ID CALM1_HUMAN Reviewed; 149 AA. AC P0DP23; P02593; P62158; P70667; P99014; Q13942; Q53S29; Q61379; Q61380; AC Q96HK3; DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2017, sequence version 1. DT 02-SEP-2026, entry version 62. DE RecName: Full=Calmodulin-1 {ECO:0000312|HGNC:HGNC:1442}; GN Name=CALM1 {ECO:0000303|PubMed:7925473, ECO:0000312|HGNC:HGNC:1442}; GN Synonyms=CALM, CAM, CAM1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6385987; RA Wawrzynczak E.J., Perham R.N.; RT "Isolation and nucleotide sequence of a cDNA encoding human calmodulin."; RL Biochem. Int. 9:177-185(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Blood; RX PubMed=7925473; DOI=10.1111/j.1432-1033.1994.00071.x; RA Rhyner J.A., Ottiger M., Wicki R., Greenwood T.M., Strehler E.E.; RT "Structure of the human CALM1 calmodulin gene and identification of two RT CALM1-related pseudogenes CALM1P1 and CALM1P2."; RL Eur. J. Biochem. 225:71-82(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Lung, Lymph, Placenta, and Urinary bladder; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, AND METHYLATION AT RP LYS-116. RC TISSUE=Brain; RX PubMed=7093203; DOI=10.1021/bi00539a041; RA Sasagawa T., Ericsson L.H., Walsh K.A., Schreiber W.E., Fischer E.H., RA Titani K.; RT "Complete amino acid sequence of human brain calmodulin."; RL Biochemistry 21:2565-2569(1982). RN [7] RP PROTEIN SEQUENCE OF 2-31 AND 92-107, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Osteosarcoma; RA Bienvenut W.V., Bensaad K., Vousden K.H.; RL Submitted (FEB-2008) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 15-31; 77-107 AND 128-149, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP INTERACTION WITH TTN. RX PubMed=9804419; DOI=10.1038/27603; RA Mayans O., van der Ven P.F.M., Wilm M., Mues A., Young P., Furst D.O., RA Wilmanns M., Gautel M.; RT "Structural basis for activation of the titin kinase domain during RT myofibrillogenesis."; RL Nature 395:863-869(1998). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [11] RP INTERACTION WITH SRY. RX PubMed=12871148; DOI=10.2174/0929866033479004; RA Kelly S., Yotis J., Macris M., Harley V.; RT "Recombinant expression, purification and characterisation of the HMG RT domain of human SRY."; RL Protein Pept. Lett. 10:281-286(2003). RN [12] RP INTERACTION WITH USP6. RX PubMed=16127172; DOI=10.1074/jbc.m505220200; RA Shen C., Ye Y., Robertson S.E., Lau A.W., Mak D.O., Chou M.M.; RT "Calcium/calmodulin regulates ubiquitination of the ubiquitin-specific RT protease TRE17/USP6."; RL J. Biol. Chem. 280:35967-35973(2005). RN [13] RP INTERACTION WITH SRY. RX PubMed=15746192; DOI=10.1210/me.2004-0334; RA Sim H., Rimmer K., Kelly S., Ludbrook L.M., Clayton A.H., Harley V.R.; RT "Defective calmodulin-mediated nuclear transport of the sex-determining RT region of the Y chromosome (SRY) in XY sex reversal."; RL Mol. Endocrinol. 19:1884-1892(2005). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [15] RP FUNCTION, INTERACTION WITH CCP110, AND SUBCELLULAR LOCATION. RX PubMed=16760425; DOI=10.1091/mbc.e06-04-0371; RA Tsang W.Y., Spektor A., Luciano D.J., Indjeian V.B., Chen Z., RA Salisbury J.L., Sanchez I., Dynlacht B.D.; RT "CP110 cooperates with two calcium-binding proteins to regulate cytokinesis RT and genome stability."; RL Mol. Biol. Cell 17:3423-3434(2006). RN [16] RP INTERACTION WITH CEP97 AND CCP110. RX PubMed=17719545; DOI=10.1016/j.cell.2007.06.027; RA Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D.; RT "Cep97 and CP110 suppress a cilia assembly program."; RL Cell 130:678-690(2007). RN [17] RP INTERACTION WITH KCNQ1. RX PubMed=18165683; DOI=10.1074/jbc.m707541200; RA Wiener R., Haitin Y., Shamgar L., Fernandez-Alonso M.C., Martos A., RA Chomsky-Hecht O., Rivas G., Attali B., Hirsch J.A.; RT "The KCNQ1 (Kv7.1) COOH terminus, a multitiered scaffold for subunit RT assembly and protein interaction."; RL J. Biol. Chem. 283:5815-5830(2008). RN [18] RP INTERACTION WITH RYR1 AND RYR2. RX PubMed=18650434; DOI=10.1074/jbc.m804432200; RA Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F., RA Weber D.J.; RT "S100A1 and calmodulin compete for the same binding site on ryanodine RT receptor."; RL J. Biol. Chem. 283:26676-26683(2008). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100 AND TYR-139, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22 AND LYS-95, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [23] RP INTERACTION WITH CDK5RAP2. RX PubMed=20466722; DOI=10.1074/jbc.m110.105965; RA Wang Z., Wu T., Shi L., Zhang L., Zheng W., Qu J.Y., Niu R., Qi R.Z.; RT "Conserved motif of CDK5RAP2 mediates its localization to centrosomes and RT the Golgi complex."; RL J. Biol. Chem. 285:22658-22665(2010). RN [24] RP INTERACTION WITH RUBELLA VIRUS PROTEASE/METHYLTRANSFERASE P150. RX PubMed=20086014; DOI=10.1074/jbc.m109.097063; RA Zhou Y., Tzeng W.P., Wong H.C., Ye Y., Jiang J., Chen Y., Huang Y., RA Suppiah S., Frey T.K., Yang J.J.; RT "Calcium-dependent association of calmodulin with the rubella virus RT nonstructural protease domain."; RL J. Biol. Chem. 285:8855-8868(2010). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [27] RP INTERACTION WITH ORAI1. RX PubMed=23109337; DOI=10.1074/jbc.m112.380964; RA Liu Y., Zheng X., Mueller G.A., Sobhany M., DeRose E.F., Zhang Y., RA London R.E., Birnbaumer L.; RT "Crystal structure of calmodulin binding domain of orai1 in complex with RT Ca2+ calmodulin displays a unique binding mode."; RL J. Biol. Chem. 287:43030-43041(2012). RN [28] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [29] RP INTERACTION WITH FCHO1. RX PubMed=22484487; DOI=10.1038/ncb2473; RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., RA Tsang M., Traub L.M.; RT "Distinct and separable activities of the endocytic clathrin-coat RT components Fcho1/2 and AP-2 in developmental patterning."; RL Nat. Cell Biol. 14:488-501(2012). RN [30] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-102, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND THR-111, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [33] RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [34] RP IDENTIFICATION IN THE SIFI COMPLEX. RX PubMed=25582440; DOI=10.1074/mcp.m114.042168; RA Hong J.H., Kaustov L., Coyaud E., Srikumar T., Wan J., Arrowsmith C., RA Raught B.; RT "KCMF1 (potassium channel modulatory