CALM1

Functionⁱ

Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium 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 (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).

6 Publications

(Microbial infection) Required for Legionella pneumophila SidJ glutamylase activity.

1 Publication

Miscellaneous

This protein has four functional calcium-binding sites.2 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	21	Calcium 1PROSITE-ProRule annotationCombined sources3 Publications	1
Metal bindingⁱ	23	Calcium 1PROSITE-ProRule annotationCombined sources3 Publications	1
Metal bindingⁱ	25	Calcium 1PROSITE-ProRule annotationCombined sources3 Publications	1
Metal bindingⁱ	27	Calcium 1PROSITE-ProRule annotationCombined sources3 Publications	1
Metal bindingⁱ	32	Calcium 1PROSITE-ProRule annotationCombined sources3 Publications	1
Metal bindingⁱ	57	Calcium 2PROSITE-ProRule annotationCombined sources3 Publications	1
Metal bindingⁱ	59	Calcium 2PROSITE-ProRule annotationCombined sources3 Publications	1
Metal bindingⁱ	61	Calcium 2PROSITE-ProRule annotationCombined sources3 Publications	1
Metal bindingⁱ	63	Calcium 2PROSITE-ProRule annotationCombined sources3 Publications	1
Metal bindingⁱ	68	Calcium 2PROSITE-ProRule annotationCombined sources3 Publications	1
Metal bindingⁱ	94	Calcium 3PROSITE-ProRule annotationCombined sources2 Publications	1
Metal bindingⁱ	96	Calcium 3PROSITE-ProRule annotationCombined sources2 Publications	1
Metal bindingⁱ	98	Calcium 3PROSITE-ProRule annotationCombined sources2 Publications	1
Metal bindingⁱ	100	Calcium 3PROSITE-ProRule annotationCombined sources2 Publications	1
Metal bindingⁱ	105	Calcium 3PROSITE-ProRule annotationCombined sources2 Publications	1
Metal bindingⁱ	130	Calcium 4PROSITE-ProRule annotationCombined sources2 Publications	1
Metal bindingⁱ	132	Calcium 4PROSITE-ProRule annotationCombined sources2 Publications	1
Metal bindingⁱ	134	Calcium 4PROSITE-ProRule annotationCombined sources2 Publications	1
Metal bindingⁱ	136	Calcium 4PROSITE-ProRule annotationCombined sources2 Publications	1
Metal bindingⁱ	141	Calcium 4PROSITE-ProRule annotationCombined sources2 Publications	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Host-virus interaction
Ligand	Calcium, Metal-binding

Enzyme and pathway databases

PathwayCommonsⁱ	P0DP23
Reactomeⁱ	R-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 SLC2A4 (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-2025928, Calcineurin activates NFAT R-HSA-203615, eNOS activation R-HSA-2151201, Transcriptional activation of mitochondrial biogenesis 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-438066, Unblocking of NMDA receptors, glutamate binding and activation R-HSA-442720, CREB1 phosphorylation through the activation of Adenylate Cyclase R-HSA-442729, CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde R-HSA-442982, Ras activation upon Ca2+ influx 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-5673000, RAF activation R-HSA-5673001, RAF/MAP kinase cascade R-HSA-6802946, Signaling by moderate kinase activity BRAF mutants R-HSA-6802952, Signaling by BRAF and RAF1 fusions R-HSA-6802955, Paradoxical activation of RAF signaling by kinase inactive BRAF R-HSA-70221, Glycogen breakdown (glycogenolysis) R-HSA-8876725, Protein methylation R-HSA-9009391, Extra-nuclear estrogen signaling R-HSA-9022535, Loss of phosphorylation of MECP2 at T308 R-HSA-9022692, Regulation of MECP2 expression and activity R-HSA-936837, Ion transport by P-type ATPases R-HSA-9617324, Negative regulation of NMDA receptor-mediated neuronal transmission R-HSA-9619229, Activation of RAC1 downstream of NMDARs R-HSA-9619483, Activation of AMPK downstream of NMDARs R-HSA-9620244, Long-term potentiation R-HSA-9648002, RAS processing R-HSA-9649948, Signaling downstream of RAS mutants R-HSA-9656223, Signaling by RAF1 mutants R-HSA-9664323, FCGR3A-mediated IL10 synthesis R-HSA-983695, Antigen activates B Cell Receptor (BCR) leading to generation of second messengers
SignaLinkⁱ	P0DP23
SIGNORⁱ	P0DP23

Protein family/group databases

MoonDBⁱ	P0DP23, Predicted

MoonDBⁱ

P0DP23, Predicted

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Calmodulin-1Imported
Gene namesⁱ	Name:CALM11 PublicationImported Synonyms:CALM, CAM, CAM1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 14

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:1442, CALM1
MIMⁱ	114180, gene
neXtProtⁱ	NX_P0DP23
VEuPathDBⁱ	HostDB:ENSG00000198668

Keywords - Cellular componentⁱ

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Flagellum

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Ventricular tachycardia, catecholaminergic polymorphic, 4 (CPVT4)4 Publications

The disease is caused by variants affecting the gene represented in this entry. Mutations in CALM1 are the cause of CPVT4.

