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Q9NRD9

- DUOX1_HUMAN

UniProt

Q9NRD9 - DUOX1_HUMAN

Protein

Dual oxidase 1

Gene

DUOX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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.2 Publications

    Catalytic activityi

    NAD(P)H + O2 = NAD(P)+ + H2O2.2 Publications

    Enzyme regulationi

    The NADPH oxidase activity is calcium-dependent. Peroxidase activity is inhibited by aminobenzohydrazide.2 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi828 – 839121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi864 – 875122PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. cuticle development Source: UniProtKB
    2. cytokine-mediated signaling pathway Source: UniProtKB
    3. hormone biosynthetic process Source: UniProtKB-KW
    4. hydrogen peroxide biosynthetic process Source: UniProtKB
    5. hydrogen peroxide catabolic process Source: UniProtKB-KW
    6. oxidation-reduction process Source: UniProtKB
    7. response to cAMP Source: UniProtKB
    8. superoxide anion generation Source: UniProtKB
    9. 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

    SABIO-RKQ9NRD9.
    UniPathwayiUPA00194.

    Protein family/group databases

    PeroxiBasei3339. HsDuOx01.
    TCDBi5.B.1.2.1. the phagocyte (gp91(phox)) nadph oxidase family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual oxidase 1 (EC:1.11.1.-, EC:1.6.3.1)
    Alternative name(s):
    Large NOX 1
    Long NOX 1
    NADPH thyroid oxidase 1
    Thyroid oxidase 1
    Gene namesi
    Name:DUOX1
    Synonyms:DUOX, LNOX1, THOX1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:3062. DUOX1.

    Subcellular locationi

    Apical cell membrane 2 Publications; Multi-pass membrane protein 2 Publications
    Note: Localizes to the apical membrane of epithelial cells.

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27516.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 15511530Dual oxidase 1PRO_0000223344Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi534 – 5341N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ9NRD9.
    PaxDbiQ9NRD9.
    PRIDEiQ9NRD9.

    PTM databases

    PhosphoSiteiQ9NRD9.

    Expressioni

    Tissue specificityi

    Expressed in thyrocytes and tracheal surface epithelial cells (at protein level). Expressed in thyroid, trachea, bronchium, and to a lower extent, in placenta, testis, prostate, pancreas and heart.4 Publications

    Developmental stagei

    Widely expressed in fetal tissues.1 Publication

    Inductioni

    By forskolin (at protein level). By thyrotropin and the Th2-specific cytokines IL-4 and IL-13.2 Publications

    Gene expression databases

    ArrayExpressiQ9NRD9.
    BgeeiQ9NRD9.
    CleanExiHS_DUOX1.
    GenevestigatoriQ9NRD9.

    Organism-specific databases

    HPAiHPA023544.

    Interactioni

    Subunit structurei

    Interacts with TXNDC11, TPO and CYBA.1 Publication

    Protein-protein interaction databases

    STRINGi9606.ENSP00000317997.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NRD9.
    SMRiQ9NRD9. Positions 8-541, 765-954.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 596575ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini618 – 1044427CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1066 – 108015ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1102 – 114847CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1172 – 118817ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1210 – 122617CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1248 – 12481ExtracellularSequence Analysis
    Topological domaini1270 – 1551282CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei597 – 61721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1045 – 106521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1081 – 110121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1149 – 117123HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1189 – 120921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1227 – 124721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1249 – 126921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini815 – 85036EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini851 – 88636EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini895 – 93036EF-hand 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1087 – 1269183Ferric oxidoreductaseAdd
    BLAST
    Domaini1270 – 1376107FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 593568Peroxidase-like; mediates peroxidase activityAdd
    BLAST
    Regioni956 – 1248293Interaction 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

