+ |
PRKCD | up-regulates
phosphorylation
|
CYBA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260892 |
Thr147 |
ERPQIGGtIKQPPSN |
in vitro |
|
pmid |
sentence |
19948736 |
Phosphorylation of p22phox on threonine 147 enhances NADPH oxidase activity by promoting p47phox binding. | Threonine 147 of p22phox Is Phosphorylated by PKC-α and PKC-δ in Vitro |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PRKCA | up-regulates
phosphorylation
|
CYBA |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260891 |
Thr147 |
ERPQIGGtIKQPPSN |
in vitro |
|
pmid |
sentence |
19948736 |
Phosphorylation of p22phox on threonine 147 enhances NADPH oxidase activity by promoting p47phox binding. | Threonine 147 of p22phox Is Phosphorylated by PKC-α and PKC-δ in Vitro |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CYBA | form complex
binding
|
Phagocyte NADPH oxidase complex |
0.74 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277634 |
|
|
Homo sapiens |
|
pmid |
sentence |
37263099 |
NADPH oxidase is composed of essential protein components in its active state: membranous subunits, including p22-phox and gp91-phox, and cytoplasmic subunits, including p47-phox, p67-phox, p40-phox, and RAC2 (in neutrophils), among which NCF4 encodes the cytoplasmic subunit p40-phox |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NCF1 | up-regulates activity
binding
|
CYBA |
0.783 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276625 |
|
|
Homo sapiens |
|
pmid |
sentence |
12672956 |
Stimulus-induced phosphorylation of p47phox causes a conformational change, by which both PX and SH3 domains become accessible to their membranous targets, phosphoinositides and p22phox, respectively. Cooperation of these two interactions, each being indispensable, enables p47phox to form a stable complex with cytochrome b558 (composed of the two subunit gp91phox and p22phox), leading to activation of the phagocyte NADPH oxidase. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |