Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P16083 (NQO2_HUMAN)

Entry version 203 (13 Feb 2019)
Sequence version 5 (11 Jan 2011)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Ribosyldihydronicotinamide dehydrogenase [quinone]

Gene

NQO2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei12FAD2 Publications1
    Binding sitei156FAD2 Publications1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi174Zinc1
    Metal bindingi178Zinc1
    Binding sitei194FAD2 Publications1
    Binding sitei201FAD2 Publications1
    Metal bindingi223Zinc1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi18 – 21FAD2 Publications4
    Nucleotide bindingi104 – 107FAD2 Publications4
    Nucleotide bindingi148 – 151FAD2 Publications4

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionOxidoreductase
    LigandFAD, Flavoprotein, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		1.10.99.2 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-HSA-211945 Phase I - Functionalization of compounds

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P16083

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:NQO2
    Synonyms:NMOR2
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...    EuPathDBi    		HostDB:ENSG00000124588.19

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:7856 NQO2

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		160998 gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_P16083

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi162N → H: Loss of activity toward CB1954, no effect toward menadione. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		4835

    MalaCards human disease database

    More...    MalaCardsi    		NQO2

    Open Targets

    More...    OpenTargetsi    		ENSG00000124588

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA31745

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL3959

    Drug and drug target database

    More...    DrugBanki    		DB04253 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

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		NQO2

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		317373581

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000716261 – 231Ribosyldihydronicotinamide dehydrogenase [quinone]Add BLAST231

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei80PhosphoserineCombined sources1
    Modified residuei197PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		P16083

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P16083

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		P16083

    PaxDb, a database of protein abundance averages across all three domains of life

    More...    PaxDbi    		P16083

    PeptideAtlas

    More...    PeptideAtlasi    		P16083

    PRoteomics IDEntifications database

    More...    PRIDEi    		P16083

    ProteomicsDB human proteome resource

    More...    ProteomicsDBi    		12689
    53285

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P16083

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...    PhosphoSitePlusi    		P16083

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000124588 Expressed in 221 organ(s), highest expression level in nephron tubule

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		P16083 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		P16083 HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		HPA021283
    HPA021332

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.4 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    View the complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		110898, 13 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...    CORUMi    		P16083

    Database of interacting proteins

    More...    DIPi    		DIP-39704N

    Protein interaction database and analysis system

    More...    IntActi    		P16083, 13 interactors

    Molecular INTeraction database

    More...    MINTi    		P16083

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000337773

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P16083

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1231
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    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[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		P16083

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		P16083

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P16083

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni127 – 129Substrate binding3

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the NAD(P)H dehydrogenase (quinone) family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG410IKWF Eukaryota
    COG2249 LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00940000156563

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000149970

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...    HOVERGENi    		HBG029104

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P16083

    KEGG Orthology (KO)

    More...    KOi    		K08071

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		WSMPALL

    Database of Orthologous Groups

    More...    OrthoDBi    		1394543at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P16083

    TreeFam database of animal gene trees

    More...    TreeFami    		TF300296

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.50.360, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR003680 Flavodoxin_fold
    IPR029039 Flavoprotein-like_sf

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF02525 Flavodoxin_2, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF52218 SSF52218, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

    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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFE1F4D577517B972
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    Q5TD07Q5TD07_HUMAN
    Ribosyldihydronicotinamide dehydrog...
    NQO2
    		193Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    Q5TD05Q5TD05_HUMAN
    Ribosyldihydronicotinamide dehydrog...
    NQO2
    		139Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    A2A2U4A2A2U4_HUMAN
    Ribosyldihydronicotinamide dehydrog...
    NQO2
    		63Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    U3KQG7U3KQG7_HUMAN
    Ribosyldihydronicotinamide dehydrog...
    NQO2
    		35Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti140G → C in AAB60642 (PubMed:8182056).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    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

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS4481.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A32667

    NCBI Reference Sequences

    More...    RefSeqi    		NP_000895.2, NM_000904.4
    NP_001277150.1, NM_001290221.1
    NP_001305869.1, NM_001318940.1

    UniGene gene-oriented nucleotide sequence clusters

    More...    UniGenei    		Hs.533050

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000338130; ENSP00000337773; ENSG00000124588
    ENST00000380430; ENSP00000369795; ENSG00000124588
    ENST00000380455; ENSP00000369822; ENSG00000124588

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		4835

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:4835

    UCSC genome browser

    More...    UCSCi    		uc003mus.3 human

    Keywords - Coding sequence diversityi

    Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    NIEHS-SNPs

    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

    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...

    Protein-protein interaction databases

    BioGridi110898, 13 interactors
    CORUMiP16083
    DIPiDIP-39704N
    IntActiP16083, 13 interactors
    MINTiP16083
    STRINGi9606.ENSP00000337773

    Chemistry databases

    BindingDBiP16083
    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

    PTM databases

    iPTMnetiP16083
    PhosphoSitePlusiP16083

    Polymorphism and mutation databases

    BioMutaiNQO2
    DMDMi317373581

    Proteomic databases

    EPDiP16083
    jPOSTiP16083
    MaxQBiP16083
    PaxDbiP16083
    PeptideAtlasiP16083
    PRIDEiP16083
    ProteomicsDBi12689
    53285

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		4835
    DisGeNETi4835
    EuPathDBiHostDB:ENSG00000124588.19

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		NQO2

    H-Invitational Database, human transcriptome db

    More...    H-InvDBi    		HIX0018967
    HGNCiHGNC:7856 NQO2
    HPAiHPA021283
    HPA021332
    MalaCardsiNQO2
    MIMi160998 gene
    neXtProtiNX_P16083
    OpenTargetsiENSG00000124588
    PharmGKBiPA31745

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiENOG410IKWF Eukaryota
    COG2249 LUCA
    GeneTreeiENSGT00940000156563
    HOGENOMiHOG000149970
    HOVERGENiHBG029104
    InParanoidiP16083
    KOiK08071
    OMAiWSMPALL
    OrthoDBi1394543at2759
    PhylomeDBiP16083
    TreeFamiTF300296

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...    ChiTaRSi    		NQO2 human
    EvolutionaryTraceiP16083

    The Gene Wiki collection of pages on human genes and proteins

    More...    GeneWikii    		NAD(P)H_dehydrogenase,_quinone_2

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...    GenomeRNAii    		4835

    Protein Ontology

    More...    PROi    		PR:P16083

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000124588 Expressed in 221 organ(s), highest expression level in nephron tubule
    ExpressionAtlasiP16083 baseline and differential
    GenevisibleiP16083 HS

    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNQO2_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P16083
    Secondary accession number(s): B2R492, Q5TD04
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 11, 2011
    Last modified: February 13, 2019
    This is version 203 of the entry and version 5 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    5. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    6. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again