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Q9NRD8

- DUOX2_HUMAN

UniProt

Q9NRD8 - DUOX2_HUMAN

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Protein
Dual oxidase 2
Gene
DUOX2, LNOX2, THOX2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi832 – 843121 Reviewed prediction
Add
BLAST
Calcium bindingi868 – 879122 Reviewed prediction
Add
BLAST

GO - Molecular functioni

  1. NAD(P)H oxidase activity Source: UniProtKB
  2. calcium ion binding Source: UniProtKB
  3. heme binding Source: InterPro
  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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 601576Extracellular Reviewed prediction
Add
BLAST
Transmembranei602 – 62221Helical; Reviewed prediction
Add
BLAST
Topological domaini623 – 1041419Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei1042 – 106221Helical; Reviewed prediction
Add
BLAST
Topological domaini1063 – 107614Extracellular Reviewed prediction
Add
BLAST
Transmembranei1077 – 109721Helical; Reviewed prediction
Add
BLAST
Topological domaini1098 – 114851Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei1149 – 116921Helical; Reviewed prediction
Add
BLAST
Topological domaini1170 – 118516Extracellular Reviewed prediction
Add
BLAST
Transmembranei1186 – 120621Helical; Reviewed prediction
Add
BLAST
Topological domaini1207 – 122317Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei1224 – 124421Helical; Reviewed prediction
Add
BLAST
Transmembranei1245 – 126521Helical; Reviewed prediction
Add
BLAST
Topological domaini1266 – 1548283Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
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 – 2525 Reviewed prediction
Add
BLAST
Chaini26 – 15481523Dual oxidase 2
PRO_0000223349Add
BLAST

Amino acid modifications

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

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.2 Publications

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini819 – 85436EF-hand 1
Add
BLAST
Domaini855 – 89036EF-hand 2
Add
BLAST
Domaini899 – 93436EF-hand 3
Add
BLAST
Domaini1084 – 1266183Ferric oxidoreductase
Add
BLAST
Domaini1267 – 1373107FAD-binding FR-type
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 596567Peroxidase-like; mediates peroxidase activity By similarity
Add
BLAST
Regioni960 – 1245286Interaction with TXNDC11 By similarity
Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the peroxidase family.
Contains 3 EF-hand domains.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251N → S in AAF73922. 1 Publication
Sequence conflicti25 – 251N → S in AAF78954. 1 Publication
Sequence conflicti984 – 9841A → V in AAF78954. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 117 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

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