| Type | Description |
|---|---|
| Definition | cardiac L-type calcium channel |
| Date | Results | Publications |
|---|---|---|
| 2017-08-05 12:33:00 | Surface biotinylation and flow cytometry assays revealed that L-type calcium channel alpha(1C) channels composed of the corresponding alpha-actinin-binding-deficient mutants result in a 35-40% reduction in surface expression compared to that of wild-type channels. | 28613835 |
| 2016-10-22 10:30:00 | a direct physical interaction between the N terminus (NT) and C terminus (CT) of the main subunit of the L-type Ca(2+) channel CaV1.2, alpha1C, is reported. | 26577286 |
| 2016-09-10 11:03:00 | These results reveal a new dimension of regulation of Ca(V)1.2 channels through phosphorylation of the Hook domains of their beta subunits. | 26271711 |
| 2016-05-14 12:22:00 | These findings suggest that N-glycosylation contributes to the surface expression and voltage-dependent gating of Cav1.2. | 25824433 |
| 2016-01-23 10:11:00 | Data show that cardiac L-type calcium (CaV1.2) channels form clusters that undergo dynamic, reciprocal, allosteric interactions. | 25714924 |
| Type | IDs |
|---|---|
| Synonymous | CACH2, CACN2, CACNL1A1, CCHL1A1, Cacna1c |
| Gene | |
| Nucleutide sequences | |
| Protein sequencees | |
| Others |
UniGene:
Ocu.1835
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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| Location | {{protein.contigId}} ( {{protein.positionStart}}..{{protein.positionEnd}} , {{protein.orientation}} ) | |||||||
| Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
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