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Protein

Calmodulin

Gene

Calm1

more
Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Regions

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

GO - Molecular functioni

  • calcium ion binding Source: MGI

GO - Biological processi

  • G2/M transition of mitotic cell cycle Source: MGI
  • membrane organization Source: Reactome
  • positive regulation of DNA binding Source: MGI
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

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-1445148. Translocation of GLUT4 to the plasma membrane.
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-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-442717. CREB phosphorylation through the activation of CaMKK.
R-MMU-442729. CREB phosphorylation through the activation of CaMKII.
R-MMU-442745. Activation of CaMK IV.
R-MMU-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
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-5673001. RAF/MAP kinase cascade.
R-MMU-70221. Glycogen breakdown (glycogenolysis).
R-MMU-936837. Ion transport by P-type ATPases.

Names & Taxonomyi

Protein namesi
Recommended name:
Calmodulin
Short name:
CaM
Gene namesi
Name:Calm1
Synonyms:Calm, Cam, Cam1
AND
Name:Calm2
Synonyms:Cam2, Camb
AND
Name:Calm3
Synonyms:Cam3, Camc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componentsi: Chromosome 12, Chromosome 17, Chromosome 7

Organism-specific databases

MGIiMGI:88251. Calm1.
MGI:103250. Calm2.
MGI:103249. Calm3.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • spindle pole Source: UniProtKB-SubCell
  • voltage-gated potassium channel complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3562176.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001982242 – 149CalmodulinAdd BLAST148

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei22N6-acetyllysine; alternateCombined sources1
Cross-linki22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei45Phosphothreonine; by CaMK4By similarity1
Modified 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

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

EPDiP62204.
MaxQBiP62204.
PaxDbiP62204.
PeptideAtlasiP62204.
PRIDEiP62204.
TopDownProteomicsiP62204.

2D gel databases

REPRODUCTION-2DPAGEP62204.
SWISS-2DPAGEP62204.

PTM databases

iPTMnetiP62204.
PhosphoSitePlusiP62204.

Expressioni

Gene expression databases

BgeeiENSMUSG00000001175.
CleanExiMM_CALM1.
MM_CALM2.
MM_CALM3.
ExpressionAtlasiP62204. baseline and differential.
GenevisibleiP62204. MM.

Interactioni

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 and RYR2 (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).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ccp110Q7TSH44EBI-397460,EBI-646843
Kcnma1Q084604EBI-397460,EBI-1633915
PPEF1O148292EBI-397460,EBI-2931238From a different organism.
PPEF2O148302EBI-397460,EBI-2931306From a different organism.

Protein-protein interaction databases

BioGridi198454. 16 interactors.
198455. 4 interactors.
198456. 2 interactors.
DIPiDIP-31550N.
IntActiP62204. 23 interactors.
MINTiMINT-4996917.
STRINGi10090.ENSMUSP00000105709.

Structurei

Secondary structure

1149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 4Combined sources3
Helixi7 – 19Combined sources13
Beta strandi22 – 29Combined sources8
Helixi30 – 32Combined sources3
Helixi33 – 39Combined sources7
Helixi46 – 54Combined sources9
Beta strandi63 – 65Combined sources3
Helixi66 – 93Combined sources28
Beta strandi98 – 102Combined sources5
Helixi103 – 112Combined sources10
Beta strandi113 – 115Combined sources3
Helixi119 – 128Combined sources10
Beta strandi131 – 133Combined sources3
Beta strandi136 – 138Combined sources3
Helixi139 – 146Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
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[»]
ProteinModelPortaliP62204.
SMRiP62204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62204.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118901.
HOVERGENiHBG012180.
InParanoidiP62204.
KOiK02183.
OMAiHRISGKA.
OrthoDBiEOG091G0V73.
PhylomeDBiP62204.
TreeFamiTF300912.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

P62204-1 [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:January 23, 2007 - v2
Checksum:i6B4BC3FCDE10727B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 conflicti142F → S in BAC39089 (PubMed:16141072).Curated1
Sequence conflicti143V → L in BAB28959 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19380 mRNA. Translation: AAA66181.1.
M19381 mRNA. Translation: AAA66182.1.
L31642 mRNA. Translation: AAA65934.1.
M27844 Genomic DNA. Translation: AAA37365.1.
AY902353 Genomic DNA. Translation: AAY21063.1.
X61432 mRNA. Translation: CAA43674.1.
AK004673 mRNA. Translation: BAB23462.1.
AK012247 mRNA. Translation: BAB28116.1.
AK012564 mRNA. Translation: BAB28319.1.
AK013068 mRNA. Translation: BAB28631.1.
AK013695 mRNA. Translation: BAB28959.1.
AK083996 mRNA. Translation: BAC39089.2.
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.
AK151610 mRNA. Translation: BAE30549.1.
AK151784 mRNA. Translation: BAE30686.1.
AK151923 mRNA. Translation: BAE30801.1.
AK151992 mRNA. Translation: BAE30856.1.
AK152148 mRNA. Translation: BAE30984.1.
AK152303 mRNA. Translation: BAE31109.1.
AK152715 mRNA. Translation: BAE31439.1.
AK152719 mRNA. Translation: BAE31442.1.
AK152754 mRNA. Translation: BAE31469.1.
AK152850 mRNA. Translation: BAE31543.1.
AK152897 mRNA. Translation: BAE31579.1.
AK153004 mRNA. Translation: BAE31644.1.
AK153179 mRNA. Translation: BAE31782.1.
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.
AK160636 mRNA. Translation: BAE35930.1.
AK161268 mRNA. Translation: BAE36280.1.
AK161302 mRNA. Translation: BAE36309.1.
AK161984 mRNA. Translation: BAE36667.1.
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.
AK168741 mRNA. Translation: BAE40582.1.
AK168803 mRNA. Translation: BAE40633.1.
AK169027 mRNA. Translation: BAE40819.1.
AK169055 mRNA. Translation: BAE40843.1.
AK169640 mRNA. Translation: BAE41271.1.
BC010730 mRNA. Translation: AAH10730.1.
BC021347 mRNA. Translation: AAH21347.1.
BC050926 mRNA. Translation: AAH50926.1.
BC051444 mRNA. Translation: AAH51444.1.
BC054805 mRNA. Translation: AAH54805.1.
BC100301 mRNA. Translation: AAI00302.1.
CCDSiCCDS36523.1.
CCDS37716.1.
CCDS39789.1.
PIRiI49567.
S37707.
RefSeqiNP_001300863.1. NM_001313934.1.
NP_031615.1. NM_007589.5.
NP_031616.1. NM_007590.3.
NP_033920.1. NM_009790.5.
UniGeneiMm.285993.
Mm.288630.
Mm.329243.

Genome annotation databases

EnsembliENSMUST00000019514; ENSMUSP00000019514; ENSMUSG00000019370.
ENSMUST00000040440; ENSMUSP00000048857; ENSMUSG00000036438.
ENSMUST00000110082; ENSMUSP00000105709; ENSMUSG00000001175.
GeneIDi12313.
12314.
12315.
KEGGimmu:12313.
mmu:12314.
mmu:12315.
UCSCiuc007osq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19380 mRNA. Translation: AAA66181.1.
M19381 mRNA. Translation: AAA66182.1.
L31642 mRNA. Translation: AAA65934.1.
M27844 Genomic DNA. Translation: AAA37365.1.
AY902353 Genomic DNA. Translation: AAY21063.1.
X61432 mRNA. Translation: CAA43674.1.
AK004673 mRNA. Translation: BAB23462.1.
AK012247 mRNA. Translation: BAB28116.1.
AK012564 mRNA. Translation: BAB28319.1.
AK013068 mRNA. Translation: BAB28631.1.
AK013695 mRNA. Translation: BAB28959.1.
AK083996 mRNA. Translation: BAC39089.2.
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.
AK151610 mRNA. Translation: BAE30549.1.
AK151784 mRNA. Translation: BAE30686.1.
AK151923 mRNA. Translation: BAE30801.1.
AK151992 mRNA. Translation: BAE30856.1.
AK152148 mRNA. Translation: BAE30984.1.
AK152303 mRNA. Translation: BAE31109.1.
AK152715 mRNA. Translation: BAE31439.1.
AK152719 mRNA. Translation: BAE31442.1.
AK152754 mRNA. Translation: BAE31469.1.
AK152850 mRNA. Translation: BAE31543.1.
AK152897 mRNA. Translation: BAE31579.1.
AK153004 mRNA. Translation: BAE31644.1.
AK153179 mRNA. Translation: BAE31782.1.
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.
AK160636 mRNA. Translation: BAE35930.1.
AK161268 mRNA. Translation: BAE36280.1.
AK161302 mRNA. Translation: BAE36309.1.
AK161984 mRNA. Translation: BAE36667.1.
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.
AK168741 mRNA. Translation: BAE40582.1.
AK168803 mRNA. Translation: BAE40633.1.
AK169027 mRNA. Translation: BAE40819.1.
AK169055 mRNA. Translation: BAE40843.1.
AK169640 mRNA. Translation: BAE41271.1.
BC010730 mRNA. Translation: AAH10730.1.
BC021347 mRNA. Translation: AAH21347.1.
BC050926 mRNA. Translation: AAH50926.1.
BC051444 mRNA. Translation: AAH51444.1.
BC054805 mRNA. Translation: AAH54805.1.
BC100301 mRNA. Translation: AAI00302.1.
CCDSiCCDS36523.1.
CCDS37716.1.
CCDS39789.1.
PIRiI49567.
S37707.
RefSeqiNP_001300863.1. NM_001313934.1.
NP_031615.1. NM_007589.5.
NP_031616.1. NM_007590.3.
NP_033920.1. NM_009790.5.
UniGeneiMm.285993.
Mm.288630.
Mm.329243.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
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[»]
ProteinModelPortaliP62204.
SMRiP62204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198454. 16 interactors.
198455. 4 interactors.
198456. 2 interactors.
DIPiDIP-31550N.
IntActiP62204. 23 interactors.
MINTiMINT-4996917.
STRINGi10090.ENSMUSP00000105709.

