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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)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi21 – 32121Add
BLAST
Calcium bindingi57 – 68122Add
BLAST
Calcium bindingi94 – 105123Add
BLAST
Calcium bindingi130 – 141124Add
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_271639. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_273079. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_278552. Activation of Ca-permeable Kainate Receptor.
REACT_292811. Glycogen breakdown (glycogenolysis).
REACT_294637. CREB phosphorylation through the activation of CaMKK.
REACT_299722. VEGFR2 mediated cell proliferation.
REACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_307071. Platelet degranulation.
REACT_309030. Cam-PDE 1 activation.
REACT_309693. CaMK IV-mediated phosphorylation of CREB.
REACT_309838. CREB phosphorylation through the activation of CaMKII.
REACT_315352. CaM pathway.
REACT_321652. Synthesis of IP3 and IP4 in the cytosol.
REACT_321965. VEGFR2 mediated vascular permeability.
REACT_324232. Smooth Muscle Contraction.
REACT_325290. DARPP-32 events.
REACT_331823. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_331940. Ca2+ pathway.
REACT_332567. Calmodulin induced events.
REACT_334845. Activation of CaMK IV.
REACT_342348. eNOS activation.
REACT_348733. FCERI mediated Ca+2 mobilization.
REACT_358203. RHO GTPases activate IQGAPs.
REACT_359280. RHO GTPases activate PAKs.
REACT_362087. CLEC7A (Dectin-1) induces NFAT activation.

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
ProteomesiUP000000589 Componentsi: Chromosome 12, Chromosome 17, Chromosome 7

Organism-specific databases

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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 149148CalmodulinPRO_0000198224Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei22 – 221N6-acetyllysine; alternate1 Publication
Cross-linki22 – 22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei45 – 451Phosphothreonine; by CaMK4By similarity
Modified residuei95 – 951N6-acetyllysineBy similarity
Modified residuei100 – 1001Phosphotyrosine1 Publication
Modified residuei102 – 1021PhosphoserineBy similarity
Modified residuei111 – 1111PhosphothreonineBy similarity
Modified residuei116 – 1161N6,N6,N6-trimethyllysineBy similarity
Modified residuei139 – 1391PhosphotyrosineBy similarity

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

MaxQBiP62204.
PaxDbiP62204.
PRIDEiP62204.

2D gel databases

REPRODUCTION-2DPAGEP62204.
SWISS-2DPAGEP62204.

PTM databases

PhosphoSiteiP62204.

Expressioni

Gene expression databases

BgeeiP62204.
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. Interacts with MYO5A.By similarity2 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. 15 interactions.
198455. 3 interactions.
198456. 1 interaction.
DIPiDIP-31550N.
IntActiP62204. 23 interactions.
MINTiMINT-4996917.
STRINGi10090.ENSMUSP00000105709.

Structurei

Secondary structure

1
149
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 43Combined sources
Helixi7 – 1913Combined sources
Beta strandi22 – 298Combined sources
Helixi30 – 323Combined sources
Helixi33 – 397Combined sources
Helixi46 – 549Combined sources
Beta strandi63 – 653Combined sources
Helixi66 – 9328Combined sources
Beta strandi98 – 1025Combined sources
Helixi103 – 11210Combined sources
Beta strandi113 – 1153Combined sources
Helixi119 – 12810Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi136 – 1383Combined sources
Helixi139 – 1468Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP62204.
SMRiP62204. Positions 1-149.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62204.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 4336EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini44 – 7936EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini81 – 11636EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini117 – 14933EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00760000118901.
HOVERGENiHBG012180.
InParanoidiP62204.
KOiK02183.
OMAiGRRKSHC.
OrthoDBiEOG7F7WBV.
PhylomeDBiP62204.
TreeFamiTF300912.

Family and domain databases

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]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261G → N in AAA66182 (PubMed:3384819).Curated
Sequence conflicti55 – 551E → V in BAE41271 (PubMed:16141072).Curated
Sequence conflicti69 – 691F → L in BAE40191 (PubMed:16141072).Curated
Sequence conflicti82 – 821S → G in BAE31439 (PubMed:16141072).Curated
Sequence conflicti82 – 821S → G in BAE31644 (PubMed:16141072).Curated
Sequence conflicti82 – 821S → G in BAE31442 (PubMed:16141072).Curated
Sequence conflicti126 – 1261I → T in BAE31579 (PubMed:16141072).Curated
Sequence conflicti142 – 1421F → S in BAC39089 (PubMed:16141072).Curated
Sequence conflicti143 – 1431V → L in BAB28959 (PubMed:16141072).Curated

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_031615.1. NM_007589.5.
NP_031616.1. NM_007590.3.
NP_033920.1. NM_009790.4.
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_031615.1. NM_007589.5.
NP_031616.1. NM_007590.3.
NP_033920.1. NM_009790.4.
UniGeneiMm.285993.
Mm.288630.
Mm.329243.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP62204.
SMRiP62204. Positions 1-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198454. 15 interactions.
198455. 3 interactions.
198456. 1 interaction.
DIPiDIP-31550N.
IntActiP62204. 23 interactions.
MINTiMINT-4996917.
STRINGi10090.ENSMUSP00000105709.

