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Protein

Calmodulin

Gene

CALM1

more
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins by Ca2+. Among the enzymes to be stimulated by the calmodulin-Ca2+ complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi21 – 321Add BLAST12
Calcium bindingi57 – 682Add BLAST12
Calcium bindingi94 – 1053Add BLAST12
Calcium bindingi130 – 1414Add BLAST12

GO - Molecular functioni

  • calcium ion binding Source: BHF-UCL
  • inositol-1,4,5-trisphosphate 3-kinase activity Source: Reactome
  • ion channel binding Source: BHF-UCL
  • ligand-gated ion channel activity Source: Reactome
  • N-terminal myristoylation domain binding Source: UniProtKB
  • phospholipase binding Source: BHF-UCL
  • protein domain specific binding Source: UniProtKB
  • protein kinase binding Source: BHF-UCL
  • protein phosphatase activator activity Source: BHF-UCL
  • protein serine/threonine kinase activator activity Source: BHF-UCL
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • thioesterase binding Source: UniProtKB
  • titin binding Source: BHF-UCL

GO - Biological processi

  • detection of calcium ion Source: BHF-UCL
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • glycogen catabolic process Source: Reactome
  • G-protein coupled receptor signaling pathway Source: UniProtKB
  • inositol phosphate metabolic process Source: Reactome
  • MAPK cascade Source: Reactome
  • muscle contraction Source: Reactome
  • negative regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
  • negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  • platelet degranulation Source: Reactome
  • positive regulation of cyclic nucleotide metabolic process Source: BHF-UCL
  • positive regulation of cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
  • positive regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
  • positive regulation of phosphoprotein phosphatase activity Source: BHF-UCL
  • positive regulation of protein autophosphorylation Source: BHF-UCL
  • positive regulation of protein dephosphorylation Source: BHF-UCL
  • positive regulation of protein serine/threonine kinase activity Source: BHF-UCL
  • positive regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  • regulation of cardiac muscle contraction Source: BHF-UCL
  • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
  • regulation of cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
  • regulation of cytokinesis Source: UniProtKB
  • regulation of heart rate Source: BHF-UCL
  • regulation of nitric-oxide synthase activity Source: Reactome
  • regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  • regulation of rhodopsin mediated signaling pathway Source: Reactome
  • response to calcium ion Source: BHF-UCL
  • substantia nigra development Source: UniProtKB
  • Wnt signaling pathway, calcium modulating pathway Source: Reactome
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000143933-MONOMER.
ZFISH:ENSG00000143933-MONOMER.
ReactomeiR-HSA-111932. CaMK IV-mediated phosphorylation of CREB.
R-HSA-111933. Calmodulin induced events.
R-HSA-111957. Cam-PDE 1 activation.
R-HSA-111997. CaM pathway.
R-HSA-114608. Platelet degranulation.
R-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-HSA-163615. PKA activation.
R-HSA-180024. DARPP-32 events.
R-HSA-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-HSA-203615. eNOS activation.
R-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-HSA-2672351. Stimuli-sensing channels.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-4086398. Ca2+ pathway.
R-HSA-418359. Reduction of cytosolic Ca++ levels.
R-HSA-425561. Sodium/Calcium exchangers.
R-HSA-442717. CREB phosphorylation through the activation of CaMKK.
R-HSA-442729. CREB phosphorylation through the activation of CaMKII.
R-HSA-442745. Activation of CaMK IV.
R-HSA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-HSA-445355. Smooth Muscle Contraction.
R-HSA-451308. Activation of Ca-permeable Kainate Receptor.
R-HSA-5210891. Uptake and function of anthrax toxins.
R-HSA-5218920. VEGFR2 mediated vascular permeability.
R-HSA-5218921. VEGFR2 mediated cell proliferation.
R-HSA-5576892. Phase 0 - rapid depolarisation.
R-HSA-5578775. Ion homeostasis.
R-HSA-5607763. CLEC7A (Dectin-1) induces NFAT activation.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5627123. RHO GTPases activate PAKs.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-70221. Glycogen breakdown (glycogenolysis).
R-HSA-936837. Ion transport by P-type ATPases.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SIGNORiP62158.