factor 1) Links RAD6 to UBR4 RT (ubiquitin N-recognin domain-containing E3 ligase 4) and lysosome-mediated RT degradation."; RL Mol. Cell. Proteomics 14:674-685(2015). RN [35] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [36] RP FUNCTION, AND INTERACTION WITH PIK3C3. RX PubMed=28890335; DOI=10.1016/j.molcel.2017.08.005; RA Zhao Y.G., Chen Y., Miao G., Zhao H., Qu W., Li D., Wang Z., Liu N., Li L., RA Chen S., Liu P., Feng D., Zhang H.; RT "The ER-Localized Transmembrane Protein EPG-3/VMP1 Regulates SERCA Activity RT to Control ER-Isolation Membrane Contacts for Autophagosome Formation."; RL Mol. Cell 67:974.e6-989.e6(2017). RN [37] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [38] RP INTERACTION WITH KIF1A. RX PubMed=30021165; DOI=10.1016/j.celrep.2018.06.071; RA Stucchi R., Plucinska G., Hummel J.J.A., Zahavi E.E., Guerra San Juan I., RA Klykov O., Scheltema R.A., Altelaar A.F.M., Hoogenraad C.C.; RT "Regulation of KIF1A-Driven Dense Core Vesicle Transport: Ca2+/CaM Controls RT DCV Binding and Liprin-alpha/TANC2 Recruits DCVs to Postsynaptic Sites."; RL Cell Rep. 24:685-700(2018). RN [39] RP INTERACTION WITH SLC9A1. RX PubMed=30287853; DOI=10.1038/s41598-018-33096-5; RA Fuchs S., Hansen S.C., Markones M., Mymrikov E.V., Heerklotz H., Hunte C.; RT "Calcineurin B homologous protein 3 binds with high affinity to the CHP RT binding domain of the human sodium/proton exchanger NHE1."; RL Sci. Rep. 8:14837-14837(2018). RN [40] RP INTERACTION WITH KCNN3. RX PubMed=31155282; DOI=10.1016/j.ajhg.2019.04.012; RA Bauer C.K., Schneeberger P.E., Kortuem F., Altmueller J., RA Santos-Simarro F., Baker L., Keller-Ramey J., White S.M., Campeau P.M., RA Gripp K.W., Kutsche K.; RT "Gain-of-function mutations in KCNN3 encoding the small-conductance Ca2+- RT activated K+ channel SK3 cause Zimmermann-Laband syndrome."; RL Am. J. Hum. Genet. 104:1139-1157(2019). RN [41] RP INTERACTION WITH LEGIONELLA PNEUMOPHILA SIDJ (MICROBIAL INFECTION), AND RP FUNCTION (MICROBIAL INFECTION). RX PubMed=31330532; DOI=10.1038/s41586-019-1440-8; RA Bhogaraju S., Bonn F., Mukherjee R., Adams M., Pfleiderer M.M., Galej W.P., RA Matkovic V., Lopez-Mosqueda J., Kalayil S., Shin D., Dikic I.; RT "Inhibition of bacterial ubiquitin ligases by SidJ-calmodulin catalysed RT glutamylation."; RL Nature 572:382-386(2019). RN [42] RP INTERACTION WITH SLC26A5. RX PubMed=33667636; DOI=10.1016/j.jsb.2021.107714; RA Costanzi E., Coletti A., Zambelli B., Macchiarulo A., Bellanda M., RA Battistutta R.; RT "Calmodulin binds to the STAS domain of SLC26A5 prestin with a calcium- RT dependent, one-lobe, binding mode."; RL J. Struct. Biol. 213:107714-107714(2021). RN [43] RP INTERACTION WITH C.VIOLACEUM COPC TOXIN (MICROBIAL INFECTION), AND FUNCTION RP (MICROBIAL INFECTION). RX PubMed=35338844; DOI=10.1016/j.molcel.2022.03.010; RA Peng T., Tao X., Xia Z., Hu S., Xue J., Zhu Q., Pan X., Zhang Q., Li S.; RT "Pathogen hijacks programmed cell death signaling by arginine ADPR- RT deacylization of caspases."; RL Mol. Cell 82:1806-1820(2022). RN [44] RP INTERACTION WITH C.VIOLACEUM COPC TOXIN (MICROBIAL INFECTION), AND FUNCTION RP (MICROBIAL INFECTION). RX PubMed=35446120; DOI=10.1128/mbio.00690-22; RA Liu Y., Zeng H., Hou Y., Li Z., Li L., Song X., Ding J., Shao F., Xu Y.; RT "Calmodulin binding activates chromobacterium CopC effector to ADP- RT riboxanate host apoptotic caspases."; RL MBio 0:0-0(2022). RN [45] RP FUNCTION, ACTIVITY REGULATION (MICROBIAL INFECTION), AND INTERACTION WITH RP S.FLEXNERI OSPC1 AND OSPC3 (MICROBIAL INFECTION). RX PubMed=35568036; DOI=10.1016/j.cell.2022.04.028; RA Alphonse N., Wanford J.J., Voak A.A., Gay J., Venkhaya S., Burroughs O., RA Mathew S., Lee T., Evans S.L., Zhao W., Frowde K., Alrehaili A., RA Dickenson R.E., Munk M., Panina S., Mahmood I.F., Llorian M., RA Stanifer M.L., Boulant S., Berchtold M.W., Bergeron J.R.C., Wack A., RA Lesser C.F., Odendall C.; RT "A family of conserved bacterial virulence factors dampens interferon RT responses by blocking calcium signaling."; RL Cell 185:2354-2369(2022). RN [46] RP IDENTIFICATION IN THE SIFI COMPLEX. RX PubMed=38297121; DOI=10.1038/s41586-023-06985-7; RA Haakonsen D.L., Heider M., Ingersoll A.J., Vodehnal K., Witus S.R., RA Uenaka T., Wernig M., Rape M.; RT "Stress response silencing by an E3 ligase mutated in neurodegeneration."; RL Nature 626:874-880(2024). RN [47] {ECO:0007744|PDB:1NKF} RP STRUCTURE BY NMR OF 95-104. RX PubMed=9927666; DOI=10.1073/pnas.96.3.903; RA Siedlecka M., Goch G., Ejchart A., Sticht H., Bierzyski A.; RT "Alpha-helix nucleation by a calcium-binding peptide loop."; RL Proc. Natl. Acad. Sci. U.S.A. 96:903-908(1999). RN [48] {ECO:0007744|PDB:1J7O, ECO:0007744|PDB:1J7P} RP STRUCTURE BY NMR OF 1-77 AND 83-149. RX PubMed=11685248; DOI=10.1038/nsb1101-990; RA Chou J.J., Li S., Klee C.B., Bax A.; RT "Solution structure of Ca(2+)-calmodulin reveals flexible hand-like RT properties of its domains."; RL Nat. Struct. Biol. 8:990-997(2001). RN [49] {ECO:0007744|PDB:1CLL} RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH CALCIUM, AND RP CALCIUM-BINDING SITES. RX PubMed=1474585; DOI=10.1016/0022-2836(92)90324-d; RA Chattopadhyaya R., Meador W.E., Means A.R., Quiocho F.A.; RT "Calmodulin structure refined at 1.7 A resolution."; RL J. Mol. Biol. 228:1177-1192(1992). RN [50] {ECO:0007744|PDB:1CTR} RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS). RX PubMed=7803388; DOI=10.1021/bi00255a006; RA Cook W.J., Walter L.J., Walter M.R.; RT "Drug binding by calmodulin: crystal structure of a calmodulin- RT trifluoperazine complex."; RL Biochemistry 33:15259-15265(1994). RN [51] {ECO:0007744|PDB:1K90, ECO:0007744|PDB:1K93} RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 6-149. RX PubMed=11807546; DOI=10.1038/415396a; RA Drum C.L., Yan S.-Z., Bard J., Shen Y.-Q., Lu D., Soelaiman S., RA Grabarek Z., Bohm A., Tang W.-J.; RT "Structural basis for the activation of anthrax adenylyl cyclase exotoxin RT by calmodulin."; RL Nature 415:396-402(2002). RN [52] {ECO:0007744|PDB:1LVC} RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 1-149 IN COMPLEX WITH ANTHRAX RP EDEMA FACTOR CYA. RX PubMed=12485993; DOI=10.1093/emboj/cdf681; RA Shen Y., Lee Y.-S., Soelaiman S., Bergson P., Lu D., Chen A., RA Beckingham K., Grabarek Z., Mrksich M., Tang W.