Calmodulin

Details

Name
Calmodulin
Synonyms
  • CALM
  • CALML2
  • CAM
  • CAM1
  • CAM2
  • CAM3
  • CAMB
  • CAMC
  • CAMIII
Gene Name
CALM1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0037013|Calmodulin
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAK
Number of residues
149
Molecular Weight
16837.47
Theoretical pI
3.84
GO Classification
Functions
calcium ion binding / ion channel binding / N-terminal myristoylation domain binding / nitric-oxide synthase regulator activity / phospholipase binding / protein domain specific binding / protein kinase binding / protein phosphatase activator activity / protein serine/threonine kinase activator activity / thioesterase binding / titin binding
Processes
activation of adenylate cyclase activity / activation of MAPKK activity / activation of phospholipase C activity / axon guidance / blood coagulation / carbohydrate metabolic process / detection of calcium ion / epidermal growth factor receptor signaling pathway / Fc-epsilon receptor signaling pathway / fibroblast growth factor receptor signaling pathway / G-protein coupled receptor signaling pathway / glucose metabolic process / glycogen catabolic process / innate immune response / inositol phosphate metabolic process / insulin receptor signaling pathway / MAPK cascade / membrane organization / muscle contraction / negative regulation of peptidyl-threonine phosphorylation / negative regulation of ryanodine-sensitive calcium-release channel activity / neurotrophin TRK receptor signaling pathway / nitric oxide metabolic process / phototransduction, visible light / platelet activation / platelet degranulation / positive regulation of cyclic nucleotide metabolic process / positive regulation of cyclic-nucleotide phosphodiesterase activity / positive regulation of nitric-oxide synthase activity / positive regulation of peptidyl-threonine phosphorylation / positive regulation of phosphoprotein phosphatase activity / positive regulation of protein autophosphorylation / positive regulation of protein dephosphorylation / positive regulation of protein serine/threonine kinase activity / positive regulation of ryanodine-sensitive calcium-release channel activity / Ras protein signal transduction / regulation of cardiac muscle contraction / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / regulation of cell communication by electrical coupling involved in cardiac conduction / regulation of cytokinesis / regulation of heart rate / regulation of high voltage-gated calcium channel activity / regulation of nitric-oxide synthase activity / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / regulation of rhodopsin mediated signaling pathway / response to amphetamine / response to calcium ion / response to corticosterone / rhodopsin mediated signaling pathway / signal transduction / small GTPase mediated signal transduction / small molecule metabolic process / stimulatory C-type lectin receptor signaling pathway / substantia nigra development / synaptic transmission / vascular endothelial growth factor receptor signaling pathway
Components
centrosome / cytoplasm / cytosol / extracellular exosome / extracellular region / growth cone / nucleoplasm / nucleus / plasma membrane / sarcomere / spindle microtubule / spindle pole / vesicle
General Function
Titin binding
Specific Function
Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins 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 CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0021651|Calmodulin (CALM1)
ATGGCTGATCAGCTGACCGAAGAACAGATTGCTGAATTCAAGGAAGCCTTCTCCCTATTT
GATAAAGATGGCGATGGCACCATCACAACAAAGGAACTTGGAACTGTCATGAGGTCACTG
GGTCAGAACCCAACAGAAGCTGAATTGCAGGATATGATCAATGAAGTGGATGCTGATGGT
AATGGCACCATTGACTTCCCCGAATTTTTGACTATGATGGCTAGAAAAATGAAAGATACA
GATAGTGAAGAAGAAATCCGTGAGGCATTCCGAGTCTTTGACAAGGATGGCAATGGTTAT
