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P62158 (CALM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (9) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·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:CALML2, CAM3, CAMC, CAMIII
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.21 Ref.45

Subunit structure

Interacts with MYO1C, MYO5A and RRAD. Interacts with MYO10 By similarity. Interacts with CEP97, CCP110, TTN/titin and SRY. Interacts with USP6; the interaction is calcium dependent. Interacts with CDK5RAP2. Interacts with SCN5A. Interacts with RYR1 and RYR2. 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. Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.28 Ref.31 Ref.33 Ref.45

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. Ref.21

Post-translational modification

Ubiquitination results in a strongly decreased activity By similarity.

Phosphorylation results in a decreased activity By similarity.

Involvement in disease

Ventricular tachycardia, catecholaminergic polymorphic, 4 (CPVT4) [MIM:614916]: An arrhythmogenic disorder characterized by stress-induced, bidirectional ventricular tachycardia that may degenerate into cardiac arrest and cause sudden death. Patients present with recurrent syncope, seizures, or sudden death after physical activity or emotional stress.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.46

Miscellaneous

This protein has four functional calcium-binding sites.

Sequence similarities

Belongs to the calmodulin family.

Contains 4 EF-hand domains.

Sequence caution

The sequence CAA36839.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityPolymorphism
   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_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

G-protein coupled receptor signaling pathway

Traceable author statement PubMed 10899953. Source: UniProtKB

activation of adenylate cyclase activity

Inferred from electronic annotation. Source: Ensembl

activation of phospholipase C activity

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Traceable author statement. Source: Reactome

detection of calcium ion

Inferred from mutant phenotype Ref.46. Source: BHF-UCL

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

glucose metabolic process

Traceable author statement. Source: Reactome

glycogen catabolic process

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

inositol phosphate metabolic process

Traceable author statement. Source: Reactome

membrane organization

Traceable author statement. Source: Reactome

muscle contraction

Traceable author statement. Source: Reactome

negative regulation of ryanodine-sensitive calcium-release channel activity

Inferred from sequence or structural similarity. Source: BHF-UCL

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

nitric oxide metabolic process

Traceable author statement. Source: Reactome

phototransduction, visible light

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of cyclic nucleotide metabolic process

Inferred from direct assay PubMed 8631777. Source: BHF-UCL

positive regulation of cyclic-nucleotide phosphodiesterase activity

Inferred from direct assay PubMed 8631777. Source: BHF-UCL

positive regulation of nitric-oxide synthase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphoprotein phosphatase activity

Inferred from direct assay PubMed 8631777. Source: BHF-UCL

positive regulation of protein dephosphorylation

Inferred from direct assay PubMed 8631777. Source: BHF-UCL

positive regulation of ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 20226167. Source: BHF-UCL

regulation of cardiac muscle contraction

Inferred from mutant phenotype Ref.46. Source: BHF-UCL

regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

Inferred by curator. Source: BHF-UCL

regulation of cell communication by electrical coupling involved in cardiac conduction

Inferred by curator. Source: BHF-UCL

regulation of cytokinesis

Inferred from mutant phenotype Ref.21. Source: UniProtKB

regulation of heart rate

Inferred from mutant phenotype Ref.46. Source: BHF-UCL

regulation of high voltage-gated calcium channel activity

Inferred from electronic annotation. Source: Ensembl

regulation of nitric-oxide synthase activity

Traceable author statement. Source: Reactome

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

Inferred from direct assay PubMed 20226167. Source: BHF-UCL

regulation of rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from direct assay PubMed 7607248. Source: BHF-UCL

response to corticosterone

Inferred from electronic annotation. Source: Ensembl

rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentcentrosome

Inferred from direct assay Ref.21. Source: UniProtKB

cytoplasm

Traceable author statement PubMed 10899953. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

