Calmodulin 1

CALM1
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	2VAY, 1Y6W, 4JPZ, 3UCY, 1WRZ, 4G28, 1ZOT, 1YRT, 1IQ5, 1CDL, 2LL6, 3HR4, 4BW7, 4BW8, 1YR5, 4J9Y, 4LZX, 1L7Z, 1ZUZ, 2BE6, 2V01, 1XFV, 2M55, 1CTR, 2I08, 2MG5, 2R28, 3O77, 4UPU, 2L7L, 2K0F, 2M0K, 4V0C, 1SW8, 2WEL, 3DVK, 2M0J, 3DVM, 2KUH, 1K90, 1K93, 4G27, 1CLL, 2KUG, 1XFX, 4DJC, 2LQC, 2LQP, 4L79, 2W73, 2LV6, 1NKF, 2JZI, 3UCT, 4GOW, 1J7O, 1PK0, 4Q5U, 2V02, 3BYA, 4Q57, 2KNE, 1YRU, 2Y4V, 2L53, 2F3Y, 3O78, 1LVC, 4M1L, 2K0E, 1S26, 4DCK, 1XFW, 3SUI, 2X0G, 3EWV, 1XFY, 2LL7, 4OVN, 3J41, 2BKI, 1SK6, 3DVJ, 3UCW, 2LGF, 4UMO, 3DVE, 4JQ0, 3OXQ, 2K61, 1XFU, 3SJQ, 2K0J, 4BYF, 1J7P, 3G43, 3EWT, 4J9Z, 1XFZ, 2F3Z, 1IWQ, 2N6A, 2HF5, 2N27, 4ZLK, 5COC
Identifiers
Aliases	CALM1, CALML2, CAMI, CPVT4, DD132, PHKD, caM, LQT14, Calmodulin 1, calmodulin 1 (phosphorylase kinase, delta), CAMC, CAMB, CAMIII, CAM3, CAM2
External IDs	OMIM: 114180; HomoloGene: 134804; GeneCards: CALM1; OMA:CALM1 - orthologs
Gene location (Human)
Chr.	Chromosome 14 (human)
End	90,408,268 bp
RNA expression pattern
	Top expressed in
	lateral nuclear group of thalamus; ; internal globus pallidus; ; parietal lobe; ; postcentral gyrus; ; Pons; ; frontal pole; ; orbitofrontal cortex; ; superior vestibular nucleus; ; paraflocculus of cerebellum; ; external globus pallidus;
	n/a
	More reference expression data
	n/a
Gene ontology
Molecular function	calcium ion binding; protein binding; calcium channel inhibitor activity; protein kinase binding; titin binding; protein serine/threonine kinase activator activity; transmembrane transporter binding; metal ion binding; protein phosphatase activator activity; adenylate cyclase binding; disordered domain specific binding; inositol-1,4,5-trisphosphate 3-kinase activity; ligand-gated ion channel activity; adenylate cyclase activator activity; protein domain specific binding; nitric-oxide synthase regulator activity; type 3 metabotropic glutamate receptor binding; N-terminal myristoylation domain binding; phosphatidylinositol 3-kinase binding; protein N-terminus binding; calcium-dependent protein binding; nitric-oxide synthase binding;
Cellular component	cytoplasm; cytosol; calcium channel complex; extracellular region; spindle microtubule; neuron projection; cytoskeleton; nucleus; centrosome; voltage-gated potassium channel complex; extracellular exosome; spindle pole; growth cone; plasma membrane; spindle; sarcomere; nucleoplasm; vesicle; postsynaptic density; catalytic complex; microtubule organizing center; synaptic vesicle membrane; mitochondrial membranes; protein-containing complex; myelin sheath;
Biological process	muscle contraction; response to amphetamine; positive regulation of protein serine/threonine kinase activity; detection of calcium ion; Fc-epsilon receptor signaling pathway; positive regulation of phosphoprotein phosphatase activity; G2/M transition of mitotic cell cycle; regulation of high voltage-gated calcium channel activity; positive regulation of DNA binding; substantia nigra development; positive regulation of protein dephosphorylation; inositol phosphate metabolic process; positive regulation of nitric-oxide synthase activity; glycogen catabolic process; positive regulation of cyclic-nucleotide phosphodiesterase activity; G protein-coupled receptor signaling pathway; regulation of cytokinesis; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; regulation of rhodopsin mediated signaling pathway; response to corticosterone; negative regulation of peptidyl-threonine phosphorylation; activation of adenylate cyclase activity; regulation of heart rate; positive regulation of ryanodine-sensitive calcium-release channel activity; response to calcium ion; regulation of ryanodine-sensitive calcium-release channel activity; regulation of nitric-oxide synthase activity; platelet degranulation; negative regulation of ryanodine-sensitive calcium-release channel activity; MAPK cascade; positive regulation of peptidyl-threonine phosphorylation; positive regulation of protein autophosphorylation; regulation of cardiac muscle contraction; regulation of cell communication by electrical coupling involved in cardiac conduction; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; calcium-mediated signaling; ion transmembrane transport; Wnt signaling pathway, calcium modulating pathway; positive regulation of GTPase activity; protein methylation; establishment of protein localization to membrane; establishment of protein localization to mitochondrial membrane; regulation of synaptic vesicle endocytosis; regulation of synaptic vesicle exocytosis;
	Sources:Amigo / QuickGO
Orthologs
	801
	n/a
	ENSG00000198668
	n/a
	P0DP23; P0DP24
	n/a
	NM_001166106; NM_006888; NM_001363669; NM_001363670
	n/a
NP_001292553; NP_001292554; NP_001292555; NP_001734; NP_001316850;
	NP_001316851; NP_001316852; NP_001316853; NP_001316854; NP_001316855; NP_005175; NP_008819; NP_001350598; NP_001350599; NP_008819; NP_001292553; NP_001292554; NP_001292555; NP_001734; NP_001316850; NP_001316851; NP_001316852; NP_001316853; NP_001316854; NP_001316855; NP_005175
	n/a
	Wikidata
View/Edit Human

Calmodulin 1 is a protein in humans that is encoded by the CALM1 gene.

Calmodulin plays a role in calcium signal transduction pathways by regulating control of ion channels, enzymes, aquaporins, and other proteins. It functions as a calcium-binding protein that has been grouped into the EF-hand motif found in eukaryotic cells. Calmodulin plays a significant role in numerous cellular pathways and it acts as a calcium detector within the cells that interact with varied target proteins. Additionally, it simulates the activation of over twenty amino acids which helps to control various physiological functions. It is also required for various regulatory roles in cell proliferation and throughout many points during the cell cycle.

Upon binding to targeted calcium (acts as ligand), calmodulin undergoes a change in shape that allows it to interact with multiple protein types including phosphatases, ion channels, and kinases. This conformational change is associated with undergoing various cellular processes: including muscle contraction, release of neurotransmitters into the bloodstream, and gene expression.