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. CPVT4 inheritance is autosomal dominant.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_069222	54	N → I in CPVT4; increased RYR2 calcium-release channel activity; not changed calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; not changed thermal stability both in the absence and presence of calcium; no effect on the calcium binding affinity; significantly increased binding of RYR2; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 PublicationsCorresponds to variant dbSNP:rs267607276EnsemblClinVar.		1
Natural variantⁱVAR_078541	98	N → S in CPVT4; the mutant has significantly reduced calcium 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; increased RYR2 calcium-release channel activity; decreased KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 PublicationsCorresponds to variant dbSNP:rs267607277EnsemblClinVar.		1

Long QT syndrome 14 (LQT14)8 Publications

The disease is caused by variants affecting the gene represented in this entry.

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.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_073275	90	F → L in LQT14; significantly decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane; decreased thermal stability in presence of calcium ions; decreased interaction with RYR2. 3 PublicationsCorresponds to variant dbSNP:rs730882253EnsemblClinVar.	1
Natural variantⁱVAR_078542	130	D → G in LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; significantly decreased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 3 PublicationsCorresponds to variant dbSNP:rs730882252EnsemblClinVar.	1
Natural variantⁱVAR_078263	141	E → G in LQT14; decreased calcium affinity; loss of CACNA1C calcium-dependent-inactivation; no effect on intracellular RYR2-mediated calcium release. 1 Publication	1
Natural variantⁱVAR_083814	141	E → V in LQT14; loss-of-function variant causing impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential; decreased calcium ion binding. 1 Publication	1
Natural variantⁱVAR_073282	142	F → L in LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; no effect on RYR2 interaction; significantly reduced ryanodine-sensitive calcium-release channel activity; impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential. 4 PublicationsCorresponds to variants dbSNP:rs1085307479 and dbSNP:rs199744595EnsemblClinVarEnsembl.	1

Keywords - Diseaseⁱ

Disease variant, Long QT syndrome

Organism-specific databases

DisGeNET More...DisGeNETⁱ	801 805 808
GeneReviewsⁱ	CALM1
MalaCards human disease database More...MalaCardsⁱ	CALM1
MIMⁱ	614916, phenotype 616247, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000143933 ENSG00000160014 ENSG00000198668
Orphanetⁱ	3286, Catecholaminergic polymorphic ventricular tachycardia 101016, Romano-Ward syndrome

Miscellaneous databases

Pharosⁱ	P0DP23, Tclin

Pharosⁱ

P0DP23, Tclin

Chemistry databases

ChEMBLⁱ	CHEMBL6093
Drug and drug target database More...DrugBankⁱ	DB08039, (3Z)-N,N-DIMETHYL-2-OXO-3-(4,5,6,7-TETRAHYDRO-1H-INDOL-2-YLMETHYLIDENE)-2,3-DIHYDRO-1H-INDOLE-5-SULFONAMIDE DB01429, Aprindine DB01244, Bepridil DB01373, Calcium DB11093, Calcium citrate DB13800, Calcium levulinate DB11348, Calcium Phosphate DB14481, Calcium phosphate dihydrate DB00477, Chlorpromazine DB00527, Cinchocaine DB02868, Deacetoxyvinzolidine DB01023, Felodipine DB04841, Flunarizine DB00623, Fluphenazine DB00753, Isoflurane DB00836, Loperamide DB01065, Melatonin DB08231, Myristic acid DB04513, N-(6-Aminohexyl)-5-Chloro-1-Naphthalenesulfonamide DB00622, Nicardipine DB01115, Nifedipine DB00850, Perphenazine DB00925, Phenoxybenzamine DB01100, Pimozide DB04825, Prenylamine DB01069, Promethazine DB03900, tert-butanol DB00831, Trifluoperazine DB03977, Trimethyllysine
DrugCentral More...DrugCentralⁱ	P0DP23

Genetic variation databases

BioMutaⁱ	CALM1

BioMutaⁱ

CALM1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources2 Publications
ChainⁱPRO_0000439932	2 – 149	Calmodulin-1Add BLAST		148

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylalanineCombined sources2 Publications	1
Modified residueⁱ	22	N6-acetyllysine; alternateCombined sources	1
Cross-linkⁱ	22	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linkⁱ	22	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residueⁱ	45	Phosphothreonine; by CaMK4By similarity	1
Modified residueⁱ	82	PhosphoserineCombined sources	1
Modified residueⁱ	95	N6-acetyllysineCombined sources	1
Modified residueⁱ	100	PhosphotyrosineCombined sources	1
Modified residueⁱ	102	PhosphoserineCombined sources	1
Modified residueⁱ	111	PhosphothreonineCombined sources	1
Modified residueⁱ	116	N6,N6,N6-trimethyllysine; alternateCombined sources1 Publication	1
Modified residueⁱ	116	N6-methyllysine; alternateCombined sources	1
Modified residueⁱ	139	PhosphotyrosineCombined sources	1

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

jPOSTⁱ	P0DP23
MassIVEⁱ	P0DP23
PeptideAtlas More...PeptideAtlasⁱ	P0DP23

PTM databases

GlyGenⁱ	P0DP23, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	P0DP23
MetOSiteⁱ	P0DP23
PhosphoSitePlusⁱ	P0DP23

Expressionⁱ

Gene expression databases

ExpressionAtlasⁱ	P0DP23, baseline and differential

ExpressionAtlasⁱ

P0DP23, baseline and differential

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000198668, Low tissue specificity

HPAⁱ

ENSG00000198668, Low tissue specificity

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 (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:27516456, PubMed:18650434, PubMed:26164367).

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).

By similarity27 Publications

(Microbial infection) Interacts with Rubella virus protease/methyltransferase p150.

1 Publication

(Microbial infection) Interacts with Legionella pneumophila glutamylase SidJ.

1 Publication

Binary interactionsⁱ

P0DP23

With	#Exp.	IntAct
IDH1 [O75874]	7	EBI-25817233,EBI-715695

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

IntActⁱ	P0DP23, 5 interactors
Molecular INTeraction database More...MINTⁱ	P0DP23
STRINGⁱ	9606.ENSP00000272298

Chemistry databases

BindingDBⁱ

P0DP23

Miscellaneous databases

RNActⁱ	P0DP23, protein

RNActⁱ

P0DP23, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	2 – 4	Combined sources	3
Helixⁱ	7 – 20	Combined sources	14
Beta strandⁱ	21 – 23	Combined sources	3
Beta strandⁱ	25 – 28	Combined sources	4
Helixⁱ	30 – 39	Combined sources	10
Helixⁱ	46 – 56	Combined sources	11
Helixⁱ	57 – 59	Combined sources	3
Beta strandⁱ	61 – 65	Combined sources	5
Helixⁱ	66 – 93	Combined sources	28
Beta strandⁱ	94 – 96	Combined sources	3
Beta strandⁱ	97 – 101	Combined sources	5
Helixⁱ	103 – 112	Combined sources	10
Beta strandⁱ	113 – 115	Combined sources	3
Helixⁱ	119 – 129	Combined sources	11
Turnⁱ	130 – 132	Combined sources	3
Beta strandⁱ	133 – 138	Combined sources	6
Helixⁱ	139 – 146	Combined sources	8

Show more details

3D structure databases

AlphaFoldDBⁱ	P0DP23
SASBDBⁱ	P0DP23
SMRⁱ	P0DP23
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	8 – 43	EF-hand 1PROSITE-ProRule annotationAdd BLAST	36
Domainⁱ	44 – 79	EF-hand 2PROSITE-ProRule annotationAdd BLAST	36
Domainⁱ	81 – 116	EF-hand 3PROSITE-ProRule annotationAdd BLAST	36
Domainⁱ	117 – 149	EF-hand 4PROSITE-ProRule annotationAdd BLAST	33

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	77 – 149	Necessary and sufficient for interaction with PCP41 PublicationAdd BLAST		73

Domainⁱ

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.1 Publication

Sequence similaritiesⁱ

Belongs to the calmodulin family.Curated

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	KOG0027, Eukaryota
OMAⁱ	SCDRHPP
Database of Orthologous Groups More...OrthoDBⁱ	1386217at2759

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00051, EFh, 2 hits
InterProⁱ	View protein in InterPro IPR011992, EF-hand-dom_pair IPR018247, EF_Hand_1_Ca_BS IPR002048, EF_hand_dom
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF13499, EF-hand_7, 2 hits
SMARTⁱ	View protein in SMART SM00054, EFh, 4 hits
SUPFAMⁱ	SSF47473, SSF47473, 1 hit
PROSITEⁱ	View protein in PROSITE PS00018, EF_HAND_1, 4 hits PS50222, EF_HAND_2, 4 hits

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

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

This entry has 1 described isoform and 11 potential isoforms that are computationally mapped.Show all Align All

P0DP23-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
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:May 10, 2017 - v1

Checksum:ⁱ6B4BC3FCDE10727B

GO

Computationally mapped potential isoform sequencesⁱ

There are 11 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name	Protein names	Gene names	Length	Annotation