Chemistry

BindingDBiP62204.

PTM databases

PhosphoSiteiP62204.

2D gel databases

REPRODUCTION-2DPAGEP62204.
SWISS-2DPAGEP62204.

Proteomic databases

MaxQBiP62204.
PaxDbiP62204.
PRIDEiP62204.

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

eggNOGiCOG5126.
GeneTreeiENSGT00760000118901.
HOVERGENiHBG012180.
InParanoidiP62204.
KOiK02183.
OMAiGRRKSHC.
OrthoDBiEOG7F7WBV.
PhylomeDBiP62204.
TreeFamiTF300912.

Enzyme and pathway databases

ReactomeiREACT_271639. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_273079. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_278552. Activation of Ca-permeable Kainate Receptor.
REACT_292811. Glycogen breakdown (glycogenolysis).
REACT_294637. CREB phosphorylation through the activation of CaMKK.
REACT_299722. VEGFR2 mediated cell proliferation.
REACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_307071. Platelet degranulation.
REACT_309030. Cam-PDE 1 activation.
REACT_309693. CaMK IV-mediated phosphorylation of CREB.
REACT_309838. CREB phosphorylation through the activation of CaMKII.
REACT_315352. CaM pathway.
REACT_321652. Synthesis of IP3 and IP4 in the cytosol.
REACT_321965. VEGFR2 mediated vascular permeability.
REACT_324232. Smooth Muscle Contraction.
REACT_325290. DARPP-32 events.
REACT_331823. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_331940. Ca2+ pathway.
REACT_332567. Calmodulin induced events.
REACT_334845. Activation of CaMK IV.
REACT_342348. eNOS activation.
REACT_348733. FCERI mediated Ca+2 mobilization.
REACT_358203. RHO GTPases activate IQGAPs.
REACT_359280. RHO GTPases activate PAKs.
REACT_362087. CLEC7A (Dectin-1) induces NFAT activation.

Miscellaneous databases

ChiTaRSiCalm1. mouse.
Calm2. mouse.
Calm3. mouse.
EvolutionaryTraceiP62204.
NextBioi280868.
PROiP62204.
SOURCEiSearch...

Gene expression databases

BgeeiP62204.
CleanExiMM_CALM1.
MM_CALM2.
MM_CALM3.
ExpressionAtlasiP62204. baseline and differential.
GenevisibleiP62204. MM.

Family and domain databases

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]
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The abundance of calmodulin mRNAs is regulated in phosphorylase kinase-deficient skeletal muscle."
    Bender P.K., Dedman J.R., Emerson C.P. Jr.
    J. Biol. Chem. 263:9733-9737(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and expression of mouse-brain calmodulin as an activator of Bordetella pertussis adenylate cyclase in Escherichia coli."
    Danchin A., Sezer O., Glaser P., Chalon P., Caput D.
    Gene 80:145-149(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  3. "Genome-wide isolation of growth and obesity QTL using mouse speed congenic strains."
    Farber C.R., Corva P.M., Medrano J.F.
    BMC Genomics 7:102-102(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CAST/EiJ.
    Tissue: Brain.
  4. "A collection of cDNA clones with specific expression patterns in mouse brain."
    Kato K.
    Eur. J. Neurosci. 2:704-711(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/c.
    Tissue: Brain.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J, DBA/2 and NOD.
    Tissue: Amnion, Bone marrow, Colon, Hippocampus, Kidney, Liver, Lung, Mammary gland, Ovary, Placenta, Stomach, Testis, Thymus and Tongue.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: 129, C57BL/6 and Czech II.
    Tissue: Brain, Mammary tumor, Placenta and Spinal ganglion.
  7. Bienvenut W.V.
    Submitted (JUL-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Liver.
  8. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 15-31; 79-87 AND 92-107, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  9. "S100A1 and calmodulin compete for the same binding site on ryanodine receptor."
    Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F., Weber D.J.
    J. Biol. Chem. 283:26676-26683(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RYR1 AND RYR2.
  10. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  12. "Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features."
    Houdusse A., Gaucher J.F., Krementsova E., Mui S., Trybus K.M., Cohen C.
    Proc. Natl. Acad. Sci. U.S.A. 103:19326-19331(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-147 IN COMPLEX WITH MYO5A.

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: July 22, 2015
This is version 138 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

External Data

Dasty 3

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 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.