growth cone

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

plasma membrane

Traceable author statement PubMed 10899953. Source: UniProtKB

sarcomere

Inferred from direct assay PubMed 20226167. Source: BHF-UCL

spindle microtubule

Inferred from direct assay Ref.21. Source: UniProtKB

spindle pole

Inferred from direct assay Ref.21. Source: UniProtKB

   Molecular_functionN-terminal myristoylation domain binding

Inferred from physical interaction PubMed 15632291. Source: UniProtKB

calcium ion binding

Inferred from direct assay Ref.46PubMed 7607248PubMed 8631777. Source: BHF-UCL

ion channel binding

Inferred from physical interaction Ref.44Ref.46. Source: BHF-UCL

nitric-oxide synthase regulator activity

Inferred from electronic annotation. Source: Ensembl

phospholipase binding

Inferred from physical interaction PubMed 12821674. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 10692436PubMed 15140941Ref.21PubMed 17582331Ref.28PubMed 3111527. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 11984006. Source: UniProtKB

protein phosphatase activator activity

Inferred from direct assay PubMed 8631777. Source: BHF-UCL

thioesterase binding

Inferred from physical interaction Ref.18. Source: UniProtKB

titin binding

Inferred from physical interaction PubMed 7607248. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13 Ref.14
Chain2 – 149148Calmodulin
PRO_0000198223

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.13 Ref.14 Ref.25 Ref.32 Ref.34
Modified residue221N6-acetyllysine; alternate Ref.27
Modified residue451Phosphothreonine; by CaMK4 By similarity
Modified residue951N6-acetyllysine Ref.27
Modified residue1001Phosphotyrosine Ref.24 Ref.26
Modified residue1021Phosphoserine Ref.30
Modified residue1161N6,N6,N6-trimethyllysine Ref.13
Modified residue1391Phosphotyrosine Ref.26
Cross-link22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Natural variations

Natural variant541N → I in CPVT4; the mutant has significantly reduced Ca(2+) affinity compared to wild-type. Ref.46
VAR_069222
Natural variant731M → T.
Corresponds to variant rs41389749 [ dbSNP | Ensembl ].
VAR_048585
Natural variant981N → S in CPVT4; the mutant has significantly reduced Ca(2+) affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations. Ref.46
VAR_069223