-J.; RT "Physiological calcium concentrations regulate calmodulin binding and RT catalysis of adenylyl cyclase exotoxins."; RL EMBO J. 21:6721-6732(2002). RN [53] {ECO:0007744|PDB:1IWQ} RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MARCKS. RX PubMed=12577052; DOI=10.1038/nsb900; RA Yamauchi E., Nakatsu T., Matsubara M., Kato H., Taniguchi H.; RT "Crystal structure of a MARCKS peptide containing the calmodulin-binding RT domain in complex with Ca2+-calmodulin."; RL Nat. Struct. Biol. 10:226-231(2003). RN [54] {ECO:0007744|PDB:2BE6} RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-150 IN COMPLEX WITH CACNA1C. RX PubMed=16299511; DOI=10.1038/nsmb1027; RA Van Petegem F., Chatelain F.C., Minor D.L. Jr.; RT "Insights into voltage-gated calcium channel regulation from the structure RT of the CaV1.2 IQ domain-Ca2+/calmodulin complex."; RL Nat. Struct. Mol. Biol. 12:1108-1115(2005). RN [55] {ECO:0007744|PDB:1XFU, ECO:0007744|PDB:1XFV, ECO:0007744|PDB:1XFW, ECO:0007744|PDB:1XFX, ECO:0007744|PDB:1XFY, ECO:0007744|PDB:1XFZ} RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH ANTHRAX EDEMA FACTOR RP CYA. RX PubMed=15719022; DOI=10.1038/sj.emboj.7600574; RA Shen Y., Zhukovskaya N.L., Guo Q., Florian J., Tang W.-J.; RT "Calcium-independent calmodulin binding and two-metal-ion catalytic RT mechanism of anthrax edema factor."; RL EMBO J. 24:929-941(2005). RN [56] RP STRUCTURE BY NMR IN COMPLEX WITH SCN5A. RX PubMed=21167176; DOI=10.1016/j.jmb.2010.11.046; RA Chagot B., Chazin W.J.; RT "Solution NMR structure of Apo-calmodulin in complex with the IQ motif of RT human cardiac sodium channel NaV1.5."; RL J. Mol. Biol. 406:106-119(2011). RN [57] {ECO:0007744|PDB:3J41} RP STRUCTURE BY ELECTRON MICROSCOPY (25 ANGSTROMS) IN COMPLEX WITH MIP, RP FUNCTION, AND INTERACTION WITH MIP. RX PubMed=23893133; DOI=10.1038/nsmb.2630; RA Reichow S.L., Clemens D.M., Freites J.A., Nemeth-Cahalan K.L., Heyden M., RA Tobias D.J., Hall J.E., Gonen T.; RT "Allosteric mechanism of water-channel gating by Ca(2+)-calmodulin."; RL Nat. Struct. Mol. Biol. 20:1085-1092(2013). RN [58] {ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C} RP X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) IN COMPLEX WITH KCNQ1 AND CALCIUM, RP FUNCTION, INTERACTION WITH KCNQ1, AND DOMAIN. RX PubMed=25441029; DOI=10.1016/j.str.2014.07.016; RA Sachyani D., Dvir M., Strulovich R., Tria G., Tobelaim W., Peretz A., RA Pongs O., Svergun D., Attali B., Hirsch J.A.; RT "Structural basis of a Kv7.1 potassium channel gating module: studies of RT the intracellular c-terminal domain in complex with calmodulin."; RL Structure 22:1582-1594(2014). RN [59] {ECO:0007744|PDB:5J03} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH CALCIUM; KCNQ2 AND RP KCNQ3, INTERACTION WITH KCNQ2 AND KCNQ3, AND CALCIUM-BINDING SITES. RX PubMed=27564677; DOI=10.1021/acs.biochem.6b00477; RA Strulovich R., Tobelaim W.S., Attali B., Hirsch J.A.; RT "Structural insights into the M-channel proximal C-terminus/calmodulin RT complex."; RL Biochemistry 55:5353-5365(2016). RN [60] {ECO:0007744|PDB:2N77} RP STRUCTURE BY NMR OF 77-149 IN COMPLEX WITH PCP4, INTERACTION WITH PCP4, AND RP REGION. RX PubMed=27876793; DOI=10.1038/ncomms13583; RA Wang X., Putkey J.A.; RT "PEP-19 modulates calcium binding to calmodulin by electrostatic RT steering."; RL Nat. Commun. 7:13583-13583(2016). RN [61] {ECO:0007744|PDB:2M55} RP STRUCTURE BY NMR, AND INTERACTION WITH ALPHA-SYNUCLEIN/SNCA. RX PubMed=23607618; DOI=10.1021/bi400199p; RA Gruschus J.M., Yap T.L., Pistolesi S., Maltsev A.S., Lee J.C.; RT "NMR structure of calmodulin complexed to an N-terminally acetylated alpha- RT synuclein peptide."; RL Biochemistry 52:3436-3445(2013). RN [62] {ECO:0007744|PDB:6CNM, ECO:0007744|PDB:6CNN, ECO:0007744|PDB:6CNO} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) IN COMPLEX WITH KCNN4 AND RP CALCIUM, SUBUNIT, AND DOMAIN. RX PubMed=29724949; DOI=10.1126/science.aas9466; RA Lee C.H., MacKinnon R.; RT "Activation mechanism of a human SK-calmodulin channel complex elucidated RT by cryo-EM structures."; RL Science 360:508-513(2018). RN [63] {ECO:0007744|PDB:7WJI} RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS) IN COMPLEX WITH NALCN; RP NALF1; UNC80 AND UNC79, AND INTERACTION WITH NALCN. RX PubMed=35387979; DOI=10.1038/s41421-022-00392-4; RA Zhou L., Liu H., Zhao Q., Wu J., Yan Z.; RT "Architecture of the human NALCN channelosome."; RL Cell Discov. 8:33-33(2022). RN [64] {ECO:0007744|PDB:7XN4, ECO:0007744|PDB:7XN5, ECO:0007744|PDB:7XN6} RP STRUCTURE BY ELECTRON MICROSCOPY (3.18 ANGSTROMS) IN COMPLEX WITH RP C.VIOLACEUM COPC AND CASP3, INTERACTION WITH C.VIOLACEUM COPC TOXIN RP (MICROBIAL INFECTION), AND FUNCTION (MICROBIAL INFECTION). RX PubMed=36423631; DOI=10.1016/j.molcel.2022.10.032; RA Zhang K., Peng T., Tao X., Tian M., Li Y., Wang Z., Ma S., Hu S., Pan X., RA Xue J., Luo J., Wu Q., Fu Y., Li S.; RT "Structural insights into caspase ADPR deacylization catalyzed by a RT bacterial effector and host calmodulin."; RL Mol. Cell 0:0-0(2022). RN [65] {ECO:0007744|PDB:7SX3, ECO:0007744|PDB:7SX4} RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) IN COMPLEX WITH NALCN; RP NALF1; UNC80 AND UNC79, AND INTERACTION WITH NALCN. RX PubMed=34929720; DOI=10.1038/s41586-021-04313-5; RA Kschonsak M., Chua H.C., Weidling C., Chakouri N., Noland C.L., Schott K., RA Chang T., Tam C., Patel N., Arthur C.P., Leitner A., Ben-Johny M., RA Ciferri C., Pless S.A., Payandeh J.; RT "Structural architecture of the human NALCN channelosome."; RL Nature 603:180-186(2022). RN [66] {ECO:0007744|PDB:7VMB} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH IQSEC1, AND RP INTERACTION WITH IQSEC1. RX PubMed=37787765; DOI=10.1083/jcb.202307117; RA Bai G., Li H., Qin P., Guo Y., Yang W., Lian Y., Ye F., Chen J., Wu M., RA Huang R., Li J., Lu Y., Zhang M.; RT "Ca2+-induced release of IQSEC2/BRAG1 autoinhibition under physiological RT and pathological conditions."; RL J. Cell Biol. 222:e202307117-e202307117(2023). RN [67] {ECO:0007744|PDB:7WR4, ECO:0007744|PDB:7WR5} RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 102-377 IN COMPLEX WITH CASP4 AND RP S.FLEXNERI OSPC3, FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH RP S.FLEXNERI OSPC3 (MICROBIAL INFECTION). RX PubMed=36624349; DOI=10.1038/s41594-022-00888-3; RA Hou Y., Zeng H., Li Z., Feng N., Meng F., Xu Y., Li