| + |
PRKACA | up-regulates activity 
phosphorylation
|
CACNA1D |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263108 |
Ser1700 |
VNSDRRDsLQQTNTT |
in vitro |
|
| pmid |
sentence |
| 19074150 |
We recently demonstrated that PKA activation led to increased alpha(1D) Ca(2+) channel activity in tsA201 cells by phosphorylation of the channel protein. Western blotting showed that the N terminus and C terminus were phosphorylated. Serines 1743 and 1816, two PKA consensus sites, were phosphorylated by PKA and identified by mass spectrometry. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263109 |
Ser1773 |
AAHGKRPsIGNLEHV |
in vitro |
|
| pmid |
sentence |
| 19074150 |
We recently demonstrated that PKA activation led to increased alpha(1D) Ca(2+) channel activity in tsA201 cells by phosphorylation of the channel protein. Western blotting showed that the N terminus and C terminus were phosphorylated. Serines 1743 and 1816, two PKA consensus sites, were phosphorylated by PKA and identified by mass spectrometry. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CACNA1D | up-regulates quantity
relocalization
|
calcium(2+) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264359 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28642685 |
Rab interacting molecules (RIMs) are multi-domain proteins that positively regulate the number of Ca2+ channels at the presynaptic active zone (AZ). Several molecular mechanisms have been demonstrated for RIM-binding to components of the presynaptic Ca2+ channel complex, the key signaling element at the AZ. Here, we report an interaction of the C2B domain of RIM2α and RIM3γ with the C-terminus of the pore-forming α–subunit of CaV1.3 channels (CaV1.3α1), which mediate stimulus-secretion coupling at the ribbon synapses of cochlear inner hair cells (IHCs). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264326 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30849329 |
Voltage-gated calcium channels mediate the influx of calcium in response to membrane depolarization in excitable cells. In presynaptic nerve terminals, this calcium influx triggers transmitter release for synaptic transmission. Several neurological and cardiac disorders are caused by pathogenic variants in genes encoding α1-subunits of voltage-gated calcium channels, including CACNA1A (MIM: 601011) (familial hemiplegic migraine [MIM: 141500], episodic ataxia [MIM: 108500], and epilepsy [MIM: 617106]),3, 4, 5 CACNA1C (MIM: 114205) (Timothy syndrome [MIM: 601005]),6, 7 CACNA1D (MIM: 114206) (primary aldosteronism, neurodevelopmental disorders [MIM: 615474]),8, 9 and CACNA1G (MIM: 604065) (spinocerebellar ataxia [MIM: 616795]). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
RIMS1 | up-regulates activity
binding
|
CACNA1D |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264358 |
|
|
Homo sapiens |
Cochlear Hair Cell |
| pmid |
sentence |
| 28642685 |
Here, we report an interaction of the C2B domain of RIM2α and RIM3γ with the C-terminus of the pore-forming α-subunit of CaV1.3 channels (CaV1.3α1), which mediate stimulus-secretion coupling at the ribbon synapses of cochlear inner hair cells (IHCs). In conclusion, we propose that RIM2α and RIM3γ directly interact with the C-terminus of the pore-forming subunit of CaV1.3 Ca2+ channels and positively regulate their plasma membrane expression in HEK293 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CACNA1D | up-regulates 
|
Excitatory_synaptic_transmission |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264331 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30849329 |
Voltage-gated calcium channels mediate the influx of calcium in response to membrane depolarization in excitable cells. In presynaptic nerve terminals, this calcium influx triggers transmitter release for synaptic transmission. Several neurological and cardiac disorders are caused by pathogenic variants in genes encoding α1-subunits of voltage-gated calcium channels, including CACNA1A (MIM: 601011) (familial hemiplegic migraine [MIM: 141500], episodic ataxia [MIM: 108500], and epilepsy [MIM: 617106]),3, 4, 5 CACNA1C (MIM: 114205) (Timothy syndrome [MIM: 601005]),6, 7 CACNA1D (MIM: 114206) (primary aldosteronism, neurodevelopmental disorders [MIM: 615474]),8, 9 and CACNA1G (MIM: 604065) (spinocerebellar ataxia [MIM: 616795]). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Central Nervous System |
| + |
RIMS2 | up-regulates activity
binding
|
CACNA1D |
0.355 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264356 |
|
|
Homo sapiens |
Cochlear Hair Cell |
| pmid |
sentence |
| 28642685 |
Here, we report an interaction of the C2B domain of RIM2α and RIM3γ with the C-terminus of the pore-forming α-subunit of CaV1.3 channels (CaV1.3α1), which mediate stimulus-secretion coupling at the ribbon synapses of cochlear inner hair cells (IHCs). In conclusion, we propose that RIM2α and RIM3γ directly interact with the C-terminus of the pore-forming subunit of CaV1.3 Ca2+ channels and positively regulate their plasma membrane expression in HEK293 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RIMS3 | up-regulates activity
binding
|
CACNA1D |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264357 |
|
|
Homo sapiens |
Cochlear Hair Cell |
| pmid |
sentence |
| 28642685 |
Here, we report an interaction of the C2B domain of RIM2α and RIM3γ with the C-terminus of the pore-forming α-subunit of CaV1.3 channels (CaV1.3α1), which mediate stimulus-secretion coupling at the ribbon synapses of cochlear inner hair cells (IHCs). In conclusion, we propose that RIM2α and RIM3γ directly interact with the C-terminus of the pore-forming subunit of CaV1.3 Ca2+ channels and positively regulate their plasma membrane expression in HEK293 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DCC | up-regulates activity
|
CACNA1D |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268292 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12827203 |
DCC activation by a netrin-1 gradient creates a high-level [Ca2+]i gradient by triggering LCC activity and by stimulating the cAMP–PKA pathway, which further activates LCC in the plasma membrane (PM) and Ca2+ channels in the ER. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CACNA1D
- 
- 