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Entry version 38 (23 Feb 2022)
Sequence version 1 (10 May 2017)
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Protein

Calmodulin-1

Gene

Calm1

Organism
Mus musculus (Mouse)
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. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2 (By similarity).

By similarity

Miscellaneous

This protein has four functional calcium-binding sites.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sourcesAdd BLAST12
Calcium bindingi57 – 682Combined sourcesAdd BLAST12
Calcium bindingi94 – 1053Combined sourcesAdd BLAST12
Calcium bindingi130 – 1414Combined sourcesAdd 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-MMU-111932, CaMK IV-mediated phosphorylation of CREB
R-MMU-111933, Calmodulin induced events
R-MMU-111957, Cam-PDE 1 activation
R-MMU-114608, Platelet degranulation
R-MMU-1474151, Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-MMU-163615, PKA activation
R-MMU-1855204, Synthesis of IP3 and IP4 in the cytosol
R-MMU-2025928, Calcineurin activates NFAT
R-MMU-203615, eNOS activation
R-MMU-2514859, Inactivation, recovery and regulation of the phototransduction cascade
R-MMU-2672351, Stimuli-sensing channels
R-MMU-2871809, FCERI mediated Ca+2 mobilization
R-MMU-4086398, Ca2+ pathway
R-MMU-418359, Reduction of cytosolic Ca++ levels
R-MMU-425561, Sodium/Calcium exchangers
R-MMU-438066, Unblocking of NMDA receptors, glutamate binding and activation
R-MMU-442729, CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde
R-MMU-445355, Smooth Muscle Contraction
R-MMU-451308, Activation of Ca-permeable Kainate Receptor
R-MMU-5218920, VEGFR2 mediated vascular permeability
R-MMU-5576892, Phase 0 - rapid depolarisation
R-MMU-5578775, Ion homeostasis
R-MMU-5607763, CLEC7A (Dectin-1) induces NFAT activation
R-MMU-5626467, RHO GTPases activate IQGAPs
R-MMU-5627123, RHO GTPases activate PAKs
R-MMU-5673000, RAF activation
R-MMU-5673001, RAF/MAP kinase cascade
R-MMU-70221, Glycogen breakdown (glycogenolysis)
R-MMU-8876725, Protein methylation
R-MMU-9009391, Extra-nuclear estrogen signaling
R-MMU-936837, Ion transport by P-type ATPases
R-MMU-9619229, Activation of RAC1 downstream of NMDARs
R-MMU-9648002, RAS processing

<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%5Fand%5Ftaxonomy%5Fsection">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-1By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Calm1Imported
Synonyms:Calm, Cam, Cam1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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> Componentsi: Chromosome 12, Chromosome 17, Chromosome 7

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:88251, Calm1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSMUSG00000001175
HostDB:ENSMUSG00000019370
HostDB:ENSMUSG00000036438

<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

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi115E → A: Decreases interaction with SCN8A in the absence of calcium. 1 Publication1
Mutagenesisi121E → A: Decreases interaction with SCN8A in the absence of calcium. 1 Publication1
Mutagenesisi124E → A: Decreases interaction with SCN8A in the absence of calcium. 1 Publication1
Mutagenesisi128E → A: Decreases interaction with SCN8A in the absence of calcium. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3562176

<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%5Fprocessing%5Fsection">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 methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004399352 – 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-acetylalanine1 Publication1
Modified residuei22N6-acetyllysine; alternateCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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); alternateBy similarity
Cross-linki22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei45Phosphothreonine; by CaMK4By similarity1
Modified residuei82PhosphoserineBy similarity1
Modified residuei95N6-acetyllysineBy similarity1
Modified residuei100PhosphotyrosineCombined sources1
Modified residuei102PhosphoserineCombined sources1
Modified residuei111PhosphothreonineBy similarity1
Modified residuei116N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei116N6-methyllysine; alternateBy similarity1
Modified residuei139PhosphotyrosineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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
P0DP26

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P0DP26

MetOSite database of methionine sulfoxide sites

More...
MetOSitei
P0DP26

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

More...
PhosphoSitePlusi
P0DP26

<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
P0DP26, baseline and differential

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with CEP97, CCP110, MYO1C, TTN/titin and SRY.