L., Shao F., Ding J.; RT "Structural mechanisms of calmodulin activation of Shigella effector OspC3 RT to ADP-riboxanate caspase-4/11 and block pyroptosis."; RL Nat. Struct. Mol. Biol. 30:261-272(2023). RN [68] {ECO:0007744|PDB:9D9Z, ECO:0007744|PDB:9NWE} RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) IN COMPLEX WITH UBR4; RP KCMF1 AND CA(2+), FUNCTION, AND SUBUNIT. RX PubMed=40328314; DOI=10.1038/s41586-025-09074-z; RA Yang Z., Haakonsen D.L., Heider M., Witus S.R., Zelter A., Beschauner T., RA MacCoss M.J., Rape M.; RT "Molecular basis of SIFI activity in the integrated stress response."; RL Nature 643:1117-1126(2025). RN [69] {ECO:0007744|PDB:9QWU, ECO:0007744|PDB:9QX0} RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) IN COMPLEX WITH UBR4 AND RP KCMF1, FUNCTION, AND SUBUNIT. RX PubMed=40875847; DOI=10.1126/science.adv9309; RA Grabarczyk D.B., Ehrmann J.F., Murphy P., Yang W.S., Kurzbauer R., RA Bell L.E., Deszcz L., Neuhold J., Schleiffer A., Shulkina A., Lee J., RA Shin J.S., Meinhart A., Versteeg G.A., Zavodszky E., Song H.K., Hegde R.S., RA Clausen T.; RT "Architecture of the UBR4 complex, a giant E4 ligase central to eukaryotic RT protein quality control."; RL Science 389:909-914(2025). RN [70] RP INVOLVEMENT IN CPVT4, VARIANTS CPVT4 ILE-54 AND SER-98, AND RP CHARACTERIZATION OF VARIANTS CPVT4 ILE-54 AND SER-98. RX PubMed=23040497; DOI=10.1016/j.ajhg.2012.08.015; RA Nyegaard M., Overgaard M.T., Sondergaard M.T., Vranas M., Behr E.R., RA Hildebrandt L.L., Lund J., Hedley P.L., Camm A.J., Wettrell G., Fosdal I., RA Christiansen M., Borglum A.D.; RT "Mutations in calmodulin cause ventricular tachycardia and sudden cardiac RT death."; RL Am. J. Hum. Genet. 91:703-712(2012). RN [71] RP INVOLVEMENT IN LQT14, VARIANTS LQT14 GLY-130 AND LEU-142, AND RP CHARACTERIZATION OF VARIANTS LQT14 GLY-130 AND LEU-142. RX PubMed=23388215; DOI=10.1161/circulationaha.112.001216; RA Crotti L., Johnson C.N., Graf E., De Ferrari G.M., Cuneo B.F., Ovadia M., RA Papagiannis J., Feldkamp M.D., Rathi S.G., Kunic J.D., Pedrazzini M., RA Wieland T., Lichtner P., Beckmann B.M., Clark T., Shaffer C., Benson D.W., RA Kaab S., Meitinger T., Strom T.M., Chazin W.J., Schwartz P.J., RA George A.L. Jr.; RT "Calmodulin mutations associated with recurrent cardiac arrest in RT infants."; RL Circulation 127:1009-1017(2013). RN [72] RP CHARACTERIZATION OF VARIANT LQT14 LEU-90. RX PubMed=25036739; DOI=10.1016/j.febslet.2014.07.007; RA Nomikos M., Thanassoulas A., Beck K., Vassilakopoulou V., Hu H., RA Calver B.L., Theodoridou M., Kashir J., Blayney L., Livaniou E., RA Rizkallah P., Nounesis G., Lai F.A.; RT "Altered RyR2 regulation by the calmodulin F90L mutation associated with RT idiopathic ventricular fibrillation and early sudden cardiac death."; RL FEBS Lett. 588:2898-2902(2014). RN [73] RP INVOLVEMENT IN LQT14, AND VARIANT LQT14 LEU-90. RX PubMed=24076290; DOI=10.1016/j.jacc.2013.07.091; RA Marsman R.F., Barc J., Beekman L., Alders M., Dooijes D., RA van den Wijngaard A., Ratbi I., Sefiani A., Bhuiyan Z.A., Wilde A.A., RA Bezzina C.R.; RT "A mutation in CALM1 encoding calmodulin in familial idiopathic ventricular RT fibrillation in childhood and adolescence."; RL J. Am. Coll. Cardiol. 63:259-266(2014). RN [74] RP VARIANTS CPVT4 ILE-54 AND SER-98, CHARACTERIZATION OF VARIANTS CPVT4 ILE-54 RP AND SER-98, VARIANTS LQT14 GLY-130 AND LEU-142, CHARACTERIZATION OF RP VARIANTS LQT14 GLY-130 AND LEU-142, AND INTERACTION WITH RYR2. RX PubMed=26164367; DOI=10.1016/j.bbagen.2015.07.001; RA Vassilakopoulou V., Calver B.L., Thanassoulas A., Beck K., Hu H., RA Buntwal L., Smith A., Theodoridou M., Kashir J., Blayney L., Livaniou E., RA Nounesis G., Lai F.A., Nomikos M.; RT "Distinctive malfunctions of calmodulin mutations associated with heart RT RyR2-mediated arrhythmic disease."; RL Biochim. Biophys. Acta 1850:2168-2176(2015). RN [75] RP VARIANTS CPVT4 ILE-54 AND SER-98, CHARACTERIZATION OF VARIANTS CPVT4 RP ILE-54; SER-98, AND INTERACTION WITH RYR2. RX PubMed=27516456; DOI=10.1161/circep.116.004161; RA Gomez-Hurtado N., Boczek N.J., Kryshtal D.O., Johnson C.N., Sun J., RA Nitu F.R., Cornea R.L., Chazin W.J., Calvert M.L., Tester D.J., RA Ackerman M.J., Knollmann B.C.; RT "Novel CPVT-Associated Calmodulin Mutation in CALM3 (CALM3-A103V) Activates RT Arrhythmogenic Ca Waves and Sparks."; RL Circ. Arrhythm. Electrophysiol. 9:0-0(2016). RN [76] RP VARIANTS LQT14 GLY-141 AND LEU-142, CHARACTERIZATION OF VARIANT LQT14 RP GLY-141, AND FUNCTION. RX PubMed=26969752; DOI=10.1161/circgenetics.115.001323; RA Boczek N.J., Gomez-Hurtado N., Ye D., Calvert M.L., Tester D.J., RA Kryshtal D.O., Hwang H.S., Johnson C.N., Chazin W.J., Loporcaro C.G., RA Shah M., Papez A.L., Lau Y.R., Kanter R., Knollmann B.C., Ackerman M.J.; RT "Spectrum and Prevalence of CALM1-, CALM2-, and CALM3-Encoded Calmodulin RT Variants in Long QT Syndrome and Functional Characterization of a Novel RT Long QT Syndrome-Associated Calmodulin Missense Variant, E141G."; RL Circ. Cardiovasc. Genet. 9:136-146(2016). RN [77] RP VARIANTS CPVT4 ILE-54 AND SER-98, CHARACTERIZATION OF VARIANTS CPVT4 ILE-54 RP AND SER-98, VARIANTS LQT14 LEU-90 AND GLY-130, CHARACTERIZATION OF VARIANTS RP LQT14 LEU-90 AND GLY-130, AND FUNCTION. RX PubMed=27165696; DOI=10.1016/j.hrthm.2016.05.009; RA Yu C.C., Ko J.S., Ai T., Tsai W.C., Chen Z., Rubart M., Vatta M., RA Everett T.H. IV, George A.L. Jr., Chen P.S.; RT "Arrhythmogenic calmodulin mutations impede activation of small-conductance RT calcium-activated potassium current."; RL Heart Rhythm 13:1716-1723(2016). RN [78] RP CHARACTERIZATION OF VARIANT LQT14 LEU-142. RX PubMed=28158429; DOI=10.1093/cvr/cvx006; RA Rocchetti M., Sala L., Dreizehnter L., Crotti L., Sinnecker D., Mura M., RA Pane L.S., Altomare C., Torre E., Mostacciuolo G., Severi S., Porta A., RA De Ferrari G.M., George A.L. Jr., Schwartz P.J., Gnecchi M., Moretti A., RA Zaza A.; RT "Elucidating arrhythmogenic mechanisms of long-QT syndrome CALM1-F142L RT mutation in patient-specific induced pluripotent stem cell-derived RT cardiomyocytes."; RL Cardiovasc. Res. 113:531-541(2017). RN [79] RP VARIANT LQT14 VAL-141, CHARACTERIZATION OF VARIANT LQT14 VAL-141, AND RP FUNCTION. RX PubMed=31454269; DOI=10.1161/circgen.119.002581; RA Wren L.M., Jimenez-Jaimez J., Al-Ghamdi S., Al-Aama J.Y., Bdeir A., RA Al-Hassnan Z.N., Kuan J.L., Foo R.Y., Potet F., Johnson C.N., Aziz M.C., RA Carvill G.L., Kaski J.P., Crotti L., Perin F., Monserrat L., Burridge P.W., RA Schwartz P.J., Chazin W.J., Bhuiyan Z.A., George A.L. Jr.; RT "Genetic mosaicism in calmodulinopathy."; RL Circ. Genom. Precis. Med. 12:375-385(2019). CC -!