    eggNOGiCOG5126.
    HOGENOMiHOG000231774.
    HOVERGENiHBG080428.
    InParanoidiQ9NRD9.
    KOiK13411.
    OMAiTRERRQK.
    OrthoDBiEOG7GN2KV.
    PhylomeDBiQ9NRD9.
    TreeFamiTF105424.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    1.10.640.10. 1 hit.
    InterProiIPR029595. DUOX1.
    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:SF37. PTHR11972:SF37. 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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NRD9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGFCLALAWT LLVGAWTPLG AQNPISWEVQ RFDGWYNNLM EHRWGSKGSR     50
    LQRLVPASYA DGVYQPLGEP HLPNPRDLSN TISRGPAGLA SLRNRTVLGV 100
    FFGYHVLSDL VSVETPGCPA EFLNIRIPPG DPMFDPDQRG DVVLPFQRSR 150
    WDPETGRSPS NPRDPANQVT GWLDGSAIYG SSHSWSDALR SFSRGQLASG 200
    PDPAFPRDSQ NPLLMWAAPD PATGQNGPRG LYAFGAERGN REPFLQALGL 250
    LWFRYHNLWA QRLARQHPDW EDEELFQHAR KRVIATYQNI AVYEWLPSFL 300
    QKTLPEYTGY RPFLDPSISS EFVAASEQFL STMVPPGVYM RNASCHFQGV 350
    INRNSSVSRA LRVCNSYWSR EHPSLQSAED VDALLLGMAS QIAEREDHVL 400
    VEDVRDFWPG PLKFSRTDHL ASCLQRGRDL GLPSYTKARA ALGLSPITRW 450
    QDINPALSRS NDTVLEATAA LYNQDLSWLE LLPGGLLESH RDPGPLFSTI 500
    VLEQFVRLRD GDRYWFENTR NGLFSKKEIE EIRNTTLQDV LVAVINIDPS 550
    ALQPNVFVWH KGDPCPQPRQ LSTEGLPACA PSVVRDYFEG SGFGFGVTIG 600
    TLCCFPLVSL LSAWIVARLR MRNFKRLQGQ DRQSIVSEKL VGGMEALEWQ 650
    GHKEPCRPVL VYLQPGQIRV VDGRLTVLRT IQLQPPQKVN FVLSSNRGRR 700
    TLLLKIPKEY DLVLLFNLEE ERQALVENLR GALKESGLSI QEWELREQEL 750
    MRAAVTREQR RHLLETFFRH LFSQVLDINQ ADAGTLPLDS SQKVREALTC 800
    ELSRAEFAES LGLKPQDMFV ESMFSLADKD GNGYLSFREF LDILVVFMKG 850
    SPEEKSRLMF RMYDFDGNGL ISKDEFIRML RSFIEISNNC LSKAQLAEVV 900
    ESMFRESGFQ DKEELTWEDF HFMLRDHNSE LRFTQLCVKG VEVPEVIKDL 950
    CRRASYISQD MICPSPRVSA RCSRSDIETE LTPQRLQCPM DTDPPQEIRR 1000
    RFGKKVTSFQ PLLFTEAHRE KFQRSCLHQT VQQFKRFIEN YRRHIGCVAV 1050
    FYAIAGGLFL ERAYYYAFAA HHTGITDTTR VGIILSRGTA ASISFMFSYI 1100
    LLTMCRNLIT FLRETFLNRY VPFDAAVDFH RLIASTAIVL TVLHSVGHVV 1150
    NVYLFSISPL SVLSCLFPGL FHDDGSELPQ KYYWWFFQTV PGLTGVVLLL 1200
    ILAIMYVFAS HHFRRRSFRG FWLTHHLYIL LYVLLIIHGS FALIQLPRFH 1250
    IFFLVPAIIY GGDKLVSLSR KKVEISVVKA ELLPSGVTHL RFQRPQGFEY 1300
    KSGQWVRIAC LALGTTEYHP FTLTSAPHED TLSLHIRAAG PWTTRLREIY 1350
    SAPTGDRCAR YPKLYLDGPF GEGHQEWHKF EVSVLVGGGI GVTPFASILK 1400
    DLVFKSSVSC QVFCKKIYFI WVTRTQRQFE WLADIIREVE ENDHQDLVSV 1450
    HIYITQLAEK FDLRTTMLYI CERHFQKVLN RSLFTGLRSI THFGRPPFEP 1500
    FFNSLQEVHP QVRKIGVFSC GPPGMTKNVE KACQLINRQD RTHFSHHYEN 1550
    F 1551
    Length:1,551
    Mass (Da):177,235
    Last modified:October 1, 2000 - v1
    Checksum:i37CF124A579446B0
    GO
    Isoform 2 (identifier: Q9NRD9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-354: Missing.
         355-405: SSVSRALRVC...EDHVLVEDVR → MWMHCCWAWP...GRGSAGLPEP

    Note: No experimental confirmation available.

    Show »
    Length:1,197
    Mass (Da):137,604
    Checksum:i44391BD31C81E18F
    GO

    Sequence cautioni

    The sequence BAD18816.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AK128591 differs from that shown. Reason: Erroneous termination at position 967. Translated as Arg.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti413 – 4131K → E in AK128591. (PubMed:14702039)Curated
    Sequence conflicti1388 – 13881G → R in BAD18816. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti962 – 9621I → T.
    Corresponds to variant rs16939743 [ dbSNP | Ensembl ].
    VAR_049104
    Natural varianti1026 – 10261C → R.1 Publication
    Corresponds to variant rs16939752 [ dbSNP | Ensembl ].
    VAR_025321
    Natural varianti1178 – 11781L → F.1 Publication
    Corresponds to variant rs2458236 [ dbSNP | Ensembl ].
    VAR_025322

