HUMAN:DUOX2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	DUOX2 (synonyms: LNOX2, THOX2)
Protein Name(s)	Dual oxidase 2 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
External Links
UniProt	Q9NRD8
EMBL	AF230496 AF267981 AC091117 AF181972 GU174495
CCDS	CCDS10117.1
RefSeq	NP_054799.4
UniGene	Hs.71377
ProteinModelPortal	Q9NRD8
SMR	Q9NRD8
STRING	9606.ENSP00000267837
BindingDB	Q9NRD8
PeroxiBase	3338
TCDB	5.B.1.2.2
PhosphoSite	Q9NRD8
DMDM	296434485
PaxDb	Q9NRD8
PRIDE	Q9NRD8
DNASU	50506
Ensembl	ENST00000603300
GeneID	50506
KEGG	hsa:50506
UCSC	uc001zun.3
CTD	50506
GeneCards	GC15M045384
H-InvDB	HIX0038086
HGNC	HGNC:13273
MIM	606759 607200
neXtProt	NX_Q9NRD8
Orphanet	95716 226316
PharmGKB	PA27517
eggNOG	NOG287712
GeneTree	ENSGT00550000074350
HOGENOM	HOG000231774
HOVERGEN	HBG080428
InParanoid	Q9NRD8
KO	K13411
OrthoDB	EOG7GN2KV
PhylomeDB	Q9NRD8
TreeFam	TF105424
BRENDA	1.6.3.1
SABIO-RK	Q9NRD8
UniPathway	UPA00194
ChiTaRS	DUOX2
GeneWiki	Dual_oxidase_2
GenomeRNAi	50506
NextBio	35489705
PRO	PR:Q9NRD8
Proteomes	UP000005640
Bgee	Q9NRD8
CleanEx	HS_DUOX2
ExpressionAtlas	Q9NRD8
Genevestigator	Q9NRD8
GO	GO:0016324 GO:0070062 GO:0016021 GO:0005509 GO:0020037 GO:0016174 GO:0004601 GO:0048855 GO:0030282 GO:0042335 GO:0019221 GO:0009566 GO:0042446 GO:0042744 GO:0048839 GO:0035264 GO:0055114 GO:0051591 GO:0009615 GO:0030878 GO:0006590
Gene3D	1.10.238.10 1.10.640.10
InterPro	IPR029592 IPR011992 IPR018247 IPR002048 IPR013112 IPR017927 IPR013130 IPR013121 IPR010255 IPR019791 IPR017938
PANTHER	PTHR11972:SF53
Pfam	PF03098 PF13499 PF08022 PF01794 PF08030
PRINTS	PR00457
SMART	SM00054
SUPFAM	SSF48113 SSF63380
PROSITE	PS00018 PS50222 PS51384 PS50292

