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Details on Person UniProt:P0DP23 CALM1
| Class:Id | ReferenceGeneProduct:9015763 |
|---|---|
| _chainChangeLog | initiator methionine:1 for 9015763 removed on Fri Nov 03 2023;initiator methionine: for 9015763 added on Fri Nov 03 2023;initiator methionine: for 9015763 removed on Fri Aug 15 2025;initiator methionine:1 for 9015763 added on Fri Aug 15 2025 |
| _displayName | UniProt:P0DP23 CALM1 |
| _timestamp | 2025-08-15 20:58:28 |
| chain | initiator methionine:1 chain:2-149 |
| checksum | 6B4BC3FCDE10727B |
| comment | 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).FUNCTION (Microbial infection) Required for Legionella pneumophila SidJ glutamylase activity.FUNCTION (Microbial infection) Required for C.violaceum CopC and S.flexneri OspC3 arginine ADP-riboxanase activity.ACTIVITY REGULATION (Microbial infection) Inactivated by S.flexneri OspC1 and OspC3 proteins, which specifically bind the apo-form of calmodulin, thereby preventing calcium-binding and activity.SUBUNIT Homotetramer (PubMed:29724949). Interacts with MYO1C, MYO5A and RRAD. Interacts with MYO10 (By similarity). Interacts with CEP97, CCP110, TTN/titin and SRY (PubMed:12871148, PubMed:15746192, PubMed:16760425, PubMed:17719545, PubMed:9804419). Interacts with USP6; the interaction is calcium dependent (PubMed:16127172). Interacts with CDK5RAP2 (PubMed:20466722). Interacts with SCN5A (PubMed:21167176). Interacts with RYR1 (PubMed:18650434). Interacts with FCHO1 (PubMed:22484487). Interacts with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic domains from two MIP subunits promotes MIP water channel closure (PubMed:23893133). Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport (By similarity). Interacts with IQCF1 (By similarity). Interacts with SYT7 (By similarity). Interacts with CEACAM1 (via cytoplasmic domain); this interaction is in a calcium dependent manner and reduces homophilic cell adhesion through dissociation of dimer (By similarity). Interacts with RYR2; regulates RYR2 calcium-release channel activity (PubMed:18650434, PubMed:26164367, PubMed:27516456). Interacts with PCP4; regulates calmodulin calcium-binding (PubMed:27876793). Interacts with the heterotetrameric KCNQ2 and KCNQ3 channel; the interaction is calcium-independent, constitutive and participates in the proper assembly of a functional heterotetrameric M channel (PubMed:27564677). Interacts with alpha-synuclein/SNCA (PubMed:23607618). Interacts with SLC9A1 in a calcium-dependent manner (PubMed:30287853). In the absence of Ca(+2), interacts with GIMAP4 (via IQ domain) (By similarity). Interacts with SCN8A; the interaction modulates the inactivation rate of SCN8A (By similarity). Interaction with KIF1A; the interaction is increased in presence of calcium and increases neuronal dense core vesicles motility (PubMed:30021165). Interacts with KCNN3 (PubMed:31155282). Interacts with KCNQ1 (via C-terminus); forms a heterooctameric structure (with 4:4 KCNQ1:CALM stoichiometry) in a calcium-independent manner (PubMed:18165683, PubMed:25441029). Interacts with PIK3C3; the interaction modulates PIK3C3 kinase activity (PubMed:28890335). Interacts with HINT1; interaction increases in the presence of calcium ions (By similarity). Interacts with HINT3 (By similarity). Interacts with GARIN2; in mature sperm flagella (By similarity). Interacts with IQUB (By similarity). Interacts with SLC26A5 (via STAS domain); this interaction is calcium-dependent and the STAS domain interacts with only one lobe of CALM which is an elongated conformation (PubMed:33667636). Ca(2+)-bound CALM1 binds CNGA1:CNGB1 channel (via CaM1 and CaM2 regions); this interaction modulates the affinity of the channel for cNMPs in response to intracellular Ca(2+) levels. Interacts with ITPR1; this interaction inhibits inositol 1,4,5 trisphosphate binding in both the presence and absence of calcium and 1,4,5 trisphosphate-induced calcium release in the presence of calcium (By similarity). Component of the SIFI complex (PubMed:25582440, PubMed:38297121). Interacts with KCNN4; this interaction allows channel opening (PubMed:29724949). Interacts with KCNN2; this interaction regulates the channel activity through calcium-binding (By similarity).SUBUNIT (Microbial infection) Interacts with Rubella virus protease/methyltransferase p150.SUBUNIT (Microbial infection) Interacts with Legionella pneumophila glutamylase SidJ.SUBUNIT (Microbial infection) Interacts with C.violaceum CopC (PubMed:35338844, PubMed:35446120, PubMed:36423631). C.violaceum CopC interacts specifically with the apo form of calmodulin (PubMed:35446120, PubMed:36423631).SUBUNIT (Microbial infection) Interacts with S.flexneri OspC1 and OspC3 (PubMed:35568036, PubMed:36624349). S.flexneri OspC1 and OspC3 interact specifically with the apo form of calmodulin and prevents calcium-binding (PubMed:35568036).INTERACTION Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules.DOMAIN The N-terminal and C-terminal lobes of CALM bind to the C-terminus of KCNQ1 in a clamp-like conformation. Binding of CALM C-terminus to KCNQ1 is calcium-independent but is essential for assembly of the structure. Binding of CALM N-terminus to KCNQ1 is calcium-dependent and regulates electrophysiological activity of the channel (PubMed:25441029). The C-lobe interacts with KCNN4 channels in a calcium-independent manner, whereas the N-lobe interacts with the S4-S5 linker of KCNN4 in a calcium-dependent manner playing a role as calcium sensor and gating the channel (PubMed:29724949).PTM Ubiquitination results in a strongly decreased activity.PTM Phosphorylation results in a decreased activity.DISEASE The disease is caused by variants affecting the gene represented in this entry. Mutations in CALM1 are the cause of CPVT4.DISEASE The disease is caused by variants affecting the gene represented in this entry.MISCELLANEOUS This protein has four functional calcium-binding sites.SIMILARITY Belongs to the calmodulin family.ONLINE INFORMATION A question of length - Issue 105 of May 2009 |
| created | [InstanceEdit:9015733] Weiser, JD |
| description | recommendedName: fullName evidence="60"Calmodulin-1 |
| geneName | CALM1 CALM CAM CAM1 |
| identifier | P0DP23 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Calcium Cell projection Cilium Cytoplasm Cytoskeleton Direct protein sequencing Disease variant Flagellum Host-virus interaction Isopeptide bond Long QT syndrome Metal-binding Methylation Phosphoprotein Reference proteome Repeat Ubl conjugation |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9909836] Weiser, Joel, 2024-05-14 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 |
| name | CALM1 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8960223] ENSEMBL:ENSG00000198668 CALM1 [Homo sapiens] |
| secondaryIdentifier | CALM1_HUMAN P02593 P62158 P70667 P99014 Q13942 Q53S29 Q61379 Q61380 Q96HK3 |
| sequenceLength | 149 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:9016706] Me3K116-CALM1 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:9016707] CALM1 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:9016841] CALM1 [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:9016871] CALM1 [nucleoplasm] [Homo sapiens] [EntityWithAccessionedSequence:9016884] CALM1 [plasma membrane] [Homo sapiens] [EntityWithAccessionedSequence:9966657] CALM1 [cilium] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:6786206] N6,N6,N6-trimethyl-L-lysine at 116 |
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No pathways have been reviewed or authored by UniProt:P0DP23 CALM1 (9015763)
