| + |
CAMK2A | up-regulates activity 
phosphorylation
|
NOX5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276329 |
Ser521 |
WTNRLYEsFKASDPL |
in vitro |
|
| pmid |
sentence |
| 21642394 |
In vitro phosphorylation assays revealed that CAMKII can directly phosphorylate Nox5 on Thr494 and Ser498 as detected by phosphorylation state-specific antibodies. Mass spectrometry (MS) analysis revealed the phosphorylation of additional, novel sites at Ser475, Ser502, and Ser675. Of these phosphorylation sites, mutation of only Ser475 to alanine prevented CAMKII-induced increases in Nox5 activity. Together, these results suggest that CAMKII can positively regulate Nox5 activity via the phosphorylation of Ser475. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCA | up-regulates
phosphorylation
|
NOX5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-204546 |
Ser536 |
GRGSKRLsRSVTMRK |
Homo sapiens |
|
| pmid |
sentence |
| 24505490 |
A constitutively active form of pkc? Robustly increased basal and pma-stimulated nox5 activity and promoted the phosphorylation of nox5 on ser490, thr494, and ser498. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-204550 |
Ser544 |
RSVTMRKsQRSSKGS |
Homo sapiens |
|
| pmid |
sentence |
| 24505490 |
A constitutively active form of pkc? Robustly increased basal and pma-stimulated nox5 activity and promoted the phosphorylation of nox5 on ser490, thr494, and ser498. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-204554 |
Thr540 |
KRLSRSVtMRKSQRS |
Homo sapiens |
|
| pmid |
sentence |
| 24505490 |
A constitutively active form of pkc? Robustly increased basal and pma-stimulated nox5 activity and promoted the phosphorylation of nox5 on ser490, thr494, and ser498. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CAMK2A |
phosphorylation
|
NOX5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276331 |
Ser544 |
RSVTMRKsQRSSKGS |
in vitro |
|
| pmid |
sentence |
| 21642394 |
In vitro phosphorylation assays revealed that CAMKII can directly phosphorylate Nox5 on Thr494 and Ser498 as detected by phosphorylation state-specific antibodies. Mass spectrometry (MS) analysis revealed the phosphorylation of additional, novel sites at Ser475, Ser502, and Ser675. Of these phosphorylation sites, mutation of only Ser475 to alanine prevented CAMKII-induced increases in Nox5 activity. Together, these results suggest that CAMKII can positively regulate Nox5 activity via the phosphorylation of Ser475. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276332 |
Ser547 |
TMRKSQRsSKGSEIL |
in vitro |
|
| pmid |
sentence |
| 21642394 |
In vitro phosphorylation assays revealed that CAMKII can directly phosphorylate Nox5 on Thr494 and Ser498 as detected by phosphorylation state-specific antibodies. Mass spectrometry (MS) analysis revealed the phosphorylation of additional, novel sites at Ser475, Ser502, and Ser675. Of these phosphorylation sites, mutation of only Ser475 to alanine prevented CAMKII-induced increases in Nox5 activity. Together, these results suggest that CAMKII can positively regulate Nox5 activity via the phosphorylation of Ser475. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276333 |
Ser548 |
MRKSQRSsKGSEILL |
in vitro |
|
| pmid |
sentence |
| 21642394 |
In vitro phosphorylation assays revealed that CAMKII can directly phosphorylate Nox5 on Thr494 and Ser498 as detected by phosphorylation state-specific antibodies. Mass spectrometry (MS) analysis revealed the phosphorylation of additional, novel sites at Ser475, Ser502, and Ser675. Of these phosphorylation sites, mutation of only Ser475 to alanine prevented CAMKII-induced increases in Nox5 activity. Together, these results suggest that CAMKII can positively regulate Nox5 activity via the phosphorylation of Ser475. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276330 |
Thr540 |
KRLSRSVtMRKSQRS |
in vitro |
|
| pmid |
sentence |
| 21642394 |
In vitro phosphorylation assays revealed that CAMKII can directly phosphorylate Nox5 on Thr494 and Ser498 as detected by phosphorylation state-specific antibodies. Mass spectrometry (MS) analysis revealed the phosphorylation of additional, novel sites at Ser475, Ser502, and Ser675. Of these phosphorylation sites, mutation of only Ser475 to alanine prevented CAMKII-induced increases in Nox5 activity. Together, these results suggest that CAMKII can positively regulate Nox5 activity via the phosphorylation of Ser475. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
MAPK1 | up-regulates
phosphorylation
|
NOX5 |
0.332 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171847 |
Ser544 |
RSVTMRKsQRSSKGS |
Homo sapiens |
|
| pmid |
sentence |
| 21297032 |
These results suggest that the mek/erk1/2 pathway is necessary but not sufficient to regulate the pma-dependent activation of nox5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOX5 | up-regulates
|
ROS |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264718 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17237347 |
Over the last years, six homologs of the cytochrome subunit of the phagocyte NADPH oxidase were found: NOX1, NOX3, NOX4, NOX5, DUOX1, and DUOX2. Together with the phagocyte NADPH oxidase itself (NOX2/gp91phox), the homologs are now referred to as the NOX family of NADPH oxidases. These enzymes share the capacity to transport electrons across the plasma membrane and to generate superoxide and other downstream reactive oxygen species (ROS). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOX5 | up-regulates quantity
chemical modification
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264725 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17237347 |
Over the last years, six homologs of the cytochrome subunit of the phagocyte NADPH oxidase were found: NOX1, NOX3, NOX4, NOX5, DUOX1, and DUOX2. Together with the phagocyte NADPH oxidase itself (NOX2/gp91phox), the homologs are now referred to as the NOX family of NADPH oxidases. These enzymes share the capacity to transport electrons across the plasma membrane and to generate superoxide and other downstream reactive oxygen species (ROS). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
NOX5
- 
- 