P62158 (CALM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	149 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Calmodulin mediates the control of a large number of enzymes, ion channels 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 CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Ref.21
Subunit structure	Interacts with MYO1C and RRAD. Interacts with MYO10 By similarity. Interacts with CEP97, CEP110, 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. Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.27 Ref.30
Subcellular location	Cytoplasm › cytoskeleton › spindle. Cytoplasm › cytoskeleton › spindle 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.41
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 component	Cytoplasm Cytoskeleton
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	Calcium Metal-binding
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor signaling pathway Traceable author statement PubMed 10899953. Source: UniProtKB activation of phospholipase C activity Traceable author statement. Source: Reactome detection of calcium ion Inferred from mutant phenotype Ref.41. 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 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 nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome nitric oxide metabolic process 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 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 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.41. Source: BHF-UCL regulation of nitric-oxide synthase activity Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome synaptic transmission Traceable author statement. Source: Reactome
Cellular_component	centrosome Inferred from direct assay Ref.21. Source: UniProtKB cytosol Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome 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_function	calcium ion binding Inferred from direct assay Ref.41PubMed 7607248PubMed 8631777. Source: BHF-UCL protein phosphatase activator activity Inferred from direct assay PubMed 8631777. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADORA2A	P29274	3	EBI-397435,EBI-2902702
ARRB1	P49407	3	EBI-397435,EBI-743313
ARRB2	P32121	3	EBI-397435,EBI-714559
CACNA1C	Q13936	2	EBI-397435,EBI-1038838
CCP110	O43303	9	EBI-397435,EBI-1566217
cya	P40136	8	EBI-397435,EBI-457011	From a different organism.
EGFR	P00533	3	EBI-397435,EBI-297353
FAS	P25445	4	EBI-397435,EBI-494743
KCNH1	O95259	2	EBI-397435,EBI-2909270
Marcks	P26645	2	EBI-397435,EBI-911805	From a different organism.
SCN5A	Q14524	2	EBI-397435,EBI-726858

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.13 Ref.14

Chain

2 – 149

148

Calmodulin

PRO_0000198223

Regions

Domain

8 – 43

36

EF-hand 1

Domain

44 – 79

36

EF-hand 2

Domain

81 – 116

36

EF-hand 3

Domain

117 – 149

33

EF-hand 4

Calcium binding

21 – 32

12

1

Calcium binding

57 – 68

12

2

Calcium binding

94 – 105

12

3

Calcium binding

130 – 141

12

4

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.13 Ref.14

Modified residue

22

1

N6-acetyllysine; alternate Ref.26

Modified residue

45

1

Phosphothreonine; by CaMK4 By similarity

Modified residue

95

1

N6-acetyllysine Ref.26

Modified residue

100

1

Phosphotyrosine Ref.24 Ref.25

Modified residue

102

1

Phosphoserine Ref.29

Modified residue

116

1

N6,N6,N6-trimethyllysine Ref.13

Modified residue

139

1

Phosphotyrosine Ref.25

Cross-link

22

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Natural variations

Natural variant

54

1

N → I in CPVT4; the mutant has significantly reduced Ca(2+) affinity compared to wild-type. Ref.41

VAR_069222

Natural variant

73

1

M → T.
Corresponds to variant rs41389749 [ dbSNP | Ensembl ].

VAR_048585

Natural variant

98

1

N → 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.41

VAR_069223

Experimental info

Sequence conflict

124

1

E → Q in AAH08437. Ref.12

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

149

Helix Strand Turn

Details...

Helix

2 – 4

3

Helix

7 – 20

14

Beta strand

25 – 28

4

Helix

30 – 39

10

Helix

46 – 56

11

Turn

57 – 59

3

Beta strand

61 – 65

5

Helix

66 – 93

28

Beta strand

94 – 96

3

Beta strand

97 – 101

5

Helix

103 – 112

10

Beta strand

113 – 115

3

Helix

119 – 129

11

Turn

130 – 132

3

Beta strand

133 – 138

6

Helix

139 – 146

8

Sequences

	Sequence		Length	Mass (Da)
	P62158 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6B4BC3FCDE10727B	FASTA	149	16,838
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, 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 CEP110, 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 CEP110.
[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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"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, MASS SPECTROMETRY.
[27]	"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.
[28]	"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].
[29]	"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, MASS SPECTROMETRY.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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).
[34]	"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).
[35]	"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.
[36]	"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.
[37]	"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.
[38]	"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.
[39]	"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.
[40]	"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.
[41]	"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.

IPI

IPI00075248.

PIR

MCHU. S48728.

RefSeq

NP_001734.1. NM_001743.4.
NP_005175.2. NM_005184.2.
NP_008819.1. NM_006888.4.

UniGene

Hs.282410.
Hs.468442.
Hs.515487.
Hs.708270.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AJI	model	-	A	5-148	[»]
1CDL	X-ray	2.00	A/B/C/D	2-147	[»]
1CLL	X-ray	1.70	A	2-149	[»]
1CTR	X-ray	2.45	A	2-149	[»]
1IWQ	X-ray	2.00	A	2-149	[»]
1J7O	NMR	-	A	2-77	[»]
1J7P	NMR	-	A	83-149	[»]
1K90	X-ray	2.75	D/E/F	2-149	[»]
1K93	X-ray	2.95	D/E/F	6-149	[»]
1L7Z	X-ray	2.30	A	2-148	[»]
1LVC	X-ray	3.60	D/E/F	1-149	[»]
1NKF	NMR	-	A	94-105	[»]
1PK0	X-ray	3.30	D/E/F	2-147	[»]
1S26	X-ray	3.00	D/E/F	2-148	[»]
1SK6	X-ray	3.20	D/E/F	2-149	[»]
1SW8	NMR	-	A	2-80	[»]
1WRZ	X-ray	2.00	A	1-149	[»]
1XFU	X-ray	3.35	O/P/Q/R/S/T	1-149	[»]
1XFV	X-ray	3.35	O/P/Q/R/S/T	1-149	[»]
1XFW	X-ray	3.40	O/P/Q/R/S/T	1-149	[»]
1XFX	X-ray	3.20	O/P/Q/R/S/T	1-149	[»]
1XFY	X-ray	3.30	O/P/Q/R/S/T	1-149	[»]
1XFZ	X-ray	3.25	O/P/Q/R/S/T	1-149	[»]
1Y6W	X-ray	2.40	A	2-148	[»]
1YR5	X-ray	1.70	A	2-148	[»]
1YRT	X-ray	2.10	B	76-149	[»]
1YRU	X-ray	2.50	B	76-149	[»]
1ZOT	X-ray	2.20	B	80-148	[»]
1ZUZ	X-ray	1.91	A	1-148	[»]
2BE6	X-ray	2.00	A/B/C	1-149	[»]
2F3Y	X-ray	1.45	A	2-148	[»]
2F3Z	X-ray	1.60	A	2-148	[»]
2HF5	NMR	-	A	47-113	[»]
2I08	X-ray	2.00	A	3-78	[»]
2JZI	NMR	-	A	2-149	[»]
2K0E	NMR	-	A	2-149	[»]
2K0F	NMR	-	A	2-149	[»]
2K0J	NMR	-	A	2-149	[»]
2K61	NMR	-	A	2-149	[»]
2KNE	NMR	-	A	2-149	[»]
2KUG	NMR	-	A	2-77	[»]
2KUH	NMR	-	A	83-149	[»]
2L53	NMR	-	A	2-149	[»]
2L7L	NMR	-	A	2-149	[»]
2LGF	NMR	-	A	4-149	[»]
2LL6	NMR	-	A	2-149	[»]
2LL7	NMR	-	A	2-149	[»]
2LQC	NMR	-	A	2-78	[»]
2LQP	NMR	-	A	79-149	[»]
2LV6	Other	-	A	2-149	[»]
2R28	X-ray	1.86	A/B	1-149	[»]
2V01	X-ray	2.15	A	1-149	[»]
2V02	X-ray	2.20	A	1-149	[»]
2VAY	X-ray	1.94	A	4-148	[»]
2W73	X-ray	1.45	A/B/E/F	1-149	[»]
2WEL	X-ray	1.90	D	1-149	[»]
2X0G	X-ray	2.20	B	2-149	[»]
2Y4V	X-ray	1.80	A	1-149	[»]
3BYA	X-ray	1.85	A	2-149	[»]
3DVE	X-ray	2.35	A	2-149	[»]
3DVJ	X-ray	2.80	A	2-149	[»]
3DVK	X-ray	2.30	A	2-149	[»]
3DVM	X-ray	2.60	A	2-149	[»]
3EWT	X-ray	2.40	A	2-149	[»]
3EWV	X-ray	2.60	A	2-149	[»]
3G43	X-ray	2.10	A/B/C/D	2-149	[»]
3HR4	X-ray	2.50	B/D/F/H	1-149	[»]
3O77	X-ray	2.35	A	3-149	[»]
3O78	X-ray	2.60	A/B	3-149	[»]
3OXQ	X-ray	2.55	A/B/C/D	1-149	[»]
3SUI	X-ray	1.95	A	1-149	[»]
3UCT	X-ray	1.90	A/B	2-80	[»]
3UCW	X-ray	1.76	A/B/C/D	2-80	[»]
3UCY	X-ray	1.80	A	2-80	[»]
4DCK	X-ray	2.20	B	1-149	[»]
4DJC	X-ray	1.35	A	1-149	[»]
4GOW	X-ray	2.60	D	4-147	[»]

ProteinModelPortal

P62158.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31794N.

IntAct

P62158. 181 interactions.

MINT

MINT-4999725.

PTM databases

PhosphoSite

P62158.

2D gel databases

DOSAC-COBS-2DPAGE

P62158.

OGP

P02593.

SWISS-2DPAGE

P62158.

Proteomic databases

PaxDb

P62158.

PRIDE

P62158.

Protocols and materials databases

DNASU

801.
805.
808.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000272298; ENSP00000272298; ENSG00000143933.
ENST00000291295; ENSP00000291295; ENSG00000160014.
ENST00000356978; ENSP00000349467; ENSG00000198668.
ENST00000596362; ENSP00000472141; ENSG00000160014.

GeneID

801.
805.
808.

KEGG

hsa:801.
hsa:805.
hsa:808.

UCSC

uc001xyl.2. human.

Organism-specific databases

CTD

801.
805.
808.

HGNC

HGNC:1442. CALM1.
HGNC:1445. CALM2.
HGNC:1449. CALM3.

HPA

CAB007790.
CAB018558.

MIM

114180. gene.
114182. gene.
114183. gene.
614916. phenotype.

neXtProt

NX_P62158.

PharmGKB

PA26042.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5126.

HOVERGEN

HBG012180.

InParanoid

P62158.

KO

K02183.

OMA

ELEDMIN.

OrthoDB

EOG4001KK.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000143933-MONOMER.

Pathway_Interaction_DB

bcr_5pathway. BCR signaling pathway.
nfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
tcrcalciumpathway. Calcium signaling in the CD4+ TCR pathway.
cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
ifngpathway. IFN-gamma pathway.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
p38_mkk3_6pathway. p38 MAPK signaling pathway.
smad2_3pathway. Regulation of cytoplasmic and nuclear SMAD2/3 signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
vegfr1_pathway. VEGFR1 specific signals.

Reactome

REACT_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_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P62158.

Bgee

P62158.

CleanEx

HS_CALM1.
HS_CALM2.

Genevestigator

P62158.

GermOnline

ENSG00000143933. Homo sapiens.
ENSG00000160014. Homo sapiens.
ENSG00000198668. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 2 hits.

InterPro

IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001125. Recoverin.
[Graphical view]

Pfam

PF13499. EF_hand_5. 2 hits.
[Graphical view]

PRINTS

PR00450. RECOVERIN.

SMART

SM00054. EFh. 4 hits.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P62158.

ChEMBL

CHEMBL6093.

ChiTaRS

CALM1. human.
CALM3. human.

DrugBank

DB01429. 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.

EvolutionaryTrace

P62158.

NextBio

3264.

SOURCE

Search...

Entry information

Entry name

CALM_HUMAN

Accession

Primary (citable) accession number: P62158
Secondary accession number(s): P02593 , 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:	May 1, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.