| + |
PRKACA | down-regulates activity 
phosphorylation
|
CACNA1H |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263110 |
Ser1107 |
LPDSRRGsSSSGDPP |
Homo sapiens |
|
| pmid |
sentence |
| 19131331 |
Here, we identify protein kinase A (PKA) as a molecular switch that allows Gbeta(2)gammax dimers to effect voltage-independent inhibition of Ca(v)3.2 channels. Inhibition requires phosphorylation of Ser(1107), a critical serine residue on the II-III loop of the channel pore protein. S1107A prevents inhibition of unitary currents by recombinant Gbeta(2)gamma(2) dimers but does not disrupt dimer binding nor change its specificity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263111 |
Ser1144 |
AWSSRRSsWSSLGRA |
Homo sapiens |
|
| pmid |
sentence |
| 19131331 |
Here, we identify protein kinase A (PKA) as a molecular switch that allows Gbeta(2)gammax dimers to effect voltage-independent inhibition of Ca(v)3.2 channels. Inhibition requires phosphorylation of Ser(1107), a critical serine residue on the II-III loop of the channel pore protein. S1107A prevents inhibition of unitary currents by recombinant Gbeta(2)gamma(2) dimers but does not disrupt dimer binding nor change its specificity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
Calcineurin | up-regulates activity 
dephosphorylation
|
CACNA1H |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277872 |
Ser2137 |
RDLRRLYsVDAQGFL |
Mus musculus |
CAD Cell |
| pmid |
sentence |
| 38001892 |
we also discovered that a novel CaMKII-phosphorylated site, S2137, underwent dephosphorylation by calcineurin. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CAMK2A | down-regulates activity
phosphorylation
|
CACNA1H |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277871 |
Ser2137 |
RDLRRLYsVDAQGFL |
Mus musculus |
CAD Cell |
| pmid |
sentence |
| 38001892 |
we also discovered that a novel CaMKII-phosphorylated site, S2137, underwent dephosphorylation by calcineurin. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CACNA1H | up-regulates quantity
relocalization
|
calcium(2+) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269278 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30736831 |
Certain types of sensory neurons express Cav3.2 calcium channels [12, 13] These channels belong to the family of low-voltage gated T-type calcium channels |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
SCNN1B | up-regulates activity
binding
|
CACNA1H |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269273 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30736831 |
This study describes the functional interaction between Cav3.2 calcium channels and the Epithelial Sodium Channel (ENaC). β- and γ-ENaC subunits could be co-immunoprecipitated with Cav3.2 calcium channels from brain lysates, dorsal horn and lumbar dorsal root ganglia. Αβγ-ENaC channels enhanced Cav3.2 calcium channel trafficking to the plasma membrane in tsA-201 cells. This effect was reciprocal such that Cav3.2 channel expression also enhanced β-ENaC trafficking to the cell surface. these findings reveal ENaC as an interactor and potential regulator of Cav3.2 calcium channels expressed in neuronal tissues. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
SCNN1A | up-regulates activity
binding
|
CACNA1H |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269272 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30736831 |
This study describes the functional interaction between Cav3.2 calcium channels and the Epithelial Sodium Channel (ENaC). β- and γ-ENaC subunits could be co-immunoprecipitated with Cav3.2 calcium channels from brain lysates, dorsal horn and lumbar dorsal root ganglia. Αβγ-ENaC channels enhanced Cav3.2 calcium channel trafficking to the plasma membrane in tsA-201 cells. This effect was reciprocal such that Cav3.2 channel expression also enhanced β-ENaC trafficking to the cell surface. these findings reveal ENaC as an interactor and potential regulator of Cav3.2 calcium channels expressed in neuronal tissues. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
SCNN1G | up-regulates activity
binding
|
CACNA1H |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269274 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30736831 |
This study describes the functional interaction between Cav3.2 calcium channels and the Epithelial Sodium Channel (ENaC). β- and γ-ENaC subunits could be co-immunoprecipitated with Cav3.2 calcium channels from brain lysates, dorsal horn and lumbar dorsal root ganglia. Αβγ-ENaC channels enhanced Cav3.2 calcium channel trafficking to the plasma membrane in tsA-201 cells. This effect was reciprocal such that Cav3.2 channel expression also enhanced β-ENaC trafficking to the cell surface. these findings reveal ENaC as an interactor and potential regulator of Cav3.2 calcium channels expressed in neuronal tissues. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
3.0
CACNA1H
- 
- 