Interacts with MYO10.

Interacts with RRAD (By similarity).

Interacts with USP6; the interaction is calcium dependent (By similarity).

Interacts with CDK5RAP2.

Interacts with SCN5A (By similarity).

Interacts with FCHO1.

Interacts with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic domains from two MIP subunits promotes MIP water channel closure.

Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport (By similarity).

Interacts with RYR1 (PubMed:18650434).

Interacts with MYO5A (PubMed:17151196).

Interacts with IQCF1 (PubMed:25380116).

Interacts with SYT7 (PubMed:24569478).

Interacts with CEACAM1 (via cytoplasmic domain); this interaction is in a calcium dependent manner and reduces homophilic cell adhesion through dissociation of dimer (By similarity).

Interacts with RYR2; regulates RYR2 calcium-release channel activity (PubMed:18650434).

Interacts with PCP4; regulates calmodulin calcium-binding (By similarity).

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 (By similarity).

Interacts with alpha-synuclein/SNCA (By similarity).

Interacts with SLC9A1 in a calcium-dependent manner (By similarity). In the absence of Ca(+2), interacts with GIMAP4 (via IQ domain) (PubMed:16569770).

Interacts with SCN8A; the interaction modulates the inactivation rate of SCN8A (PubMed:23942337). Interaction with KIF1A; the interaction is increased in presence of calcium and increases neuronal dense core vesicles motility (By similarity).

Interacts with KCNN3 (By similarity).

Interacts with KCNQ1 (via C-terminus); forms a heterooctameric structure (with 4:4 KCNQ1:CALM stoichiometry) in a calcium-independent manner (By similarity).

Interacts with PIK3C3; the interaction modulates PIK3C3 kinase activity (By similarity).

Interacts with HINT1; interaction increases in the presence of calcium ions (PubMed:31088288).

Interacts with HINT3 (PubMed:31088288).

By similarity7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1006, Calcineurin-Calmodulin-AKAP5 complex, beta-R1 variant
CPX-1007, Calcineurin-Calmodulin complex, gamma-R1 variant
CPX-1008, Calcineurin-Calmodulin complex, beta-R2 variant
CPX-1010, Calcineurin-Calmodulin complex, alpha-R1 variant
CPX-1011, Calcineurin-Calmodulin complex, beta-R1 variant
CPX-1049, Calcineurin-Calmodulin complex, alpha-R2 variant
CPX-1051, Calcineurin-Calmodulin complex, gamma-R2 variant
CPX-106, DAPK1 - calmodulin complex
CPX-1113, Calcineurin-Calmodulin-AKAP5 complex, gamma-R1 variant
CPX-1115, Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant
CPX-1117, Calcineurin-Calmodulin-AKAP5 complex, beta-R2 variant
CPX-1119, Calcineurin-Calmodulin-AKAP5 complex, gamma-R2 variant
CPX-5826, Kv7.1 channel complex
CPX-881, Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant

Protein interaction database and analysis system

More...
IntActi
P0DP26, 24 interactors

Molecular INTeraction database

More...
MINTi
P0DP26

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000019514

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P0DP26, protein

<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
P0DP26

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%5Fand%5Fdomains%5Fsection">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 PCP4By similarityAdd BLAST73

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.By similarity

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0027, Eukaryota

Identification of Orthologs from Complete Genome Data

More...
OMAi
DEMIREP

Database of Orthologous Groups

More...
OrthoDBi
1386217at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00051, EFh, 2 hits

Integrated resource of protein families, domains and functional sites

More...
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

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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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