ATCAGTGCAGCAGAACTACGTCACGTCATGACAAACTTAGGAGAAAAACTAACAGATGAA
GAAGTAGATGAAATGATCAGAGAAGCAGATATTGATGGAGACGGACAAGTCAACTATGAA
GAATTCGTACAGATGATGACTGCAAAATGA
Chromosome Location
19
Locus
14q24-q31
External Identifiers
ResourceLink
UniProtKB IDP0DP23
UniProtKB Entry NameCALM_HUMAN
GenBank Protein ID179888
GenBank Gene IDJ04046
GenAtlas IDCALM1
HGNC IDHGNC:1442
General References
  1. Wawrzynczak EJ, Perham RN: Isolation and nucleotide sequence of a cDNA encoding human calmodulin. Biochem Int. 1984 Aug;9(2):177-85. [PubMed:6385987]
  2. SenGupta B, Friedberg F, Detera-Wadleigh SD: Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species. J Biol Chem. 1987 Dec 5;262(34):16663-70. [PubMed:2445749]
  3. Fischer R, Koller M, Flura M, Mathews S, Strehler-Page MA, Krebs J, Penniston JT, Carafoli E, Strehler EE: Multiple divergent mRNAs code for a single human calmodulin. J Biol Chem. 1988 Nov 15;263(32):17055-62. [PubMed:3182832]
  4. Koller M, Schnyder B, Strehler EE: Structural organization of the human CaMIII calmodulin gene. Biochim Biophys Acta. 1990 Oct 23;1087(2):180-9. [PubMed:2223880]
  5. Rhyner JA, Ottiger M, Wicki R, Greenwood TM, Strehler EE: Structure of the human CALM1 calmodulin gene and identification of two CALM1-related pseudogenes CALM1P1 and CALM1P2. Eur J Biochem. 1994 Oct 1;225(1):71-82. [PubMed:7925473]
  6. Toutenhoofd SL, Foletti D, Wicki R, Rhyner JA, Garcia F, Tolon R, Strehler EE: Characterization of the human CALM2 calmodulin gene and comparison of the transcriptional activity of CALM1, CALM2 and CALM3. Cell Calcium. 1998 May;23(5):323-38. [PubMed:9681195]
  7. Heilig R, Eckenberg R, Petit JL, 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, Bruls 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, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed:12508121]
  8. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, 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 EA, 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 SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed:15815621]
  9. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334]
  10. Sasagawa T, Ericsson LH, Walsh KA, Schreiber WE, Fischer EH, Titani K: Complete amino acid sequence of human brain calmodulin. Biochemistry. 1982 May 11;21(10):2565-9. [PubMed:7093203]
  11. Mayans O, van der Ven PF, Wilm M, Mues A, Young P, Furst DO, Wilmanns M, Gautel M: Structural basis for activation of the titin kinase domain during myofibrillogenesis. Nature. 1998 Oct 29;395(6705):863-9. [PubMed:9804419]
  12. Kelly S, Yotis J, Macris M, Harley V: Recombinant expression, purification and characterisation of the HMG domain of human SRY. Protein Pept Lett. 2003 Jun;10(3):281-6. [PubMed:12871148]
  13. Shen C, Ye Y, Robertson SE, Lau AW, Mak DO, Chou MM: Calcium/calmodulin regulates ubiquitination of the ubiquitin-specific protease TRE17/USP6. J Biol Chem. 2005 Oct 28;280(43):35967-73. Epub 2005 Aug 26. [PubMed:16127172]
  14. Sim H, Rimmer K, Kelly S, Ludbrook LM, Clayton AH, Harley VR: Defective calmodulin-mediated nuclear transport of the sex-determining region of the Y chromosome (SRY) in XY sex reversal. Mol Endocrinol. 2005 Jul;19(7):1884-92. Epub 2005 Mar 3. [PubMed:15746192]
  15. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed:15592455]
  16. Tsang WY, Spektor A, Luciano DJ, Indjeian VB, Chen Z, Salisbury JL, Sanchez I, Dynlacht BD: CP110 cooperates with two calcium-binding proteins to regulate cytokinesis and genome stability. Mol Biol Cell. 2006 Aug;17(8):3423-34. Epub 2006 Jun 7. [PubMed:16760425]
  17. Spektor A, Tsang WY, Khoo D, Dynlacht BD: Cep97 and CP110 suppress a cilia assembly program. Cell. 2007 Aug 24;130(4):678-90. [PubMed:17719545]
  18. Wright NT, Prosser BL, Varney KM, Zimmer DB, Schneider MF, Weber DJ: S100A1 and calmodulin compete for the same binding site on ryanodine receptor. J Biol Chem. 2008 Sep 26;283(39):26676-83. doi: 10.1074/jbc.M804432200. Epub 2008 Jul 23. [PubMed:18650434]