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 354354Missing in isoform 2. 1 PublicationVSP_017262Add
    BLAST
    Alternative sequencei355 – 40551SSVSR…VEDVR → MWMHCCWAWPPRSQSERTMC WLKMCGVSLRLSLQVVNSWP LGRGSAGLPEP in isoform 2. 1 PublicationVSP_017263Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF230495 mRNA. Translation: AAF73921.1.
    AF213465 mRNA. Translation: AAF71295.1.
    AK128591 mRNA. No translation available.
    AK172859 mRNA. Translation: BAD18816.1. Different initiation.
    AC051619 Genomic DNA. No translation available.
    BC114628 mRNA. Translation: AAI14629.1.
    CCDSiCCDS32221.1. [Q9NRD9-1]
    RefSeqiNP_059130.2. NM_017434.4. [Q9NRD9-1]
    NP_787954.1. NM_175940.2. [Q9NRD9-1]
    UniGeneiHs.272813.

    Genome annotation databases

    EnsembliENST00000321429; ENSP00000317997; ENSG00000137857. [Q9NRD9-1]
    ENST00000389037; ENSP00000373689; ENSG00000137857. [Q9NRD9-1]
    ENST00000561166; ENSP00000454065; ENSG00000137857. [Q9NRD9-2]
    GeneIDi53905.
    KEGGihsa:53905.
    UCSCiuc001zus.1. human. [Q9NRD9-1]

    Polymorphism databases

    DMDMi74719102.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF230495 mRNA. Translation: AAF73921.1 .
    AF213465 mRNA. Translation: AAF71295.1 .
    AK128591 mRNA. No translation available.
    AK172859 mRNA. Translation: BAD18816.1 . Different initiation.
    AC051619 Genomic DNA. No translation available.
    BC114628 mRNA. Translation: AAI14629.1 .
    CCDSi CCDS32221.1. [Q9NRD9-1 ]
    RefSeqi NP_059130.2. NM_017434.4. [Q9NRD9-1 ]
    NP_787954.1. NM_175940.2. [Q9NRD9-1 ]
    UniGenei Hs.272813.

    3D structure databases

    ProteinModelPortali Q9NRD9.
    SMRi Q9NRD9. Positions 8-541, 765-954.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000317997.

    Protein family/group databases

    PeroxiBasei 3339. HsDuOx01.
    TCDBi 5.B.1.2.1. the phagocyte (gp91(phox)) nadph oxidase family.

    PTM databases

    PhosphoSitei Q9NRD9.

    Polymorphism databases

    DMDMi 74719102.

    Proteomic databases

    MaxQBi Q9NRD9.
    PaxDbi Q9NRD9.
    PRIDEi Q9NRD9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321429 ; ENSP00000317997 ; ENSG00000137857 . [Q9NRD9-1 ]
    ENST00000389037 ; ENSP00000373689 ; ENSG00000137857 . [Q9NRD9-1 ]
    ENST00000561166 ; ENSP00000454065 ; ENSG00000137857 . [Q9NRD9-2 ]
    GeneIDi 53905.
    KEGGi hsa:53905.
    UCSCi uc001zus.1. human. [Q9NRD9-1 ]

    Organism-specific databases

    CTDi 53905.
    GeneCardsi GC15P045422.
    HGNCi HGNC:3062. DUOX1.
    HPAi HPA023544.
    MIMi 606758. gene.
    neXtProti NX_Q9NRD9.
    PharmGKBi PA27516.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5126.
    HOGENOMi HOG000231774.
    HOVERGENi HBG080428.
    InParanoidi Q9NRD9.
    KOi K13411.
    OMAi TRERRQK.
    OrthoDBi EOG7GN2KV.
    PhylomeDBi Q9NRD9.
    TreeFami TF105424.

    Enzyme and pathway databases

    UniPathwayi UPA00194 .
    SABIO-RK Q9NRD9.

    Miscellaneous databases

    GeneWikii Dual_oxidase_1.
    GenomeRNAii 53905.
    NextBioi 56216.
    PROi Q9NRD9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRD9.
    Bgeei Q9NRD9.
    CleanExi HS_DUOX1.
    Genevestigatori Q9NRD9.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    1.10.640.10. 1 hit.
    InterProi IPR029595. DUOX1.
    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:SF37. PTHR11972:SF37. 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] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
      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] (ISOFORM 1), VARIANT PHE-1178, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
      Tissue: Lung.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1030-1551 (ISOFORMS 1/2), VARIANT ARG-1026.
      Tissue: Lung and Trachea.
    4. "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].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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. "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.
    8. "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: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. "Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium."
      Harper R.W., Xu C., Eiserich J.P., Chen Y., Kao C.-Y., Thai P., Setiadi H., Wu R.
      FEBS Lett. 579:4911-4917(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    10. "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.
    11. Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.

    Entry informationi

    Entry nameiDUOX1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRD9
    Secondary accession number(s): A6NH28
    , Q14C94, Q6ZMB3, Q6ZR09, Q9NZC1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2006
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 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