DUOX1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0004601 peroxidase activity	IDA NOT PMID:19460756 Caenorhabditis elegans and human dual oxidase 1 (DUOX1) "per...	ACCEPT	Summary: peroxidase activity: This is a NOT annotation: the isolated human N-terminal DUOX1 peroxidase-like domain did not bind heme or exhibit intrinsic peroxidase activity. It does not negate heme binding in the separate transmembrane oxidase domain. Reason: This is a NOT annotation: the isolated human N-terminal DUOX1 peroxidase-like domain did not bind heme or exhibit intrinsic peroxidase activity. It does not negate heme binding in the separate transmembrane oxidase domain. Supporting Evidence: PMID:19460756 the isolated hDUOX1(1-593) does not bind heme and has no intrinsic peroxidase activity.
GO:0005509 calcium ion binding	IDA PMID:33420071 Structures of human dual oxidase 1 complex in low-calcium an...	ACCEPT	Summary: calcium ion binding: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0005509 calcium ion binding	IEA GO_REF:0000002	ACCEPT	Summary: calcium ion binding: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0005515 protein binding	IPI PMID:19339556 Heterodimerization controls localization of Duox-DuoxA NADPH...	UNDECIDED	Summary: protein binding: The PMID:19339556 interaction annotation does not by itself identify a molecular role for DUOX1. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:19339556 interaction annotation does not by itself identify a molecular role for DUOX1. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:19339556 Heterodimerization controls localization of Duox-DuoxA NADPH...	UNDECIDED	Summary: protein binding: The PMID:19339556 interaction annotation does not by itself identify a molecular role for DUOX1. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:19339556 interaction annotation does not by itself identify a molecular role for DUOX1. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:19339556 Heterodimerization controls localization of Duox-DuoxA NADPH...	UNDECIDED	Summary: protein binding: The PMID:19339556 interaction annotation does not by itself identify a molecular role for DUOX1. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:19339556 interaction annotation does not by itself identify a molecular role for DUOX1. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:33420071 Structures of human dual oxidase 1 complex in low-calcium an...	UNDECIDED	Summary: protein binding: The PMID:33420071 interaction annotation does not by itself identify a molecular role for DUOX1. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:33420071 interaction annotation does not by itself identify a molecular role for DUOX1. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005515 protein binding	IPI PMID:39126279 The NADPH oxidases DUOX1 and DUOX2 are sorted to the apical ...	UNDECIDED	Summary: protein binding: The PMID:39126279 interaction annotation does not by itself identify a molecular role for DUOX1. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title. Reason: The PMID:39126279 interaction annotation does not by itself identify a molecular role for DUOX1. The relevant bait/prey or complex evidence must be examined before choosing a more informative binding/regulatory term; no wrong-gene inference is made from a high-throughput study title.
GO:0005783 endoplasmic reticulum	IDA PMID:19339556 Heterodimerization controls localization of Duox-DuoxA NADPH...	KEEP AS NON CORE	Summary: endoplasmic reticulum: Endoplasmic-reticulum residence is part of DUOX1 maturation and trafficking; the mature oxidase acts at the plasma membrane with DUOXA1. Reason: Endoplasmic-reticulum residence is part of DUOX1 maturation and trafficking; the mature oxidase acts at the plasma membrane with DUOXA1. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0005886 plasma membrane	IBA GO_REF:0000033	ACCEPT	Summary: plasma membrane: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0005886 plasma membrane	IDA PMID:19339556 Heterodimerization controls localization of Duox-DuoxA NADPH...	ACCEPT	Summary: plasma membrane: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0005886 plasma membrane	IEA GO_REF:0000107	ACCEPT	Summary: plasma membrane: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0005886 plasma membrane	TAS Reactome:R-HSA-209815	ACCEPT	Summary: plasma membrane: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0005886 plasma membrane	TAS Reactome:R-HSA-209840	ACCEPT	Summary: plasma membrane: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0005886 plasma membrane	TAS Reactome:R-HSA-209925	ACCEPT	Summary: plasma membrane: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0005886 plasma membrane	TAS Reactome:R-HSA-209973	ACCEPT	Summary: plasma membrane: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0005886 plasma membrane	TAS Reactome:R-HSA-350901	ACCEPT	Summary: plasma membrane: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0005886 plasma membrane	TAS Reactome:R-HSA-5693681	ACCEPT	Summary: plasma membrane: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0006590 thyroid hormone generation	IEA GO_REF:0000041	UNDECIDED	Summary: thyroid hormone generation: The available evidence examined for DUOX1 does not resolve the exact claim of thyroid hormone generation. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000041 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DUOX1 does not resolve the exact claim of thyroid hormone generation. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000041 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0006952 defense response	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: defense response: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Reason: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0006979 response to oxidative stress	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: response to oxidative stress: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Reason: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0009615 response to virus	IEA GO_REF:0000117	UNDECIDED	Summary: response to virus: The available evidence examined for DUOX1 does not resolve the exact claim of response to virus. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000117 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DUOX1 does not resolve the exact claim of response to virus. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000117 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0009986 cell surface	IGI PMID:22814254 The type of DUOX-dependent ROS production is dictated by def...	ACCEPT	Summary: cell surface: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0009986 cell surface	IGI PMID:22814254 The type of DUOX-dependent ROS production is dictated by def...	ACCEPT	Summary: cell surface: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0016174 NAD(P)H oxidase H2O2-forming activity	EXP PMID:15972824 Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generati...	ACCEPT	Summary: NAD(P)H oxidase H2O2-forming activity: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0016174 NAD(P)H oxidase H2O2-forming activity	IBA GO_REF:0000033	ACCEPT	Summary: NAD(P)H oxidase H2O2-forming activity: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0016174 NAD(P)H oxidase H2O2-forming activity	IEA GO_REF:0000120	ACCEPT	Summary: NAD(P)H oxidase H2O2-forming activity: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0016174 NAD(P)H oxidase H2O2-forming activity	NAS PMID:10806195 Cloning of two human thyroid cDNAs encoding new members of t...	ACCEPT	Summary: NAD(P)H oxidase H2O2-forming activity: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0016174 NAD(P)H oxidase H2O2-forming activity	TAS Reactome:R-HSA-5693681	ACCEPT	Summary: NAD(P)H oxidase H2O2-forming activity: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0016175 superoxide-generating NAD(P)H oxidase activity	IBA GO_REF:0000033	UNDECIDED	Summary: superoxide-generating NAD(P)H oxidase activity: The available evidence examined for DUOX1 does not resolve the exact claim of superoxide-generating NAD(P)H oxidase activity. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000033 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DUOX1 does not resolve the exact claim of superoxide-generating NAD(P)H oxidase activity. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000033 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0016324 apical plasma membrane	EXP PMID:15210697 NADPH oxidase-dependent acid production in airway epithelial...	ACCEPT	Summary: apical plasma membrane: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0016324 apical plasma membrane	EXP PMID:34784249 Dual NADPH oxidases DUOX1 and DUOX2 synthesize NAADP and are...	ACCEPT	Summary: apical plasma membrane: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0016324 apical plasma membrane	IDA PMID:39126279 The NADPH oxidases DUOX1 and DUOX2 are sorted to the apical ...	ACCEPT	Summary: apical plasma membrane: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0016324 apical plasma membrane	IEA GO_REF:0000120	ACCEPT	Summary: apical plasma membrane: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0016324 apical plasma membrane	NAS PMID:10806195 Cloning of two human thyroid cDNAs encoding new members of t...	ACCEPT	Summary: apical plasma membrane: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0016491 oxidoreductase activity	IEA GO_REF:0000002	MODIFY	Summary: oxidoreductase activity: The specific peroxide-forming NAD(P)H oxidase activity is experimentally established and is more informative than generic oxidoreductase activity. Reason: The specific peroxide-forming NAD(P)H oxidase activity is experimentally established and is more informative than generic oxidoreductase activity. Proposed replacements: NAD(P)H oxidase H2O2-forming activity Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0019221 cytokine-mediated signaling pathway	IDA PMID:16111680 Differential regulation of dual NADPH oxidases/peroxidases, ...	KEEP AS NON CORE	Summary: cytokine-mediated signaling pathway: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Reason: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0020037 heme binding	IDA PMID:33420071 Structures of human dual oxidase 1 complex in low-calcium an...	ACCEPT	Summary: heme binding: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0020037 heme binding	IEA GO_REF:0000120	ACCEPT	Summary: heme binding: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0020037 heme binding	ISS GO_REF:0000024	ACCEPT	Summary: heme binding: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0031252 cell leading edge	IEA GO_REF:0000117	UNDECIDED	Summary: cell leading edge: The available evidence examined for DUOX1 does not resolve the exact claim of cell leading edge. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000117 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DUOX1 does not resolve the exact claim of cell leading edge. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000117 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0031252 cell leading edge	IGI PMID:19339556 Heterodimerization controls localization of Duox-DuoxA NADPH...	UNDECIDED	Summary: cell leading edge: The available evidence examined for DUOX1 does not resolve the exact claim of cell leading edge. The specific experiment or traced orthology/phylogenetic inference behind PMID:19339556 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DUOX1 does not resolve the exact claim of cell leading edge. The specific experiment or traced orthology/phylogenetic inference behind PMID:19339556 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0032757 positive regulation of interleukin-8 production	IMP PMID:19386603 ATP-mediated activation of the NADPH oxidase DUOX1 mediates ...	