- FUNCTION: Calmodulin acts as part of a calcium signal transduction CC pathway by mediating the control of a large number of enzymes, ion CC channels, aquaporins and other proteins through calcium-binding CC (PubMed:16760425, PubMed:23893133, PubMed:26969752, PubMed:27165696, CC PubMed:28890335, PubMed:31454269, PubMed:35568036). Calcium-binding is CC required for the activation of calmodulin (PubMed:16760425, CC PubMed:23893133, PubMed:26969752, PubMed:27165696, PubMed:28890335, CC PubMed:31454269, PubMed:35568036). Among the enzymes to be stimulated CC by the calmodulin-calcium complex are a number of protein kinases, such CC as myosin light-chain kinases and calmodulin-dependent protein kinase CC type II (CaMK2), and phosphatases (PubMed:16760425, PubMed:23893133, CC PubMed:26969752, PubMed:27165696, PubMed:28890335, PubMed:31454269, CC PubMed:35568036). Together with CCP110 and centrin, is involved in a CC genetic pathway that regulates the centrosome cycle and progression CC through cytokinesis (PubMed:16760425). Is a regulator of voltage- CC dependent L-type calcium channels (PubMed:31454269). Mediates calcium- CC dependent inactivation of CACNA1C (PubMed:26969752). Positively CC regulates calcium-activated potassium channel activity of KCNN2 CC (PubMed:27165696). Forms a potassium channel complex with KCNQ1 and CC regulates electrophysiological activity of the channel via calcium- CC binding (PubMed:25441029). Acts as a sensor to modulate the endoplasmic CC reticulum contacts with other organelles mediated by VMP1:ATP2A2 CC (PubMed:28890335). Component of the silencing factor of the integrated CC stress response (SIFI) complex, a multiprotein complex required to turn CC off the mitochondrial stress response after a specific stress event has CC been resolved (PubMed:38297121, PubMed:40328314, PubMed:40875847). CC {ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:23893133, CC ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:26969752, CC ECO:0000269|PubMed:27165696, ECO:0000269|PubMed:28890335, CC ECO:0000269|PubMed:31454269, ECO:0000269|PubMed:35568036, CC ECO:0000269|PubMed:38297121, ECO:0000269|PubMed:40328314, CC ECO:0000269|PubMed:40875847}. CC -!- FUNCTION: (Microbial infection) Required for Legionella pneumophila CC SidJ glutamylase activity. {ECO:0000269|PubMed:31330532}. CC -!- FUNCTION: (Microbial infection) Required for C.violaceum CopC and CC S.flexneri OspC3 arginine ADP-riboxanase activity. CC {ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120, CC ECO:0000269|PubMed:36423631, ECO:0000269|PubMed:36624349}. CC -!- ACTIVITY REGULATION: (Microbial infection) Inactivated by S.flexneri CC OspC1 and OspC3 proteins, which specifically bind the apo-form of CC calmodulin, thereby preventing calcium-binding and activity. CC {ECO:0000269|PubMed:35568036}. CC -!- SUBUNIT: Homotetramer (PubMed:29724949). Component of the SIFI complex, CC which is a dimer of 2 heterotrimers, comprising two copies each of CC UBR4, KCMF1 and calmodulin (CALM1, CALM2 or CALM3) (PubMed:25582440, CC PubMed:38297121, PubMed:40328314, PubMed:40875847). Component of the CC NALCN channelosome complex; within the complex interacts with NALCN CC (PubMed:35387979, PubMed:34929720). Interacts with MYO1C, MYO5A and CC RRAD. Interacts with MYO10 (By similarity). Interacts with CEP97, CC CCP110, TTN/titin and SRY (PubMed:12871148, PubMed:15746192, CC PubMed:16760425, PubMed:17719545, PubMed:9804419). Interacts with USP6; CC the interaction is calcium dependent (PubMed:16127172). Interacts with CC CDK5RAP2 (PubMed:20466722). Interacts with SCN5A (PubMed:21167176). CC Interacts with RYR1 (PubMed:18650434). Interacts with FCHO1 CC (PubMed:22484487). Interacts with MIP in a 1:2 stoichiometry; the CC interaction with the cytoplasmic domains from two MIP subunits promotes CC MIP water channel closure (PubMed:23893133). Interacts with ORAI1; this CC may play a role in the regulation of ORAI1-mediated calcium transport CC (By similarity). Interacts with IQCF1 (By similarity). Interacts with CC SYT7 (By similarity). Interacts with CEACAM1 (via cytoplasmic domain); CC this interaction is in a calcium dependent manner and reduces CC homophilic cell adhesion through dissociation of dimer (By similarity). CC Interacts with RYR2; regulates RYR2 calcium-release channel activity CC (PubMed:18650434, PubMed:26164367, PubMed:27516456). Interacts with CC PCP4; regulates calmodulin calcium-binding (PubMed:27876793). Interacts CC with the heterotetrameric KCNQ2 and KCNQ3 channel; the interaction is CC calcium-independent, constitutive and participates in the proper CC assembly of a functional heterotetrameric M channel (PubMed:27564677). CC Interacts with alpha-synuclein/SNCA (PubMed:23607618). Interacts with CC SLC9A1 in a calcium-dependent manner (PubMed:30287853). In the absence CC of Ca(+2), interacts with GIMAP4 (via IQ domain) (By similarity). CC Interacts with SCN8A; the interaction modulates the inactivation rate CC of SCN8A (By similarity). Interaction with KIF1A; the interaction is CC increased in presence of calcium and increases neuronal dense core CC vesicles motility (PubMed:30021165). Interacts with KCNN3 CC (PubMed:31155282). Interacts with KCNQ1 (via C-terminus); forms a CC heterooctameric structure (with 4:4 KCNQ1:CALM stoichiometry) in a CC calcium-independent manner (PubMed:18165683, PubMed:25441029). CC Interacts with PIK3C3; the interaction modulates PIK3C3 kinase activity CC (PubMed:28890335). Interacts with HINT1; interaction increases in the CC presence of calcium ions (By similarity). Interacts with HINT3 (By CC similarity). Interacts with GARIN2; in mature sperm flagella (By CC similarity). Interacts with IQUB (By similarity). Interacts with CC SLC26A5 (via STAS domain); this interaction is calcium-dependent and CC the STAS domain interacts with only one lobe of CALM which is an CC elongated conformation (PubMed:33667636). Ca(2+)-bound CALM1 binds CC CNGA1:CNGB1 channel (via CaM1 and CaM2 regions); this interaction