Protein family/group databases

TCDBi8.A.82.1.1. the calmodulin calcium binding protein (calmodulin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Calmodulin
Short name:
CaM
Gene namesi
Name:CALM1
Synonyms:CALM, CAM, CAM1
AND
Name:CALM2
Synonyms:CAM2, CAMB
AND
Name:CALM3
Synonyms:CALML2, CAM3, CAMC, CAMIII
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componentsi: Chromosome 14, Chromosome 19, Chromosome 2

Organism-specific databases

HGNCiHGNC:1442. CALM1.
HGNC:1445. CALM2.
HGNC:1449. CALM3.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • sarcomere Source: BHF-UCL
  • spindle microtubule Source: UniProtKB
  • spindle pole Source: UniProtKB
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Ventricular tachycardia, catecholaminergic polymorphic, 4 (CPVT4)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn arrhythmogenic disorder characterized by stress-induced, bidirectional ventricular tachycardia that may degenerate into cardiac arrest and cause sudden death. Patients present with recurrent syncope, seizures, or sudden death after physical activity or emotional stress.
See also OMIM:614916
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06922254N → I in CPVT4; the mutant has significantly reduced Ca(2+) affinity compared to wild-type. 1 PublicationCorresponds to variant rs267607276dbSNPEnsembl.1
Natural variantiVAR_06922398N → S in CPVT4 and LQT15; the mutant has significantly reduced Ca(2+) affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations. 2 PublicationsCorresponds to variant rs398124647dbSNPEnsembl.1
Long QT syndrome 14 (LQT14)2 Publications
The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of LQT14.
Disease descriptionA form of long QT syndrome, a heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy.
See also OMIM:616247
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07327590F → L in LQT14. 1 PublicationCorresponds to variant rs730882253dbSNPEnsembl.1
Natural variantiVAR_073278130D → G in LQT14; reduction in Ca(2+) affinity. 1 PublicationCorresponds to variant rs730882252dbSNPEnsembl.1
Natural variantiVAR_073282142F → L in LQT14; reduction in Ca(2+) affinity. 1 PublicationCorresponds to variant rs11551462dbSNPEnsembl.1
Long QT syndrome 15 (LQT15)2 Publications
The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM2 are the cause of LQT15.
Disease descriptionA form of long QT syndrome, a heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy.
See also OMIM:616249
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07327696D → V in LQT15; reduction in Ca(2+) affinity. 1 PublicationCorresponds to variant rs730882254dbSNPEnsembl.1
Natural variantiVAR_07327798N → I in LQT15; reduction in Ca(2+) affinity. 1 PublicationCorresponds to variant rs398124647dbSNPEnsembl.1
Natural variantiVAR_06922398N → S in CPVT4 and LQT15; the mutant has significantly reduced Ca(2+) affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations. 2 PublicationsCorresponds to variant rs398124647dbSNPEnsembl.1
Natural variantiVAR_073279132D → E in LQT15; reduction in Ca(2+) affinity. 1 PublicationCorresponds to variant rs398124648dbSNPEnsembl.1
Natural variantiVAR_073280134D → H in LQT15; reduction in Ca(2+) affinity. 1 PublicationCorresponds to variant rs398124650dbSNPEnsembl.1
Natural variantiVAR_073281136Q → P in LQT15; reduction in Ca(2+) affinity. 1 PublicationCorresponds to variant rs398124649dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Long QT syndrome

Organism-specific databases

DisGeNETi801.
805.
808.
MalaCardsiCALM1.
MIMi614916. phenotype.
616247. phenotype.
616249. phenotype.
OpenTargetsiENSG00000143933.
ENSG00000160014.
ENSG00000198668.
Orphaneti3286. Catecholaminergic polymorphic ventricular tachycardia.
PharmGKBiPA26042.

Chemistry databases

ChEMBLiCHEMBL6093.
DrugBankiDB01429. Aprindine.
DB01244. Bepridil.
DB00477. Chlorpromazine.
DB00527. Cinchocaine.
DB01023. Felodipine.
DB04841. Flunarizine.
DB00623. Fluphenazine.
DB00753. Isoflurane.
DB00836. Loperamide.
DB01065. Melatonin.
DB00622. Nicardipine.
DB01115. Nifedipine.
DB00850. Perphenazine.
DB00925. Phenoxybenzamine.
DB01100. Pimozide.
DB01069. Promethazine.
DB00831. Trifluoperazine.

Polymorphism and mutation databases

BioMutaiCALM1.
DMDMi49037474.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00001982232 – 149CalmodulinAdd BLAST148

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources2 Publications1
Modified residuei22N6-acetyllysine; alternateCombined sources1
Cross-linki22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei45Phosphothreonine; by CaMK4By similarity1
Modified residuei82PhosphoserineCombined sources1
Modified residuei95N6-acetyllysineCombined sources1
Modified residuei100PhosphotyrosineCombined sources1
Modified residuei102PhosphoserineCombined sources1
Modified residuei111PhosphothreonineCombined sources1
Modified residuei116N6,N6,N6-trimethyllysine; alternateCombined sources1 Publication1
Modified residuei116N6-methyllysine; alternateCombined sources1
Modified residuei139PhosphotyrosineCombined sources1

Post-translational modificationi

Ubiquitination results in a strongly decreased activity.By similarity
Phosphorylation results in a decreased activity.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP62158.
MaxQBiP62158.
PaxDbiP62158.
PeptideAtlasiP62158.
PRIDEiP62158.
TopDownProteomicsiP62158.

