Reviewed,
UniProtKB/Swiss-Prot P62158 (CALM_HUMAN)
Last modified
November 25, 2008.
Version 74.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Calmodulin Short name=CaM | ||||||||||||||
| Gene names |
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| 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 Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) 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. |
| Subunit structure | 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. |
| 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
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 | ||||||||||||||||||||||||||||
| 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 | ||||||||||||||||||||||||||||
| Modified residue | 45 | 1 | Phosphothreonine; by CaMK4 By similarity | ||||||||||||||||||||||||||||
| Modified residue | 100 | 1 | Phosphotyrosine | ||||||||||||||||||||||||||||
| Modified residue | 116 | 1 | N6,N6,N6-trimethyllysine | ||||||||||||||||||||||||||||
| Cross-link | 22 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | |||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||
| Sequence conflict | 124 | 1 | E → Q in AAH08437. Ref.12 | ||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||
| 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
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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: 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. 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. 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. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 92-107, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell. |
| [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. 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] | "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. |
| [26] | "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. |
| [27] | "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). |
| [28] | "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). |
| [29] | "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. |
| [30] | "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. |
| [31] | "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] [ |

Clusters with