CC modulates the affinity of the channel for cNMPs in response to CC intracellular Ca(2+) levels. Interacts with ITPR1; this interaction CC inhibits inositol 1,4,5 trisphosphate binding in both the presence and CC absence of calcium and 1,4,5 trisphosphate-induced calcium release in CC the presence of calcium (By similarity). Interacts with KCNN4; this CC interaction allows channel opening (PubMed:29724949). Interacts with CC KCNN2; this interaction regulates the channel activity through calcium- CC binding (By similarity). Interacts with IQSEC1 (via IQ and SEC7 CC domains) (PubMed:37787765). {ECO:0000250|UniProtKB:P0DP26, CC ECO:0000250|UniProtKB:P0DP29, ECO:0000250|UniProtKB:P62157, CC ECO:0000250|UniProtKB:P62161, ECO:0000250|UniProtKB:P62204, CC ECO:0000269|PubMed:12485993, ECO:0000269|PubMed:12577052, CC ECO:0000269|PubMed:12871148, ECO:0000269|PubMed:15719022, CC ECO:0000269|PubMed:15746192, ECO:0000269|PubMed:16127172, CC ECO:0000269|PubMed:16299511, ECO:0000269|PubMed:16760425, CC ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:18165683, CC ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:20466722, CC ECO:0000269|PubMed:21167176, ECO:0000269|PubMed:22484487, CC ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:23607618, CC ECO:0000269|PubMed:23893133, ECO:0000269|PubMed:25441029, CC ECO:0000269|PubMed:25582440, ECO:0000269|PubMed:26164367, CC ECO:0000269|PubMed:27516456, ECO:0000269|PubMed:27564677, CC ECO:0000269|PubMed:27876793, ECO:0000269|PubMed:28890335, CC ECO:0000269|PubMed:29724949, ECO:0000269|PubMed:30021165, CC ECO:0000269|PubMed:30287853, ECO:0000269|PubMed:31155282, CC ECO:0000269|PubMed:33667636, ECO:0000269|PubMed:34929720, CC ECO:0000269|PubMed:35387979, ECO:0000269|PubMed:37787765, CC ECO:0000269|PubMed:38297121, ECO:0000269|PubMed:40328314, CC ECO:0000269|PubMed:40875847, ECO:0000269|PubMed:9804419}. CC -!- SUBUNIT: (Microbial infection) Interacts with Rubella virus CC protease/methyltransferase p150. {ECO:0000269|PubMed:20086014}. CC -!- SUBUNIT: (Microbial infection) Interacts with Legionella pneumophila CC glutamylase SidJ. {ECO:0000269|PubMed:31330532}. CC -!- SUBUNIT: (Microbial infection) Interacts with C.violaceum CopC CC (PubMed:35338844, PubMed:35446120, PubMed:36423631). C.violaceum CopC CC interacts specifically with the apo form of calmodulin CC (PubMed:35446120, PubMed:36423631). {ECO:0000269|PubMed:35338844, CC ECO:0000269|PubMed:35446120, ECO:0000269|PubMed:36423631}. CC -!- SUBUNIT: (Microbial infection) Interacts with S.flexneri OspC1 and CC OspC3 (PubMed:35568036, PubMed:36624349). S.flexneri OspC1 and OspC3 CC interact specifically with the apo form of calmodulin and prevents CC calcium-binding (PubMed:35568036). {ECO:0000269|PubMed:35568036, CC ECO:0000269|PubMed:36624349}. CC -!- INTERACTION: CC P0DP23; O75874: IDH1; NbExp=7; IntAct=EBI-25817233, EBI-715695; CC P0DP23; Q5JU85: IQSEC2; NbExp=2; IntAct=EBI-25817233, EBI-11028607; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, spindle pole CC {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cell CC projection, cilium, flagellum {ECO:0000250|UniProtKB:P0DP26}. CC Note=Distributed throughout the cell during interphase, but during CC mitosis becomes dramatically localized to the spindle poles and the CC spindle microtubules. CC -!- DOMAIN: The N-terminal and C-terminal lobes of CALM bind to the C- CC terminus of KCNQ1 in a clamp-like conformation. Binding of CALM C- CC terminus to KCNQ1 is calcium-independent but is essential for assembly CC of the structure. Binding of CALM N-terminus to KCNQ1 is calcium- CC dependent and regulates electrophysiological activity of the channel CC (PubMed:25441029). The C-lobe interacts with KCNN4 channels in a CC calcium-independent manner, whereas the N-lobe interacts with the S4-S5 CC linker of KCNN4 in a calcium-dependent manner playing a role as calcium CC sensor and gating the channel (PubMed:29724949). CC {ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:29724949}. CC -!- PTM: Ubiquitination results in a strongly decreased activity. CC {ECO:0000250}. CC -!- PTM: Phosphorylation results in a decreased activity. CC {ECO:0000250|UniProtKB:P0DP29}. CC -!- DISEASE: Ventricular tachycardia, catecholaminergic polymorphic, 4 CC (CPVT4) [MIM:614916]: An arrhythmogenic disorder characterized by CC stress-induced, bidirectional ventricular tachycardia that may CC degenerate into cardiac arrest and cause sudden death. Patients present CC with recurrent syncope, seizures, or sudden death after physical CC activity or emotional stress. CPVT4 inheritance is autosomal dominant. CC {ECO:0000269|PubMed:23040497, ECO:0000269|PubMed:26164367, CC ECO:0000269|PubMed:27165696, ECO:0000269|PubMed:27516456}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. Mutations in CALM1 are the cause of CPVT4. CC -!- DISEASE: Long QT syndrome 14 (LQT14) [MIM:616247]: A form of long QT CC syndrome, a heart disorder characterized by a prolonged QT interval on CC the ECG and polymorphic ventricular arrhythmias. They cause syncope and CC sudden death in response to exercise or emotional stress, and can CC present with a sentinel event of sudden cardiac death in infancy. CC {ECO:0000269|PubMed:23388215, ECO:0000269|PubMed:24076290, CC ECO:0000269|PubMed:25036739, ECO:0000269|PubMed:26164367, CC ECO:0000269|PubMed:26969752, ECO:0000269|PubMed:27165696, CC ECO:0000269|PubMed:28158429, ECO:0000269|PubMed:31454269}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites. CC {ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677}. CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A question of length - Issue CC 105 of May 2009; CC URL="https://www.proteinspotlight.org/back_issues/105"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M27319; AAA35635.1; -; mRNA. DR EMBL; U12022; AAB60644.1; -; Genomic_DNA. DR EMBL; U11886; AAB60644.1; JOINED; Genomic_DNA. DR EMBL; BT006818; AAP35464.1; -; mRNA. DR EMBL; AC006536; AAD45181.1; -; Genomic_DNA. DR EMBL; AL512791; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000454; AAH00454.1; -; mRNA. DR EMBL; BC008597; AAH08597.1; -; mRNA. DR EMBL; BC011834; AAH11834.1; -; mRNA. DR EMBL; BC047523; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS9892.1; -. DR PIR; S48728; MCHU. DR RefSeq; NP_001316851.1; NM_001329922.1. DR RefSeq; NP_001734.1; NM_001743.6. DR RefSeq; NP_005175.2; NM_005184.4. DR RefSeq; NP_008819.1; NM_006888.6. DR PDB; 12DK; EM; 3.47 A; B/D/F/H=1-149. DR PDB; 1CDL; X-ray; 2.00 A; A/B/C/D=2-148. DR PDB; 1CLL; X-ray; 1.70 A; A=2-149. DR PDB; 1CTR; X-ray; 2.45 A; A=2-149. DR PDB; 1IWQ; X-ray; 2.00 A; A=2-149. DR PDB; 1J7O; NMR; -; A=2-77. DR PDB; 1J7P; NMR; -; A=83-149. DR PDB; 1K90; X-ray; 2.75 A; D/E/F=2-149. DR PDB; 1K93; X-ray; 2.95 A; D/E/F=6-149. DR PDB; 1L7Z; X-ray; 2.30 A; A=2-149. DR PDB; 1LVC; X-ray; 3.60 A; D/E/F=1-149. DR PDB; 1NKF; NMR; -; A=94-105. DR PDB; 1PK0; X-ray; 3.30 A; D/E/F=2-148. DR PDB; 1S26; X-ray; 3.00 A; D/E/F=2-149. DR PDB; 1SK6; X-ray; 3.20 A; D/E/F=2-149. DR PDB; 1SW8; NMR; -; A=2-80. DR PDB; 1UP5; X-ray; 1.90 A; A/B=2-149. DR PDB; 1WRZ; X-ray; 2.00 A; A=1-149. DR PDB; 1XFU; X-ray; 3.35 A; O/P/Q/R/S/T=1-149. DR PDB; 1XFV; X-ray; 3.35 A; O/P/Q/R/S/T=1-149. DR PDB; 1XFW; X-ray; 3.40 A; O/P/Q/R/S/T=1-149. DR PDB; 1XFX; X-ray; 3.20 A; O/P/Q/R/S/T=1-149. DR PDB; 1XFY; X-ray; 3.30 A; O/P/Q/R/S/T=1-149. DR PDB; 1XFZ; X-ray; 3.25 A; O/P/Q/R/S/T=1-149. DR PDB; 1Y6W; X-ray; 2.40 A; A=2-149. DR PDB; 1YR5; X-ray; 1.70 A; A=2-149. DR PDB; 1YRT; X-ray; 2.10 A; B=76-149. DR PDB; 1YRU; X-ray; 2.50 A; B=76-149. DR PDB; 1ZOT; X-ray; 2.20 A; B=80-148. DR PDB; 1ZUZ; X-ray; 1.91 A; A=1-149. DR PDB; 2BE6; X-ray; 2.00 A; A/B/C=1-149. DR PDB; 2F3Y; X-ray; 1.45 A; A=2-149. DR PDB; 2F3Z; X-ray; 1.60 A; A=2-149. DR PDB; 2HF5; NMR; -; A=47-114. DR PDB; 2I08; X-ray; 2.00 A; A=2-79. DR PDB; 2JZI; NMR; -; A=2-149. DR PDB; 2K0E; NMR; -; A=2-149. DR PDB; 2K0F; NMR; -; A=2-149. DR PDB; 2K0J; NMR; -; A=3-149. DR PDB; 2K61; NMR; -; A=2-149. DR PDB; 2KNE; NMR; -; A=2-149. DR PDB; 2KUG; NMR; -; A=2-149. DR PDB; 2KUH; NMR; -; A=83-149. DR PDB; 2L53; NMR; -; A=2-149. DR PDB; 2L7L; NMR; -; A=2-149. DR PDB; 2LGF; NMR; -; A=3-149. DR PDB; 2LL6; NMR; -; A=2-149. DR PDB; 2LL7; NMR; -; A=2-149. DR PDB; 2LQC; NMR; -; A=2-78. DR PDB; 2LQP; NMR; -; A=79-149. DR PDB; 2LV6; Other; -; A=2-149. DR PDB; 2M0J; NMR; -; A=2-149. DR PDB; 2M0K; NMR; -; A=2-149. DR PDB; 2M55; NMR; -; A=2-149. DR PDB; 2MG5; NMR; -; A=2-149. DR PDB; 2N27; NMR; -; A=2-149. DR PDB; 2N6A; NMR; -; A=6-147. DR PDB; 2N77; NMR; -; A=77-149. DR PDB; 2N8J; NMR; -; A=2-149. DR PDB; 2R28; X-ray; 1.86 A; A/B=1-149. DR PDB; 2V01; X-ray; 2.15 A; A=1-149. DR PDB; 2V02; X-ray; 2.20 A; A=1-149. DR PDB; 2VAY; X-ray; 1.94 A; A=4-149. DR PDB; 2W73; X-ray; 1.45 A; A/B/E/F=1-149. DR PDB; 2WEL; X-ray; 1.90 A; D=1-149. DR PDB; 2X0G; X-ray; 2.20 A; B=2-149. DR PDB; 2Y4V; X-ray; 1.80 A; A=1-149. DR PDB; 3BYA; X-ray; 1.85 A; A=2-149. DR PDB; 3DVE; X-ray; 2.35 A; A=2-149. DR PDB; 3DVJ; X-ray; 2.80 A; A=2-149. DR PDB; 3DVK; X-ray; 2.30 A; A=2-149. DR PDB; 3DVM; X-ray; 2.60 A; A=2-149. DR PDB; 3EVV; X-ray; 2.60 A; A=5-149. DR PDB; 3EWT; X-ray; 2.40 A; A=2-149. DR PDB; 3EWV; X-ray; 2.60 A; A=2-149. DR PDB; 3G43; X-ray; 2.10 A; A/B/C/D=2-149. DR PDB; 3HR4; X-ray; 2.50 A; B/D/F/H=1-149. DR PDB; 3J41; EM; 25.00 A; E/F=1-149. DR PDB; 3O77; X-ray; 2.35 A; A=1-149. DR PDB; 3O78; X-ray; 2.60 A; A/B=1-149. DR PDB; 3OXQ; X-ray; 2.55 A; A/B/C/D=1-149. DR PDB; 3SUI; X-ray; 1.95 A; A=1-149. DR PDB; 3UCT; X-ray; 1.90 A; A/B=2-80. DR PDB; 3UCW; X-ray; 1.76 A; A/B/C/D=2-80. DR PDB; 3UCY; X-ray; 1.80 A; A=2-80. DR PDB; 4BW7; X-ray; 1.81 A; A/C=1-149. DR PDB; 4BW8; X-ray; 1.80 A; A/B=1-149. DR PDB; 4BYF; X-ray; 2.74 A; B/D=1-149. DR PDB; 4DCK; X-ray; 2.20 A; B=1-149. DR PDB; 4DJC; X-ray; 1.35 A; A=1-149. DR PDB; 4GOW; X-ray; 2.60 A; D=4-147. DR PDB; 4JPZ; X-ray; 3.02 A; C/I=1-149. DR PDB; 4JQ0; X-ray; 3.84 A; C=1-149. DR PDB; 4L79; X-ray; 2.30 A; B=1-149. DR PDB; 4LZX; X-ray; 1.50 A; A=2-149. DR PDB; 4M1L; X-ray; 2.10 A; A=2-149. DR PDB; 4OVN; X-ray; 2.80 A; A/B/C/D/E=1-149. DR PDB; 4Q57; X-ray; 1.80 A; A=10-74. DR PDB; 4Q5U; X-ray; 1.95 A; A=1-149. DR PDB; 4UMO; X-ray; 3.00 A; C/D=1-149. DR PDB; 4UPU; X-ray; 2.34 A; A=2-149. DR PDB; 4V0C; X-ray; 2.86 A; C/D=1-149. DR PDB; 5COC; X-ray; 2.67 A; A=5-78. DR PDB; 5DBR; X-ray; 2.25 A; A=5-149. DR PDB; 5DOW; X-ray; 1.70 A; A/C/E/G=2-149. DR PDB; 5DSU; X-ray; 1.93 A; A=3-78. DR PDB; 5GGM; NMR; -; A=2-149. DR PDB; 5I0I; X-ray; 3.15 A; C/E=3-147, G=84-126, I=84-147. DR PDB; 5J03; X-ray; 2.00 A; B=1-149. DR PDB; 5J8H; NMR; -; A=2-149. DR PDB; 5JQA; X-ray; 1.80 A; A=1-149. DR PDB; 5JTH; X-ray; 1.84 A; A=1-149. DR PDB; 5K7L; EM; 3.78 A; B=1-149. DR PDB; 5K8Q; X-ray; 1.74 A; A=1-149. DR PDB; 5OEO; NMR; -; A=1-149. DR PDB; 5TP5; NMR; -; A=2-149. DR PDB; 5TP6; NMR; -; A=2-149. DR PDB; 5V02; X-ray; 1.78 A; R=1-149. DR PDB; 5V03; X-ray; 1.58 A; R=1-149. DR PDB; 5V7X; X-ray; 3.14 A; B=1-149. DR PDB; 5WBX; X-ray; 1.90 A; R=5-148. DR PDB; 5WC5; X-ray; 2.30 A; R=5-148. DR PDB; 6B8L; X-ray; 2.30 A; B/D/F/H=1-149. DR PDB; 6B8M; X-ray; 2.30 A; B/D/F/H=1-149. DR PDB; 6B8N; X-ray; 2.20 A; B/D/F/H=1-149. DR PDB; 6B8P; X-ray; 2.20 A; B/D/F/H=1-149. DR PDB; 6B8Q; X-ray; 2.60 A; B/D/F/H=1-149. DR PDB; 6BUT; NMR; -; A=2-149. DR PDB; 6C1D; EM; 3.20 A; R=2-149. DR PDB; 6C1G; EM; 3.80 A; R=2-149. DR PDB; 6C1H; EM; 3.90 A; R=2-149. DR PDB; 6CNM; EM; 3.40 A; E/F/G/H=1-149. DR PDB; 6CNN; EM; 3.50 A; E/F/G/H=1-149. DR PDB; 6CNO; EM; 4.70 A; E/F/G/H=1-149. DR PDB; 6DAD; X-ray; 1.65 A; A/B=2-149. DR PDB; 6DAE; X-ray; 2.00 A; A/B=2-149. DR PDB; 6DAF; X-ray; 2.40 A; A/B=2-149. DR PDB; 6DAH; X-ray; 2.50 A; A/B/C/D=1-149. DR PDB; 6E2F; EM; 3.90 A; E=1-149. DR PDB; 6E2G; EM; 3.60 A; E=1-149. DR PDB; 6EEB; X-ray; 1.96 A; A=1-149. DR PDB; 6FEG; NMR; -; B=1-149. DR PDB; 6FEH; NMR; -; B=1-149. DR PDB; 6GDK; NMR; -; A=2-149. DR PDB; 6GDL; NMR; -; A=2-149. DR PDB; 6HCS; X-ray; 2.00 A; A/C/E/G=1-149. DR PDB; 6HR1; X-ray; 1.90 A; A/B=2-149. DR PDB; 6JI8; EM; 3.60 A; C/F/I/L=1-149. DR PDB; 6JII; EM; 4.20 A; C/F/I/L=1-149. DR PDB; 6JIU; EM; 4.20 A; C/F/I/L=1-149. DR PDB; 6JIY; EM; 3.90 A; C/F/I/L=1-149. DR PDB; 6JRS; EM; 3.70 A; C/F/I/L=1-149. DR PDB; 6JV2; EM; 4.40 A; B/D/F/H=1-149. DR PDB; 6K4K; X-ray; 2.71 A; C/D=1-149. DR PDB; 6K4L; X-ray; 2.95 A; C/D=1-149. DR PDB; 6K4R; X-ray; 3.11 A; C/D=1-149. DR PDB; 6M2W; EM; 3.80 A; C/F/I/L=1-149. DR PDB; 6M7H; X-ray; 1.60 A; A=2-148. DR PDB; 6MUD; X-ray; 2.69 A; A=1-149. DR PDB; 6MUE; X-ray; 1.90 A; A=1-149. DR PDB; 6N5W; X-ray; 2.15 A; C=1-149. DR PDB; 6O5G; X-ray; 1.89 A; A=1-149. DR PDB; 6OS4; X-ray; 2.05 A; A=2-149. DR PDB; 6PAW; X-ray; 2.95 A; C/D/G/H=1-149. DR PDB; 6PBX; EM; 4.00 