EC Number   |
Posttranslational Modification |
Reference |
|---|
   1.6.3.1 | glycoprotein |
- |
636500, 688991, 742557 |
| 1.6.3.1 | glycoprotein |
3 loops of Nox2 are extracellular and include consensus asparagine glycosylation sites. Phosphorylation of p67phox, mediated by PKCdelta, ERK2 and p38 MAPK, increases superoxide production by Nox2 |
724778 |
| 1.6.3.1 | glycoprotein |
5 N-glycosylation sites |
636490 |
| 1.6.3.1 | glycoprotein |
cytochrome b558 subunit gp91-phox of the multicomponent complex is heavily glycosylated |
394275 |
| 1.6.3.1 | glycoprotein |
isoform Duox2, partial glycosylation. Post-translational modifications during the maturation process may be implicated in the mechanism of H2O2 formation by favoring intramolecular superoxide dismutation |
674466 |
| 1.6.3.1 | more |
coexpression of enzyme and enzyme maturation factor DuoxA2 allows ER-to-Golgi transition, maturation, and translocation to the plasma membrane of functional isoform Duox2 in a heterologous system |
674589 |
| 1.6.3.1 | more |
oxidative folding of wild-type protein in the endoplasmic reticulum is the rate-limiting step in the maturation, which is not faciltated by the speific maturation factor DUOXA2. DUOXA2 may allow for rapid exit of folded protein from the endoplasmatic reticulum or enahnced degradation of mutant protein |
688991 |
| 1.6.3.1 | phosphoprotein |
- |
710782, 741954 |
| 1.6.3.1 | phosphoprotein |
adenosine A2A receptor regulates subunit p47phox phosphorylation and cardiac reactive oxygen species production by NADPH oxidase through MAPK signaling |
686878 |
| 1.6.3.1 | phosphoprotein |
Conditional expression of p21-activated kinase-1 PAK1 dominant-positive mutants enhances NADPH oxidase-mediated superoxide generation stimulated by formyl-methionyl-leucylphenylalanine. Stimulation by p21-activated kinase-1 PAK1 is mediated through phosphorylation of subunit p47phox |
687798 |
