Application | Comment | Organism |
---|---|---|
medicine | inactivating mutations of Duox2 are linked to congenital hypothyroidism, and epigenetic silencing of Duox is frequently observed in lung cancer | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
medicine | epigenetic silencing of Duox is frequently observed in lung cancer | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | Duox NADPH oxidases generate hydrogen peroxide at the air-liquid interface of the respiratory tract and at apical membranes of thyroid follicular cells | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9NRD8 | - |
- |
Homo sapiens | Q9NRD9 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
lung epithelial cell | Duox1 and Duox2 localize distinctly in lung epithelial cells as well as in ex-vivo differentiated lung epithelia. The localization of functional Duox-DuoxA heterodimers seems to be controlled by the associated DuoxA subunit | Homo sapiens | - |
lung epithelial cell | Duox1 and Duox2 localize distinctly in lung epithelial cells as well as in ex-vivo differentiated lung epithelia. The localization of functional Duox-DuoxA heterodimers seems to be controlled by the associated DuoxA subunit, including Duox2 expression in ciliated cells in an ex vivo differentiated lung epithelium | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Duox NADPH oxidases generate hydrogen peroxide at the air-liquid interface of the respiratory tract and at apical membranes of thyroid follicular cells | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | Duox proteins form functional heterodimers with their respective DuoxA subunits, in close analogy to the phagocyte NADPH oxidase. Characterization of novel DuoxA1 isoforms and mispaired Duox-DuoxA complexes reveals that heterodimerization is a prerequisite for reactive oxygen species production. Functional Duox1 and Duox2 localize to the leading edge of migrating cells, augmenting motility and wound healing. DuoxA subunits are responsible for targeting functional oxidases to distinct cellular compartments in lung epithelial cells | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
Duox-DuoxA NADPH oxidase | - |
Homo sapiens |
Duox1 | - |
Homo sapiens |
Duox2 | - |
Homo sapiens |