2D gel databases

DOSAC-COBS-2DPAGEP62158.
OGPiP02593.
SWISS-2DPAGEP62158.

PTM databases

iPTMnetiP62158.
PhosphoSitePlusiP62158.

Expressioni

Gene expression databases

BgeeiENSG00000143933.
CleanExiHS_CALM1.
HS_CALM2.
ExpressionAtlasiP62158. baseline and differential.
GenevisibleiP62158. HS.

Organism-specific databases

HPAiCAB007790.
CAB018558.
HPA044999.

Interactioni

Subunit structurei

Interacts with MYO1C, MYO5A and RRAD. Interacts with MYO10 (By similarity). Interacts with CEP97, CCP110, TTN/titin and SRY (PubMed:9804419, PubMed:12871148, PubMed:15746192, PubMed:16760425, PubMed:17719545). Interacts with USP6; the interaction is calcium dependent (PubMed:16127172). Interacts with CDK5RAP2 (PubMed:20466722). Interacts with SCN5A (PubMed:21167176). Interacts with RYR1 and RYR2 (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).By similarity16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9Z3052EBI-397435,EBI-9084208From a different organism.
ADORA2AP292743EBI-397435,EBI-2902702
ARRB1P494073EBI-397435,EBI-743313
ARRB2P321213EBI-397435,EBI-714559
C11orf65Q8NCR39EBI-397435,EBI-744790
CACNA1CQ1393612EBI-397435,EBI-1038838
CCP110O4330314EBI-397435,EBI-1566217
CEP290O150785EBI-397435,EBI-1811944
cyaP401368EBI-397435,EBI-457011From a different organism.
DAPK1P533556EBI-397435,EBI-358616
EGFRP005334EBI-397435,EBI-297353
FASP254454EBI-397435,EBI-494743
IQCB1Q150517EBI-397435,EBI-2805823
IQCB1Q15051-25EBI-397435,EBI-11944935
KCNH1O952594EBI-397435,EBI-2909270
KCNH1O95259-28EBI-397435,EBI-9836801
KIAA1683A0A087WXN06EBI-397435,EBI-12150263
KIAA1683A0JP073EBI-397435,EBI-10171456
KIAA1683Q9H0B34EBI-397435,EBI-745878
MarcksP266452EBI-397435,EBI-911805From a different organism.
MYO10Q9HD672EBI-397435,EBI-307061
RCHY1Q96PM52EBI-397435,EBI-947779
SCN5AQ145242EBI-397435,EBI-726858
TBC1D1Q86TI04EBI-397435,EBI-1644036
TTNQ8WZ422EBI-397435,EBI-681210
YWHAZP631042EBI-397435,EBI-347088

GO - Molecular functioni

  • ion channel binding Source: BHF-UCL
  • N-terminal myristoylation domain binding Source: UniProtKB
  • phospholipase binding Source: BHF-UCL
  • protein domain specific binding Source: UniProtKB
  • protein kinase binding Source: BHF-UCL
  • thioesterase binding Source: UniProtKB
  • titin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi107252. 397 interactors.
107256. 38 interactors.
107259. 32 interactors.
DIPiDIP-31794N.
IntActiP62158. 241 interactors.
MINTiMINT-4999725.
STRINGi9606.ENSP00000349467.

Chemistry databases

BindingDBiP62158.