	G3V226	G3V226_HUMAN	Calmodulin Calmodulin	CALM1	76	Annotation score:
	Q96HY3	Q96HY3_HUMAN	CALM1 protein CALM1 protein (Calmodulin 2 (Phosphorylase kinase, delta), isoform CRA_a) (Calmodulin 3 (Phosphorylase kinase, delta), isoform CRA_a) (Calmodulin-1) (Calmodulin-2) (Calmodulin-3) (LP7057 protein)	CALM2 CALM1, CALM3, hCG_17033, hCG_20313	113	Annotation score:
	G3V361	G3V361_HUMAN	Calmodulin-1 Calmodulin-1	CALM1	98	Annotation score:
	A0A590UJC0	A0A590UJC0_HUMAN	Calmodulin-2 Calmodulin-2	CALM2	59	Annotation score:
	A0A590UJI2	A0A590UJI2_HUMAN	Calmodulin-2 Calmodulin-2	CALM2	104	Annotation score:
	M0QZ52	M0QZ52_HUMAN	Calmodulin 3 (Phosphorylase kinase,... Calmodulin 3 (Phosphorylase kinase, delta), isoform CRA_d (Calmodulin-3)	CALM3 hCG_20313	83	Annotation score:
	E7EMB3	E7EMB3_HUMAN	Calmodulin-2 Calmodulin-2	CALM2	196	Annotation score:
	G3V479	G3V479_HUMAN	Calmodulin-1 Calmodulin-1	CALM1	83	Annotation score:
	F8WBR5	F8WBR5_HUMAN	Calmodulin-2 Calmodulin-2	CALM2	65	Annotation score:
	A0A590UJD7	A0A590UJD7_HUMAN	Calmodulin-3 Calmodulin-3	CALM3	36	Annotation score:
There is more potential isoformShow all

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_069222	54	N → I in CPVT4; increased RYR2 calcium-release channel activity; not changed calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; not changed thermal stability both in the absence and presence of calcium; no effect on the calcium binding affinity; significantly increased binding of RYR2; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 PublicationsCorresponds to variant dbSNP:rs267607276EnsemblClinVar.	1
Natural variantⁱVAR_073275	90	F → L in LQT14; significantly decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane; decreased thermal stability in presence of calcium ions; decreased interaction with RYR2. 3 PublicationsCorresponds to variant dbSNP:rs730882253EnsemblClinVar.	1
Natural variantⁱVAR_078541	98	N → S in CPVT4; the mutant has significantly reduced calcium 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; increased RYR2 calcium-release channel activity; decreased KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 PublicationsCorresponds to variant dbSNP:rs267607277EnsemblClinVar.	1
Natural variantⁱVAR_078542	130	D → G in LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; significantly decreased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 3 PublicationsCorresponds to variant dbSNP:rs730882252EnsemblClinVar.	1
Natural variantⁱVAR_078263	141	E → G in LQT14; decreased calcium affinity; loss of CACNA1C calcium-dependent-inactivation; no effect on intracellular RYR2-mediated calcium release. 1 Publication	1
Natural variantⁱVAR_083814	141	E → V in LQT14; loss-of-function variant causing impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential; decreased calcium ion binding. 1 Publication	1
Natural variantⁱVAR_073282	142	F → L in LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; no effect on RYR2 interaction; significantly reduced ryanodine-sensitive calcium-release channel activity; impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential. 4 PublicationsCorresponds to variants dbSNP:rs1085307479 and dbSNP:rs199744595EnsemblClinVarEnsembl.	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M27319 mRNA Translation: AAA35635.1 U12022, U11886 Genomic DNA Translation: AAB60644.1 BT006818 mRNA Translation: AAP35464.1 AC006536 Genomic DNA Translation: AAD45181.1 AL512791 Genomic DNA No translation available. BC000454 mRNA Translation: AAH00454.1 BC008597 mRNA Translation: AAH08597.1 BC011834 mRNA Translation: AAH11834.1 BC047523 mRNA No translation available.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS9892.1
PIRⁱ	S48728, MCHU
NCBI Reference Sequences More...RefSeqⁱ	NP_001316851.1, NM_001329922.1 NP_001734.1, NM_001743.5 NP_005175.2, NM_005184.3 NP_008819.1, NM_006888.4

Genome annotation databases

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P0DP23	Calmodulin-1	)	MOUSE		149	UniRef100_P0DP23
Calmodulin-1	)	RAT		149
Calmodulin-1	)	XENLA		149
Calmodulin-2	)	HUMAN		149
Calmodulin	)	ANAPL		149
+703

Protein	Similar proteins		Species	Score	Length	Source
P0DP23	Calmodulin-1	)	MOUSE		149	UniRef90_P0DP23
Calmodulin-1	)	RAT		149
Calmodulin-1	)	XENLA		149
Calmodulin-2	)	HUMAN		149
Calmodulin	)	ANAPL		149
+703

Protein	Similar proteins		Species	Score	Length	Source
P0DP23	Calmodulin-1	)	MOUSE		149	UniRef50_P0DP23
Calmodulin-1	)	RAT		149
Calmodulin-1	)	XENLA		149
Calmodulin-2	)	HUMAN		149
Calmodulin	)	ANAPL		149
+715

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	M27319 mRNA Translation: AAA35635.1 U12022, U11886 Genomic DNA Translation: AAB60644.1 BT006818 mRNA Translation: AAP35464.1 AC006536 Genomic DNA Translation: AAD45181.1 AL512791 Genomic DNA No translation available. BC000454 mRNA Translation: AAH00454.1 BC008597 mRNA Translation: AAH08597.1 BC011834 mRNA Translation: AAH11834.1 BC047523 mRNA No translation available.
CCDSⁱ	CCDS9892.1
PIRⁱ	S48728, MCHU
RefSeqⁱ	NP_001316851.1, NM_001329922.1 NP_001734.1, NM_001743.5 NP_005175.2, NM_005184.3 NP_008819.1, NM_006888.4

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1CDL	X-ray	2.00	A/B/C/D	2-148	[»]
	1CLL	X-ray	1.70	A	2-149	[»]
	1CTR	X-ray	2.45	A	2-149	[»]
	1IWQ	X-ray	2.00	A	2-149	[»]
	1J7O	NMR	-	A	2-77	[»]
	1J7P	NMR	-	A	83-149	[»]
	1K90	X-ray	2.75	D/E/F	2-149	[»]
	1K93	X-ray	2.95	D/E/F	6-149	[»]
	1L7Z	X-ray	2.30	A	2-149	[»]
	1LVC	X-ray	3.60	D/E/F	1-149	[»]
	1NKF	NMR	-	A	94-105	[»]
	1PK0	X-ray	3.30	D/E/F	2-148	[»]
	1S26	X-ray	3.00	D/E/F	2-149	[»]
	1SK6	X-ray	3.20	D/E/F	2-149	[»]
	1SW8	NMR	-	A	2-80	[»]
	1UP5	X-ray	1.90	A/B	2-149	[»]
	1WRZ	X-ray	2.00	A	1-149	[»]
	1XFU	X-ray	3.35	O/P/Q/R/S/T	1-149	[»]
	1XFV	X-ray	3.35	O/P/Q/R/S/T	1-149	[»]
	1XFW	X-ray	3.40	O/P/Q/R/S/T	1-149	[»]
	1XFX	X-ray	3.20	O/P/Q/R/S/T	1-149	[»]
	1XFY	X-ray	3.30	O/P/Q/R/S/T	1-149	[»]
	1XFZ	X-ray	3.25	O/P/Q/R/S/T	1-149	[»]
	1Y6W	X-ray	2.40	A	2-149	[»]
	1YR5	X-ray	1.70	A	2-149	[»]
	1YRT	X-ray	2.10	B	76-149	[»]
	1YRU	X-ray	2.50	B	76-149	[»]
	1ZOT	X-ray	2.20	B	80-148	[»]
	1ZUZ	X-ray	1.91	A	1-149	[»]
	2BE6	X-ray	2.00	A/B/C	1-149	[»]
	2F3Y	X-ray	1.45	A	2-149	[»]
	2F3Z	X-ray	1.60	A	2-149	[»]
	2HF5	NMR	-	A	47-114	[»]
	2I08	X-ray	2.00	A	3-79	[»]
	2JZI	NMR	-	A	2-149	[»]
	2K0E	NMR	-	A	2-149	[»]
	2K0F	NMR	-	A	2-149	[»]
	2K0J	NMR	-	A	3-149	[»]
	2K61	NMR	-	A	2-149	[»]
	2KNE	NMR	-	A	2-149	[»]
	2KUG	NMR	-	A	2-77	[»]
	2KUH	NMR	-	A	83-149	[»]
	2L53	NMR	-	A	2-149	[»]
	2L7L	NMR	-	A	2-149	[»]
	2LGF	NMR	-	A	3-149	[»]
	2LL6	NMR	-	A	2-149	[»]
	2LL7	NMR	-	A	2-149	[»]
	2LQC	NMR	-	A	2-78	[»]
	2LQP	NMR	-	A	79-149	[»]
	2LV6	Other	-	A	2-149	[»]
	2M0J	NMR	-	A	2-149	[»]
	2M0K	NMR	-	A	2-149	[»]
	2M55	NMR	-	A	2-149	[»]
	2MG5	NMR	-	A	2-149	[»]
	2N27	NMR	-	A	2-149	[»]
	2N6A	NMR	-	A	6-147	[»]
	2N77	NMR	-	A	77-149	[»]
	2N8J	NMR	-	A	2-149	[»]
	2R28	X-ray	1.86	A/B	1-149	[»]
	2V01	X-ray	2.15	A	2-149	[»]
	2V02	X-ray	2.20	A	2-149	[»]
	2VAY	X-ray	1.94	A	4-149	[»]
	2W73	X-ray	1.45	A/B/E/F	1-149	[»]
2WEL	X-ray	1.90	D	1-149	[»]
2X0G	X-ray	2.20	B	2-149	[»]
2Y4V	X-ray	1.80	A	1-149	[»]
3BYA	X-ray	1.85	A	2-149	[»]
3DVE	X-ray	2.35	A	2-149	[»]
3DVJ	X-ray	2.80	A	2-149	[»]
3DVK	X-ray	2.30	A	2-149	[»]
3DVM	X-ray	2.60	A	2-149	[»]
3EVV	X-ray	2.60	A	5-149	[»]
3EWT	X-ray	2.40	A	2-149	[»]
3EWV	X-ray	2.60	A	2-149	[»]
3G43	X-ray	2.10	A/B/C/D	2-149	[»]
3HR4	X-ray	2.50	B/D/F/H	1-149	[»]
3J41	electron microscopy	25.00	E/F	1-149	[»]
3O77	X-ray	2.35	A	1-149	[»]
3O78	X-ray	2.60	A/B	1-149	[»]
3OXQ	X-ray	2.55	A/B/C/D	1-149	[»]
3SUI	X-ray	1.95	A	1-149	[»]
3UCT	X-ray	1.90	A/B	2-80	[»]
3UCW	X-ray	1.76	A/B/C/D	2-80	[»]
3UCY	X-ray	1.80	A	2-80	[»]
4BW7	X-ray	1.81	A/C	1-149	[»]
4BW8	X-ray	1.80	A/B	1-149	[»]
4BYF	X-ray	2.74	B/D	1-149	[»]
4DCK	X-ray	2.20	B	1-149	[»]
4DJC	X-ray	1.35	A	1-149	[»]
4GOW	X-ray	2.60	D	4-147	[»]
4JPZ	X-ray	3.02	C/I	1-149	[»]
4JQ0	X-ray	3.84	C	1-149	[»]
4L79	X-ray	2.30	B	1-149	[»]
4LZX	X-ray	1.50	A	2-149	[»]
4M1L	X-ray	2.10	A	2-149	[»]
4OVN	X-ray	2.80	A/B/C/D/E	1-149	[»]
4Q57	X-ray	1.80	A	10-74	[»]
4Q5U	X-ray	1.95	A	1-149	[»]
4UMO	X-ray	3.00	C/D	1-149	[»]
4UPU	X-ray	2.34	A	2-149	[»]
4V0C	X-ray	2.86	C/D	1-149	[»]
5COC	X-ray	2.67	A	5-78	[»]
5DBR	X-ray	2.25	A	5-149	[»]
5DOW	X-ray	1.70	A/C/E/G	2-149	[»]
5DSU	X-ray	1.93	A	3-78	[»]
5GGM	NMR	-	A	2-149	[»]
5I0I	X-ray	3.15	C/E	3-147	[»]
			G	84-126	[»]
			I	84-147	[»]
5J03	X-ray	2.00	B	1-149	[»]
5J8H	NMR	-	A	2-149	[»]
5JQA	X-ray	1.80	A	1-149	[»]
5JTH	X-ray	1.84	A	1-149	[»]
5K7L	electron microscopy	3.78	B	1-149	[»]
5K8Q	X-ray	1.74	A	1-149	[»]
5OEO	NMR	-	A	1-149	[»]
5TP5	NMR	-	A	2-149	[»]
5TP6	NMR	-	A	2-149	[»]
5V02	X-ray	1.78	R	1-149	[»]
5V03	X-ray	1.58	R	1-149	[»]
5V7X	X-ray	3.14	B	1-149	[»]
5WBX	X-ray	1.90	R	5-148	[»]
5WC5	X-ray	2.30	R	5-148	[»]
6B8L	X-ray	2.30	B/D/F/H	1-149	[»]
6B8M	X-ray	2.30	B/D/F/H	1-149	[»]
6B8N	X-ray	2.20	B/D/F/H	1-149	[»]
6B8P	X-ray	2.20	B/D/F/H	1-149	[»]
6B8Q	X-ray	2.60	B/D/F/H	1-149	[»]
6BUT	NMR	-	A	2-149	[»]
6C1D	electron microscopy	3.20	R	2-149	[»]
6C1G	electron microscopy	3.80	R	2-149	[»]
6C1H	electron microscopy	3.90	R	2-149	[»]
6CNM	electron microscopy	3.40	E/F/G/H	1-149	[»]
6CNN	electron microscopy	3.50	E/F/G/H	1-149	[»]
6CNO	electron microscopy	4.70	E/F/G/H	1-149	[»]
6DAD	X-ray	1.65	A/B	2-149	[»]
6DAE	X-ray	2.00	A/B	2-149	[»]
6DAF	X-ray	2.40	A/B	2-149	[»]
6DAH	X-ray	2.50	A/B/C/D	1-149	[»]
6E2F	electron microscopy	3.90	E	1-149	[»]
6E2G	electron microscopy	3.60	E	1-149	[»]
6EEB	X-ray	1.96	A	1-149	[»]
6FEG	NMR	-	B	1-149	[»]
6FEH	NMR	-	B	1-149	[»]
6GDK	NMR	-	A	2-149	[»]
6GDL	NMR	-	A	2-80	[»]
6HCS	X-ray	2.00	A/C/E/G	1-149	[»]
6HR1	X-ray	1.90	A/B	2-149	[»]
6JI8	electron microscopy	3.60	C/F/I/L	1-149	[»]
6JII	electron microscopy	4.20	C/F/I/L	1-149	[»]
6JIU	electron microscopy	4.20	C/F/I/L	1-149	[»]
6JIY	electron microscopy	3.90	C/F/I/L	1-149	[»]
6JRS	electron microscopy	3.70	C/F/I/L	1-149	[»]
6JV2	electron microscopy	4.40	B/D/F/H	1-149	[»]
6K4K	X-ray	2.71	C/D	1-149	[»]
6K4L	X-ray	2.95	C/D	1-149	[»]
6K4R	X-ray	3.11	C/D	1-149	[»]
6M2W	electron microscopy	3.80	C/F/I/L	1-149	[»]
6M7H	X-ray	1.60	A	2-148	[»]
6MUD	X-ray	2.69	A	1-149	[»]
6MUE	X-ray	1.90	A	1-149	[»]
6N5W	X-ray	2.15	C	1-149	[»]
6O5G	X-ray	1.89	A	1-149	[»]
6OS4	X-ray	2.05	A	2-149	[»]
6PAW	X-ray	2.95	C/D/G/H	1-149	[»]
6PBX	electron microscopy	4.00	B/D/F/H	1-149	[»]
6PBY	electron microscopy	3.67	B/D/F/H	1-149	[»]
6U39	X-ray	2.40	A/C/E/G/I/K/M/O/Q/S	2-149	[»]
6U3A	X-ray	1.65	A/B	2-149	[»]
6U3B	X-ray	1.70	A	2-149	[»]
6U3D	X-ray	1.75	A/B	2-149	[»]
6UZZ	electron microscopy	3.10	B/D/F/H	1-149	[»]
6V00	electron microscopy	3.10	B/E/H/K	1-149	[»]
6V01	electron microscopy	3.90	B/E/H/K	1-149	[»]
6X32	electron microscopy	3.80	C/F/I/L	3-148	[»]
6X33	electron microscopy	4.20	C/F/I/L	1-148	[»]
6X35	electron microscopy	4.20	C/F/I/L	1-148	[»]
6X36	electron microscopy	4.70	C/F/I/L	1-148	[»]
6XXX	X-ray	1.25	AAA	1-149	[»]
6XY3	X-ray	2.00	AAA	1-149	[»]
6XYR	X-ray	2.08	A	2-149	[»]
6Y4P	X-ray	2.13	A	1-149	[»]
6Y94	NMR	-	A	2-149	[»]
6Y95	NMR	-	A	2-149	[»]
6YNS	X-ray	3.94	A/B/C/D/E/F/G/H/I/J/K/L	2-149	[»]
6YNU	X-ray	3.12	A/C	2-149	[»]
6ZBI	NMR	-	A	2-149	[»]
7BF1	X-ray	1.24	AAA	1-149	[»]
7BF2	X-ray	1.43	AAA	1-149	[»]
7KL5	X-ray	1.65	A	1-149	[»]
7SX3	electron microscopy	3.10	C	1-149	[»]
7SX4	electron microscopy	3.50	C	1-149	[»]
AlphaFoldDBⁱ	P0DP23
SASBDBⁱ	P0DP23
SMRⁱ	P0DP23
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

IntActⁱ	P0DP23, 5 interactors
MINTⁱ	P0DP23
STRINGⁱ	9606.ENSP00000272298

Chemistry databases

BindingDBⁱ	P0DP23
ChEMBLⁱ	CHEMBL6093
DrugBankⁱ	DB08039, (3Z)-N,N-DIMETHYL-2-OXO-3-(4,5,6,7-TETRAHYDRO-1H-INDOL-2-YLMETHYLIDENE)-2,3-DIHYDRO-1H-INDOLE-5-SULFONAMIDE DB01429, Aprindine DB01244, Bepridil DB01373, Calcium DB11093, Calcium citrate DB13800, Calcium levulinate DB11348, Calcium Phosphate DB14481, Calcium phosphate dihydrate DB00477, Chlorpromazine DB00527, Cinchocaine DB02868, Deacetoxyvinzolidine DB01023, Felodipine DB04841, Flunarizine DB00623, Fluphenazine DB00753, Isoflurane DB00836, Loperamide DB01065, Melatonin DB08231, Myristic acid DB04513, N-(6-Aminohexyl)-5-Chloro-1-Naphthalenesulfonamide DB00622, Nicardipine DB01115, Nifedipine DB00850, Perphenazine DB00925, Phenoxybenzamine DB01100, Pimozide DB04825, Prenylamine DB01069, Promethazine DB03900, tert-butanol DB00831, Trifluoperazine DB03977, Trimethyllysine
DrugCentralⁱ	P0DP23

Protein family/group databases

MoonDBⁱ	P0DP23, Predicted

MoonDBⁱ

P0DP23, Predicted

PTM databases

GlyGenⁱ	P0DP23, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	P0DP23
MetOSiteⁱ	P0DP23
PhosphoSitePlusⁱ	P0DP23

Genetic variation databases

BioMutaⁱ	CALM1

BioMutaⁱ

CALM1

Proteomic databases

jPOSTⁱ	P0DP23
MassIVEⁱ	P0DP23
PeptideAtlasⁱ	P0DP23

Protocols and materials databases

Antibodypediaⁱ	4344, 534 antibodies from 33 providers
The DNASU plasmid repository More...DNASUⁱ	801

