SubmitCancel

Skip Header

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

Q9NRD9

- DUOX1_HUMAN

UniProt

Q9NRD9 - DUOX1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dual oxidase 1

Gene
DUOX1, DUOX, LNOX1, THOX1
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.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 – 839121 Reviewed predictionAdd
BLAST
Calcium bindingi864 – 875122 Reviewed predictionAdd
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
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

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 596575Extracellular Reviewed predictionAdd
BLAST
Transmembranei597 – 61721Helical; Reviewed predictionAdd
BLAST
Topological domaini618 – 1044427Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei1045 – 106521Helical; Reviewed predictionAdd
BLAST
Topological domaini1066 – 108015Extracellular Reviewed predictionAdd
BLAST
Transmembranei1081 – 110121Helical; Reviewed predictionAdd
BLAST
Topological domaini1102 – 114847Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei1149 – 117123Helical; Reviewed predictionAdd
BLAST
Topological domaini1172 – 118817Extracellular Reviewed predictionAdd
BLAST
Transmembranei1189 – 120921Helical; Reviewed predictionAdd
BLAST
Topological domaini1210 – 122617Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei1227 – 124721Helical; Reviewed predictionAdd
BLAST
Topological domaini1248 – 12481Extracellular Reviewed prediction
Transmembranei1249 – 126921Helical; Reviewed predictionAdd
BLAST
Topological domaini1270 – 1551282Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27516.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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-13.4 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.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 593568Peroxidase-like; mediates peroxidase activityAdd
BLAST
Regioni956 – 1248293Interaction with TXNDC11 By similarityAdd
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

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.

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. VSP_017262Add
BLAST
Alternative sequencei355 – 40551SSVSR…VEDVR → MWMHCCWAWPPRSQSERTMC WLKMCGVSLRLSLQVVNSWP LGRGSAGLPEP in isoform 2. VSP_017263Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti413 – 4131K → E in AK128591. 1 Publication
Sequence conflicti1388 – 13881G → R in BAD18816. 1 Publication

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

« 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] (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: September 3, 2014
This is version 116 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

Similar proteinsi