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Entry version 29 (13 Nov 2019)
Sequence version 1 (10 May 2017)
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Protein

Calmodulin-1

Gene

CALM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).4 Publications
(Microbial infection) Required for Legionella pneumophila SidJ glutamylase activity.1 Publication

Miscellaneous

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi21 – 321Combined sources2 PublicationsAdd BLAST12
Calcium bindingi57 – 682Combined sources2 PublicationsAdd BLAST12
Calcium bindingi94 – 1053Combined sources2 PublicationsAdd BLAST12
Calcium bindingi130 – 1414Combined sources2 PublicationsAdd BLAST12

<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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
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 RAF 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-9649948 Signaling downstream of RAS mutants
R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...
MoonDBi
P0DP23 Predicted

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Calmodulin-1Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CALM11 PublicationImported
Synonyms:CALM, CAM, CAM1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 14

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:1442 CALM1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
114180 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P0DP23

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Ventricular tachycardia, catecholaminergic polymorphic, 4 (CPVT4)4 Publications
The disease is caused by mutations 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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_06922254N → 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_07854198N → 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 calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; significantly reduced 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:rs398124647EnsemblClinVar.1
Long QT syndrome 14 (LQT14)5 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07327590F → L in LQT14; significantly decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 2 PublicationsCorresponds to variant dbSNP:rs730882253EnsemblClinVar.1
Natural variantiVAR_078542130D → 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. 4 PublicationsCorresponds to variant dbSNP:rs730882252EnsemblClinVar.1
Natural variantiVAR_078263141E → G in LQT14; decreased calcium affinity; loss of CACNA1C calcium-dependent-inactivation; no effect on intracellular RYR2-mediated calcium release. 1 Publication1
Natural variantiVAR_073282142F → 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. 3 PublicationsCorresponds to variant dbSNP:rs11551462Ensembl.1

Keywords - Diseasei

Disease mutation, Long QT syndrome

Organism-specific databases

DisGeNET

More...
DisGeNETi
801
805
808

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...
GeneReviewsi
CALM1

MalaCards human disease database

More...
MalaCardsi
CALM1
MIMi614916 phenotype
616247 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000143933
ENSG00000160014
ENSG00000198668

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P0DP23

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
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
DB03900 2-Methyl-2-Propanol
DB02868 3''-(Beta-Chloroethyl)-2'',4''-Dioxo-3, 5''-Spiro-Oxazolidino-4-Deacetoxy-Vinblastine
DB01429 Aprindine
DB01244 Bepridil
DB01373 Calcium
DB11093 Calcium Citrate
DB13800 Calcium levulinate
DB11348 Calcium Phosphate
DB14481 Calcium phosphate dihydrate
DB00477 Chlorpromazine
DB00527 Cinchocaine
DB01023 Felodipine
DB04841 Flunarizine
DB00623 Fluphenazine
DB00753 Isoflurane
DB00836 Loperamide
DB01065 Melatonin
DB08231 Myristic acid
DB04513 N-(6-Aminohexyl)-5-Chloro-1-Naphthalenesulfonamide
DB03977 N-Trimethyllysine
DB00622 Nicardipine
DB01115 Nifedipine
DB00850 Perphenazine
DB00925 Phenoxybenzamine
DB01100 Pimozide
DB04825 Prenylamine
DB01069 Promethazine
DB00831 Trifluoperazine

DrugCentral

More...
DrugCentrali
P0DP23

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CALM1

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004399322 – 149Calmodulin-1Add BLAST148

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources2 Publications1
Modified residuei22N6-acetyllysine; alternateCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0DP23

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
P0DP23

PeptideAtlas

More...
PeptideAtlasi
P0DP23

PRoteomics IDEntifications database

More...
PRIDEi
P0DP23

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P0DP23

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P0DP23

<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

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P0DP23 baseline and differential

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA044999

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 to 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).

By similarity22 Publications

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

1 Publication

(Microbial infection) Interacts with Legionella pneumophila glutamylase SidJ.

1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000349467

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P0DP23

<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

1149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0DP23

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni77 – 149Necessary and sufficient for interaction with PCP41 PublicationAdd BLAST73

<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

Belongs to the calmodulin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K02183

Identification of Orthologs from Complete Genome Data

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OMAi
SPHESSN

Database of Orthologous Groups

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OrthoDBi
1386217at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00051 EFh, 2 hits

Database of protein disorder

More...
DisProti
DP02013

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR039030 Calmodulin
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom

The PANTHER Classification System

More...
PANTHERi
PTHR23050:SF379 PTHR23050:SF379, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13499 EF-hand_7, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00054 EFh, 4 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47473 SSF47473, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00018 EF_HAND_1, 4 hits
PS50222 EF_HAND_2, 4 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

P0DP23-1 [UniParc]FASTAAdd 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6B4BC3FCDE10727B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V361G3V361_HUMAN
Calmodulin-1
CALM1
98Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V226G3V226_HUMAN
Calmodulin-1
CALM1
76Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V479G3V479_HUMAN
Calmodulin-1
CALM1
83Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A590UK56A0A590UK56_HUMAN
Calmodulin-1
CALM1
150Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06922254N → 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_07327590F → L in LQT14; significantly decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 2 PublicationsCorresponds to variant dbSNP:rs730882253EnsemblClinVar.1
Natural variantiVAR_07854198N → 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 calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; significantly reduced 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:rs398124647EnsemblClinVar.1
Natural variantiVAR_078542130D → 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. 4 PublicationsCorresponds to variant dbSNP:rs730882252EnsemblClinVar.1
Natural variantiVAR_078263141E → G in LQT14; decreased calcium affinity; loss of CACNA1C calcium-dependent-inactivation; no effect on intracellular RYR2-mediated calcium release. 1 Publication1
Natural variantiVAR_073282142F → 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. 3 PublicationsCorresponds to variant dbSNP:rs11551462Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
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

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000356978; ENSP00000349467; ENSG00000198668

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
801
805
808

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:801
hsa:805
hsa:808

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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_references_section">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

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.
CCDSiCCDS9892.1
PIRiS48728 MCHU
RefSeqiNP_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 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-A94-105[»]
1PK0X-ray3.30D/E/F2-148[»]
1S26X-ray3.00D/E/F2-149[»]
1SK6X-ray3.20D/E/F2-149[»]
1SW8NMR-A2-80[»]
1UP5X-ray1.90A/B2-149[»]
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[»]
2N77NMR-A77-149[»]
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[»]
5DBRX-ray2.25A5-149[»]
5DOWX-ray1.70A/C/E/G2-149[»]
5DSUX-ray1.93A3-78[»]
5GGMNMR-A2-149[»]
5I0IX-ray3.15C/E3-147[»]
G84-126[»]
I84-147[»]
5J03X-ray2.00B1-149[»]
5J8HNMR-A2-149[»]
5JQAX-ray1.80A1-149[»]
5JTHX-ray1.84A1-149[»]
5K7Lelectron microscopy3.78B1-149[»]
5K8QX-ray1.74A1-149[»]
5OEONMR-A1-149[»]
5TP5NMR-A2-149[»]
5TP6NMR-A2-149[»]
5V02X-ray1.78R1-149[»]
5V03X-ray1.58R1-149[»]
5V7XX-ray3.14B1-149[»]
5WBXX-ray1.90R5-148[»]
5WC5X-ray2.30R5-148[»]
6B8LX-ray2.30B/D/F/H1-149[»]
6B8MX-ray2.30B/D/F/H1-149[»]
6B8NX-ray2.20B/D/F/H1-149[»]
6B8PX-ray2.20B/D/F/H1-149[»]
6B8QX-ray2.60B/D/F/H1-149[»]
6BUTNMR-A2-149[»]
6C1Delectron microscopy3.20R2-149[»]
6C1Gelectron microscopy3.80R2-149[»]
6C1Helectron microscopy3.90R2-149[»]
6CNMelectron microscopy3.40E/F/G/H1-149[»]
6CNNelectron microscopy3.50E/F/G/H1-149[»]
6CNOelectron microscopy4.70E/F/G/H1-149[»]
6DADX-ray1.65A/B2-149[»]
6DAEX-ray2.00A/B2-149[»]
6DAFX-ray2.40A/B2-149[»]
6DAHX-ray2.50A/B/C/D1-149[»]
6E2Felectron microscopy3.90E1-149[»]
6E2Gelectron microscopy3.60E1-149[»]
6EEBX-ray1.96A1-149[»]
6FEGNMR-B1-149[»]
6FEHNMR-B1-149[»]
6GDKNMR-A2-149[»]
6GDLNMR-A2-80[»]
6HCSX-ray2.00A/C/E/G1-149[»]
6JI8electron microscopy3.60C/F/I/L1-149[»]
6JIIelectron microscopy4.20C/F/I/L1-149[»]
6JIUelectron microscopy4.20C/F/I/L1-149[»]
6JIYelectron microscopy3.90C/F/I/L1-149[»]
6JRSelectron microscopy3.70C/F/I/L1-149[»]
6JV2electron microscopy4.40B/D/F/H1-149[»]
6K4KX-ray2.71C/D1-149[»]
6K4LX-ray2.95C/D1-149[»]
6K4RX-ray3.11C/D1-149[»]
6MUDX-ray2.69A1-149[»]
6MUEX-ray1.90A1-149[»]
6N5WX-ray2.15C1-149[»]
6O5GX-ray1.89A1-149[»]
6PBXelectron microscopy4.00B/D/F/H1-149[»]
6PBYelectron microscopy3.67B/D/F/H1-149[»]
SMRiP0DP23
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000349467