Experimental info

Sequence conflict1241E → Q in AAH08437. Ref.12

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P62158 [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]"Isolation and nucleotide sequence of a cDNA encoding human calmodulin."
Wawrzynczak E.J., Perham R.N.
Biochem. Int. 9:177-185(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species."
Sengupta B., Friedberg F., Detera-Wadleigh S.D.
J. Biol. Chem. 262:16663-16670(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Multiple divergent mRNAs code for a single human calmodulin."
Fischer R., Koller M., Flura M., Mathews S., Strehler-Page M.A., Krebs J., Penniston J.T., Carafoli E., Strehler E.E.
J. Biol. Chem. 263:17055-17062(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Structural organization of the human CaMIII calmodulin gene."
Koller M., Schnyder B., Strehler E.E.
Biochim. Biophys. Acta 1087:180-189(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CALM3).
Tissue: Blood.
[5]"Structure of the human CALM1 calmodulin gene and identification of two CALM1-related pseudogenes CALM1P1 and CALM1P2."
Rhyner J.A., Ottiger M., Wicki R., Greenwood T.M., Strehler E.E.
Eur. J. Biochem. 225:71-82(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CALM1).
Tissue: Blood.
[6]"Human calmodulin cDNA."
Kato S.
Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lymphoma.
[7]"Characterization of the human CALM2 calmodulin gene and comparison of the transcriptional activity of CALM1, CALM2 and CALM3."
Toutenhoofd S.L., Foletti D., Wicki R., Rhyner J.A., Garcia F., Tolon R., Strehler E.E.
Cell Calcium 23:323-338(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CALM2).
[8]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (CALM1; CALM2 AND CALM3).
[9]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (CALM2).
[10]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (CALM1).
[11]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (CALM2).
[12]"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] (CALM1; CALM2 AND CALM3).
Tissue: Brain, Lung, Lymph, Placenta and Urinary bladder.
[13]"Complete amino acid sequence of human brain calmodulin."
Sasagawa T., Ericsson L.H., Walsh K.A., Schreiber W.E., Fischer E.H., Titani K.
Biochemistry 21:2565-2569(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, METHYLATION AT LYS-116.
Tissue: Brain.
[14]Bienvenut W.V., Bensaad K., Vousden K.H.
Submitted (FEB-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-31 AND 92-107, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Osteosarcoma.
[15]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 15-31; 77-107 AND 128-149, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[16]"Structural basis for activation of the titin kinase domain during myofibrillogenesis."
Mayans O., van der Ven P.F.M., Wilm M., Mues A., Young P., Furst D.O., Wilmanns M., Gautel M.
Nature 395:863-869(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TTN.
[17]"Recombinant expression, purification and characterisation of the HMG domain of human SRY."
Kelly S., Yotis J., Macris M., Harley V.
Protein Pept. Lett. 10:281-286(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRY.
[18]"Calcium/calmodulin regulates ubiquitination of the ubiquitin-specific protease TRE17/USP6."
Shen C., Ye Y., Robertson S.E., Lau A.W., Mak D.O., Chou M.M.
J. Biol. Chem. 280:35967-35973(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH USP6.
[19]"Defective calmodulin-mediated nuclear transport of the sex-determining region of the Y chromosome (SRY) in XY sex reversal."
Sim H., Rimmer K., Kelly S., Ludbrook L.M., Clayton A.H., Harley V.R.
Mol. Endocrinol. 19:1884-1892(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRY.
[20]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"CP110 cooperates with two calcium-binding proteins to regulate cytokinesis and genome stability."
Tsang W.Y., Spektor A., Luciano D.J., Indjeian V.B., Chen Z., Salisbury J.L., Sanchez I., Dynlacht B.D.
Mol. Biol. Cell 17:3423-3434(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CCP110, SUBCELLULAR LOCATION.
[22]"Cep97 and CP110 suppress a cilia assembly program."
Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D.
Cell 130:678-690(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CEP97 AND CCP110.
