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Q9NRD8

- DUOX2_HUMAN

UniProt

Q9NRD8 - DUOX2_HUMAN

Protein

Dual oxidase 2

Gene

DUOX2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain.1 Publication

    Catalytic activityi

    NAD(P)H + O2 = NAD(P)+ + H2O2.1 Publication

    Enzyme regulationi

    Peroxidase activity is inhibited by aminobenzohydrazide By similarity. The NADPH oxidase activity is calcium-dependent.By similarity1 Publication

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi832 – 843121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi868 – 879122PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. heme binding Source: InterPro
    3. NAD(P)H oxidase activity Source: UniProtKB
    4. peroxidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. adenohypophysis morphogenesis Source: Ensembl
    2. bone mineralization Source: Ensembl
    3. cuticle development Source: UniProtKB
    4. cytokine-mediated signaling pathway Source: UniProtKB
    5. fertilization Source: Ensembl
    6. hormone biosynthetic process Source: UniProtKB-KW
    7. hydrogen peroxide catabolic process Source: UniProtKB-KW
    8. inner ear development Source: Ensembl
    9. multicellular organism growth Source: Ensembl
    10. oxidation-reduction process Source: UniProtKB
    11. response to cAMP Source: UniProtKB
    12. response to virus Source: UniProtKB
    13. thyroid gland development Source: Ensembl
    14. thyroid hormone generation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide, Thyroid hormones biosynthesis

    Keywords - Ligandi

    Calcium, FAD, Flavoprotein, Metal-binding, NADP

    Enzyme and pathway databases

    BRENDAi1.6.3.1. 2681.
    SABIO-RKQ9NRD8.
    UniPathwayiUPA00194.

    Protein family/group databases

    PeroxiBasei3338. HsDuOx02.
    TCDBi5.B.1.2.2. the phagocyte (gp91(phox)) nadph oxidase family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual oxidase 2 (EC:1.11.1.-, EC:1.6.3.1)
    Alternative name(s):
    Large NOX 2
    Long NOX 2
    NADH/NADPH thyroid oxidase p138-tox
    NADPH oxidase/peroxidase DUOX2
    NADPH thyroid oxidase 2
    Thyroid oxidase 2
    p138 thyroid oxidase
    Gene namesi
    Name:DUOX2
    Synonyms:LNOX2, THOX2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:13273. DUOX2.

    Subcellular locationi

    Apical cell membrane 1 Publication; Multi-pass membrane protein 1 Publication
    Note: Localizes to the apical membrane of epithelial cells.

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Thyroid dyshormonogenesis 6 (TDH6) [MIM:607200]: A disorder due to a defective conversion of accumulated iodide to organically bound iodine. The iodide organification defect can be partial or complete.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361Q → H in TDH6. 1 Publication
    VAR_025323
    Natural varianti376 – 3761R → W in TDH6. 1 Publication
    VAR_025325
    Natural varianti1518 – 15181G → S in TDH6; the enzyme is non-functional; expressed at the cell surface of cells albeit at low level. 1 Publication
    VAR_064619

    Keywords - Diseasei

    Congenital hypothyroidism, Disease mutation

    Organism-specific databases

    MIMi607200. phenotype.
    Orphaneti95716. Familial thyroid dyshormonogenesis.
    226316. Genetic transient congenital hypothyroidism.
    PharmGKBiPA27517.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 15481523Dual oxidase 2PRO_0000223349Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi348 – 3481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi455 – 4551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi537 – 5371N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9NRD8.
    PRIDEiQ9NRD8.

    PTM databases

    PhosphoSiteiQ9NRD8.

    Expressioni

    Tissue specificityi

    Expressed in colon, small intestine, duodenum and tracheal surface epithelial cells (at protein level). Expressed in thyrocytes. Also detected in kidney, liver, lung, pancreas, prostate, salivary glands, rectum and testis.5 Publications

    Developmental stagei

    Widely expressed in fetal tissues.1 Publication

    Inductioni

    By forskolin, thyrotropin and the Th1-specific cytokine IFNG/IFN-gamma.1 Publication

    Gene expression databases

    BgeeiQ9NRD8.
    CleanExiHS_DUOX2.
    GenevestigatoriQ9NRD8.

    Interactioni

    Subunit structurei

    Interacts with TXNDC11, TPO and CYBA.1 Publication

    Protein-protein interaction databases

    STRINGi9606.ENSP00000267837.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NRD8.
    SMRiQ9NRD8. Positions 43-540, 772-928.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 601576ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini623 – 1041419CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1063 – 107614ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1098 – 114851CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1170 – 118516ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1207 – 122317CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1266 – 1548283CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei602 – 62221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1042 – 106221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1077 – 109721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1149 – 116921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1186 – 120621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1224 – 124421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1245 – 126521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini819 – 85436EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini855 – 89036EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini899 – 93436EF-hand 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1084 – 1266183Ferric oxidoreductaseAdd
    BLAST
    Domaini1267 – 1373107FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 596567Peroxidase-like; mediates peroxidase activityBy similarityAdd
    BLAST
    Regioni960 – 1245286Interaction with TXNDC11By similarityAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the peroxidase family.Curated
    Contains 3 EF-hand domains.PROSITE-ProRule annotation
    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
    Contains 1 ferric oxidoreductase domain.Curated

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG287712.
    HOGENOMiHOG000231774.
    HOVERGENiHBG080428.
    KOiK13411.
    OrthoDBiEOG7GN2KV.
    PhylomeDBiQ9NRD8.
    TreeFamiTF105424.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    1.10.640.10. 1 hit.
    InterProiIPR029592. DUOX2.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR013112. FAD-bd_8.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR013130. Fe3_Rdtase_TM_dom.
    IPR013121. Fe_red_NAD-bd_6.
    IPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PANTHERiPTHR11972:SF53. PTHR11972:SF53. 1 hit.
    PfamiPF03098. An_peroxidase. 1 hit.
    PF13499. EF-hand_7. 1 hit.
    PF08022. FAD_binding_8. 1 hit.
    PF01794. Ferric_reduct. 1 hit.
    PF08030. NAD_binding_6. 1 hit.
    [Graphical view]
    PRINTSiPR00457. ANPEROXIDASE.
    SMARTiSM00054. EFh. 2 hits.
    [Graphical view]
    SUPFAMiSSF48113. SSF48113. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    PS51384. FAD_FR. 1 hit.
    PS50292. PEROXIDASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9NRD8-1 [UniParc]FASTAAdd to Basket

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    MLRARPEALM LLGALLTGSL GPSGNQDALS LPWEVQRYDG WFNNLRHHER     50
    GAVGCRLQRR VPANYADGVY QALEEPQLPN PRRLSNAATR GIAGLPSLHN 100
    RTVLGVFFGY HVLSDVVSVE TPGCPAEFLN IRIPPGDPVF DPDQRGDVVL 150
    PFQRSRWDPE TGRSPSNPRD LANQVTGWLD GSAIYGSSHS WSDALRSFSG 200
    GQLASGPDPA FPRDSQNPLL MWAAPDPATG QNGPRGLYAF GAERGNREPF 250
    LQALGLLWFR YHNLWAQRLA RQHPDWEDEE LFQHARKRVI ATYQNIAVYE 300
    WLPSFLQKTL PEYTGYRPFL DPSISPEFVV ASEQFFSTMV PPGVYMRNAS 350
    CHFRKVLNKG FQSSQALRVC NNYWIRENPN LNSTQEVNEL LLGMASQISE 400
    LEDNIVVEDL RDYWPGPGKF SRTDYVASSI QRGRDMGLPS YSQALLAFGL 450
    DIPRNWSDLN PNVDPQVLEA TAALYNQDLS QLELLLGGLL ESHGDPGPLF 500
    SAIVLDQFVR LRDGDRYWFE NTRNGLFSKK EIEDIRNTTL RDVLVAVINI 550
    DPSALQPNVF VWHKGAPCPQ PKQLTTDGLP QCAPLTVLDF FEGSSPGFAI 600
    TIIALCCLPL VSLLLSGVVA YFRGREHKKL QKKLKESVKK EAAKDGVPAM 650
    EWPGPKERSS PIIIQLLSDR CLQVLNRHLT VLRVVQLQPL QQVNLILSNN 700
    RGCRTLLLKI PKEYDLVLLF SSEEERGAFV QQLWDFCVRW ALGLHVAEMS 750
    EKELFRKAVT KQQRERILEI FFRHLFAQVL DINQADAGTL PLDSSQKVRE 800
    ALTCELSRAE FAESLGLKPQ DMFVESMFSL ADKDGNGYLS FREFLDILVV 850
    FMKGSPEDKS RLMFTMYDLD ENGFLSKDEF FTMMRSFIEI SNNCLSKAQL 900
    AEVVESMFRE SGFQDKEELT WEDFHFMLRD HDSELRFTQL CVKGGGGGGN 950
    GIRDIFKQNI SCRVSFITRT PGERSHPQGL GPPAPEAPEL GGPGLKKRFG 1000
    KKAAVPTPRL YTEALQEKMQ RGFLAQKLQQ YKRFVENYRR HIVCVAIFSA 1050
    ICVGVFADRA YYYGFASPPS DIAQTTLVGI ILSRGTAASV SFMFSYILLT 1100
    MCRNLITFLR ETFLNRYVPF DAAVDFHRWI AMAAVVLAIL HSAGHAVNVY 1150
    IFSVSPLSLL ACIFPNVFVN DGSKLPQKFY WWFFQTVPGM TGVLLLLVLA 1200
    IMYVFASHHF RRRSFRGFWL THHLYILLYA LLIIHGSYAL IQLPTFHIYF 1250
    LVPAIIYGGD KLVSLSRKKV EISVVKAELL PSGVTYLQFQ RPQGFEYKSG 1300
    QWVRIACLAL GTTEYHPFTL TSAPHEDTLS LHIRAVGPWT TRLREIYSSP 1350
    KGNGCAGYPK LYLDGPFGEG HQEWHKFEVS VLVGGGIGVT PFASILKDLV 1400
    FKSSLGSQML CKKIYFIWVT RTQRQFEWLA DIIQEVEEND HQDLVSVHIY 1450
    VTQLAEKFDL RTTMLYICER HFQKVLNRSL FTGLRSITHF GRPPFEPFFN 1500
    SLQEVHPQVR KIGVFSCGPP GMTKNVEKAC QLVNRQDRAH FMHHYENF 1548
    Length:1,548
    Mass (Da):175,364
    Last modified:May 18, 2010 - v2
    Checksum:i7BAA2350EC0A2A7E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251N → S in AAF73922. (PubMed:10806195)Curated
    Sequence conflicti25 – 251N → S in AAF78954. (PubMed:11514595)Curated
    Sequence conflicti984 – 9841A → V in AAF78954. (PubMed:11514595)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361Q → H in TDH6. 1 Publication
    VAR_025323
    Natural varianti138 – 1381P → L.1 Publication
    Corresponds to variant rs2001616 [ dbSNP | Ensembl ].
    VAR_025324
    Natural varianti376 – 3761R → W in TDH6. 1 Publication
    VAR_025325
    Natural varianti678 – 6781H → R.
    Corresponds to variant rs57659670 [ dbSNP | Ensembl ].
    VAR_061177
    Natural varianti1067 – 10671S → L.3 Publications
    Corresponds to variant rs269868 [ dbSNP | Ensembl ].
    VAR_047075
    Natural varianti1518 – 15181G → S in TDH6; the enzyme is non-functional; expressed at the cell surface of cells albeit at low level. 1 Publication
    VAR_064619

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF230496 mRNA. Translation: AAF73922.1.
    AF267981 mRNA. Translation: AAF78954.1.
    AC091117 Genomic DNA. No translation available.
    AF181972 mRNA. Translation: AAF20055.1.
    GU174495 Genomic DNA. Translation: ADB22378.1.
    CCDSiCCDS10117.1.
    RefSeqiNP_054799.4. NM_014080.4.
    UniGeneiHs.71377.

    Genome annotation databases

    EnsembliENST00000603300; ENSP00000475084; ENSG00000140279.
    GeneIDi50506.
    KEGGihsa:50506.
    UCSCiuc001zun.3. human.

    Polymorphism databases

    DMDMi296434485.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF230496 mRNA. Translation: AAF73922.1 .
    AF267981 mRNA. Translation: AAF78954.1 .
    AC091117 Genomic DNA. No translation available.
    AF181972 mRNA. Translation: AAF20055.1 .
    GU174495 Genomic DNA. Translation: ADB22378.1 .
    CCDSi CCDS10117.1.
    RefSeqi NP_054799.4. NM_014080.4.
    UniGenei Hs.71377.

    3D structure databases

    ProteinModelPortali Q9NRD8.
    SMRi Q9NRD8. Positions 43-540, 772-928.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000267837.

    Protein family/group databases

    PeroxiBasei 3338. HsDuOx02.
    TCDBi 5.B.1.2.2. the phagocyte (gp91(phox)) nadph oxidase family.

    PTM databases

    PhosphoSitei Q9NRD8.

    Polymorphism databases

    DMDMi 296434485.

    Proteomic databases

    PaxDbi Q9NRD8.
    PRIDEi Q9NRD8.

    Protocols and materials databases

    DNASUi 50506.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000603300 ; ENSP00000475084 ; ENSG00000140279 .
    GeneIDi 50506.
    KEGGi hsa:50506.
    UCSCi uc001zun.3. human.

    Organism-specific databases

    CTDi 50506.
    GeneCardsi GC15M045384.
    H-InvDB HIX0038086.
    HGNCi HGNC:13273. DUOX2.
    MIMi 606759. gene.
    607200. phenotype.
    neXtProti NX_Q9NRD8.
    Orphaneti 95716. Familial thyroid dyshormonogenesis.
    226316. Genetic transient congenital hypothyroidism.
    PharmGKBi PA27517.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG287712.
    HOGENOMi HOG000231774.
    HOVERGENi HBG080428.
    KOi K13411.
    OrthoDBi EOG7GN2KV.
    PhylomeDBi Q9NRD8.
    TreeFami TF105424.

    Enzyme and pathway databases

    UniPathwayi UPA00194 .
    BRENDAi 1.6.3.1. 2681.
    SABIO-RK Q9NRD8.

    Miscellaneous databases

    ChiTaRSi DUOX2. human.
    GeneWikii Dual_oxidase_2.
    GenomeRNAii 50506.
    NextBioi 35489705.
    PROi Q9NRD8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NRD8.
    CleanExi HS_DUOX2.
    Genevestigatori Q9NRD8.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    1.10.640.10. 1 hit.
    InterProi IPR029592. DUOX2.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR013112. FAD-bd_8.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR013130. Fe3_Rdtase_TM_dom.
    IPR013121. Fe_red_NAD-bd_6.
    IPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    PANTHERi PTHR11972:SF53. PTHR11972:SF53. 1 hit.
    Pfami PF03098. An_peroxidase. 1 hit.
    PF13499. EF-hand_7. 1 hit.
    PF08022. FAD_binding_8. 1 hit.
    PF01794. Ferric_reduct. 1 hit.
    PF08030. NAD_binding_6. 1 hit.
    [Graphical view ]
    PRINTSi PR00457. ANPEROXIDASE.
    SMARTi SM00054. EFh. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48113. SSF48113. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEi PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    PS51384. FAD_FR. 1 hit.
    PS50292. PEROXIDASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family."
      De Deken X., Wang D., Many M.-C., Costagliola S., Libert F., Vassart G., Dumont J.E., Miot F.
      J. Biol. Chem. 275:23227-23233(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY, VARIANT LEU-1067.
      Tissue: Thyroid.
    2. "Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox."
      Edens W.A., Sharling L., Cheng G., Shapira R., Kinkade J.M., Lee T., Edens H.A., Tang X., Sullards C., Flaherty D.B., Benian G.M., Lambeth J.D.
      J. Cell Biol. 154:879-891(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-138 AND LEU-1067, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
      Tissue: Pancreas and Thyroid.
    3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cDNAs."
      Dupuy C., Ohayon R., Valent A., Noel-Hudson M.-S., Deme D., Virion A.
      J. Biol. Chem. 274:37265-37269(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 339-1548, VARIANT LEU-1067.
      Tissue: Thyroid.
    5. "Compound heterozygosity for a novel hemizygous missense mutation and a partial deletion affecting the catalytic core of the H2O2-generating enzyme DUOX2 associated with transient congenital hypothyroidism."
      Hoste C., Rigutto S., Van Vliet G., Miot F., De Deken X.
      Hum. Mutat. 31:E1304-E1319(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1509-1548, VARIANT TDH6 SER-1518, CHARACTERIZATION OF VARIANT TDH6 SER-1518.
    6. "Characterization of ThOX proteins as components of the thyroid H(2)O(2)-generating system."
      De Deken X., Wang D., Dumont J.E., Miot F.
      Exp. Cell Res. 273:187-196(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION.
    7. "Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and congenital hypothyroidism."
      Moreno J.C., Bikker H., Kempers M.J.E., van Trotsenburg A.S., Baas F., de Vijlder J.J.M., Vulsma T., Ris-Stalpers C.
      N. Engl. J. Med. 347:95-102(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN TDH6.
    8. "Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense."
      Geiszt M., Witta J., Baffi J., Lekstrom K., Leto T.L.
      FASEB J. 17:1502-1504(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    9. "NADPH oxidase-dependent acid production in airway epithelial cells."
      Schwarzer C., Machen T.E., Illek B., Fischer H.
      J. Biol. Chem. 279:36454-36461(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    10. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    11. "Identification of a novel partner of duox: EFP1, a thioredoxin-related protein."
      Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E., Miot F.
      J. Biol. Chem. 280:3096-3103(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TXNDC11; TPO AND CYBA.
    12. Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
    13. "Persistent mild hypothyroidism associated with novel sequence variants of the DUOX2 gene in two siblings."
      Vigone M.C., Fugazzola L., Zamproni I., Passoni A., Di Candia S., Chiumello G., Persani L., Weber G.
      Hum. Mutat. 26:395-395(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TDH6 TRP-376.
    14. "Three mutations (p.Q36H, p.G418fsX482, and g.IVS19-2A-->C) in the dual oxidase 2 gene responsible for congenital goiter and iodide organification defect."
      Varela V., Rivolta C.M., Esperante S.A., Gruneiro-Papendieck L., Chiesa A., Targovnik H.M.
      Clin. Chem. 52:182-191(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TDH6 HIS-36.

    Entry informationi

    Entry nameiDUOX2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRD8
    Secondary accession number(s): A8MQ13
    , D2XI64, Q9NR02, Q9UHF9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2006
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 of the sequence. [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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3