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0016174	NAD(P)H oxidase activity	PMID:21565790^[1]	ECO:0000315			F		Figure 1 shows that HeLa cells transfected with different expression vectors have different amounts of hydrogen peroxide generation based on. The mutant proteins produced significantly less hydrogen peroxide compared to wildtype protein.	complete CACAO 9753
involved_in	GO:0050665	hydrogen peroxide biosynthetic process	PMID:16651268^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q1HG44	P		Seeded From UniProt	complete
involved_in	GO:0050665	hydrogen peroxide biosynthetic process	PMID:22814254^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q1HG44	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:16651268^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q1HG44	C		Seeded From UniProt	complete
part_of	GO:0031252	cell leading edge	PMID:19339556^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q1HG44	C		Seeded From UniProt	complete
involved_in	GO:2000147	positive regulation of cell motility	PMID:19339556^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q1HG44	P		Seeded From UniProt	complete
involved_in	GO:0050665	hydrogen peroxide biosynthetic process	PMID:25761904^[5]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q1HG44	P		Seeded From UniProt	complete
involved_in	GO:0042554	superoxide anion generation	PMID:22814254^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q1HG43	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:19339556^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:19339556^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:19339556^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0050665	hydrogen peroxide biosynthetic process	PMID:19339556^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q1HG44	P		Seeded From UniProt	complete
part_of	GO:0045177	apical part of cell	PMID:25761904^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002257)	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:25761904^[5]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q1HG44	C		Seeded From UniProt	complete
involved_in	GO:0090303	positive regulation of wound healing	PMID:19339556^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q1HG44	P		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:22814254^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q1HG44	C		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:22814254^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q1HG43	C		Seeded From UniProt	complete
enables	GO:0016174	NAD(P)H oxidase activity	PMID:21565790^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[6]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
involved_in	GO:0051591	response to cAMP	PMID:15062544^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051591	response to cAMP	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9NRD9	P		Seeded From UniProt	complete
involved_in	GO:0042335	cuticle development	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9NRD9	P		Seeded From UniProt	complete
involved_in	GO:0019221	cytokine-mediated signaling pathway	PMID:16111680^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019221	cytokine-mediated signaling pathway	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9NRD9	P		Seeded From UniProt	complete
enables	GO:0016174	NAD(P)H oxidase activity	PMID:15972824^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0009615	response to virus	PMID:16111680^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:15972824^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0283531 MGI:MGI:1354184 MGI:MGI:2450016 MGI:MGI:2681162 PANTHER:PTN001735877 PomBase:SPBC1683.09c RGD:620600 SGD:S000003128 SGD:S000004037 SGD:S000005512 TAIR:locus:2017789 TAIR:locus:2024603 TAIR:locus:2025351 TAIR:locus:2025366 TAIR:locus:2157032 TAIR:locus:2157348 TAIR:locus:2157697 TAIR:locus:2160917 TAIR:locus:2178677 TAIR:locus:2178687 UniProtKB:P04839 UniProtKB:Q96PH1 UniProtKB:Q9NPH5 UniProtKB:Q9NRD8 UniProtKB:Q9SBI0 UniProtKB:Q9Y5S8 WB:WBGene00000253 dictyBase:DDB_G0287101 dictyBase:DDB_G0289653	P		Seeded From UniProt	complete
part_of	GO:0043020	NADPH oxidase complex	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:2681162 MGI:MGI:88574 PANTHER:PTN000239643 RGD:620574 RGD:620598 RGD:620600 UniProtKB:P04839 UniProtKB:Q9Y5S8	C		Seeded From UniProt	complete
involved_in	GO:0042554	superoxide anion generation	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1354184 MGI:MGI:2450016 MGI:MGI:2681162 PANTHER:PTN000239643 RGD:620598 UniProtKB:P04839 UniProtKB:Q96PH1 UniProtKB:Q9Y5S8 dictyBase:DDB_G0287101	P		Seeded From UniProt	complete
enables	GO:0016175	superoxide-generating NADPH oxidase activity	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1354184 MGI:MGI:2450016 MGI:MGI:2681162 PANTHER:PTN000239643 UniProtKB:Q96PH1 UniProtKB:Q9Y5S8 dictyBase:DDB_G0287101 dictyBase:DDB_G0289653	F		Seeded From UniProt	complete
involved_in	GO:0006952	defense response	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0283531 MGI:MGI:88574 PANTHER:PTN000239643 UniProtKB:P04839 ZFIN:ZDB-GENE-091117-14 dictyBase:DDB_G0287101 dictyBase:DDB_G0289653 dictyBase:DDB_G0291117	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:2139422 MGI:MGI:2681162 MGI:MGI:88574 PANTHER:PTN001735877 RGD:620574 RGD:620598 RGD:620600 SGD:S000005512 TAIR:locus:2024603 TAIR:locus:2025351 TAIR:locus:2157027 TAIR:locus:2157348 TAIR:locus:2157697 TAIR:locus:2160917 UniProtKB:O81209 UniProtKB:P04839 UniProtKB:Q9Y5S8 WB:WBGene00000253	C		Seeded From UniProt	complete
involved_in	GO:0098869	cellular oxidant detoxification	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004601	P		Seeded From UniProt	complete
involved_in	GO:0098869	cellular oxidant detoxification	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004601	P		Seeded From UniProt	complete
enables	GO:0004601	peroxidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010255	F		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002048	F		Seeded From UniProt	complete
involved_in	GO:0006979	response to oxidative stress	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010255	P		Seeded From UniProt	complete
enables	GO:0016174	NAD(P)H oxidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR034818	F		Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013112 InterPro:IPR013121 InterPro:IPR017927	F		Seeded From UniProt	complete
enables	GO:0020037	heme binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010255	F		Seeded From UniProt	complete
involved_in	GO:0050665	hydrogen peroxide biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR034818	P		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010255 InterPro:IPR013112 InterPro:IPR013121 InterPro:IPR017927	P		Seeded From UniProt	complete
enables	GO:0016174	NAD(P)H oxidase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.6.3.1	F		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	PMID:10601291^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006590	thyroid hormone generation	Reactome:R-HSA-209968	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-HSA-5693681	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0042744	hydrogen peroxide catabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0376	P		Seeded From UniProt	complete
involved_in	GO:0042446	hormone biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0893	P		Seeded From UniProt	complete
part_of	GO:0030054	cell junction	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0965 UniProtKB-SubCell:SL-0038	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P		Seeded From UniProt	complete
enables	GO:0004601	peroxidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0575	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F		Seeded From UniProt	complete
part_of	GO:0016324	apical plasma membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0015	C		Seeded From UniProt	complete
involved_in	GO:0006590	thyroid hormone generation	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00194	P		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 De Marco, G et al. (2011) Identification and functional analysis of novel dual oxidase 2 (DUOX2) mutations in children with congenital or subclinical hypothyroidism. J. Clin. Endocrinol. Metab. 96 E1335-9 PubMed GONUTS page
↑ ^2.0 ^2.1 Grasberger, H & Refetoff, S (2006) Identification of the maturation factor for dual oxidase. Evolution of an eukaryotic operon equivalent. J. Biol. Chem. 281 18269-72 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Hoste, C et al. (2012) The type of DUOX-dependent ROS production is dictated by defined sequences in DUOXA. Exp. Cell Res. 318 2353-64 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 Luxen, S et al. (2009) Heterodimerization controls localization of Duox-DuoxA NADPH oxidases in airway cells. J. Cell. Sci. 122 1238-47 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Carré, A et al. (2015) When an Intramolecular Disulfide Bridge Governs the Interaction of DUOX2 with Its Partner DUOXA2. Antioxid. Redox Signal. 23 724-33 PubMed GONUTS page
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ Pachucki, J et al. (2004) Structural and functional characterization of the two human ThOX/Duox genes and their 5'-flanking regions. Mol. Cell. Endocrinol. 214 53-62 PubMed GONUTS page
↑ ^8.0 ^8.1 Harper, RW et al. (2005) Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium. FEBS Lett. 579 4911-7 PubMed GONUTS page
↑ ^9.0 ^9.1 Ameziane-El-Hassani, R et al. (2005) Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity. J. Biol. Chem. 280 30046-54 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Dupuy, C et al. (1999) Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cdnas. J. Biol. Chem. 274 37265-9 PubMed GONUTS page