Structurei

Secondary structure

1149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 4Combined sources3
Helixi7 – 20Combined sources14
Beta strandi21 – 23Combined sources3
Beta strandi25 – 28Combined sources4
Helixi30 – 39Combined sources10
Helixi46 – 56Combined sources11
Helixi57 – 59Combined sources3
Beta strandi61 – 65Combined sources5
Helixi66 – 93Combined sources28
Beta strandi94 – 96Combined sources3
Beta strandi97 – 101Combined sources5
Helixi103 – 112Combined sources10
Beta strandi113 – 115Combined sources3
Helixi119 – 129Combined sources11
Turni130 – 132Combined sources3
Beta strandi133 – 138Combined sources6
Helixi139 – 146Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AJImodel-A5-148[»]
1CDLX-ray2.00A/B/C/D2-148[»]
1CLLX-ray1.70A2-149[»]
1CTRX-ray2.45A2-149[»]
1IWQX-ray2.00A2-149[»]
1J7ONMR-A2-77[»]
1J7PNMR-A83-149[»]
1K90X-ray2.75D/E/F2-149[»]
1K93X-ray2.95D/E/F6-149[»]
1L7ZX-ray2.30A2-149[»]
1LVCX-ray3.60D/E/F1-149[»]
1NKFNMR-A99-105[»]
1PK0X-ray3.30D/E/F2-148[»]
1S26X-ray3.00D/E/F2-149[»]
1SK6X-ray3.20D/E/F2-149[»]
1SW8NMR-A2-80[»]
1WRZX-ray2.00A1-149[»]
1XFUX-ray3.35O/P/Q/R/S/T1-149[»]
1XFVX-ray3.35O/P/Q/R/S/T1-149[»]
1XFWX-ray3.40O/P/Q/R/S/T1-149[»]
1XFXX-ray3.20O/P/Q/R/S/T1-149[»]
1XFYX-ray3.30O/P/Q/R/S/T1-149[»]
1XFZX-ray3.25O/P/Q/R/S/T1-149[»]
1Y6WX-ray2.40A2-149[»]
1YR5X-ray1.70A2-149[»]
1YRTX-ray2.10B76-149[»]
1YRUX-ray2.50B76-149[»]
1ZOTX-ray2.20B80-148[»]
1ZUZX-ray1.91A1-149[»]
2BE6X-ray2.00A/B/C1-149[»]
2F3YX-ray1.45A2-149[»]
2F3ZX-ray1.60A2-149[»]
2HF5NMR-A47-114[»]
2I08X-ray2.00A3-79[»]
2JZINMR-A2-149[»]
2K0ENMR-A2-149[»]
2K0FNMR-A2-149[»]
2K0JNMR-A3-149[»]
2K61NMR-A2-149[»]
2KNENMR-A2-149[»]
2KUGNMR-A2-77[»]
2KUHNMR-A83-149[»]
2L53NMR-A2-149[»]
2L7LNMR-A2-149[»]
2LGFNMR-A3-149[»]
2LL6NMR-A2-149[»]
2LL7NMR-A2-149[»]
2LQCNMR-A2-78[»]
2LQPNMR-A79-149[»]
2LV6Other-A2-149[»]
2M0JNMR-A2-149[»]
2M0KNMR-A2-149[»]
2M55NMR-A2-149[»]
2MG5NMR-A2-149[»]
2N27NMR-A2-149[»]
2N6ANMR-A6-147[»]
2N8JNMR-A2-149[»]
2R28X-ray1.86A/B1-149[»]
2V01X-ray2.15A2-149[»]
2V02X-ray2.20A2-149[»]
2VAYX-ray1.94A4-149[»]
2W73X-ray1.45A/B/E/F1-149[»]
2WELX-ray1.90D1-149[»]
2X0GX-ray2.20B2-149[»]
2Y4VX-ray1.80A1-149[»]
3BYAX-ray1.85A2-149[»]
3DVEX-ray2.35A2-149[»]
3DVJX-ray2.80A2-149[»]
3DVKX-ray2.30A2-149[»]
3DVMX-ray2.60A2-149[»]
3EWTX-ray2.40A2-149[»]
3EWVX-ray2.60A2-149[»]
3G43X-ray2.10A/B/C/D2-149[»]
3HR4X-ray2.50B/D/F/H1-149[»]
3J41electron microscopy25.0E/F1-149[»]
3O77X-ray2.35A1-149[»]
3O78X-ray2.60A/B1-149[»]
3OXQX-ray2.55A/B/C/D1-149[»]
3SUIX-ray1.95A1-149[»]
3UCTX-ray1.90A/B2-80[»]
3UCWX-ray1.76A/B/C/D2-80[»]
3UCYX-ray1.80A2-80[»]
4BW7X-ray1.81A/C1-149[»]
4BW8X-ray1.80A/B1-149[»]
4BYFX-ray2.74B/D1-149[»]
4DCKX-ray2.20B1-149[»]
4DJCX-ray1.35A1-149[»]
4GOWX-ray2.60D4-147[»]
4JPZX-ray3.02C/I1-149[»]
4JQ0X-ray3.84C1-149[»]
4L79X-ray2.30B1-149[»]
4LZXX-ray1.50A2-149[»]
4M1LX-ray2.10A2-149[»]
4OVNX-ray2.80A/B/C/D/E1-149[»]
4Q57X-ray1.80A10-74[»]
4Q5UX-ray1.95A1-149[»]
4UMOX-ray3.00C/D1-149[»]
4UPUX-ray2.34A2-149[»]
4V0CX-ray2.86C/D1-149[»]
5COCX-ray2.67A5-78[»]
5DOWX-ray1.70A/C/E/G2-149[»]
5GGMNMR-A2-149[»]
5I0IX-ray3.15C/E3-147[»]
G84-126[»]
I84-147[»]
5J03X-ray2.00B1-149[»]
5J8HNMR-A2-149[»]
5K7Lelectron microscopy3.78B1-149[»]
5K8QX-ray1.74A1-149[»]
ProteinModelPortaliP62158.
SMRiP62158.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62158.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 43EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini44 – 79EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini81 – 116EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini117 – 149EF-hand 4PROSITE-ProRule annotationAdd BLAST33

Sequence similaritiesi

Belongs to the calmodulin family.Curated
Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118901.
HOVERGENiHBG012180.
InParanoidiP62158.
KOiK02183.
OMAiHRISGKA.
OrthoDBiEOG091G0V73.
PhylomeDBiP62158.
TreeFamiTF300912.

Family and domain databases

CDDicd00051. EFh. 2 hits.
Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62158-1 [UniParc]FASTAAdd to basket

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MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ
60 70 80 90 100
DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY
110 120 130 140
ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK
Length:149
Mass (Da):16,838
Last modified:January 23, 2007 - v2
Checksum:i6B4BC3FCDE10727B
GO

Sequence cautioni

The sequence CAA36839 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti124E → Q in AAH08437 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06922254N → I in CPVT4; the mutant has significantly reduced Ca(2+) affinity compared to wild-type. 1 PublicationCorresponds to variant rs267607276dbSNPEnsembl.1
Natural variantiVAR_04858573M → T.Corresponds to variant rs41389749dbSNPEnsembl.1
Natural variantiVAR_07327590F → L in LQT14. 1 PublicationCorresponds to variant rs730882253dbSNPEnsembl.1
Natural variantiVAR_07327696D → V in LQT15; reduction in Ca(2+) affinity. 1 PublicationCorresponds to variant rs730882254dbSNPEnsembl.1
Natural variantiVAR_07327798N → I in LQT15; reduction in Ca(2+) affinity. 1 PublicationCorresponds to variant rs398124647dbSNPEnsembl.1
Natural variantiVAR_06922398N → S in CPVT4 and LQT15; the mutant has significantly reduced Ca(2+) affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations. 2 PublicationsCorresponds to variant rs398124647dbSNPEnsembl.1
Natural variantiVAR_073278130D → G in LQT14; reduction in Ca(2+) affinity. 1 PublicationCorresponds to variant rs730882252dbSNPEnsembl.1
Natural variantiVAR_073279132D → E in LQT15; reduction in Ca(2+) affinity. 1 PublicationCorresponds to variant rs398124648dbSNPEnsembl.1
Natural variantiVAR_073280134D → H in LQT15; reduction in Ca(2+) affinity. 1 PublicationCorresponds to variant rs398124650dbSNPEnsembl.1
Natural variantiVAR_073281136Q → P in LQT15; reduction in Ca(2+) affinity. 1 PublicationCorresponds to variant rs398124649dbSNPEnsembl.1
Natural variantiVAR_073282142F → L in LQT14; reduction in Ca(2+) affinity. 1 PublicationCorresponds to variant rs11551462dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04046 mRNA. Translation: AAA51918.1.
M19311 mRNA. Translation: AAA35641.1.
M27319 mRNA. Translation: AAA35635.1.
X52606, X52607, X52608 Genomic DNA. Translation: CAA36839.1. Sequence problems.
U12022, U11886 Genomic DNA. Translation: AAB60644.1.
D45887 mRNA. Translation: BAA08302.1.
U94728, U94725, U94726 Genomic DNA. Translation: AAC83174.1.
BT006818 mRNA. Translation: AAP35464.1.
BT006855 mRNA. Translation: AAP35501.1.
BT009916 mRNA. Translation: AAP88918.1.
CR541990 mRNA. Translation: CAG46787.1.
CR542021 mRNA. Translation: CAG46818.1.
AC006536 Genomic DNA. Translation: AAD45181.1.
AC073283 Genomic DNA. Translation: AAY24085.1.
BC000454 mRNA. Translation: AAH00454.1.
BC003354 mRNA. Translation: AAH03354.1.
BC005137 mRNA. Translation: AAH05137.1.
BC006464 mRNA. Translation: AAH06464.1.
BC008437 mRNA. Translation: AAH08437.1.
BC008597 mRNA. Translation: AAH08597.1.
BC011834 mRNA. Translation: AAH11834.1.
BC017385 mRNA. Translation: AAH17385.1.
BC018677 mRNA. Translation: AAH18677.1.
BC026065 mRNA. Translation: AAH26065.1.
BC047523 mRNA. No translation available.
CCDSiCCDS1832.1.
CCDS33061.1.
CCDS9892.1.
PIRiS48728. MCHU.
RefSeqiNP_001292553.1. NM_001305624.1.
NP_001292554.1. NM_001305625.1.
NP_001292555.1. NM_001305626.1.
NP_001316851.1. NM_001329922.1.
NP_001316852.1. NM_001329923.1.
NP_001316853.1. NM_001329924.1.
NP_001316854.1. NM_001329925.1.
NP_001316855.1. NM_001329926.1.
NP_001734.1. NM_001743.5.
NP_005175.2. NM_005184.3.
NP_008819.1. NM_006888.4.
UniGeneiHs.282410.
Hs.468442.
Hs.515487.