Chemistry databases

BindingDBiP0DP23
ChEMBLiCHEMBL6093
DrugBankiDB08039 (3Z)-N,N-DIMETHYL-2-OXO-3-(4,5,6,7-TETRAHYDRO-1H-INDOL-2-YLMETHYLIDENE)-2,3-DIHYDRO-1H-INDOLE-5-SULFONAMIDE
DB03900 2-Methyl-2-Propanol
DB02868 3''-(Beta-Chloroethyl)-2'',4''-Dioxo-3, 5''-Spiro-Oxazolidino-4-Deacetoxy-Vinblastine
DB01429 Aprindine
DB01244 Bepridil
DB01373 Calcium
DB11093 Calcium Citrate
DB13800 Calcium levulinate
DB11348 Calcium Phosphate
DB14481 Calcium phosphate dihydrate
DB00477 Chlorpromazine
DB00527 Cinchocaine
DB01023 Felodipine
DB04841 Flunarizine
DB00623 Fluphenazine
DB00753 Isoflurane
DB00836 Loperamide
DB01065 Melatonin
DB08231 Myristic acid
DB04513 N-(6-Aminohexyl)-5-Chloro-1-Naphthalenesulfonamide
DB03977 N-Trimethyllysine
DB00622 Nicardipine
DB01115 Nifedipine
DB00850 Perphenazine
DB00925 Phenoxybenzamine
DB01100 Pimozide
DB04825 Prenylamine
DB01069 Promethazine
DB00831 Trifluoperazine
DrugCentraliP0DP23

Protein family/group databases

MoonDBiP0DP23 Predicted

PTM databases

iPTMnetiP0DP23
PhosphoSitePlusiP0DP23

Polymorphism and mutation databases

BioMutaiCALM1

Proteomic databases

jPOSTiP0DP23
MassIVEiP0DP23
PeptideAtlasiP0DP23
PRIDEiP0DP23

Genome annotation databases

EnsembliENST00000356978; ENSP00000349467; ENSG00000198668
GeneIDi801
805
808
KEGGihsa:801
hsa:805
hsa:808

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
801
805
808
DisGeNETi801
805
808

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CALM1
GeneReviewsiCALM1
HGNCiHGNC:1442 CALM1
HPAiHPA044999
MalaCardsiCALM1
MIMi114180 gene
614916 phenotype
616247 phenotype
neXtProtiNX_P0DP23
OpenTargetsiENSG00000143933
ENSG00000160014
ENSG00000198668

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

KOiK02183
OMAiSPHESSN
OrthoDBi1386217at2759

Enzyme and pathway databases

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 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 RAF 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-9649948 Signaling downstream of RAS mutants
R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
CALM1 human
PharosiP0DP23

Protein Ontology

More...
PROi
PR:P0DP23

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

ExpressionAtlasiP0DP23 baseline and differential

Family and domain databases

CDDicd00051 EFh, 2 hits
DisProtiDP02013
InterProiView protein in InterPro
IPR039030 Calmodulin
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
PANTHERiPTHR23050:SF379 PTHR23050:SF379, 1 hit
PfamiView protein in Pfam
PF13499 EF-hand_7, 2 hits
SMARTiView protein in SMART
SM00054 EFh, 4 hits
SUPFAMiSSF47473 SSF47473, 1 hit
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 4 hits
PS50222 EF_HAND_2, 4 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCALM1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0DP23
Secondary accession number(s): P02593
, P62158, P70667, P99014, Q13942, Q53S29, Q61379, Q61380, Q96HK3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2017
Last sequence update: May 10, 2017
Last modified: November 13, 2019
This is version 29 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. SIMILARITY comments
    Index of protein domains and families
  4. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  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
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