P0DP26-1 [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
A0A3Q4EHJ0A0A3Q4EHJ0_MOUSE
Calmodulin-1
Calm1 Calm2
113Annotation 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>
G3UX57G3UX57_MOUSE
Calmodulin-3
Calm3
39Annotation 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>
G3UZ90G3UZ90_MOUSE
Calmodulin-3
Calm3
65Annotation 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>
A0A571BE58A0A571BE58_MOUSE
Calmodulin-2
Calm2
37Annotation 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>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti26G → N in AAA66182 (PubMed:3384819).Curated1
Sequence conflicti55E → V in BAE41271 (PubMed:16141072).Curated1
Sequence conflicti69F → L in BAE40191 (PubMed:16141072).Curated1
Sequence conflicti82S → G in BAE31439 (PubMed:16141072).Curated1
Sequence conflicti82S → G in BAE31644 (PubMed:16141072).Curated1
Sequence conflicti82S → G in BAE31442 (PubMed:16141072).Curated1
Sequence conflicti126I → T in BAE31579 (PubMed:16141072).Curated1
Sequence conflicti143V → L in BAB28959 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M19381 mRNA Translation: AAA66182.1
X61432 mRNA Translation: CAA43674.1
AK004673 mRNA Translation: BAB23462.1
AK013695 mRNA Translation: BAB28959.1
AK088141 mRNA Translation: BAC40168.1
AK150288 mRNA Translation: BAE29443.1
AK150978 mRNA Translation: BAE30007.1
AK151001 mRNA Translation: BAE30025.1
AK151552 mRNA Translation: BAE30497.1
AK151784 mRNA Translation: BAE30686.1
AK151923 mRNA Translation: BAE30801.1
AK151992 mRNA Translation: BAE30856.1
AK152148 mRNA Translation: BAE30984.1
AK152715 mRNA Translation: BAE31439.1
AK152719 mRNA Translation: BAE31442.1
AK152850 mRNA Translation: BAE31543.1
AK152897 mRNA Translation: BAE31579.1
AK153004 mRNA Translation: BAE31644.1
AK153348 mRNA Translation: BAE31924.1
AK153426 mRNA Translation: BAE31985.1
AK153546 mRNA Translation: BAE32083.1
AK159762 mRNA Translation: BAE35353.1
AK160057 mRNA Translation: BAE35595.1
AK160508 mRNA Translation: BAE35832.1
AK161302 mRNA Translation: BAE36309.1
AK162314 mRNA Translation: BAE36849.1
AK166308 mRNA Translation: BAE38695.1
AK167353 mRNA Translation: BAE39452.1
AK168002 mRNA Translation: BAE39990.1
AK168241 mRNA Translation: BAE40191.1
AK168663 mRNA Translation: BAE40516.1
AK168803 mRNA Translation: BAE40633.1
AK169027 mRNA Translation: BAE40819.1
AK169055 mRNA Translation: BAE40843.1
AK169640 mRNA Translation: BAE41271.1
BC054805 mRNA Translation: AAH54805.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS36523.1

Protein sequence database of the Protein Information Resource

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PIRi
I49567

NCBI Reference Sequences

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RefSeqi
NP_001300863.1, NM_001313934.1
NP_031615.1, NM_007589.5
NP_031616.1, NM_007590.3
NP_033920.1, NM_009790.5

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000019514; ENSMUSP00000019514; ENSMUSG00000019370
ENSMUST00000040440; ENSMUSP00000048857; ENSMUSG00000036438
ENSMUST00000110082; ENSMUSP00000105709; ENSMUSG00000001175