Genome annotation databases

EnsembliENST00000272298; ENSP00000272298; ENSG00000143933.
ENST00000291295; ENSP00000291295; ENSG00000160014.
ENST00000356978; ENSP00000349467; ENSG00000198668.
ENST00000596362; ENSP00000472141; ENSG00000160014.
GeneIDi801.
805.
808.
KEGGihsa:801.
hsa:805.
hsa:808.
UCSCiuc001xyl.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

A question of length - Issue 105 of May 2009

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04046 mRNA. Translation: AAA51918.1.
M19311 mRNA. Translation: AAA35641.1.
M27319 mRNA. Translation: AAA35635.1.
X52606, X52607, X52608 Genomic DNA. Translation: CAA36839.1. Sequence problems.
U12022, U11886 Genomic DNA. Translation: AAB60644.1.
D45887 mRNA. Translation: BAA08302.1.
U94728, U94725, U94726 Genomic DNA. Translation: AAC83174.1.
BT006818 mRNA. Translation: AAP35464.1.
BT006855 mRNA. Translation: AAP35501.1.
BT009916 mRNA. Translation: AAP88918.1.
CR541990 mRNA. Translation: CAG46787.1.
CR542021 mRNA. Translation: CAG46818.1.
AC006536 Genomic DNA. Translation: AAD45181.1.
AC073283 Genomic DNA. Translation: AAY24085.1.
BC000454 mRNA. Translation: AAH00454.1.
BC003354 mRNA. Translation: AAH03354.1.
BC005137 mRNA. Translation: AAH05137.1.
BC006464 mRNA. Translation: AAH06464.1.
BC008437 mRNA. Translation: AAH08437.1.
BC008597 mRNA. Translation: AAH08597.1.
BC011834 mRNA. Translation: AAH11834.1.
BC017385 mRNA. Translation: AAH17385.1.
BC018677 mRNA. Translation: AAH18677.1.
BC026065 mRNA. Translation: AAH26065.1.
BC047523 mRNA. No translation available.
CCDSiCCDS1832.1.
CCDS33061.1.
CCDS9892.1.
PIRiS48728. MCHU.
RefSeqiNP_001292553.1. NM_001305624.1.
NP_001292554.1. NM_001305625.1.
NP_001292555.1. NM_001305626.1.
NP_001316851.1. NM_001329922.1.
NP_001316852.1. NM_001329923.1.
NP_001316853.1. NM_001329924.1.
NP_001316854.1. NM_001329925.1.
NP_001316855.1. NM_001329926.1.
NP_001734.1. NM_001743.5.
NP_005175.2. NM_005184.3.
NP_008819.1. NM_006888.4.
UniGeneiHs.282410.
Hs.468442.
Hs.515487.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AJImodel-A5-148[»]
1CDLX-ray2.00A/B/C/D2-148[»]
1CLLX-ray1.70A2-149[»]
1CTRX-ray2.45A2-149[»]
1IWQX-ray2.00A2-149[»]
1J7ONMR-A2-77[»]
1J7PNMR-A83-149[»]
1K90X-ray2.75D/E/F2-149[»]
1K93X-ray2.95D/E/F6-149[»]
1L7ZX-ray2.30A2-149[»]
1LVCX-ray3.60D/E/F1-149[»]
1NKFNMR-A99-105[»]
1PK0X-ray3.30D/E/F2-148[»]
1S26X-ray3.00D/E/F2-149[»]
1SK6X-ray3.20D/E/F2-149[»]
1SW8NMR-A2-80[»]
1WRZX-ray2.00A1-149[»]
1XFUX-ray3.35O/P/Q/R/S/T1-149[»]
1XFVX-ray3.35O/P/Q/R/S/T1-149[»]
1XFWX-ray3.40O/P/Q/R/S/T1-149[»]
1XFXX-ray3.20O/P/Q/R/S/T1-149[»]
1XFYX-ray3.30O/P/Q/R/S/T1-149[»]
1XFZX-ray3.25O/P/Q/R/S/T1-149[»]