[23]"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.
[24]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100 AND TYR-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[27]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22 AND LYS-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Conserved motif of CDK5RAP2 mediates its localization to centrosomes and the Golgi complex."
Wang Z., Wu T., Shi L., Zhang L., Zheng W., Qu J.Y., Niu R., Qi R.Z.
J. Biol. Chem. 285:22658-22665(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDK5RAP2.
[29]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"Crystal structure of calmodulin binding domain of orai1 in complex with Ca2+ calmodulin displays a unique binding mode."
Liu Y., Zheng X., Mueller G.A., Sobhany M., DeRose E.F., Zhang Y., London R.E., Birnbaumer L.
J. Biol. Chem. 287:43030-43041(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ORAI1.
[32]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning."
Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M.
Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCHO1.
[34]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]"Alpha-helix nucleation by a calcium-binding peptide loop."
Siedlecka M., Goch G., Ejchart A., Sticht H., Bierzyski A.
Proc. Natl. Acad. Sci. U.S.A. 96:903-908(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 95-104.
[36]"Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains."
Chou J.J., Li S., Klee C.B., Bax A.
Nat. Struct. Biol. 8:990-997(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-77 AND 83-149.
[37]"Calmodulin structure refined at 1.7 A resolution."
Chattopadhyaya R., Meador W.E., Means A.R., Quiocho F.A.
J. Mol. Biol. 228:1177-1192(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[38]"Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex."
Cook W.J., Walter L.J., Walter M.R.
Biochemistry 33:15259-15265(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
[39]"Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin."
Drum C.L., Yan S.-Z., Bard J., Shen Y.-Q., Lu D., Soelaiman S., Grabarek Z., Bohm A., Tang W.-J.
Nature 415:396-402(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 6-149.
[40]"Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins."
Shen Y., Lee Y.-S., Soelaiman S., Bergson P., Lu D., Chen A., Beckingham K., Grabarek Z., Mrksich M., Tang W.-J.
EMBO J. 21:6721-6732(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 1-149 IN COMPLEX WITH ANTHRAX EDEMA FACTOR CYA.
[41]"Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin."
Yamauchi E., Nakatsu T., Matsubara M., Kato H., Taniguchi H.
Nat. Struct. Biol. 10:226-231(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MARCKS.
[42]"Insights into voltage-gated calcium channel regulation from the structure of the CaV1.2 IQ domain-Ca2+/calmodulin complex."
Van Petegem F., Chatelain F.C., Minor D.L. Jr.
Nat. Struct. Mol. Biol. 12:1108-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-150 IN COMPLEX WITH CACNA1C.
[43]"Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor."
Shen Y., Zhukovskaya N.L., Guo Q., Florian J., Tang W.-J.
EMBO J. 24:929-941(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH ANTHRAX EDEMA FACTOR CYA.
[44]"Solution NMR structure of Apo-calmodulin in complex with the IQ motif of human cardiac sodium channel NaV1.5."
Chagot B., Chazin W.J.
J. Mol. Biol. 406:106-119(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR IN COMPLEX WITH SCN5A.
[45]"Allosteric mechanism of water-channel gating by Ca(2+)-calmodulin."
Reichow S.L., Clemens D.M., Freites J.A., Nemeth-Cahalan K.L., Heyden M., Tobias D.J., Hall J.E., Gonen T.
Nat. Struct. Mol. Biol. 20:1085-1092(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (25 ANGSTROMS) IN COMPLEX WITH MIP, FUNCTION, INTERACTION WITH MIP.
[46]"Mutations in calmodulin cause ventricular tachycardia and sudden cardiac death."
Nyegaard M., Overgaard M.T., Sondergaard M.T., Vranas M., Behr E.R., Hildebrandt L.L., Lund J., Hedley P.L., Camm A.J., Wettrell G., Fosdal I., Christiansen M., Borglum A.D.
Am. J. Hum. Genet. 91:703-712(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CPVT4 ILE-54 AND SER-98, CHARACTERIZATION OF VARIANTS CPVT4 ILE-54 AND SER-98.
+Additional computationally mapped references.