Genome annotation databases

Ensemblⁱ	ENST00000356978.9; ENSP00000349467.4; ENSG00000198668.14
GeneIDⁱ	801 805 808
KEGGⁱ	hsa:801 hsa:805 hsa:808
MANE-Selectⁱ	ENST00000272298.12; ENSP00000272298.7; NM_001743.6; NP_001734.1 ENST00000291295.14; ENSP00000291295.8; NM_005184.4; NP_005175.2 ENST00000356978.9; ENSP00000349467.4; NM_006888.6; NP_008819.1

Organism-specific databases

CTDⁱ	801 805 808
DisGeNETⁱ	801 805 808
GeneCardsⁱ	CALM1
GeneReviewsⁱ	CALM1
HGNCⁱ	HGNC:1442, CALM1
HPAⁱ	ENSG00000198668, Low tissue specificity
MalaCardsⁱ	CALM1
MIMⁱ	114180, gene 614916, phenotype 616247, phenotype
neXtProtⁱ	NX_P0DP23
OpenTargetsⁱ	ENSG00000143933 ENSG00000160014 ENSG00000198668
Orphanetⁱ	3286, Catecholaminergic polymorphic ventricular tachycardia 101016, Romano-Ward syndrome
VEuPathDBⁱ	HostDB:ENSG00000198668
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0027, Eukaryota
OMAⁱ	SCDRHPP
OrthoDBⁱ	1386217at2759

Enzyme and pathway databases

PathwayCommonsⁱ	P0DP23
Reactomeⁱ	R-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 SLC2A4 (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-2025928, Calcineurin activates NFAT R-HSA-203615, eNOS activation R-HSA-2151201, Transcriptional activation of mitochondrial biogenesis 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-438066, Unblocking of NMDA receptors, glutamate binding and activation R-HSA-442720, CREB1 phosphorylation through the activation of Adenylate Cyclase R-HSA-442729, CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde R-HSA-442982, Ras activation upon Ca2+ influx 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-5673000, RAF activation R-HSA-5673001, RAF/MAP kinase cascade R-HSA-6802946, Signaling by moderate kinase activity BRAF mutants R-HSA-6802952, Signaling by BRAF and RAF1 fusions R-HSA-6802955, Paradoxical activation of RAF signaling by kinase inactive BRAF R-HSA-70221, Glycogen breakdown (glycogenolysis) R-HSA-8876725, Protein methylation R-HSA-9009391, Extra-nuclear estrogen signaling R-HSA-9022535, Loss of phosphorylation of MECP2 at T308 R-HSA-9022692, Regulation of MECP2 expression and activity R-HSA-936837, Ion transport by P-type ATPases R-HSA-9617324, Negative regulation of NMDA receptor-mediated neuronal transmission R-HSA-9619229, Activation of RAC1 downstream of NMDARs R-HSA-9619483, Activation of AMPK downstream of NMDARs R-HSA-9620244, Long-term potentiation R-HSA-9648002, RAS processing R-HSA-9649948, Signaling downstream of RAS mutants R-HSA-9656223, Signaling by RAF1 mutants R-HSA-9664323, FCGR3A-mediated IL10 synthesis R-HSA-983695, Antigen activates B Cell Receptor (BCR) leading to generation of second messengers
SignaLinkⁱ	P0DP23
SIGNORⁱ	P0DP23

Miscellaneous databases

BioGRID-ORCSⁱ	801, 10 hits in 1080 CRISPR screens 805, 35 hits in 960 CRISPR screens 808, 45 hits in 1080 CRISPR screens
ChiTaRSⁱ	CALM1, human
Pharosⁱ	P0DP23, Tclin
Protein Ontology More...PROⁱ	PR:P0DP23
RNActⁱ	P0DP23, protein
SOURCEⁱ	Search...

Gene expression databases

ExpressionAtlasⁱ

P0DP23, baseline and differential

Family and domain databases

CDDⁱ	cd00051, EFh, 2 hits
InterProⁱ	View protein in InterPro IPR011992, EF-hand-dom_pair IPR018247, EF_Hand_1_Ca_BS IPR002048, EF_hand_dom
Pfamⁱ	View protein in Pfam PF13499, EF-hand_7, 2 hits
SMARTⁱ	View protein in SMART SM00054, EFh, 4 hits
SUPFAMⁱ	SSF47473, SSF47473, 1 hit
PROSITEⁱ	View protein in PROSITE PS00018, EF_HAND_1, 4 hits PS50222, EF_HAND_2, 4 hits
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CALM1_HUMAN
Accessionⁱ	P0DP23Primary (citable) accession number: P0DP23 Secondary accession number(s): P02593 Q96HK3
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 10, 2017
	Last sequence update:	May 10, 2017
	Last modified:	May 25, 2022
	This is version 42 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing, Reference proteome

Documents

Human chromosome 14
Human chromosome 14: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Protein Spotlight
Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0DP23 (CALM1_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Calmodulin-1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoskeleton

Other locations

Cytoskeleton

Cytosol

Extracellular region or secreted

Nucleus

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P0DP23

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Natural variant

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