Reviewed, UniProtKB/Swiss-Prot P62158 (CALM_HUMAN)

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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 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.20
Subunit structure	Interacts with MYO1C By similarity. Interacts with CEP97, CEP110, TTN/titin and SRY.
Subcellular location	Spindle. Note: Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. Ref.20
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.
Sequence caution	The sequence CAA36839.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	Calcium
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	G-protein coupled receptor protein signaling pathway Traceable author statement. Source: UniProtKB negative regulation of ryanodine-sensitive calcium-release channel activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of ryanodine-sensitive calcium-release channel activity Inferred from sequence or structural similarity. Source: UniProtKB regulation of cytokinesis Ref.20 Inferred from mutant phenotype. Source: UniProtKB regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB response to calcium ion Inferred from direct assay. Source: UniProtKB
Cellular component	centrosome Ref.20 Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome plasma membrane Traceable author statement. Source: UniProtKB spindle microtubule Ref.20 Inferred from direct assay. Source: UniProtKB spindle pole Ref.20 Inferred from direct assay. Source: UniProtKB
Molecular function	N-terminal myristoylation domain binding Inferred from physical interaction. Source: UniProtKB calcium ion binding Ref.4 Ref.7 Traceable author statement. Source: UniProtKB protein domain specific binding Inferred from physical interaction. Source: UniProtKB titin binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARRB1	P49407	1	EBI-397435,EBI-743313
ARRB2	P32121	1	EBI-397435,EBI-714559
CACNA1C	Q13936	1	EBI-397435,EBI-1038838
CAMK2A	Q9UQM7	1	EBI-397435,EBI-1383687
CEP110	O43303	5	EBI-397435,EBI-1566217
cya	P40136	1	EBI-397435,EBI-457011	From a different organism.
EGFR	P00533	1	EBI-397435,EBI-297353
FAS	P25445	3	EBI-397435,EBI-494743
HNF1A	P20823	1	EBI-397435,EBI-636034
OBSCN	Q5VST9	1	EBI-397435,EBI-941850
PINX1	Q96BK5	1	EBI-397435,EBI-721782
RIOK3	O14730	1	EBI-397435,EBI-1047061

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

45

1

Phosphothreonine; by CaMK4 By similarity

Modified residue

100

1

Phosphotyrosine Ref.19 Ref.22 Ref.23 Ref.24

Modified residue

116

1

N6,N6,N6-trimethyllysine Ref.13

Cross-link

22

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

Natural variations

Natural variant

73

1

M → T: dbSNP rs41389749.

VAR_048585

Experimental info

Sequence conflict

124

1

E → Q in AAH08437. Ref.12

Secondary structure

1

.

.

.

.

.

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.

.

.

.

.

.

.

.

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.

.

.

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.

.

.

.

149

Helix Strand Turn

Details...

Helix

7 – 20

14

Beta strand

25 – 28

4

Helix

30 – 39

10

Helix

46 – 56

11

Beta strand

61 – 65

5

Helix

66 – 78

13

Helix

84 – 93

10

Beta strand

98 – 101

4

Helix

103 – 112

10

Helix

119 – 129

11

Beta strand

134 – 138

5

Helix

139 – 147

9

Sequences

	Sequence		Length	Mass (Da)
	P62158-1 [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: 6385987] [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: 2445749] [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: 3182832] [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: 2223880] [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: 7925473] [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: 9681195] [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: 12508121] [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: 15815621] [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: 15489334] [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: 7093203] [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: 9804419] [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: 12871148] [Abstract] Cited for: INTERACTION WITH SRY.
[18]	"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: 15746192] [Abstract] Cited for: INTERACTION WITH SRY.
[19]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, MASS SPECTROMETRY.
[20]	"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: 16760425] [Abstract] Cited for: FUNCTION, INTERACTION WITH CEP110, SUBCELLULAR LOCATION.
[21]	"Cep97 and CP110 suppress a cilia assembly program." Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D. Cell 130:678-690(2007) [PubMed: 17719545] [Abstract] Cited for: INTERACTION WITH CEP97 AND CEP110.
[22]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, MASS SPECTROMETRY.
[23]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, MASS SPECTROMETRY.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, MASS SPECTROMETRY.
[25]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[26]	"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: 9927666] [Abstract] Cited for: STRUCTURE BY NMR OF 95-104.
[27]	"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: 11685248] [Abstract] Cited for: STRUCTURE BY NMR OF 1-77 AND 83-149.
[28]	"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: 1474585] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[29]	"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: 7803388] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
[30]	"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: 11807546] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 6-149.
[31]	"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: 12485993] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 1-149 IN COMPLEX WITH ANTHRAX EDEMA FACTOR CYA.
[32]	"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: 12577052] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MARCKS.
[33]	"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: 16299511] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-150 IN COMPLEX WITH CACNA1C.
[34]	"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: 15719022] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH ANTHRAX EDEMA FACTOR CYA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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. Translation: AAH47523.1.

IPI

IPI00075248.

PIR

MCHU. S48728.

RefSeq

NP_001734.1.
NP_005175.2.
NP_008819.1.

UniGene

Hs.282410
Hs.515487
Hs.643483
Hs.706125
Hs.708270
Hs.713288

3D structure databases

PDBPDBe

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	76-148	[»]
1YRU	X-ray	2.50	B	76-148	[»]
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	[»]
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	[»]
2WEL	X-ray	1.90	D	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	[»]
3G43	X-ray	2.10	A/B/C/D	2-149	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P62158. 191 interactions.

PTM databases

PhosphoSite

P62158.

2-D gel databases

SWISS-2DPAGE

P62158.

Aarhus/Ghent-2DPAGE

9048. IEF.

DOSAC-COBS-2DPAGE

P62158.

OGP

P02593.

Proteomic databases

PRIDE

P62158.

Genome annotation databases

Ensembl

ENSG00000143933. Homo sapiens. [Contig view]
ENSG00000160014. Homo sapiens. [Contig view]
ENSG00000198668. Homo sapiens. [Contig view]

GeneID

801.
805.
808.

KEGG

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

Organism-specific databases

GeneCards

GC02M047298.
GC14P089933.
GC19P051799.

H-InvDB

HIX0002039.
HIX0011883.
HIX0015255.

HGNC

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

HPA

CAB007790.
CAB018558.

MIM

114180. gene.
114182. gene.
114183. gene.

PharmGKB

PA26035.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P62158.

OMA

P62158. DEQIAEF.

Enzyme and pathway databases

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_12508. Metabolism of nitric oxide.
REACT_474. Metabolism of carbohydrates.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P62158.

Bgee

P62158.

CleanEx

HS_CALM1.
HS_CALM2.

GermOnline

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

Family and domain databases

InterPro

IPR011992. EF-Hand_type.
IPR018248. EF_hand.
IPR018247. EF_HAND_1.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
IPR001125. Recoverin.
[Graphical view]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 1 hit.

Pfam

PF00036. efhand. 4 hits.
[Graphical view]

PRINTS

PR00450. RECOVERIN.

ProDom

PD000012. EF-hand. 2 hits.
[Graphical view] [Entries sharing at least one domain]

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 Resources

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.

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:	June 16, 2009
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)