Web resources

Protein Spotlight

A question of length - Issue 105 of May 2009

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04046 mRNA. Translation: AAA51918.1.
M19311 mRNA. Translation: AAA35641.1.
M27319 mRNA. Translation: AAA35635.1.
X52606, X52607, X52608 Genomic DNA. Translation: CAA36839.1. Sequence problems.
U12022, U11886 Genomic DNA. Translation: AAB60644.1.
D45887 mRNA. Translation: BAA08302.1.
U94728, U94725, U94726 Genomic DNA. Translation: AAC83174.1.
BT006818 mRNA. Translation: AAP35464.1.
BT006855 mRNA. Translation: AAP35501.1.
BT009916 mRNA. Translation: AAP88918.1.
CR541990 mRNA. Translation: CAG46787.1.
CR542021 mRNA. Translation: CAG46818.1.
AC006536 Genomic DNA. Translation: AAD45181.1.
AC073283 Genomic DNA. Translation: AAY24085.1.
BC000454 mRNA. Translation: AAH00454.1.
BC003354 mRNA. Translation: AAH03354.1.
BC005137 mRNA. Translation: AAH05137.1.
BC006464 mRNA. Translation: AAH06464.1.
BC008437 mRNA. Translation: AAH08437.1.
BC008597 mRNA. Translation: AAH08597.1.
BC011834 mRNA. Translation: AAH11834.1.
BC017385 mRNA. Translation: AAH17385.1.
BC018677 mRNA. Translation: AAH18677.1.
BC026065 mRNA. Translation: AAH26065.1.
BC047523 mRNA. No translation available.
CCDSCCDS1832.1.
CCDS33061.1.
CCDS9892.1.
PIRMCHU. S48728.
RefSeqNP_001734.1. NM_001743.4.
NP_005175.2. NM_005184.2.
NP_008819.1. NM_006888.4.
UniGeneHs.282410.
Hs.468442.
Hs.515487.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJImodel-A5-148[»]
1CDLX-ray2.00A/B/C/D2-148[»]
1CLLX-ray1.70A2-149[»]
1CTRX-ray2.45A2-149[»]
1IWQX-ray2.00A2-149[»]
1J7ONMR-A2-77[»]
1J7PNMR-A83-149[»]
1K90X-ray2.75D/E/F2-149[»]
1K93X-ray2.95D/E/F6-149[»]
1L7ZX-ray2.30A2-149[»]
1LVCX-ray3.60D/E/F1-149[»]
1NKFNMR-A94-105[»]
1PK0X-ray3.30D/E/F2-148[»]
1S26X-ray3.00D/E/F2-149[»]
1SK6X-ray3.20D/E/F2-149[»]
1SW8NMR-A2-80[»]
1WRZX-ray2.00A1-149[»]
1XFUX-ray3.35O/P/Q/R/S/T1-149[»]
1XFVX-ray3.35O/P/Q/R/S/T1-149[»]
1XFWX-ray3.40O/P/Q/R/S/T1-149[»]
1XFXX-ray3.20O/P/Q/R/S/T1-149[»]
1XFYX-ray3.30O/P/Q/R/S/T1-149[»]
1XFZX-ray3.25O/P/Q/R/S/T1-149[»]
1Y6WX-ray2.40A2-149[»]
1YR5X-ray1.70A2-149[»]
1YRTX-ray2.10B76-149[»]
1YRUX-ray2.50B76-149[»]
1ZOTX-ray2.20B80-148[»]
1ZUZX-ray1.91A1-149[»]
2BE6X-ray2.00A/B/C1-149[»]
2F3YX-ray1.45A2-149[»]
2F3ZX-ray1.60A2-149[»]
2HF5NMR-A47-113[»]
2I08X-ray2.00A3-79[»]
2JZINMR-A2-149[»]
2K0ENMR-A2-149[»]
2K0FNMR-A2-149[»]
2K0JNMR-A3-149[»]
2K61NMR-A2-149[»]
2KNENMR-A2-149[»]
2KUGNMR-A2-77[»]
2KUHNMR-A83-149[»]
2L53NMR-A2-149[»]
2L7LNMR-A2-149[»]
2LGFNMR-A4-149[»]
2LL6NMR-A2-149[»]
2LL7NMR-A2-149[»]
2LQCNMR-A2-78[»]
2LQPNMR-A79-149[»]
2LV6Other-A2-149[»]
2M0JNMR-A2-149[»]
2M0KNMR-A2-149[»]
2M55NMR-A2-149[»]
2MG5NMR-A2-149[»]
2R28X-ray1.86A/B1-149[»]
2V01X-ray2.15A2-149[»]
2V02X-ray2.20A2-149[»]
2VAYX-ray1.94A4-149[»]
2W73X-ray1.45A/B/E/F1-149[»]
2WELX-ray1.90D1-149[»]
2X0GX-ray2.20B2-149[»]
2Y4VX-ray1.80A1-149[»]
3BYAX-ray1.85A2-149[»]
3DVEX-ray2.35A2-149[»]
3DVJX-ray2.80A2-149[»]
3DVKX-ray2.30A2-149[»]
3DVMX-ray2.60A2-149[»]
3EWTX-ray2.40A2-149[»]
3EWVX-ray2.60A2-149[»]
3G43X-ray2.10A/B/C/D2-149[»]
3HR4X-ray2.50B/D/F/H1-149[»]
3J41electron microscopy25.0E/F1-149[»]
3O77X-ray2.35A3-149[»]
3O78X-ray2.60A/B3-149[»]
3OXQX-ray2.55A/B/C/D1-149[»]
3SUIX-ray1.95A1-149[»]
3UCTX-ray1.90A/B2-80[»]
3UCWX-ray1.76A/B/C/D2-80[»]
3UCYX-ray1.80A2-80[»]
4BW7X-ray1.81A/C1-149[»]
4BW8X-ray1.80A/B1-149[»]
4BYFX-ray2.74B/D1-149[»]
4DCKX-ray2.20B1-149[»]
4DJCX-ray1.35A1-149[»]
4GOWX-ray2.60D4-147[»]
4JPZX-ray3.02C/I1-149[»]
4JQ0X-ray3.84C1-149[»]
4L79X-ray2.30B1-149[»]
4LZXX-ray1.50A2-149[»]
4M1LX-ray2.10A2-149[»]
ProteinModelPortalP62158.
SMRP62158. Positions 1-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107252. 374 interactions.
107256. 25 interactions.
107259. 20 interactions.
DIPDIP-31794N.
IntActP62158. 191 interactions.
MINTMINT-4999725.