Database of genes from NCBI RefSeq genomes

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GeneIDi
12313
12314
12315

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:12313
mmu:12314
mmu:12315

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19381 mRNA Translation: AAA66182.1
X61432 mRNA Translation: CAA43674.1
AK004673 mRNA Translation: BAB23462.1
AK013695 mRNA Translation: BAB28959.1
AK088141 mRNA Translation: BAC40168.1
AK150288 mRNA Translation: BAE29443.1
AK150978 mRNA Translation: BAE30007.1
AK151001 mRNA Translation: BAE30025.1
AK151552 mRNA Translation: BAE30497.1
AK151784 mRNA Translation: BAE30686.1
AK151923 mRNA Translation: BAE30801.1
AK151992 mRNA Translation: BAE30856.1
AK152148 mRNA Translation: BAE30984.1
AK152715 mRNA Translation: BAE31439.1
AK152719 mRNA Translation: BAE31442.1
AK152850 mRNA Translation: BAE31543.1
AK152897 mRNA Translation: BAE31579.1
AK153004 mRNA Translation: BAE31644.1
AK153348 mRNA Translation: BAE31924.1
AK153426 mRNA Translation: BAE31985.1
AK153546 mRNA Translation: BAE32083.1
AK159762 mRNA Translation: BAE35353.1
AK160057 mRNA Translation: BAE35595.1
AK160508 mRNA Translation: BAE35832.1
AK161302 mRNA Translation: BAE36309.1
AK162314 mRNA Translation: BAE36849.1
AK166308 mRNA Translation: BAE38695.1
AK167353 mRNA Translation: BAE39452.1
AK168002 mRNA Translation: BAE39990.1
AK168241 mRNA Translation: BAE40191.1
AK168663 mRNA Translation: BAE40516.1
AK168803 mRNA Translation: BAE40633.1
AK169027 mRNA Translation: BAE40819.1
AK169055 mRNA Translation: BAE40843.1
AK169640 mRNA Translation: BAE41271.1
BC054805 mRNA Translation: AAH54805.1
CCDSiCCDS36523.1
PIRiI49567
RefSeqiNP_001300863.1, NM_001313934.1
NP_031615.1, NM_007589.5
NP_031616.1, NM_007590.3
NP_033920.1, NM_009790.5

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UP5X-ray1.90A/B2-149[»]
2DFSelectron microscopy24.00B/C/D/E/F/G/N/O/P/Q/R/S2-149[»]
2IX7X-ray2.50A/B3-147[»]
3WFNX-ray1.95B/C/D/E1-149[»]
4E50X-ray2.70A1-149[»]
4E53X-ray2.69A/B1-149[»]
4HEXX-ray2.00A/B1-149[»]
4ZLKX-ray2.50B1-149[»]
7B1Gelectron microscopy3.60E1-149[»]
7CQPX-ray1.90B1-78[»]
SMRiP0DP26
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-1006, Calcineurin-Calmodulin-AKAP5 complex, beta-R1 variant
CPX-1007, Calcineurin-Calmodulin complex, gamma-R1 variant
CPX-1008, Calcineurin-Calmodulin complex, beta-R2 variant
CPX-1010, Calcineurin-Calmodulin complex, alpha-R1 variant
CPX-1011, Calcineurin-Calmodulin complex, beta-R1 variant
CPX-1049, Calcineurin-Calmodulin complex, alpha-R2 variant
CPX-1051, Calcineurin-Calmodulin complex, gamma-R2 variant
CPX-106, DAPK1 - calmodulin complex
CPX-1113, Calcineurin-Calmodulin-AKAP5 complex, gamma-R1 variant
CPX-1115, Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant
CPX-1117, Calcineurin-Calmodulin-AKAP5 complex, beta-R2 variant
CPX-1119, Calcineurin-Calmodulin-AKAP5 complex, gamma-R2 variant
CPX-5826, Kv7.1 channel complex
CPX-881, Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant
IntActiP0DP26, 24 interactors
MINTiP0DP26
STRINGi10090.ENSMUSP00000019514

Chemistry databases

ChEMBLiCHEMBL3562176

PTM databases

iPTMnetiP0DP26
MetOSiteiP0DP26
PhosphoSitePlusiP0DP26

Proteomic databases

jPOSTiP0DP26

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
39411, 181 antibodies from 17 providers
4344, 534 antibodies from 33 providers
53945, 70 antibodies from 14 providers

The DNASU plasmid repository

More...
DNASUi
12313

Genome annotation databases

EnsembliENSMUST00000019514; ENSMUSP00000019514; ENSMUSG00000019370
ENSMUST00000040440; ENSMUSP00000048857; ENSMUSG00000036438
ENSMUST00000110082; ENSMUSP00000105709; ENSMUSG00000001175
GeneIDi12313
12314
12315
KEGGimmu:12313
mmu:12314
mmu:12315

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
801
805
808
MGIiMGI:88251, Calm1
VEuPathDBiHostDB:ENSMUSG00000001175
HostDB:ENSMUSG00000019370
HostDB:ENSMUSG00000036438

Phylogenomic databases

eggNOGiKOG0027, Eukaryota
OMAiDEMIREP
OrthoDBi1386217at2759

Enzyme and pathway databases

ReactomeiR-MMU-111932, CaMK IV-mediated phosphorylation of CREB
R-MMU-111933, Calmodulin induced events
R-MMU-111957, Cam-PDE 1 activation
R-MMU-114608, Platelet degranulation
R-MMU-1474151, Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-MMU-163615, PKA activation
R-MMU-1855204, Synthesis of IP3 and IP4 in the cytosol
R-MMU-2025928, Calcineurin activates NFAT
R-MMU-203615, eNOS activation
R-MMU-2514859, Inactivation, recovery and regulation of the phototransduction cascade
R-MMU-2672351, Stimuli-sensing channels
R-MMU-2871809, FCERI mediated Ca+2 mobilization
R-MMU-4086398, Ca2+ pathway
R-MMU-418359, Reduction of cytosolic Ca++ levels
R-MMU-425561, Sodium/Calcium exchangers
R-MMU-438066, Unblocking of NMDA receptors, glutamate binding and activation
R-MMU-442729, CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde
R-MMU-445355, Smooth Muscle Contraction
R-MMU-451308, Activation of Ca-permeable Kainate Receptor
R-MMU-5218920, VEGFR2 mediated vascular permeability
R-MMU-5576892, Phase 0 - rapid depolarisation
R-MMU-5578775, Ion homeostasis
R-MMU-5607763, CLEC7A (Dectin-1) induces NFAT activation
R-MMU-5626467, RHO GTPases activate IQGAPs
R-MMU-5627123, RHO GTPases activate PAKs
R-MMU-5673000, RAF activation
R-MMU-5673001, RAF/MAP kinase cascade
R-MMU-70221, Glycogen breakdown (glycogenolysis)
R-MMU-8876725, Protein methylation
R-MMU-9009391, Extra-nuclear estrogen signaling
R-MMU-936837, Ion transport by P-type ATPases
R-MMU-9619229, Activation of RAC1 downstream of NMDARs
R-MMU-9648002, RAS processing

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
12313, 4 hits in 67 CRISPR screens
12314, 1 hit in 62 CRISPR screens
12315, 1 hit in 64 CRISPR screens

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

More...
ChiTaRSi
Calm1, mouse

Protein Ontology

More...
PROi
PR:P0DP26
RNActiP0DP26, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

ExpressionAtlasiP0DP26, baseline and differential

Family and domain databases

CDDicd00051, EFh, 2 hits
InterProiView protein in InterPro
IPR011992, EF-hand-dom_pair
IPR018247, EF_Hand_1_Ca_BS
IPR002048, EF_hand_dom
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

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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_MOUSE
<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: P0DP26
Secondary accession number(s): P02593
, P62204, P70667, P99014, Q3TEH7, Q3THK5, Q3U6Z5, Q3U7C7, Q498A3, Q61379, Q61380, Q8BNC9, Q91VQ9, Q9D6G4
<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%5Fand%5Fisoforms">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: February 23, 2022
This is version 38 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

<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, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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