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| Parameter | Value |
|---|---|
| Gene | CACNA1S |
| Protein Name | CAC1S_HUMAN |
| Organism | Homo sapiens (Human) |
| Alternative name(s) | Voltage-dependent L-type calcium channel subunit alpha-1S (Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle) (Voltage-gated calcium channel subunit alpha Cav1.1) |
| Protein Family | Calcium channel alpha-1 subunit (TC 1.A.1.11) family |
| NCBI Gene ID | 779 |
| UniProt ID | Q13698 |
| Enzyme Class | - |
| Molecular Weight | 212350 |
| Protein Length | 1873 |
| Protein Domain | InterPro | Pfam |
| 3D Structure |
PDBe |
PDBj |
RCSB PDB |
DrugPort
ModBase | SwissModel |
| Gene Expression | Gene Expression Atlas |
| Function and Disease | OMIM |
| Protein-protein Interaction Database | STRING | IntAct | MINT |
| Kinase Database | Phospho.ELM | PhosphoSite | NetworKIN |
| Catalytic Activity (UniProt annotation) | - |
| Localization | Cell membrane, sarcolemma |
| Function (UniProt annotation) | Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. |
| Gene Ontology | GO:0005245; GO:0005516; GO:0005737; GO:0005886; GO:0005891; GO:0006816; GO:0006936; GO:0008331; GO:0030315; GO:0031674; GO:0034765; GO:0046872; GO:0070509; GO:0071313; GO:1990454 |
| Gene Name | Organism | P-Site | Sequence(+/-7) | Conservation | Disorder | Curator Assessment | Reliability | Evidence Class | Evidence Logic | PubMed | Phospho-ELM | PhosphoSite-Plus |
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| CAMK2A (Q9UQM7) | Homo sapiens | S1575 | PEICRTVSGDLAAEE | N/A | 0.4766 | - | - | - | - | - | - |
|
Reactome Pathways
No KEGG pathways found
No NCI Nature pathways found