Chemistry

BindingDBP62158.
ChEMBLCHEMBL6093.
DrugBankDB01429. Aprindine.
DB01244. Bepridil.
DB00527. Dibucaine.
DB01023. Felodipine.
DB04841. Flunarizine.
DB00623. Fluphenazine.
DB00753. Isoflurane.
DB00836. Loperamide.
DB01110. Miconazole.
DB00850. Perphenazine.
DB00925. Phenoxybenzamine.
DB01100. Pimozide.
DB01069. Promethazine.

Protein family/group databases

TCDB9.C.15.1.1. the animal calmodulin-dependent e.r. secretion pathway (csp) family.

PTM databases

PhosphoSiteP62158.

Polymorphism databases

DMDM49037474.

2D gel databases

DOSAC-COBS-2DPAGEP62158.
OGPP02593.
SWISS-2DPAGEP62158.

Proteomic databases

MaxQBP62158.
PaxDbP62158.
PRIDEP62158.

Protocols and materials databases

DNASU801.
805.
808.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272298; ENSP00000272298; ENSG00000143933.
ENST00000291295; ENSP00000291295; ENSG00000160014.
ENST00000356978; ENSP00000349467; ENSG00000198668.
ENST00000596362; ENSP00000472141; ENSG00000160014.
GeneID801.
805.
808.
KEGGhsa:801.
hsa:805.
hsa:808.
UCSCuc001xyl.2. human.

Organism-specific databases

CTD801.
805.
808.
GeneCardsGC02M047272.
GC14P090863.
GC19P047105.
GeneReviewsCALM1.
HGNCHGNC:1442. CALM1.
HGNC:1445. CALM2.
HGNC:1449. CALM3.
HPACAB007790.
CAB018558.
MIM114180. gene.
114182. gene.
114183. gene.
614916. phenotype.
neXtProtNX_P62158.
Orphanet3286. Catecholaminergic polymorphic ventricular tachycardia.
PharmGKBPA26042.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5126.
HOVERGENHBG012180.
InParanoidP62158.
KOK02183.
OMAKEVMAST.
PhylomeDBP62158.
TreeFamTF300912.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000143933-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_11123. Membrane Trafficking.
REACT_116125. Disease.
REACT_118664. Calcineurin dephosphorylates NFATC1,2,3.
REACT_13685. Neuronal System.
REACT_17044. Muscle contraction.
REACT_200751. Organelle biogenesis and maintenance.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP62158.
BgeeP62158.
CleanExHS_CALM1.
HS_CALM2.
GenevestigatorP62158.

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. human.
CALM3. human.
EvolutionaryTraceP62158.
GeneWikiCALM2.
CALM3.
Calmodulin_1.
NextBio3264.
PROP62158.
SOURCESearch...

Entry information

Entry nameCALM_HUMAN
AccessionPrimary (citable) accession number: P62158
Secondary accession number(s): P02593 expand/collapse secondary AC list , P70667, P99014, Q13942, Q53S29, Q61379, Q61380, Q96HK3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM