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P62204 (CALM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calmodulin

Short name=CaM
Gene names
Name:Calm1
Synonyms:Calm, Cam, Cam1
AND
Name:Calm2
Synonyms:Cam2, Camb
AND
Name:Calm3
Synonyms:Cam3, Camc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.9

Subcellular location

Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonspindle pole. Note: Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules By similarity.

Post-translational modification

Ubiquitination results in a strongly decreased activity By similarity.

Phosphorylation results in a decreased activity By similarity.

Miscellaneous

This protein has four functional calcium-binding sites.

Sequence similarities

Belongs to the calmodulin family.

Contains 4 EF-hand domains.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   DomainRepeat
   LigandCalcium
Metal-binding
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of adenylate cyclase activity

Inferred from electronic annotation. Source: Ensembl

calcium-mediated signaling

Inferred from electronic annotation. Source: Ensembl

detection of calcium ion

Inferred from electronic annotation. Source: Ensembl

positive regulation of cyclic-nucleotide phosphodiesterase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric-oxide synthase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein dephosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of ryanodine-sensitive calcium-release channel activity

Inferred from electronic annotation. Source: Ensembl

regulation of cardiac muscle contraction

Inferred from electronic annotation. Source: Ensembl

regulation of cytokinesis

Inferred from electronic annotation. Source: Ensembl

regulation of heart rate

Inferred from electronic annotation. Source: Ensembl

regulation of high voltage-gated calcium channel activity

Inferred from electronic annotation. Source: Ensembl

regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

response to corticosterone

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcalcium channel complex

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

growth cone

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

sarcomere

Inferred from electronic annotation. Source: Ensembl

spindle microtubule

Inferred from electronic annotation. Source: Ensembl

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: Ensembl

nitric-oxide synthase regulator activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 12051765PubMed 15102471PubMed 19423573. Source: IntAct

protein phosphatase activator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 149148Calmodulin
PRO_0000198224

Regions

Domain8 – 4336EF-hand 1
Domain44 – 7936EF-hand 2
Domain81 – 11636EF-hand 3
Domain117 – 14933EF-hand 4
Calcium binding21 – 32121
Calcium binding57 – 68122
Calcium binding94 – 105123
Calcium binding130 – 141124

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Modified residue221N6-acetyllysine; alternate Ref.11
Modified residue451Phosphothreonine; by CaMK4 By similarity
Modified residue951N6-acetyllysine By similarity
Modified residue1001Phosphotyrosine Ref.10
Modified residue1021Phosphoserine By similarity
Modified residue1161N6,N6,N6-trimethyllysine By similarity
Modified residue1391Phosphotyrosine By similarity
Cross-link22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Experimental info

Sequence conflict261G → N in AAA66182. Ref.1
Sequence conflict551E → V in BAE41271. Ref.5
Sequence conflict691F → L in BAE40191. Ref.5
Sequence conflict821S → G in BAE31439. Ref.5
Sequence conflict821S → G in BAE31644. Ref.5
Sequence conflict821S → G in BAE31442. Ref.5
Sequence conflict1261I → T in BAE31579. Ref.5
Sequence conflict1421F → S in BAC39089. Ref.5
Sequence conflict1431V → L in BAB28959. Ref.5

Secondary structure

......................... 149
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62204 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6B4BC3FCDE10727B

FASTA14916,838
        10         20         30         40         50         60 
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG 

        70         80         90        100        110        120 
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE 

       130        140 
EVDEMIREAD IDGDGQVNYE EFVQMMTAK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS36523.1.
CCDS37716.1.
CCDS39789.1.
PIRI49567.
S37707.
RefSeqNP_031615.1. NM_007589.5.
NP_031616.1. NM_007590.3.
NP_033920.1. NM_009790.4.
UniGeneMm.285993.
Mm.288630.
Mm.329243.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP62204.
SMRP62204. Positions 1-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198454. 13 interactions.
198455. 3 interactions.
198456. 1 interaction.
IntActP62204. 23 interactions.
MINTMINT-4996917.

Chemistry

BindingDBP62204.

PTM databases

PhosphoSiteP62204.

2D gel databases

REPRODUCTION-2DPAGEP62204.
SWISS-2DPAGEP62204.

Proteomic databases

MaxQBP62204.
PaxDbP62204.
PRIDEP62204.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019514; ENSMUSP00000019514; ENSMUSG00000019370.
ENSMUST00000040440; ENSMUSP00000048857; ENSMUSG00000036438.
ENSMUST00000110082; ENSMUSP00000105709; ENSMUSG00000001175.
GeneID12313.
12314.
12315.
KEGGmmu:12313.
mmu:12314.
mmu:12315.
UCSCuc007osq.1. mouse.

Organism-specific databases

CTD801.
805.
808.
MGIMGI:88251. Calm1.
MGI:103250. Calm2.
MGI:103249. Calm3.

Phylogenomic databases

eggNOGCOG5126.
GeneTreeENSGT00690000101867.
HOVERGENHBG012180.
InParanoidP62204.
KOK02183.
OMATEQISEF.
OrthoDBEOG7F7WBV.
PhylomeDBP62204.
TreeFamTF300912.

Enzyme and pathway databases

ReactomeREACT_118809. Calcineurin Dephosphorylates Nfatc2.
REACT_147847. Translocation of Glut4 to the Plasma Membrane.
REACT_209837. Membrane Trafficking.

Gene expression databases

ArrayExpressP62204.
BgeeP62204.
CleanExMM_CALM1.
MM_CALM2.
MM_CALM3.
GenevestigatorP62204.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTSM00054. EFh. 4 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCALM1. mouse.
CALM2. mouse.
CALM3. mouse.
EvolutionaryTraceP62204.
NextBio280868.
PROP62204.
SOURCESearch...

Entry information

Entry nameCALM_MOUSE
AccessionPrimary (citable) accession number: P62204
Secondary accession number(s): P02593 expand/collapse secondary AC list , P70667, P99014, Q3TEH7, Q3THK5, Q3U6Z5, Q3U7C7, Q498A3, Q61379, Q61380, Q8BNC9, Q91VQ9, Q9D6G4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot