databases

    ChEMBLiCHEMBL3959
    DrugBankiDB04253 CB1954
    DB06695 Dabigatran etexilate
    DB03147 Flavin adenine dinucleotide
    DB01065 Melatonin
    DB00170 Menadione
    DB08190 N-[2-(2-iodo-5-methoxy-1H-indol-3-yl)ethyl]acetamide
    DB00157 NADH
    DB01087 Primaquine
    DB02709 Resveratrol

    Polymorphism and mutation databases

    BioMutaiNQO2
    DMDMi317373581

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000716261 – 231Ribosyldihydronicotinamide dehydrogenase [quinone]Add BLAST231

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei80PhosphoserineCombined sources1
    Modified residuei197PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    EPDiP16083
    MaxQBiP16083
    PaxDbiP16083
    PeptideAtlasiP16083
    PRIDEiP16083

    PTM databases

    iPTMnetiP16083
    PhosphoSitePlusiP16083

    Expressioni

    Gene expression databases

    BgeeiENSG00000124588
    CleanExiHS_NQO2
    ExpressionAtlasiP16083 baseline and differential
    GenevisibleiP16083 HS

    Organism-specific databases

    HPAiHPA021283
    HPA021332

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Binary interactionsi

    Show more details

    GO - Molecular functioni

    • protein homodimerization activity Source: CAFA

    Protein-protein interaction databases

    BioGridi110898, 12 interactors
    DIPiDIP-39704N
    IntActiP16083, 12 interactors
    MINTiP16083
    STRINGi9606.ENSP00000337773

    Chemistry databases

    BindingDBiP16083

    Structurei

    Secondary structure

    1231
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 10Combined sources6
    Helixi18 – 33Combined sources16
    Beta strandi36 – 41Combined sources6
    Turni42 – 46Combined sources5
    Helixi53 – 55Combined sources3
    Beta strandi63 – 65Combined sources3
    Helixi68 – 77Combined sources10
    Helixi83 – 94Combined sources12
    Beta strandi96 – 103Combined sources8
    Beta strandi105 – 108Combined sources4
    Helixi111 – 120Combined sources10
    Turni123 – 125Combined sources3
    Beta strandi129 – 132Combined sources4
    Helixi133 – 135Combined sources3
    Turni137 – 140Combined sources4
    Beta strandi142 – 148Combined sources7
    Turni153 – 156Combined sources4
    Beta strandi160 – 162Combined sources3
    Helixi165 – 173Combined sources9
    Helixi174 – 178Combined sources5
    Turni179 – 181Combined sources3
    Beta strandi188 – 190Combined sources3
    Turni193 – 195Combined sources3
    Helixi198 – 212Combined sources15
    Helixi213 – 217Combined sources5
    Helixi225 – 229Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1QR2X-ray2.10A/B2-231[»]
    1SG0X-ray1.50A/B2-231[»]
    1XI2X-ray1.50A/B2-231[»]
    1ZX1X-ray2.16A/B1-231[»]
    2BZSX-ray2.00A/B2-231[»]
    2QMYX-ray2.50A/B2-231[»]
    2QMZX-ray2.10A/B2-231[»]
    2QR2X-ray2.45A/B2-231[»]
    2QWXX-ray1.50A/B1-231[»]
    2QX4X-ray1.65A/B2-231[»]
    2QX6X-ray1.75A/B2-231[»]
    2QX8X-ray1.60A/B2-231[»]
    2QX9X-ray2.31A/B2-231[»]
    3FW1X-ray1.75A1-231[»]
    3G5MX-ray1.84A/B1-231[»]
    3GAMX-ray1.98A/B1-231[»]
    3NFRX-ray1.57A/B2-231[»]
    3NHFX-ray2.00A/B2-231[»]
    3NHJX-ray2.33A/B2-231[»]
    3NHKX-ray1.96A/B2-231[»]
    3NHLX-ray1.57A/B2-231[»]
    3NHPX-ray1.70A/B2-231[»]
    3NHRX-ray1.80A/B2-231[»]
    3NHSX-ray1.78A/B2-231[»]
    3NHUX-ray1.90A/B2-231[»]
    3NHWX-ray1.65A/B2-231[»]
    3NHYX-ray1.90A/B2-231[»]
    3O2NX-ray1.60A/B2-231[»]
    3O73X-ray2.00A/B1-231[»]
    3OVMX-ray2.09A/B1-231[»]
    3OWHX-ray2.28A/B1-231[»]
    3OWXX-ray1.85A/B1-231[»]
    3OX1X-ray2.00A/B1-231[»]
    3OX2X-ray2.41A/B1-231[»]
    3OX3X-ray1.80A/B1-231[»]
    3TE7X-ray1.70A/B3-230[»]
    3TEMX-ray1.45A/B3-230[»]
    3TZBX-ray2.19A/B/C/D3-230[»]
    3UXEX-ray1.50A/B2-231[»]
    3UXHX-ray1.53A/B2-231[»]
    4FGJX-ray1.35A/B1-231[»]
    4FGKX-ray1.40A/B1-231[»]
    4FGLX-ray1.20A/B/C/D1-231[»]
    4GQIX-ray1.95A/B2-231[»]
    4GR9X-ray2.29A/B2-231[»]
    4QODX-ray1.35A/B1-231[»]
    4QOEX-ray1.45A/B1-231[»]
    4QOFX-ray1.55A/B1-231[»]
    4QOGX-ray1.40A/B1-231[»]
    4QOHX-ray1.60A/B1-231[»]
    4QOIX-ray1.55A/B1-231[»]
    4QOJX-ray1.85A/B1-231[»]
    4U7FX-ray1.80A/B2-231[»]
    4U7GX-ray1.96A/B2-231[»]
    4U7HX-ray1.48A/B2-231[»]
    4XDGX-ray1.50A/B1-231[»]
    4XDHX-ray1.90A/B1-231[»]
    4ZVKX-ray1.87A/B2-231[»]
    4ZVLX-ray1.90A/B2-231[»]
    4ZVMX-ray1.97A/B2-231[»]
    4ZVNX-ray1.87A/B2-231[»]
    5BUCX-ray1.87A/B2-231[»]
    5LBTX-ray1.75A/B1-231[»]
    5LBUX-ray1.65A/B1-231[»]
    5LBWX-ray1.90A/B1-231[»]
    5LBYX-ray1.40A/B1-231[»]
    5LBZX-ray1.40A/B1-231[»]
    ProteinModelPortaliP16083
    SMRiP16083
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16083