Chemistry databases

ChEMBLiCHEMBL3562176.

PTM databases

iPTMnetiP62204.
PhosphoSitePlusiP62204.

2D gel databases

REPRODUCTION-2DPAGEP62204.
SWISS-2DPAGEP62204.

Proteomic databases

EPDiP62204.
MaxQBiP62204.
PaxDbiP62204.
PeptideAtlasiP62204.
PRIDEiP62204.
TopDownProteomicsiP62204.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019514; ENSMUSP00000019514; ENSMUSG00000019370.
ENSMUST00000040440; ENSMUSP00000048857; ENSMUSG00000036438.
ENSMUST00000110082; ENSMUSP00000105709; ENSMUSG00000001175.
GeneIDi12313.
12314.
12315.
KEGGimmu:12313.
mmu:12314.
mmu:12315.
UCSCiuc007osq.1. mouse.

Organism-specific databases

CTDi801.
805.
808.
MGIiMGI:88251. Calm1.
MGI:103250. Calm2.
MGI:103249. Calm3.

Phylogenomic databases

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118901.
HOVERGENiHBG012180.
InParanoidiP62204.
KOiK02183.
OMAiHRISGKA.
OrthoDBiEOG091G0V73.
PhylomeDBiP62204.
TreeFamiTF300912.

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-1445148. Translocation of GLUT4 to the plasma membrane.
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-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-442717. CREB phosphorylation through the activation of CaMKK.
R-MMU-442729. CREB phosphorylation through the activation of CaMKII.
R-MMU-442745. Activation of CaMK IV.
R-MMU-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
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-5673001. RAF/MAP kinase cascade.
R-MMU-70221. Glycogen breakdown (glycogenolysis).
R-MMU-936837. Ion transport by P-type ATPases.

Miscellaneous databases

ChiTaRSiCalm1. mouse.
Calm2. mouse.
Calm3. mouse.
EvolutionaryTraceiP62204.
PROiP62204.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000001175.
CleanExiMM_CALM1.
MM_CALM2.
MM_CALM3.
ExpressionAtlasiP62204. baseline and differential.
GenevisibleiP62204. MM.

Family and domain databases

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

Entry informationi

Entry nameiCALM_MOUSE
AccessioniPrimary (citable) accession number: P62204
Secondary accession number(s): P02593
, P70667, P99014, Q3TEH7, Q3THK5, Q3U6Z5, Q3U7C7, Q498A3, Q61379, Q61380, Q8BNC9, Q91VQ9, Q9D6G4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein has four functional calcium-binding sites.

Keywords - Technical termi

3D-structure, Complete proteome, 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

Similar proteinsi

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