| + |
CDK5 | down-regulates 
phosphorylation
|
NOS3 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164080 |
Ser114 |
RKLQGRPsPGPPAPE |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 20213743 |
Together, our data suggest that cdk5 can phosphorylate enos at the ser-113 site and down-regulate enos-derived no levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT | up-regulates 
phosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244322 |
Ser1177 |
TSRIRTQsFSLQERQ |
Homo sapiens |
|
| pmid |
sentence |
| 11729179 |
Recently many investigators have shown that protein phosphorylation of enos by several serine/threonine kinases is a critical control step for no production by endothelial cells. Phosphorylation by amp kinase, akt (or protein kinase b), or protein kinase a on serine 1179 (bovine) or serine 1177 (human) of enos leads to enhanced activity of the enzyme and, thus, augmented production of no. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | VEGF Signaling |
| + |
AMPK | up-regulates
phosphorylation
|
NOS3 |
0.264 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216445 |
Ser1177 |
TSRIRTQsFSLQERQ |
Homo sapiens |
|
| pmid |
sentence |
| 11729179 |
Recently many investigators have shown that protein phosphorylation of enos by several serine/threonine kinases is a critical control step for no production by endothelial cells. Phosphorylation by amp kinase, akt (or protein kinase b), or protein kinase a on serine 1179 (bovine) or serine 1177 (human) of enos leads to enhanced activity of the enzyme and, thus, augmented production of no. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216627 |
Ser1177 |
TSRIRTQsFSLQERQ |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18303014 |
The central finding of this report is that rosiglitazone rapidly stimulates no production and enos ser-1177 phosphorylation in an ampk-dependent manner |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKAA1 | up-regulates
phosphorylation
|
NOS3 |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160838 |
Ser1177 |
TSRIRTQsFSLQERQ |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18303014 |
The central finding of this report is that rosiglitazone rapidly stimulates no production and enos ser-1177 phosphorylation in an ampk-dependent manner |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACG | up-regulates
phosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112375 |
Ser1177 |
TSRIRTQsFSLQERQ |
Homo sapiens |
|
| pmid |
sentence |
| 11729179 |
Recently many investigators have shown that protein phosphorylation of enos by several serine/threonine kinases is a critical control step for no production by endothelial cells. Phosphorylation by amp kinase, akt (or protein kinase b), or protein kinase a on serine 1179 (bovine) or serine 1177 (human) of enos leads to enhanced activity of the enzyme and, thus, augmented production of no. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAB1 | up-regulates
phosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112367 |
Ser1177 |
TSRIRTQsFSLQERQ |
Homo sapiens |
|
| pmid |
sentence |
| 11729179 |
Recently many investigators have shown that protein phosphorylation of enos by several serine/threonine kinases is a critical control step for no production by endothelial cells. Phosphorylation by amp kinase, akt (or protein kinase b), or protein kinase a on serine 1179 (bovine) or serine 1177 (human) of enos leads to enhanced activity of the enzyme and, thus, augmented production of no. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT1 | up-regulates
phosphorylation
|
NOS3 |
0.878 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112363 |
Ser1177 |
TSRIRTQsFSLQERQ |
Homo sapiens |
|
| pmid |
sentence |
| 11729179 |
Recently many investigators have shown that protein phosphorylation of enos by several serine/threonine kinases is a critical control step for no production by endothelial cells. Phosphorylation by amp kinase, akt (or protein kinase b), or protein kinase a on serine 1179 (bovine) or serine 1177 (human) of enos leads to enhanced activity of the enzyme and, thus, augmented production of no. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates
phosphorylation
|
NOS3 |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112371 |
Ser1177 |
TSRIRTQsFSLQERQ |
Homo sapiens |
|
| pmid |
sentence |
| 11729179 |
Recently many investigators have shown that protein phosphorylation of enos by several serine/threonine kinases is a critical control step for no production by endothelial cells. Phosphorylation by amp kinase, akt (or protein kinase b), or protein kinase aon serine 1179 (bovine) or serine 1177 (human) of enos leads to enhanced activity of the enzyme and, thus, augmented production of no. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT1 | up-regulates activity
phosphorylation
|
NOS3 |
0.878 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251622 |
Ser615 |
SYKIRFNsISCSDPL |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates activity
phosphorylation
|
NOS3 |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251617 |
Ser615 |
SYKIRFNsISCSDPL |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251616 |
Ser633 |
WRRKRKEsSNTDSAG |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AKT | up-regulates activity
phosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251628 |
Ser615 |
SYKIRFNsISCSDPL |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | VEGF Signaling |
| + |
AKT3 | up-regulates activity
phosphorylation
|
NOS3 |
0.481 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251626 |
Ser615 |
SYKIRFNsISCSDPL |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates activity
phosphorylation
|
NOS3 |
0.501 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251624 |
Ser615 |
SYKIRFNsISCSDPL |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1CA | up-regulates activity
dephosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248558 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
Endothelial Cell |
| pmid |
sentence |
| 19036824 |
The increase in eNOS activity coincided with specific dephosphorylation of eNOS-Thr495, known to enhance eNOS activity. Inhibition of protein phosphatase 1 (PP1) by calyculin A, tautomycetin, or siRNA against PP1 reversed NF-induced eNOS-Thr495 dephosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCA | down-regulates activity
phosphorylation
|
NOS3 |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251620 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | VEGF Signaling |
| + |
PRKCE | down-regulates activity
phosphorylation
|
NOS3 |
0.333 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251632 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
|
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP1 | up-regulates activity
dephosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264668 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
Endothelial Cell |
| pmid |
sentence |
| 19036824 |
The increase in eNOS activity coincided with specific dephosphorylation of eNOS-Thr495, known to enhance eNOS activity. Inhibition of protein phosphatase 1 (PP1) by calyculin A, tautomycetin, or siRNA against PP1 reversed NF-induced eNOS-Thr495 dephosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMPK | down-regulates activity
phosphorylation
|
NOS3 |
0.264 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251618 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCI | down-regulates activity
phosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251635 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
|
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCH | down-regulates activity
phosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251634 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCG | down-regulates activity
phosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251633 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
|
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1CC | up-regulates activity
dephosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248501 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
Endothelial Cell |
| pmid |
sentence |
| 19036824 |
The increase in eNOS activity coincided with specific dephosphorylation of eNOS-Thr495, known to enhance eNOS activity. Inhibition of protein phosphatase 1 (PP1) by calyculin A, tautomycetin, or siRNA against PP1 reversed NF-induced eNOS-Thr495 dephosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | down-regulates activity
phosphorylation
|
NOS3 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251637 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
|
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1CB | up-regulates activity
dephosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248574 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
Endothelial Cell |
| pmid |
sentence |
| 19036824 |
The increase in eNOS activity coincided with specific dephosphorylation of eNOS-Thr495, known to enhance eNOS activity. Inhibition of protein phosphatase 1 (PP1) by calyculin A, tautomycetin, or siRNA against PP1 reversed NF-induced eNOS-Thr495 dephosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCB | down-regulates activity
phosphorylation
|
NOS3 |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251630 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCD | down-regulates activity
phosphorylation
|
NOS3 |
0.566 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251631 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | down-regulates activity
phosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251636 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA1 | up-regulates activity
phosphorylation
|
NOS3 |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251619 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
|
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK2B | down-regulates
phosphorylation
|
NOS3 |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161824 |
Tyr657 |
FGLGSRAyPHFCAFA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19934023 |
We found that fluid shear stress induces the association of enos with the proline-rich tyrosine kinase 2 (pyk2) in endothelial cells and that the enos immunoprecipitated from enos- and pyk2-overexpressing hek293 cells was tyrosine-phosphorylated on tyr657. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178648 |
Tyr657 |
FGLGSRAyPHFCAFA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18483407 |
We found that fluid shear stress induces the association of enos with the proline-rich tyrosine kinase 2 (pyk2) in endothelial cells and that the enos immunoprecipitated from enos- and pyk2-overexpressing hek293 cells was tyrosine-phosphorylated on tyr657. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates activity
phosphorylation
|
NOS3 |
0.423 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277520 |
Tyr81 |
WEVGSITyDTLSAQA |
Homo sapiens |
|
| pmid |
sentence |
| 32653904 |
Two kinases, i.e. abelson-tyrosine protein kinase (ABL)1 and Src were identified as eNOS Tyr81 kinases as their inhibition and down-regulation significantly reduced the basal and Yoda1-induced tyrosine phosphorylation and activity of eNOS. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ABL1 | up-regulates activity
phosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277519 |
Tyr81 |
WEVGSITyDTLSAQA |
Homo sapiens |
|
| pmid |
sentence |
| 32653904 |
Two kinases, i.e. abelson-tyrosine protein kinase (ABL)1 and Src were identified as eNOS Tyr81 kinases as their inhibition and down-regulation significantly reduced the basal and Yoda1-induced tyrosine phosphorylation and activity of eNOS. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRB | down-regulates activity
dephosphorylation
|
NOS3 |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277521 |
Tyr81 |
WEVGSITyDTLSAQA |
Homo sapiens |
|
| pmid |
sentence |
| 32653904 |
VE-PTP interacts with eNOS and dephosphorylates Tyr81 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277041 |
Tyr81 |
WEVGSITyDTLSAQA |
Homo sapiens |
|
| pmid |
sentence |
| 32653904 |
VE-PTP inhibition enhances eNOS activity to improve endothelial function and decrease blood pressure indirectly, through the activation of Tie-2 and the CD31/VE, cadherin, and VEGFR2 complex, and directly by dephosphorylating eNOS Tyr81.|VE-PTP, on the other hand, formed a complex with eNOS in endothelial cells and directly dephosphorylated eNOS Tyr81 in vitro. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CALM2 | up-regulates activity
binding
|
NOS3 |
0.507 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266323 |
|
|
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
Electrons flow from the C-terminal reductase domain of one NOS monomer to the N-terminal oxygenase domain of the other NOS monomer (Siddhanta et al., 1998). The primary mode of enzyme activation is the binding of calcium-bound calmodulin to the N-terminal CaM-binding domain. This facilitates a structure change and the flow of electrons from NADPH through the flavins to the oxygenase domain of the other eNOS monomer |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CRP | down-regulates quantity by destabilization 
|
NOS3 |
0.467 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252217 |
|
|
|
|
| pmid |
sentence |
| 17942113 |
C-reactive protein (CRP), a cardiovascular risk marker, induces endothelial dysfunction. CRP decreases endothelial nitric oxide synthase (eNOS) expression and bioactivity in human aortic endothelial cells (HAECs). CRP treatment significantly decreased levels of BH4 thereby promoting eNOS uncoupling. we found that CRP decreased the eNOS dimer/monomer ratio further supporting eNOS uncoupling. |
|
| Publications: |
1 |
| + |
NOS3 | up-regulates quantity
chemical modification
|
nitric oxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251629 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24379783 |
Nitric oxide (NO) is a major mediator of endothelial function and is synthesized in endothelial cells by endothelial nitric oxide synthase (eNOS). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | VEGF Signaling |
| + |
HSP90AA1 | up-regulates
binding
|
NOS3 |
0.76 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-57211 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9580552 |
The binding of hsp90 to enos enhances the activation of enos. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKC | down-regulates activity
phosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269971 |
|
|
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM1 | up-regulates activity
binding
|
NOS3 |
0.759 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251615 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24379783 |
Electrons flow from the C-terminal reductase domain of one NOS monomer to the N-terminal oxygenase domain of the other NOS monomer (Siddhanta et al., 1998). The primary mode of enzyme activation is the binding of calcium-bound calmodulin to the N-terminal CaM-binding domain. This facilitates a structure change and the flow of electrons from NADPH through the flavins to the oxygenase domain of the other eNOS monomer |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | VEGF Signaling |
| + |
HSP90AB1 | up-regulates activity
binding
|
NOS3 |
0.545 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252214 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9580552 |
Here we show that Hsp90 associates with endothelial nitric oxide synthase (eNOS) and is rapidly recruited to the eNOS complex by agonists that stimulate production of nitric oxide, namely vascular endothelial growth factor, histamine and fluid shear stress. Moreover, the binding of Hsp90 to eNOS enhances the activation of eNOS. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM3 | up-regulates activity
binding
|
NOS3 |
0.568 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266339 |
|
|
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
Electrons flow from the C-terminal reductase domain of one NOS monomer to the N-terminal oxygenase domain of the other NOS monomer (Siddhanta et al., 1998). The primary mode of enzyme activation is the binding of calcium-bound calmodulin to the N-terminal CaM-binding domain. This facilitates a structure change and the flow of electrons from NADPH through the flavins to the oxygenase domain of the other eNOS monomer |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
NOS3
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- 