1Y6WX-ray2.40A2-149[»]
1YR5X-ray1.70A2-149[»]
1YRTX-ray2.10B76-149[»]
1YRUX-ray2.50B76-149[»]
1ZOTX-ray2.20B80-148[»]
1ZUZX-ray1.91A1-149[»]
2BE6X-ray2.00A/B/C1-149[»]
2F3YX-ray1.45A2-149[»]
2F3ZX-ray1.60A2-149[»]
2HF5NMR-A47-114[»]
2I08X-ray2.00A3-79[»]
2JZINMR-A2-149[»]
2K0ENMR-A2-149[»]
2K0FNMR-A2-149[»]
2K0JNMR-A3-149[»]
2K61NMR-A2-149[»]
2KNENMR-A2-149[»]
2KUGNMR-A2-77[»]
2KUHNMR-A83-149[»]
2L53NMR-A2-149[»]
2L7LNMR-A2-149[»]
2LGFNMR-A3-149[»]
2LL6NMR-A2-149[»]
2LL7NMR-A2-149[»]
2LQCNMR-A2-78[»]
2LQPNMR-A79-149[»]
2LV6Other-A2-149[»]
2M0JNMR-A2-149[»]
2M0KNMR-A2-149[»]
2M55NMR-A2-149[»]
2MG5NMR-A2-149[»]
2N27NMR-A2-149[»]
2N6ANMR-A6-147[»]
2N8JNMR-A2-149[»]
2R28X-ray1.86A/B1-149[»]
2V01X-ray2.15A2-149[»]
2V02X-ray2.20A2-149[»]
2VAYX-ray1.94A4-149[»]
2W73X-ray1.45A/B/E/F1-149[»]
2WELX-ray1.90D1-149[»]
2X0GX-ray2.20B2-149[»]
2Y4VX-ray1.80A1-149[»]
3BYAX-ray1.85A2-149[»]
3DVEX-ray2.35A2-149[»]
3DVJX-ray2.80A2-149[»]
3DVKX-ray2.30A2-149[»]
3DVMX-ray2.60A2-149[»]
3EWTX-ray2.40A2-149[»]
3EWVX-ray2.60A2-149[»]
3G43X-ray2.10A/B/C/D2-149[»]
3HR4X-ray2.50B/D/F/H1-149[»]
3J41electron microscopy25.0E/F1-149[»]
3O77X-ray2.35A1-149[»]
3O78X-ray2.60A/B1-149[»]
3OXQX-ray2.55A/B/C/D1-149[»]
3SUIX-ray1.95A1-149[»]
3UCTX-ray1.90A/B2-80[»]
3UCWX-ray1.76A/B/C/D2-80[»]
3UCYX-ray1.80A2-80[»]
4BW7X-ray1.81A/C1-149[»]
4BW8X-ray1.80A/B1-149[»]
4BYFX-ray2.74B/D1-149[»]
4DCKX-ray2.20B1-149[»]
4DJCX-ray1.35A1-149[»]
4GOWX-ray2.60D4-147[»]
4JPZX-ray3.02C/I1-149[»]
4JQ0X-ray3.84C1-149[»]
4L79X-ray2.30B1-149[»]
4LZXX-ray1.50A2-149[»]
4M1LX-ray2.10A2-149[»]
4OVNX-ray2.80A/B/C/D/E1-149[»]
4Q57X-ray1.80A10-74[»]
4Q5UX-ray1.95A1-149[»]
4UMOX-ray3.00C/D1-149[»]
4UPUX-ray2.34A2-149[»]
4V0CX-ray2.86C/D1-149[»]
5COCX-ray2.67A5-78[»]
5DOWX-ray1.70A/C/E/G2-149[»]
5GGMNMR-A2-149[»]
5I0IX-ray3.15C/E3-147[»]
G84-126[»]
I84-147[»]
5J03X-ray2.00B1-149[»]
5J8HNMR-A2-149[»]
5K7Lelectron microscopy3.78B1-149[»]
5K8QX-ray1.74A1-149[»]
ProteinModelPortaliP62158.
SMRiP62158.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107252. 397 interactors.
107256. 38 interactors.
107259. 32 interactors.
DIPiDIP-31794N.
IntActiP62158. 241 interactors.
MINTiMINT-4999725.
STRINGi9606.ENSP00000349467.

Chemistry databases

BindingDBiP62158.
ChEMBLiCHEMBL6093.
DrugBankiDB01429. Aprindine.
DB01244. Bepridil.
DB00477. Chlorpromazine.
DB00527. Cinchocaine.
DB01023. Felodipine.
DB04841. Flunarizine.
DB00623. Fluphenazine.
DB00753. Isoflurane.
DB00836. Loperamide.
DB01065. Melatonin.
DB00622. Nicardipine.
DB01115. Nifedipine.
DB00850. Perphenazine.
DB00925. Phenoxybenzamine.
DB01100. Pimozide.
DB01069. Promethazine.
DB00831. Trifluoperazine.

