| + |
CAMK1 | down-regulates activity 
phosphorylation
|
NOS1 |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250614 |
Ser852 |
SYKVRFNsVSSYSDS |
in vitro |
|
| pmid |
sentence |
| 10400690 |
It was found that purified recombinant nNOS was phosphorylated by CaM-K Ialpha, CaM-K IIalpha, and CaM-K IV at Ser847 in vitro. Replacement of Ser847 with Ala (S847A) prevented phosphorylation by CaM kinases. Phosphorylated recombinant wild-type nNOS at Ser847 (approximately 0.5 mol of phosphate incorporation into nNOS) exhibited a 30% decrease of Vmax with little change of both the Km for L-arginine and Kact for CaM relative to unphosphorylated enzyme. The activity of mutant S847D was decreased to a level 50-60% as much as the wild-type enzyme. The decreased NOS enzyme activity of phosphorylated nNOS at Ser847 and mutant S847D was partially due to suppression of CaM binding, but not to impairment of dimer formation which is thought to be essential for enzyme activation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CAMK2A | down-regulates activity
phosphorylation
|
NOS1 |
0.451 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250635 |
Ser852 |
SYKVRFNsVSSYSDS |
|
|
| pmid |
sentence |
| 10400690 |
It was found that purified recombinant nNOS was phosphorylated by CaM-K Ialpha, CaM-K IIalpha, and CaM-K IV at Ser847 in vitro. Replacement of Ser847 with Ala (S847A) prevented phosphorylation by CaM kinases. Phosphorylated recombinant wild-type nNOS at Ser847 (approximately 0.5 mol of phosphate incorporation into nNOS) exhibited a 30% decrease of Vmax with little change of both the Km for L-arginine and Kact for CaM relative to unphosphorylated enzyme. The activity of mutant S847D was decreased to a level 50-60% as much as the wild-type enzyme. The decreased NOS enzyme activity of phosphorylated nNOS at Ser847 and mutant S847D was partially due to suppression of CaM binding, but not to impairment of dimer formation which is thought to be essential for enzyme activation. |
|
| Publications: |
1 |
| + |
CAMK4 | down-regulates activity
phosphorylation
|
NOS1 |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250713 |
Ser852 |
SYKVRFNsVSSYSDS |
|
|
| pmid |
sentence |
| 10400690 |
It was found that purified recombinant nNOS was phosphorylated by CaM-K Ialpha, CaM-K IIalpha, and CaM-K IV at Ser847 in vitro. Replacement of Ser847 with Ala (S847A) prevented phosphorylation by CaM kinases. Phosphorylated recombinant wild-type nNOS at Ser847 (approximately 0.5 mol of phosphate incorporation into nNOS) exhibited a 30% decrease of Vmax with little change of both the Km for L-arginine and Kact for CaM relative to unphosphorylated enzyme. The activity of mutant S847D was decreased to a level 50-60% as much as the wild-type enzyme. The decreased NOS enzyme activity of phosphorylated nNOS at Ser847 and mutant S847D was partially due to suppression of CaM binding, but not to impairment of dimer formation which is thought to be essential for enzyme activation. |
|
| Publications: |
1 |
| + |
PRKCA |
|
NOS1 |
0.491 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248848 |
|
|
in vitro |
|
| pmid |
sentence |
| 1375933 |
We now report that NOS is stoichiometrically phosphorylated by cAMP dependent protein kinase, protein kinase C, and calcium/calmodulin-dependent protein kinase, with each kinase phosphorylating a different serine site on NOS. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKACA |
phosphorylation
|
NOS1 |
0.327 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250021 |
|
|
in vitro |
|
| pmid |
sentence |
| 1375933 |
NOS is stoichiometrically phosphorylated by PKA, PKC, and CaMK, with each enzyme predominantly phosphorylating a distinct serine. CPT-CAMP has no effect on NOS activity |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
NOS1 | up-regulates quantity 
chemical modification
|
nitric oxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243957 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21890489 |
Nitric oxide (NO), the smallest signalling molecule known, is produced by three isoforms of NO synthase (NOS; EC 1.14.13.39). They all utilize l-arginine and molecular oxygen as substrates |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOS1 | form complex 
binding
|
DGC |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255996 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15117830 |
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOS1 | down-regulates activity
s-nitrosylation
|
HDAC2 |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236919 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 19047631 |
we found that restoration of NO signaling in vivo, by adenoviral-mediated expression of a constitutively active endothelial NOS mutant in MDX muscles, and in vitro, by exposing MDX-derived satellite cells to NO donors, resulted in HDAC2 blockade by cysteine S-nitrosylation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Skeletal Muscle |
| + |
DLG4 | up-regulates activity
binding
|
NOS1 |
0.726 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264227 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 11052931 |
Neuronal NOS, a Ca2+-activated form of NOS, can bind to PSD-95 through a class III PDZ domain interaction in which its own amino-terminal PDZ domain binds to a PDZ domain of PSD-95. PSD-95 may concentrate nNOS near the NMDA receptor at postsynaptic sites in these neurons. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SNTA1 | up-regulates
relocalization
|
NOS1 |
0.574 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236916 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12456711 |
biochemical studies showed that the N-terminal PDZ domain of nNOS binds to a similar PDZ domain of syntrophin (Fig. 1), a dystrophin-associated protein |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
3.0
NOS1
- 
- 