Function in SwissProt
Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding (PubMed:16760425, PubMed:23893133, PubMed:26969752, PubMed:27165696, PubMed:28890335, PubMed:31454269, PubMed:35568036). Calcium-binding is required for the activation of calmodulin (PubMed:16760425, PubMed:23893133, PubMed:26969752, PubMed:27165696, PubMed:28890335, PubMed:31454269, PubMed:35568036). Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases (PubMed:16760425, PubMed:23893133, PubMed:26969752, PubMed:27165696, PubMed:28890335, PubMed:31454269, PubMed:35568036). Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (PubMed:16760425). Is a regulator of voltage-dependent L-type calcium channels (PubMed:31454269). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696). Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding (PubMed:25441029). Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2 (PubMed:28890335).
(Microbial infection) Required for Legionella pneumophila SidJ glutamylase activity.
(Microbial infection) Required for C.violaceum CopC and S.flexneri OspC3 arginine ADP-riboxanase activity.
Biological Process
| See also |
| Diagram with PDB data |
| NFATC1/PPP3CA/PPP3R1 | Structure of Calcineurin in complex with NFATc1 LxVP peptide |
| MYLK2/CALM1 | SOLUTION STRUCTURE OF A CALMODULIN-TARGET PEPTIDE COMPLEX BY MULTIDIMENSIONAL NMR |
| Camk2b/CALM1 | Crystal structure of CaM-peptide complex containing AzF at position 108 |
| Mylk/CALM1 | TARGET
ENZYME RECOGNITION BY CALMODULIN: 2.4 ANGSTROMS STRUCTURE OF A
CALMODULIN-PEPTIDE COMPLEX |
| AKAP5/CALM1 | Crystal Structure of AKAP79 calmodulin binding domain peptide in complex with Ca2+/Calmodulin |
| PPP3CA/CALM1 | Structure of calmodulin bound to its recognition site from calcineurin |
| CAMK2D/CALM1 | 2.65 Angstrom crystal structure of Ca/CaM:CaMKIIdelta peptide complex |
| MYLK/CALM1 | Calmodulin complexed with calmodulin-binding peptide from smooth muscle myosin light chain kinase |
| Camk1/CALM1 | Solution structure of Ca2+/calmodulin complexed with a peptide representing the calmodulin-binding domain of calmodulin kinase I |
| Diagram without PDB data |
| DAPK2 | Crystal structure of DAPK2 S308A Calcium/Calmodulin complex |