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UniProtKB - Q9NRD8 (DUOX2_HUMAN)

Entry version 158 (10 Apr 2019)
Sequence version 2 (18 May 2010)
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Protein

Dual oxidase 2

Gene

DUOX2

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

Annotation score:5 out of 5

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

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

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

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

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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: thyroid hormone biosynthesis

This protein is involved in the pathway thyroid hormone biosynthesis, which is part of Hormone biosynthesis.
View all proteins of this organism that are known to be involved in the pathway thyroid hormone biosynthesis and in Hormone biosynthesis.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi832 – 8431PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi868 – 8792PROSITE-ProRule annotationAdd BLAST12

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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

Molecular functionOxidoreductase, Peroxidase
Biological processHydrogen peroxide, Thyroid hormones biosynthesis
LigandCalcium, FAD, Flavoprotein, Metal-binding, NADP

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.6.3.1 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-209968 Thyroxine biosynthesis

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q9NRD8

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi
UPA00194

Protein family/group databases

PeroxiBase, a peroxidase database

More...PeroxiBasei		3338 HsDuOx02

Transport Classification Database

More...TCDBi		5.B.1.1.7 the phagocyte (gp91(phox)) nadph oxidase family

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DUOX2
Synonyms:LNOX2, THOX2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 15

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000140279.12

Human Gene Nomenclature Database

More...HGNCi		HGNC:13273 DUOX2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		606759 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9NRD8

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini26 – 601ExtracellularSequence analysisAdd BLAST576
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei602 – 622HelicalSequence analysisAdd BLAST21
Topological domaini623 – 1041CytoplasmicSequence analysisAdd BLAST419
Transmembranei1042 – 1062HelicalSequence analysisAdd BLAST21
Topological domaini1063 – 1076ExtracellularSequence analysisAdd BLAST14
Transmembranei1077 – 1097HelicalSequence analysisAdd BLAST21
Topological domaini1098 – 1128CytoplasmicSequence analysisAdd BLAST31
Transmembranei1129 – 1151HelicalSequence analysisAdd BLAST23
Topological domaini1152 – 1185ExtracellularSequence analysisAdd BLAST34
Transmembranei1186 – 1206HelicalSequence analysisAdd BLAST21
Topological domaini1207 – 1223CytoplasmicSequence analysisAdd BLAST17
Transmembranei1224 – 1244HelicalSequence analysisAdd BLAST21
Transmembranei1245 – 1265HelicalSequence analysisAdd BLAST21
Topological domaini1266 – 1548CytoplasmicSequence analysisAdd BLAST283

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Thyroid dyshormonogenesis 6 (TDH6)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder due to a defective conversion of accumulated iodide to organically bound iodine. The iodide organification defect can be partial or complete.
See also OMIM:607200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02532336Q → H in TDH6. 1 Publication1
Natural variantiVAR_025325376R → W in TDH6. 1 PublicationCorresponds to variant dbSNP:rs119472029EnsemblClinVar.1
Natural variantiVAR_0646191518G → S in TDH6; the enzyme is non-functional; expressed at the cell surface of cells albeit at low level. 1 PublicationCorresponds to variant dbSNP:rs368512412Ensembl.1
Defects in DUOX2 may play a role in the pathogenesis of very early onset inflammatory bowel disease (VEOIBD), a chronic, relapsing inflammation of the gastrointestinal tract with a complex etiology diagnosed before 6 years of age. VEOIBD is subdivided into Crohn disease and ulcerative colitis phenotypes. Crohn disease may affect any part of the gastrointestinal tract from the mouth to the anus, but the phenotype of children with onset of Crohn disease occurring younger than the age of 10 is predominantly colonic, with a lower risk of ileal disease. Bowel inflammation is transmural and discontinuous; it may contain granulomas or be associated with intestinal or perianal fistulas. In contrast, in ulcerative colitis, the inflammation is continuous and limited to rectal and colonic mucosal layers; fistulas and granulomas are not observed. Both diseases include extraintestinal inflammation of the skin, eyes, or joints.1 Publication

Keywords - Diseasei

Congenital hypothyroidism, Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		50506

MalaCards human disease database

More...MalaCardsi		DUOX2
MIMi607200 phenotype

Open Targets

More...OpenTargetsi		ENSG00000140279

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		95716 Familial thyroid dyshormonogenesis
226316 Genetic transient congenital hypothyroidism

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27517

Chemistry databases

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2999

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		DUOX2

Domain mapping of disease mutations (DMDM)

More...DMDMi		296434485

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25Sequence analysisAdd BLAST25
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000022334926 – 1548Dual oxidase 2Add BLAST1523

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi100N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi124 ↔ 11621 Publication
Glycosylationi348N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi382N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi455N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi537N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi568Interchain (with C-167 in DUOXA2)1 Publication
Disulfide bondi582Interchain (with C-233 in DUOXA2)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9NRD8

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9NRD8

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

More...PaxDbi		Q9NRD8

PeptideAtlas

More...PeptideAtlasi		Q9NRD8

PRoteomics IDEntifications database

More...PRIDEi		Q9NRD8

ProteomicsDB human proteome resource

More...ProteomicsDBi		82340

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9NRD8

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

More...PhosphoSitePlusi		Q9NRD8

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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Widely expressed in fetal tissues.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000140279 Expressed in 119 organ(s), highest expression level in nasal cavity epithelium

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9NRD8 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9NRD8 HS

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

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

Heterodimer with DUOXA2; disulfide-linked. Interacts with TXNDC11, TPO and CYBA.2 Publications

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		Q9NRD8, 1 interactor

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000475084

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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q9NRD8

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini819 – 854EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini855 – 890EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini899 – 934EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini1084 – 1266Ferric oxidoreductaseAdd BLAST183
Domaini1267 – 1373FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST107

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni30 – 596Peroxidase-like; mediates peroxidase activityBy similarityAdd BLAST567
Regioni960 – 1245Interaction with TXNDC11By similarityAdd BLAST286

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

In the N-terminal section; belongs to the peroxidase family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0039 Eukaryota
ENOG410XNZY LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160291

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000231774

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG080428

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9NRD8

KEGG Orthology (KO)

More...KOi		K13411

Database of Orthologous Groups

More...OrthoDBi		27424at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9NRD8

TreeFam database of animal gene trees

More...TreeFami		TF105424

Family and domain databases

Conserved Domains Database

More...CDDi		cd09820 dual_peroxidase_like, 1 hit
cd00051 EFh, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.640.10, 1 hit
3.40.50.80, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR034818 DUOX2
IPR034821 DUOX_peroxidase
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR013112 FAD-bd_8
IPR017927 FAD-bd_FR_type
IPR013130 Fe3_Rdtase_TM_dom
IPR013121 Fe_red_NAD-bd_6
IPR039261 FNR_nucleotide-bd
IPR019791 Haem_peroxidase_animal
IPR010255 Haem_peroxidase_sf
IPR037120 Haem_peroxidase_sf_animal
IPR017938 Riboflavin_synthase-like_b-brl

The PANTHER Classification System

More...PANTHERi		PTHR11972:SF67 PTHR11972:SF67, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03098 An_peroxidase, 1 hit
PF00036 EF-hand_1, 1 hit
PF08022 FAD_binding_8, 1 hit
PF01794 Ferric_reduct, 1 hit
PF08030 NAD_binding_6, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00457 ANPEROXIDASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00054 EFh, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47473 SSF47473, 1 hit
SSF48113 SSF48113, 1 hit
SSF52343 SSF52343, 1 hit
SSF63380 SSF63380, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00018 EF_HAND_1, 2 hits
PS50222 EF_HAND_2, 3 hits
PS51384 FAD_FR, 1 hit
PS50292 PEROXIDASE_3, 1 hit

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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q9NRD8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLRARPEALM LLGALLTGSL GPSGNQDALS LPWEVQRYDG WFNNLRHHER 
        60         70         80         90        100
GAVGCRLQRR VPANYADGVY QALEEPQLPN PRRLSNAATR GIAGLPSLHN 
       110        120        130        140        150
RTVLGVFFGY HVLSDVVSVE TPGCPAEFLN IRIPPGDPVF DPDQRGDVVL 
       160        170        180        190        200
PFQRSRWDPE TGRSPSNPRD LANQVTGWLD GSAIYGSSHS WSDALRSFSG 
       210        220        230        240        250
GQLASGPDPA FPRDSQNPLL MWAAPDPATG QNGPRGLYAF GAERGNREPF 
       260        270        280        290        300
LQALGLLWFR YHNLWAQRLA RQHPDWEDEE LFQHARKRVI ATYQNIAVYE 
       310        320        330        340        350
WLPSFLQKTL PEYTGYRPFL DPSISPEFVV ASEQFFSTMV PPGVYMRNAS 
       360        370        380        390        400
CHFRKVLNKG FQSSQALRVC NNYWIRENPN LNSTQEVNEL LLGMASQISE 
       410        420        430        440        450
LEDNIVVEDL RDYWPGPGKF SRTDYVASSI QRGRDMGLPS YSQALLAFGL 
       460        470        480        490        500
DIPRNWSDLN PNVDPQVLEA TAALYNQDLS QLELLLGGLL ESHGDPGPLF 
       510        520        530        540        550
SAIVLDQFVR LRDGDRYWFE NTRNGLFSKK EIEDIRNTTL RDVLVAVINI 
       560        570        580        590        600
DPSALQPNVF VWHKGAPCPQ PKQLTTDGLP QCAPLTVLDF FEGSSPGFAI 
       610        620        630        640        650
TIIALCCLPL VSLLLSGVVA YFRGREHKKL QKKLKESVKK EAAKDGVPAM 
       660        670        680        690        700
EWPGPKERSS PIIIQLLSDR CLQVLNRHLT VLRVVQLQPL QQVNLILSNN 
       710        720        730        740        750
RGCRTLLLKI PKEYDLVLLF SSEEERGAFV QQLWDFCVRW ALGLHVAEMS 
       760        770        780        790        800
EKELFRKAVT KQQRERILEI FFRHLFAQVL DINQADAGTL PLDSSQKVRE 
       810        820        830        840        850
ALTCELSRAE FAESLGLKPQ DMFVESMFSL ADKDGNGYLS FREFLDILVV 
       860        870        880        890        900
FMKGSPEDKS RLMFTMYDLD ENGFLSKDEF FTMMRSFIEI SNNCLSKAQL 
       910        920        930        940        950
AEVVESMFRE SGFQDKEELT WEDFHFMLRD HDSELRFTQL CVKGGGGGGN 
       960        970        980        990       1000
GIRDIFKQNI SCRVSFITRT PGERSHPQGL GPPAPEAPEL GGPGLKKRFG 
      1010       1020       1030       1040       1050
KKAAVPTPRL YTEALQEKMQ RGFLAQKLQQ YKRFVENYRR HIVCVAIFSA 
      1060       1070       1080       1090       1100
ICVGVFADRA YYYGFASPPS DIAQTTLVGI ILSRGTAASV SFMFSYILLT 
      1110       1120       1130       1140       1150
MCRNLITFLR ETFLNRYVPF DAAVDFHRWI AMAAVVLAIL HSAGHAVNVY 
      1160       1170       1180       1190       1200
IFSVSPLSLL ACIFPNVFVN DGSKLPQKFY WWFFQTVPGM TGVLLLLVLA 
      1210       1220       1230       1240       1250
IMYVFASHHF RRRSFRGFWL THHLYILLYA LLIIHGSYAL IQLPTFHIYF 
      1260       1270       1280       1290       1300
LVPAIIYGGD KLVSLSRKKV EISVVKAELL PSGVTYLQFQ RPQGFEYKSG 
      1310       1320       1330       1340       1350
QWVRIACLAL GTTEYHPFTL TSAPHEDTLS LHIRAVGPWT TRLREIYSSP 
      1360       1370       1380       1390       1400
KGNGCAGYPK LYLDGPFGEG HQEWHKFEVS VLVGGGIGVT PFASILKDLV 
      1410       1420       1430       1440       1450
FKSSLGSQML CKKIYFIWVT RTQRQFEWLA DIIQEVEEND HQDLVSVHIY 
      1460       1470       1480       1490       1500
VTQLAEKFDL RTTMLYICER HFQKVLNRSL FTGLRSITHF GRPPFEPFFN 
      1510       1520       1530       1540 
SLQEVHPQVR KIGVFSCGPP GMTKNVEKAC QLVNRQDRAH FMHHYENF
Length:1,548
Mass (Da):175,364
Last modified:May 18, 2010 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7BAA2350EC0A2A7E
GO

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

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
X6RAN8X6RAN8_HUMAN
Dual oxidase 2
DUOX2
1,548Annotation score:

Annotation score:2 out of 5

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti25N → S in AAF73922 (PubMed:10806195).Curated1
Sequence conflicti25N → S in AAF78954 (PubMed:11514595).Curated1
Sequence conflicti984A → V in AAF78954 (PubMed:11514595).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02532336Q → H in TDH6. 1 Publication1
Natural variantiVAR_025324138P → L1 PublicationCorresponds to variant dbSNP:rs2001616EnsemblClinVar.1
Natural variantiVAR_025325376R → W in TDH6. 1 PublicationCorresponds to variant dbSNP:rs119472029EnsemblClinVar.1
Natural variantiVAR_061177678H → R. Corresponds to variant dbSNP:rs57659670EnsemblClinVar.1
Natural variantiVAR_0470751067S → L3 PublicationsCorresponds to variant dbSNP:rs269868EnsemblClinVar.1
Natural variantiVAR_0755491211R → C Found in a patient with very early onset inflammatory bowel disease; unknown pathological significance; no effect on subcellular location; significantly reduced ROS generation, which may decrease resistance to infection by enteric pathogens, such as Escherichia coli. 1 PublicationCorresponds to variant dbSNP:rs374410986Ensembl.1
Natural variantiVAR_0755501492R → C Found in a patient with very early onset inflammatory bowel disease; unknown pathological significance; no effect on subcellular location; significantly reduced ROS generation, which may decrease resistance to infection by enteric pathogens, such as Escherichia coli. 1 PublicationCorresponds to variant dbSNP:rs374410986Ensembl.1
Natural variantiVAR_0646191518G → S in TDH6; the enzyme is non-functional; expressed at the cell surface of cells albeit at low level. 1 PublicationCorresponds to variant dbSNP:rs368512412Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS10117.1
CCDS86454.1

NCBI Reference Sequences

More...RefSeqi		NP_054799.4, NM_014080.4

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.71377

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000603300; ENSP00000475084; ENSG00000140279

Database of genes from NCBI RefSeq genomes

More...GeneIDi		50506

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:50506

UCSC genome browser

More...UCSCi		uc010bea.4 human

Keywords - Coding sequence diversityi

Polymorphism

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

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

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

Undiagnosed Disease Network

DUOX2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
CCDS86454.1
RefSeqiNP_054799.4, NM_014080.4
UniGeneiHs.71377

3D structure databases

ProteinModelPortaliQ9NRD8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9NRD8, 1 interactor
STRINGi9606.ENSP00000475084

Chemistry databases

GuidetoPHARMACOLOGYi2999

Protein family/group databases

PeroxiBasei3338 HsDuOx02
TCDBi5.B.1.1.7 the phagocyte (gp91(phox)) nadph oxidase family

PTM databases

iPTMnetiQ9NRD8
PhosphoSitePlusiQ9NRD8

Polymorphism and mutation databases

BioMutaiDUOX2
DMDMi296434485

Proteomic databases

EPDiQ9NRD8
jPOSTiQ9NRD8
PaxDbiQ9NRD8
PeptideAtlasiQ9NRD8
PRIDEiQ9NRD8
ProteomicsDBi82340

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		50506
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000603300; ENSP00000475084; ENSG00000140279
GeneIDi50506
KEGGihsa:50506
UCSCiuc010bea.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		50506
DisGeNETi50506
EuPathDBiHostDB:ENSG00000140279.12

GeneCards: human genes, protein and diseases

More...GeneCardsi		DUOX2

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0038086
HGNCiHGNC:13273 DUOX2
MalaCardsiDUOX2
MIMi606759 gene
607200 phenotype
neXtProtiNX_Q9NRD8
OpenTargetsiENSG00000140279
Orphaneti95716 Familial thyroid dyshormonogenesis
226316 Genetic transient congenital hypothyroidism
PharmGKBiPA27517

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0039 Eukaryota
ENOG410XNZY LUCA
GeneTreeiENSGT00940000160291
HOGENOMiHOG000231774
HOVERGENiHBG080428
InParanoidiQ9NRD8
KOiK13411
OrthoDBi27424at2759
PhylomeDBiQ9NRD8
TreeFamiTF105424

Enzyme and pathway databases

UniPathwayi
UPA00194

BRENDAi1.6.3.1 2681
ReactomeiR-HSA-209968 Thyroxine biosynthesis
SABIO-RKiQ9NRD8

Miscellaneous databases

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

More...ChiTaRSi		DUOX2 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Dual_oxidase_2

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

More...GenomeRNAii		50506

Protein Ontology

More...PROi		PR:Q9NRD8

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000140279 Expressed in 119 organ(s), highest expression level in nasal cavity epithelium
ExpressionAtlasiQ9NRD8 baseline and differential
GenevisibleiQ9NRD8 HS

Family and domain databases

CDDicd09820 dual_peroxidase_like, 1 hit
cd00051 EFh, 2 hits
Gene3Di1.10.640.10, 1 hit
3.40.50.80, 1 hit
InterProiView protein in InterPro
IPR034818 DUOX2
IPR034821 DUOX_peroxidase
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR013112 FAD-bd_8
IPR017927 FAD-bd_FR_type
IPR013130 Fe3_Rdtase_TM_dom
IPR013121 Fe_red_NAD-bd_6
IPR039261 FNR_nucleotide-bd
IPR019791 Haem_peroxidase_animal
IPR010255 Haem_peroxidase_sf
IPR037120 Haem_peroxidase_sf_animal
IPR017938 Riboflavin_synthase-like_b-brl
PANTHERiPTHR11972:SF67 PTHR11972:SF67, 1 hit
PfamiView protein in Pfam
PF03098 An_peroxidase, 1 hit
PF00036 EF-hand_1, 1 hit
PF08022 FAD_binding_8, 1 hit
PF01794 Ferric_reduct, 1 hit
PF08030 NAD_binding_6, 1 hit
PRINTSiPR00457 ANPEROXIDASE
SMARTiView protein in SMART
SM00054 EFh, 2 hits
SUPFAMiSSF47473 SSF47473, 1 hit
SSF48113 SSF48113, 1 hit
SSF52343 SSF52343, 1 hit
SSF63380 SSF63380, 1 hit
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 2 hits
PS50222 EF_HAND_2, 3 hits
PS51384 FAD_FR, 1 hit
PS50292 PEROXIDASE_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDUOX2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9NRD8
Secondary accession number(s): A8MQ13
, D2XI64, Q9NR02, Q9UHF9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: May 18, 2010
Last modified: April 10, 2019
This is version 158 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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