  19. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648]
  20. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330]
  21. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332]
  22. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861]
  23. Wang Z, Wu T, Shi L, Zhang L, Zheng W, Qu JY, Niu R, Qi RZ: Conserved motif of CDK5RAP2 mediates its localization to centrosomes and the Golgi complex. J Biol Chem. 2010 Jul 16;285(29):22658-65. doi: 10.1074/jbc.M110.105965. Epub 2010 May 13. [PubMed:20466722]
  24. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [PubMed:21269460]
  25. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. [PubMed:21406692]
  26. Liu Y, Zheng X, Mueller GA, Sobhany M, DeRose EF, Zhang Y, London RE, Birnbaumer L: Crystal structure of calmodulin binding domain of orai1 in complex with Ca2+ calmodulin displays a unique binding mode. J Biol Chem. 2012 Dec 14;287(51):43030-41. doi: 10.1074/jbc.M112.380964. Epub 2012 Oct 29. [PubMed:23109337]
  27. Bienvenut WV, Sumpton D, Martinez A, Lilla S, Espagne C, Meinnel T, Giglione C: Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-alpha-acetylation features. Mol Cell Proteomics. 2012 Jun;11(6):M111.015131. doi: 10.1074/mcp.M111.015131. Epub 2012 Jan 5. [PubMed:22223895]
  28. Umasankar PK, Sanker S, Thieman JR, Chakraborty S, Wendland B, Tsang M, Traub LM: Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning. Nat Cell Biol. 2012 Apr 8;14(5):488-501. doi: 10.1038/ncb2473. [PubMed:22484487]
  29. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [PubMed:22814378]
  30. Crotti L, Johnson CN, Graf E, De Ferrari GM, Cuneo BF, Ovadia M, Papagiannis J, Feldkamp MD, Rathi SG, Kunic JD, Pedrazzini M, Wieland T, Lichtner P, Beckmann BM, Clark T, Shaffer C, Benson DW, Kaab S, Meitinger T, Strom TM, Chazin WJ, Schwartz PJ, George AL Jr: Calmodulin mutations associated with recurrent cardiac arrest in infants. Circulation. 2013 Mar 5;127(9):1009-17. doi: 10.1161/CIRCULATIONAHA.112.001216. Epub 2013 Feb 6. [PubMed:23388215]
  31. Makita N, Yagihara N, Crotti L, Johnson CN, Beckmann BM, Roh MS, Shigemizu D, Lichtner P, Ishikawa T, Aiba T, Homfray T, Behr ER, Klug D, Denjoy I, Mastantuono E, Theisen D, Tsunoda T, Satake W, Toda T, Nakagawa H, Tsuji Y, Tsuchiya T, Yamamoto H, Miyamoto Y, Endo N, Kimura A, Ozaki K, Motomura H, Suda K, Tanaka T, Schwartz PJ, Meitinger T, Kaab S, Guicheney P, Shimizu W, Bhuiyan ZA, Watanabe H, Chazin WJ, George AL Jr: Novel calmodulin mutations associated with congenital arrhythmia susceptibility. Circ Cardiovasc Genet. 2014 Aug;7(4):466-74. doi: 10.1161/CIRCGENETICS.113.000459. Epub 2014 Jun 10. [PubMed:24917665]
  32. Marsman RF, Barc J, Beekman L, Alders M, Dooijes D, van den Wijngaard A, Ratbi I, Sefiani A, Bhuiyan ZA, Wilde AA, Bezzina CR: A mutation in CALM1 encoding calmodulin in familial idiopathic ventricular fibrillation in childhood and adolescence. J Am Coll Cardiol. 2014 Jan 28;63(3):259-66. doi: 10.1016/j.jacc.2013.07.091. Epub 2013 Sep 25. [PubMed:24076290]
  33. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569]
  34. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [PubMed:25944712]
  35. Siedlecka M, Goch G, Ejchart A, Sticht H, Bierzynski A: Alpha-helix nucleation by a calcium-binding peptide loop. Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):903-8. [PubMed:9927666]
  36. Chou JJ, Li S, Klee CB, Bax A: Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains. Nat Struct Biol. 2001 Nov;8(11):990-7. [PubMed:11685248]
  37. Chattopadhyaya R, Meador WE, Means AR, Quiocho FA: Calmodulin structure refined at 1.7 A resolution. J Mol Biol. 1992 Dec 20;228(4):1177-92. [PubMed:1474585]
  38. Cook WJ, Walter LJ, Walter MR: Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex. Biochemistry. 1994 Dec 27;33(51):15259-65. [PubMed:7803388]
  39. Drum CL, Yan SZ, Bard J, Shen YQ, Lu D, Soelaiman S, Grabarek Z, Bohm A, Tang WJ: Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature. 2002 Jan 24;415(6870):396-402. [PubMed:11807546]
  40. Shen Y, Lee YS, Soelaiman S, Bergson P, Lu D, Chen A, Beckingham K, Grabarek Z, Mrksich M, Tang WJ: Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins. EMBO J. 2002 Dec 16;21(24):6721-32. [PubMed:12485993]
  41. Yamauchi E, Nakatsu T, Matsubara M, Kato H, Taniguchi H: Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin. Nat Struct Biol. 2003 Mar;10(3):226-31. [PubMed:12577052]
  42. Van Petegem F, Chatelain FC, Minor DL Jr: Insights into voltage-gated calcium channel regulation from the structure of the CaV1.2 IQ domain-Ca2+/calmodulin complex. Nat Struct Mol Biol. 2005 Dec;12(12):1108-15. Epub 2005 Nov 20. [PubMed:16299511]
  43. Shen Y, Zhukovskaya NL, Guo Q, Florian J, Tang WJ: Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor. EMBO J. 2005 Mar 9;24(5):929-41. Epub 2005 Feb 17. [PubMed:15719022]
  44. Chagot B, Chazin WJ: Solution NMR structure of Apo-calmodulin in complex with the IQ motif of human cardiac sodium channel NaV1.5. J Mol Biol. 2011 Feb 11;406(1):106-19. doi: 10.1016/j.jmb.2010.11.046. Epub 2010 Dec 15. [PubMed:21167176]
  45. Reichow SL, Clemens DM, Freites JA, Nemeth-Cahalan KL, Heyden M, Tobias DJ, Hall JE, Gonen T: Allosteric mechanism of water-channel gating by Ca2+-calmodulin. Nat Struct Mol Biol. 2013 Sep;20(9):1085-92. doi: 10.1038/nsmb.2630. Epub 2013 Jul 28. [PubMed:23893133]
  46. Nyegaard M, Overgaard MT, Sondergaard MT, Vranas M, Behr ER, Hildebrandt LL, Lund J, Hedley PL, Camm AJ, Wettrell G, Fosdal I, Christiansen M, Borglum AD: Mutations in calmodulin cause ventricular tachycardia and sudden cardiac death. Am J Hum Genet. 2012 Oct 5;91(4):703-12. doi: 10.1016/j.ajhg.2012.08.015. [PubMed:23040497]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00836LoperamideapprovedunknowninhibitorDetails
DB00527Cinchocaineapproved, vet_approvedunknowninhibitorDetails
DB00623FluphenazineapprovedunknowninhibitorDetails
DB00753Isofluraneapproved, vet_approvedunknownother/unknownDetails
DB00850PerphenazineapprovedunknowninhibitorDetails
DB00925PhenoxybenzamineapprovedunknowninhibitorDetails
DB01023Felodipineapproved, investigationalunknownotherDetails
DB01069Promethazineapproved, investigationalunknowninhibitorDetails
DB01100PimozideapprovedunknowninhibitorDetails
DB01373Calciumapproved, nutraceuticalunknownDetails
DB01429AprindineexperimentalunknowninhibitorDetails
DB028683''-(Beta-Chloroethyl)-2'',4''-Dioxo-3, 5''-Spiro-Oxazolidino-4-Deacetoxy-VinblastineexperimentalunknownDetails
DB03977N-TrimethyllysineexperimentalunknownDetails
DB039002-Methyl-2-PropanolexperimentalunknownDetails
DB04841FlunarizineapprovedunknownDetails
DB01244Bepridilapproved, withdrawnunknownbinderDetails
DB01065Melatoninapproved, nutraceutical, vet_approvedunknownDetails
DB04825Prenylamineapproved, withdrawnunknownDetails
DB01115NifedipineapprovedunknowninhibitorDetails
DB00622Nicardipineapproved, investigationalunknownother/unknownDetails
DB08039(3Z)-N,N-DIMETHYL-2-OXO-3-(4,5,6,7-TETRAHYDRO-1H-INDOL-2-YLMETHYLIDENE)-2,3-DIHYDRO-1H-INDOLE-5-SULFONAMIDEexperimentalunknownDetails
DB08231Myristic acidexperimentalunknownDetails
DB04513N-(6-Aminohexyl)-5-Chloro-1-NaphthalenesulfonamideexperimentalunknownDetails
DB00831Trifluoperazineapproved, investigationalunknowninhibitorDetails
DB00477Chlorpromazineapproved, investigational, vet_approvedunknowninhibitorDetails
DB11093Calcium Citrateapproved, investigationalunknownagonistDetails
DB11348Calcium PhosphateapprovedunknownagonistDetails
DB13800Calcium levulinateapproved, experimentalunknownagonistDetails
DB14481Calcium phosphate dihydrateapprovedunknownDetails