KEEP AS NON CORE	Summary: positive regulation of interleukin-8 production: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Reason: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0042335 cuticle development	IMP PMID:11514595 Tyrosine cross-linking of extracellular matrix is catalyzed ...	UNDECIDED	Summary: cuticle development: The cuticle-development annotation must be checked against the actual gene and organism tested in the full paper. Nematode DUOX biology cannot simply be transferred to human skin, but an abstract-only or family-level inference is insufficient to overrule the experimental curator. Reason: The cuticle-development annotation must be checked against the actual gene and organism tested in the full paper. Nematode DUOX biology cannot simply be transferred to human skin, but an abstract-only or family-level inference is insufficient to overrule the experimental curator. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0042554 superoxide anion generation	IBA GO_REF:0000033	UNDECIDED	Summary: superoxide anion generation: The available evidence examined for DUOX1 does not resolve the exact claim of superoxide anion generation. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000033 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DUOX1 does not resolve the exact claim of superoxide anion generation. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000033 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0042554 superoxide anion generation	NAS PMID:10806195 Cloning of two human thyroid cDNAs encoding new members of t...	UNDECIDED	Summary: superoxide anion generation: The available evidence examined for DUOX1 does not resolve the exact claim of superoxide anion generation. The specific experiment or traced orthology/phylogenetic inference behind PMID:10806195 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DUOX1 does not resolve the exact claim of superoxide anion generation. The specific experiment or traced orthology/phylogenetic inference behind PMID:10806195 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0043020 NADPH oxidase complex	IBA GO_REF:0000033	ACCEPT	Summary: NADPH oxidase complex: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0043020 NADPH oxidase complex	IEA GO_REF:0000120	ACCEPT	Summary: NADPH oxidase complex: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0043020 NADPH oxidase complex	IPI PMID:33420071 Structures of human dual oxidase 1 complex in low-calcium an...	ACCEPT	Summary: NADPH oxidase complex: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0046982 protein heterodimerization activity	IEA GO_REF:0000107	UNDECIDED	Summary: protein heterodimerization activity: The available evidence examined for DUOX1 does not resolve the exact claim of protein heterodimerization activity. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000107 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DUOX1 does not resolve the exact claim of protein heterodimerization activity. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000107 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0046982 protein heterodimerization activity	ISS GO_REF:0000024	UNDECIDED	Summary: protein heterodimerization activity: The available evidence examined for DUOX1 does not resolve the exact claim of protein heterodimerization activity. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000024 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DUOX1 does not resolve the exact claim of protein heterodimerization activity. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000024 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0050661 NADP binding	NAS PMID:10806195 Cloning of two human thyroid cDNAs encoding new members of t...	ACCEPT	Summary: NADP binding: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0050665 hydrogen peroxide biosynthetic process	IDA PMID:33420071 Structures of human dual oxidase 1 complex in low-calcium an...	ACCEPT	Summary: hydrogen peroxide biosynthetic process: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0050665 hydrogen peroxide biosynthetic process	IEA GO_REF:0000120	ACCEPT	Summary: hydrogen peroxide biosynthetic process: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0050665 hydrogen peroxide biosynthetic process	IGI PMID:19339556 Heterodimerization controls localization of Duox-DuoxA NADPH...	ACCEPT	Summary: hydrogen peroxide biosynthetic process: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0050665 hydrogen peroxide biosynthetic process	IGI PMID:22814254 The type of DUOX-dependent ROS production is dictated by def...	ACCEPT	Summary: hydrogen peroxide biosynthetic process: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0050665 hydrogen peroxide biosynthetic process	NAS PMID:10806195 Cloning of two human thyroid cDNAs encoding new members of t...	ACCEPT	Summary: hydrogen peroxide biosynthetic process: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0050665 hydrogen peroxide biosynthetic process	TAS Reactome:R-HSA-5693681	ACCEPT	Summary: hydrogen peroxide biosynthetic process: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0051591 response to cAMP	IDA PMID:15062544 Structural and functional characterization of the two human ...	UNDECIDED	Summary: response to cAMP: The available evidence examined for DUOX1 does not resolve the exact claim of response to cAMP. The specific experiment or traced orthology/phylogenetic inference behind PMID:15062544 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DUOX1 does not resolve the exact claim of response to cAMP. The specific experiment or traced orthology/phylogenetic inference behind PMID:15062544 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0051591 response to cAMP	IEA GO_REF:0000117	UNDECIDED	Summary: response to cAMP: The available evidence examined for DUOX1 does not resolve the exact claim of response to cAMP. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000117 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DUOX1 does not resolve the exact claim of response to cAMP. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000117 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0051591 response to cAMP	ISS GO_REF:0000024	UNDECIDED	Summary: response to cAMP: The available evidence examined for DUOX1 does not resolve the exact claim of response to cAMP. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000024 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DUOX1 does not resolve the exact claim of response to cAMP. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000024 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0070402 NADPH binding	IDA PMID:33420071 Structures of human dual oxidase 1 complex in low-calcium an...	ACCEPT	Summary: NADPH binding: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0070402 NADPH binding	IEA GO_REF:0000107	ACCEPT	Summary: NADPH binding: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0070402 NADPH binding	ISS GO_REF:0000024	ACCEPT	Summary: NADPH binding: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0071345 cellular response to cytokine stimulus	IEA GO_REF:0000117	UNDECIDED	Summary: cellular response to cytokine stimulus: The available evidence examined for DUOX1 does not resolve the exact claim of cellular response to cytokine stimulus. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000117 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DUOX1 does not resolve the exact claim of cellular response to cytokine stimulus. The specific experiment or traced orthology/phylogenetic inference behind GO_REF:0000117 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.
GO:0071949 FAD binding	IDA PMID:33420071 Structures of human dual oxidase 1 complex in low-calcium an...	ACCEPT	Summary: FAD binding: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0071949 FAD binding	IEA GO_REF:0000107	ACCEPT	Summary: FAD binding: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0071949 FAD binding	ISS GO_REF:0000024	ACCEPT	Summary: FAD binding: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Reason: Human DUOX1–DUOXA1 structures and functional experiments establish a membrane oxidase complex using heme, FAD and NADPH to generate extracellular H2O2, regulated by calcium-binding EF-hand elements. These are direct components of the oxidase mechanism. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0090303 positive regulation of wound healing	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: positive regulation of wound healing: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Reason: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0090303 positive regulation of wound healing	IGI PMID:19339556 Heterodimerization controls localization of Duox-DuoxA NADPH...	KEEP AS NON CORE	Summary: positive regulation of wound healing: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Reason: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0140374 antiviral innate immune response	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: antiviral innate immune response: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Reason: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:0140374 antiviral innate immune response	IMP PMID:34168077 Dual oxidase 1 promotes antiviral innate immunity.	KEEP AS NON CORE	Summary: antiviral innate immune response: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Reason: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:1900426 positive regulation of defense response to bacterium	IDA PMID:19386603 ATP-mediated activation of the NADPH oxidase DUOX1 mediates ...	KEEP AS NON CORE	Summary: positive regulation of defense response to bacterium: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Reason: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:2000147 positive regulation of cell motility	IGI PMID:19339556 Heterodimerization controls localization of Duox-DuoxA NADPH...	KEEP AS NON CORE	Summary: positive regulation of cell motility: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Reason: DUOX1-generated extracellular H2O2 participates in epithelial defense and redox signaling. The annotated response or tissue-level effect is a context-dependent consequence of this oxidase function, rather than an additional intrinsic molecular activity. Supporting Evidence: PMID:33420071 Dual oxidases (DUOXs) produce hydrogen peroxide by transferring electrons from intracellular NADPH to extracellular oxygen. They are involved in many crucial biological processes and human diseases, especially in thyroid diseases. DUOXs are protein complexes co-assembled from the catalytic DUOX subunits and the auxiliary DUOXA subunits and their activities are regulated by intracellular calcium concentrations.
GO:2000609 regulation of thyroid hormone generation	NAS PMID:25761904 When an Intramolecular Disulfide Bridge Governs the Interact...	UNDECIDED	Summary: regulation of thyroid hormone generation: The available evidence examined for DUOX1 does not resolve the exact claim of regulation of thyroid hormone generation. The specific experiment or traced orthology/phylogenetic inference behind PMID:25761904 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper. Reason: The available evidence examined for DUOX1 does not resolve the exact claim of regulation of thyroid hormone generation. The specific experiment or traced orthology/phylogenetic inference behind PMID:25761904 is needed; the annotation is not rejected from absence in a summary or from a different main focus of the paper.

Gene Description

Existing Annotations Review

Core Functions

DUOX1 is a membrane NADPH oxidase that assembles with DUOXA1 and generates extracellular hydrogen peroxide.

References

Deep Research

Manual

📚 Additional Documentation

Notes

📄 View Raw YAML