Search Results
Overview
| Uniprot ID | P0DP23 |
|---|---|
| Protein Name | Calmodulin-1 |
| Gene Name | CALM1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 78 | TMMARKMKDTDSEEE |
| 95 | EAFRVFDKDGNGYIS |
Function
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). Component of the silencing factor of the integrated stress response (SIFI) complex, a multiprotein complex required to turn off the mitochondrial stress response after a specific stress event has been resolved (PubMed:38297121, PubMed:40328314, PubMed:40875847)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0034704 | calcium channel complex |
| Cellular Component | GO:0044305 | calyx of Held |
| Cellular Component | GO:1902494 | catalytic complex |
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0043209 | myelin sheath |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0099523 | presynaptic cytosol |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0030017 | sarcomere |
| Cellular Component | GO:0097225 | sperm midpiece |
| Cellular Component | GO:0005876 | spindle microtubule |
| Cellular Component | GO:0000922 | spindle pole |
| Cellular Component | GO:0031982 | vesicle |
| Cellular Component | GO:0008076 | voltage-gated potassium channel complex |
| Molecular Function | GO:0010856 | adenylate cyclase activator activity |
| Molecular Function | GO:0019855 | calcium channel inhibitor activity |
| Molecular Function | GO:0005246 | calcium channel regulator activity |
| Molecular Function | GO:0005509 | calcium ion binding |
| Molecular Function | GO:0048306 | calcium-dependent protein binding |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0072542 | protein phosphatase activator activity |
| Molecular Function | GO:0043539 | protein serine/threonine kinase activator activity |
| Molecular Function | GO:0031432 | titin binding |
| Molecular Function | GO:0044325 | transmembrane transporter binding |
| Biological Process | GO:0016240 | autophagosome membrane docking |
| Biological Process | GO:0097720 | calcineurin-mediated signaling |
| Biological Process | GO:0035458 | cellular response to interferon-beta |
| Biological Process | GO:0071346 | cellular response to type II interferon |
| Biological Process | GO:0005513 | detection of calcium ion |
| Biological Process | GO:0007186 | G protein-coupled receptor signaling pathway |
| Biological Process | GO:0060291 | long-term synaptic potentiation |
| Biological Process | GO:1990456 | mitochondrion-endoplasmic reticulum membrane tethering |
| Biological Process | GO:1905913 | negative regulation of calcium ion export across plasma membrane |
| Biological Process | GO:1901842 | negative regulation of high voltage-gated calcium channel activity |
| Biological Process | GO:0060315 | negative regulation of ryanodine-sensitive calcium-release channel activity |
| Biological Process | GO:0140056 | organelle localization by membrane tethering |
| Biological Process | GO:0046427 | positive regulation of receptor signaling pathway via JAK-STAT |
| Biological Process | GO:0140238 | presynaptic endocytosis |
| Biological Process | GO:0098901 | regulation of cardiac muscle cell action potential |
| Biological Process | GO:0055117 | regulation of cardiac muscle contraction |
| Biological Process | GO:0010881 | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
| Biological Process | GO:1901844 | regulation of cell communication by electrical coupling involved in cardiac conduction |
| Biological Process | GO:0032465 | regulation of cytokinesis |
| Biological Process | GO:0002027 | regulation of heart rate |
| Biological Process | GO:0010880 | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
| Biological Process | GO:0060314 | regulation of ryanodine-sensitive calcium-release channel activity |
| Biological Process | GO:0051592 | response to calcium ion |
| Biological Process | GO:0021762 | substantia nigra development |
Reference
[1] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.