Protein family/group databases

TCDBi8.A.82.1.1. the calmodulin calcium binding protein (calmodulin) family.

PTM databases

iPTMnetiP62158.
PhosphoSitePlusiP62158.

Polymorphism and mutation databases

BioMutaiCALM1.
DMDMi49037474.

2D gel databases

DOSAC-COBS-2DPAGEP62158.
OGPiP02593.
SWISS-2DPAGEP62158.

Proteomic databases

EPDiP62158.
MaxQBiP62158.
PaxDbiP62158.
PeptideAtlasiP62158.
PRIDEiP62158.
TopDownProteomicsiP62158.

Protocols and materials databases

DNASUi801.
805.
808.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272298; ENSP00000272298; ENSG00000143933.
ENST00000291295; ENSP00000291295; ENSG00000160014.
ENST00000356978; ENSP00000349467; ENSG00000198668.
ENST00000596362; ENSP00000472141; ENSG00000160014.
GeneIDi801.
805.
808.
KEGGihsa:801.
hsa:805.
hsa:808.
UCSCiuc001xyl.3. human.

Organism-specific databases

CTDi801.
805.
808.
DisGeNETi801.
805.
808.
GeneCardsiCALM1.
CALM2.
CALM3.
GeneReviewsiCALM1.
HGNCiHGNC:1442. CALM1.
HGNC:1445. CALM2.
HGNC:1449. CALM3.
HPAiCAB007790.
CAB018558.
HPA044999.
MalaCardsiCALM1.
MIMi114180. gene.
114182. gene.
114183. gene.
614916. phenotype.
616247. phenotype.
616249. phenotype.
neXtProtiNX_P62158.
OpenTargetsiENSG00000143933.
ENSG00000160014.
ENSG00000198668.
Orphaneti3286. Catecholaminergic polymorphic ventricular tachycardia.
PharmGKBiPA26042.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118901.
HOVERGENiHBG012180.
InParanoidiP62158.
KOiK02183.
OMAiHRISGKA.
OrthoDBiEOG091G0V73.
PhylomeDBiP62158.
TreeFamiTF300912.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000143933-MONOMER.
ZFISH:ENSG00000143933-MONOMER.
ReactomeiR-HSA-111932. CaMK IV-mediated phosphorylation of CREB.
R-HSA-111933. Calmodulin induced events.
R-HSA-111957. Cam-PDE 1 activation.
R-HSA-111997. CaM pathway.
R-HSA-114608. Platelet degranulation.
R-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-HSA-163615. PKA activation.
R-HSA-180024. DARPP-32 events.
R-HSA-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-HSA-203615. eNOS activation.
R-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-HSA-2672351. Stimuli-sensing channels.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-4086398. Ca2+ pathway.
R-HSA-418359. Reduction of cytosolic Ca++ levels.
R-HSA-425561. Sodium/Calcium exchangers.
R-HSA-442717. CREB phosphorylation through the activation of CaMKK.
R-HSA-442729. CREB phosphorylation through the activation of CaMKII.
R-HSA-442745. Activation of CaMK IV.
R-HSA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-HSA-445355. Smooth Muscle Contraction.
R-HSA-451308. Activation of Ca-permeable Kainate Receptor.
R-HSA-5210891. Uptake and function of anthrax toxins.
R-HSA-5218920. VEGFR2 mediated vascular permeability.
R-HSA-5218921. VEGFR2 mediated cell proliferation.
R-HSA-5576892. Phase 0 - rapid depolarisation.
R-HSA-5578775. Ion homeostasis.
R-HSA-5607763. CLEC7A (Dectin-1) induces NFAT activation.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5627123. RHO GTPases activate PAKs.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-70221. Glycogen breakdown (glycogenolysis).
R-HSA-936837. Ion transport by P-type ATPases.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SIGNORiP62158.

Miscellaneous databases

ChiTaRSiCALM1. human.
CALM3. human.
EvolutionaryTraceiP62158.
GeneWikiiCALM2.
CALM3.
Calmodulin_1.
PROiP62158.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143933.
CleanExiHS_CALM1.
HS_CALM2.
ExpressionAtlasiP62158. baseline and differential.
GenevisibleiP62158. HS.

Family and domain databases

CDDicd00051. EFh. 2 hits.
Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCALM_HUMAN
AccessioniPrimary (citable) accession number: P62158
Secondary accession number(s): P02593
, P70667, P99014, Q13942, Q53S29, Q61379, Q61380, Q96HK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

This protein has four functional calcium-binding sites.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  3. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  8. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  9. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.