[PMID:21565790-1] 1.0 ^1.1 De Marco, G et al. (2011) Identification and functional analysis of novel dual oxidase 2 (DUOX2) mutations in children with congenital or subclinical hypothyroidism. J. Clin. Endocrinol. Metab. 96 E1335-9 PubMed GONUTS page

[PMID:16651268-2] 2.0 ^2.1 Grasberger, H & Refetoff, S (2006) Identification of the maturation factor for dual oxidase. Evolution of an eukaryotic operon equivalent. J. Biol. Chem. 281 18269-72 PubMed GONUTS page

[PMID:22814254-3] 3.0 ^3.1 ^3.2 ^3.3 Hoste, C et al. (2012) The type of DUOX-dependent ROS production is dictated by defined sequences in DUOXA. Exp. Cell Res. 318 2353-64 PubMed GONUTS page

[PMID:19339556-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 Luxen, S et al. (2009) Heterodimerization controls localization of Duox-DuoxA NADPH oxidases in airway cells. J. Cell. Sci. 122 1238-47 PubMed GONUTS page

[PMID:25761904-5] 5.0 ^5.1 ^5.2 Carré, A et al. (2015) When an Intramolecular Disulfide Bridge Governs the Interaction of DUOX2 with Its Partner DUOXA2. Antioxid. Redox Signal. 23 724-33 PubMed GONUTS page

[PMID:19199708-6] Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page

[PMID:15062544-7] Pachucki, J et al. (2004) Structural and functional characterization of the two human ThOX/Duox genes and their 5'-flanking regions. Mol. Cell. Endocrinol. 214 53-62 PubMed GONUTS page

[PMID:16111680-8] 8.0 ^8.1 Harper, RW et al. (2005) Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium. FEBS Lett. 579 4911-7 PubMed GONUTS page

[PMID:15972824-9] 9.0 ^9.1 Ameziane-El-Hassani, R et al. (2005) Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity. J. Biol. Chem. 280 30046-54 PubMed GONUTS page

[PMID:21873635-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:10601291-11] Dupuy, C et al. (1999) Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cdnas. J. Biol. Chem. 274 37265-9 PubMed GONUTS page

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HUMAN:DUOX2

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