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni127 – 129Substrate binding3

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG410IKWF Eukaryota
    COG2249 LUCA
    GeneTreeiENSGT00440000033410
    HOGENOMiHOG000149970
    HOVERGENiHBG029104
    InParanoidiP16083
    KOiK08071
    OMAiWSMPALL
    OrthoDBiEOG091G183R
    PhylomeDBiP16083
    TreeFamiTF300296

    Family and domain databases

    Gene3Di3.40.50.360, 1 hit
    InterProiView protein in InterPro
    IPR003680 Flavodoxin_fold
    IPR029039 Flavoprotein-like_sf
    PfamiView protein in Pfam
    PF02525 Flavodoxin_2, 1 hit
    SUPFAMiSSF52218 SSF52218, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P16083-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAGKKVLIVY AHQEPKSFNG SLKNVAVDEL SRQGCTVTVS DLYAMNLEPR
    60 70 80 90 100
    ATDKDITGTL SNPEVFNYGV ETHEAYKQRS LASDITDEQK KVREADLVIF
    110 120 130 140 150
    QFPLYWFSVP AILKGWMDRV LCQGFAFDIP GFYDSGLLQG KLALLSVTTG
    160 170 180 190 200
    GTAEMYTKTG VNGDSRYFLW PLQHGTLHFC GFKVLAPQIS FAPEIASEEE
    210 220 230
    RKGMVAAWSQ RLQTIWKEEP IPCTAHWHFG Q
    Length:231
    Mass (Da):25,919
    Last modified:January 11, 2011 - v5
    Checksum:iFE1F4D577517B972
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti140G → C in AAB60642 (PubMed:8182056).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_02139916K → R1 PublicationCorresponds to variant dbSNP:rs28383623Ensembl.1
    Natural variantiVAR_02140029E → G1 PublicationCorresponds to variant dbSNP:rs17136117Ensembl.1
    Natural variantiVAR_02140147L → F7 PublicationsCorresponds to variant dbSNP:rs1143684Ensembl.1
    Natural variantiVAR_02140258G → D1 PublicationCorresponds to variant dbSNP:rs17300141Ensembl.1
    Natural variantiVAR_021403184V → A1 PublicationCorresponds to variant dbSNP:rs28383651Ensembl.1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J02888 mRNA Translation: AAA60239.1
    AY299456 Genomic DNA Translation: AAB60642.3
    AB050248 Genomic DNA Translation: BAB16974.1
    AY855291 Genomic DNA Translation: AAW29945.1
    AK311746 mRNA Translation: BAG34689.1
    AL133351 Genomic DNA No translation available.
    CH471087 Genomic DNA Translation: EAW55107.1
    BC006096 mRNA Translation: AAH06096.1
    CCDSiCCDS4481.1
    PIRiA32667
    RefSeqiNP_000895.2, NM_000904.4
    NP_001277150.1, NM_001290221.1
    NP_001305869.1, NM_001318940.1
    UniGeneiHs.533050

    Genome annotation databases

    EnsembliENST00000338130; ENSP00000337773; ENSG00000124588
    ENST00000380430; ENSP00000369795; ENSG00000124588
    ENST00000380455; ENSP00000369822; ENSG00000124588
    GeneIDi4835
    KEGGihsa:4835
    UCSCiuc003mus.3 human

    Keywords - Coding sequence diversityi

    Polymorphism

    Similar proteinsi

    Entry informationi

    Entry nameiNQO2_HUMAN
    AccessioniPrimary (citable) accession number: P16083
    Secondary accession number(s): B2R492, Q5TD04
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 11, 2011
    Last modified: May 23, 2018
    This is version 196 of the entry and version 5 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

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