A; B/D/F/H=1-149. DR PDB; 6PBY; EM; 3.67 A; B/D/F/H=1-149. DR PDB; 6TV7; X-ray; 2.90 A; A=3-149. DR PDB; 6U39; X-ray; 2.40 A; A/C/E/G/I/K/M/O/Q/S=2-149. DR PDB; 6U3A; X-ray; 1.65 A; A/B=2-149. DR PDB; 6U3B; X-ray; 1.70 A; A=2-149. DR PDB; 6U3D; X-ray; 1.75 A; A/B=2-149. DR PDB; 6UZZ; EM; 3.10 A; B/D/F/H=1-149. DR PDB; 6V00; EM; 3.10 A; B/E/H/K=1-149. DR PDB; 6V01; EM; 3.90 A; B/E/H/K=1-149. DR PDB; 6X32; EM; 3.80 A; C/F/I/L=3-148. DR PDB; 6X33; EM; 4.20 A; C/F/I/L=1-148. DR PDB; 6X35; EM; 4.20 A; C/F/I/L=1-148. DR PDB; 6X36; EM; 4.70 A; C/F/I/L=1-148. DR PDB; 6XXX; X-ray; 1.25 A; AAA=1-149. DR PDB; 6XY3; X-ray; 2.00 A; AAA=1-149. DR PDB; 6XYR; X-ray; 2.08 A; A=2-149. DR PDB; 6Y4P; X-ray; 2.13 A; A=1-149. DR PDB; 6Y94; NMR; -; A=2-149. DR PDB; 6Y95; NMR; -; A=2-149. DR PDB; 6YA9; X-ray; 2.15 A; A=3-149. DR PDB; 6YNS; X-ray; 3.94 A; A/B/C/D/E/F/G/H/I/J/K/L=2-149. DR PDB; 6YNU; X-ray; 3.12 A; A/C=2-149. DR PDB; 6ZBI; NMR; -; A=2-149. DR PDB; 7AUG; X-ray; 2.04 A; A=3-149. DR PDB; 7BF1; X-ray; 1.24 A; AAA=1-149. DR PDB; 7BF2; X-ray; 1.43 A; AAA=1-149. DR PDB; 7KL5; X-ray; 1.65 A; A=1-149. DR PDB; 7L8V; NMR; -; A=1-149. DR PDB; 7PSZ; X-ray; 1.90 A; A=2-149. DR PDB; 7PU9; X-ray; 2.28 A; A=2-149. DR PDB; 7SHQ; X-ray; 2.34 A; B=2-149. DR PDB; 7SX3; EM; 3.10 A; C=1-149. DR PDB; 7SX4; EM; 3.50 A; C=1-149. DR PDB; 7T2Q; X-ray; 1.95 A; A=2-149. DR PDB; 7TCI; EM; 3.90 A; B/D/F/H=1-149. DR PDB; 7TCP; EM; 3.84 A; B/D/F/H=1-149. DR PDB; 7TZC; EM; 2.45 A; C/D/E/K=1-149. DR PDB; 7U9T; EM; 2.68 A; I/J/K/L=1-149. DR PDB; 7UA3; EM; 2.97 A; I/J/K/L=1-149. DR PDB; 7UA4; EM; 2.93 A; I/J/K/L=1-149. DR PDB; 7VMB; X-ray; 2.00 A; C=1-149. DR PDB; 7VUO; X-ray; 2.68 A; C=2-149. DR PDB; 7VUR; X-ray; 1.70 A; A/B=77-149. DR PDB; 7VUS; X-ray; 1.70 A; A/B/C/D=77-149. DR PDB; 7VUT; X-ray; 1.70 A; A/B=77-149. DR PDB; 7VUU; X-ray; 1.95 A; A/B/C/D=77-149. DR PDB; 7VVD; X-ray; 3.13 A; C/E=1-149. DR PDB; 7VVH; X-ray; 2.30 A; C=1-149. DR PDB; 7WJI; EM; 4.50 A; E=1-149. DR PDB; 7WR3; X-ray; 1.87 A; C/D=1-149. DR PDB; 7WR4; X-ray; 2.75 A; B=1-149. DR PDB; 7WR5; X-ray; 3.10 A; B=1-149. DR PDB; 7WZS; X-ray; 3.60 A; C=1-149. DR PDB; 7XN4; EM; 3.35 A; D=1-149. DR PDB; 7XN5; EM; 3.18 A; D=1-149. DR PDB; 7XN6; EM; 3.45 A; D=1-149. DR PDB; 7ZRP; X-ray; 2.65 A; A/C=2-149. DR PDB; 7ZRQ; X-ray; 1.68 A; A=2-149. DR PDB; 8AHS; X-ray; 2.48 A; A=1-149. DR PDB; 8B6Q; X-ray; 2.60 A; A=3-148. DR PDB; 8BFG; NMR; -; A=2-149. DR PDB; 8DGH; NMR; -; A=1-149. DR PDB; 8DGK; NMR; -; A=1-149. DR PDB; 8DUJ; EM; 3.70 A; C/F/I/L=1-149. DR PDB; 8DVE; EM; 3.84 A; C/F/I/L=1-149. DR PDB; 8EOW; EM; 3.90 A; E/F/G/H=7-148. DR PDB; 8EP0; EM; 4.90 A; E/F/G/H=7-148. DR PDB; 8EP1; EM; 5.40 A; E/F/G/H=7-148. DR PDB; 8FNY; X-ray; 2.22 A; B/D=2-149. DR PDB; 8FO6; X-ray; 2.55 A; B=2-149. DR PDB; 8GM4; X-ray; 2.12 A; B=2-149. DR PDB; 8GM5; X-ray; 2.12 A; B=2-149. DR PDB; 8IJK; EM; 3.40 A; E/F/G/H=1-149. DR PDB; 8J00; EM; 3.00 A; E/F/G/H=1-149. DR PDB; 8J01; EM; 3.10 A; C/E/F/H=1-149. DR PDB; 8J02; EM; 3.50 A; C/E/F/H=1-149. DR PDB; 8J03; EM; 2.70 A; E/F/H/J=1-149. DR PDB; 8J04; EM; 2.70 A; C/E/F/H=1-149. DR PDB; 8J05; EM; 2.70 A; C/E/F/H=1-149. DR PDB; 8J07; EM; 4.10 A; W=1-149. DR PDB; 8JFK; EM; 2.90 A; D/H/L/P=1-149. DR PDB; 8ODZ; EM; 3.60 A; D=5-149. DR PDB; 8OE0; EM; 4.60 A; D=5-149. DR PDB; 8OE4; EM; 3.60 A; C=5-149. DR PDB; 8PB1; EM; 3.50 A; D=5-149. DR PDB; 8SIK; EM; 2.90 A; B/D/F/H=1-149. DR PDB; 8SIM; EM; 6.20 A; B/D/F/H=1-149. DR PDB; 8SIN; EM; 6.80 A; B/D/F/H=1-149. DR PDB; 8UXL; EM; 3.12 A; I/J/K/L=1-149. DR PDB; 8UXM; EM; 3.56 A; I/J/K/L=1-149. DR PDB; 8W4U; EM; 3.30 A; C/E/F/H=1-149. DR PDB; 8X43; EM; 3.00 A; B/D/F/H=1-149. DR PDB; 8XJI; EM; 3.91 A; I/J/K/L=1-148. DR PDB; 8XKH; EM; 3.87 A; I/J/K/L=1-149. DR PDB; 8XLF; EM; 3.62 A; I/J/K/L=1-148. DR PDB; 8XLH; EM; 3.62 A; I/J/K/L=1-149. DR PDB; 8XO1; EM; 3.80 A; C/E/G/H=1-149. DR PDB; 8XYA; EM; 2.70 A; D=1-149. DR PDB; 8XYB; EM; 3.10 A; D=1-149. DR PDB; 8Y40; EM; 3.58 A; I/J/K/L=1-149. DR PDB; 9CUI; EM; 3.42 A; E=1-149. DR PDB; 9CUK; EM; 3.26 A; E=1-149. DR PDB; 9D9Z; EM; 3.40 A; C/D=1-149. DR PDB; 9E17; EM; 2.45 A; C/D/E/K=1-149. DR PDB; 9EL6; X-ray; 2.25 A; C/E=1-149. DR PDB; 9HXW; EM; 3.10 A; E/F=1-149. DR PDB; 9IXZ; EM; 3.20 A; E/F/G/H=1-149. DR PDB; 9J38; EM; 2.40 A; E/F/G/H=1-149. DR PDB; 9JQI; X-ray; 2.10 A; A/B/C=1-149. DR PDB; 9K8W; X-ray; 2.65 A; A=1-149. DR PDB; 9K8X; X-ray; 2.05 A; A=1-149. DR PDB; 9KUI; X-ray; 2.68 A; C=1-149. DR PDB; 9KUO; X-ray; 3.13 A; C/E=1-149. DR PDB; 9KUU; X-ray; 2.50 A; C/E=1-149. DR PDB; 9KUZ; X-ray; 2.07 A; C/F=1-149. DR PDB; 9KV1; X-ray; 2.30 A; C=1-149. DR PDB; 9KV9; X-ray; 2.05 A; C=1-149. DR PDB; 9KVB; X-ray; 2.77 A; C=1-149. DR PDB; 9KVO; X-ray; 3.14 A; C/D=1-149. DR PDB; 9MVW; X-ray; 1.58 A; A=1-149. DR PDB; 9MXD; X-ray; 1.17 A; A=1-149. DR PDB; 9MY3; EM; 3.46 A; B/D/F/H=1-149. DR PDB; 9MY4; EM; 3.53 A; B/D/F/H=1-149. DR PDB; 9NVN; EM; 2.89 A; E/F=1-74. DR PDB; 9NVO; EM; 2.49 A; E/F=1-74. DR PDB; 9NVP; EM; 2.85 A; E/F=1-149. DR PDB; 9NVQ; EM; 3.01 A; E/F=1-74. DR PDB; 9NVR; EM; 3.13 A; E/F=1-149. DR PDB; 9NWE; EM; 3.20 A; C/D=1-149. DR PDB; 9O48; EM; 3.10 A; E/F/G/H=1-149. DR PDB; 9O51; EM; 3.40 A; E/F/G/H=1-149. DR PDB; 9O52; EM; 3.18 A; E/F/G/H=1-149. DR PDB; 9O53; EM; 3.30 A; E/F/G/H=1-149. DR PDB; 9O5O; EM; 3.10 A; E/F/G/H=1-149. DR PDB; 9OCW; X-ray; 2.27 A; A=77-149. DR PDB; 9PCQ; X-ray; 2.30 A; B00A=3-149. DR PDB; 9PQH; NMR; -; A=1-149. DR PDB; 9PQI; NMR; -; A=1-149. DR PDB; 9QWS; EM; 3.10 A; E/F=1-149. DR PDB; 9QWU; EM; 3.10 A; E/F=1-149. DR PDB; 9QX0; EM; 3.40 A; F=1-149. DR PDB; 9U7F; EM; 2.90 A; B/E/H/K=1-149. DR PDB; 9UC8; EM; 3.36 A; B/E/H/K=1-149. DR PDB; 9UJ4; EM; 2.59 A; B/D/F/H=1-149. DR PDB; 9UPG; EM; 2.87 A; H=1-149. DR PDB; 9VEC; EM; 2.70 A; B/E/H/K=1-149. DR PDB; 9VEI; EM; 3.90 A; B/E/H/K=1-149. DR PDB; 9VEN; EM; 3.80 A; B/D/F/H=1-149. DR PDB; 9VEO; EM; 3.70 A; B/D/F/H=1-149. DR PDB; 9VU9; EM; 3.34 A; E/F/G=1-149. DR PDB; 9VUA; EM; 3.23 A; E/F/G=1-149. DR PDB; 9VUB; EM; 3.35 A; E/F/G/H=1-149. DR PDB; 9VUC; EM; 2.96 A; E/F/G=1-149. DR PDB; 9WD8; EM; 3.90 A; B/E/H/K=1-149. DR PDB; 9XB9; EM; 3.10 A; E/F/G/H=1-149. DR PDB; 9XED; EM; 3.40 A; E/F/G/H=1-149. DR PDB; 9Y5Q; EM; 4.73 A; E/F/G/H=3-148. DR PDB; 9YDZ; EM; 3.40 A; E/F/G/H=82-148. DR PDB; 9ZPO; EM; 3.67 A; E/F/G/H=3-148. DR PDB; 9ZPT; EM; 3.39 A; E/F/G/H=82-148. DR PDB; 9ZRK; EM; 2.99 A; E/F/G/H=3-148. DR PDB; 9ZRL; EM; 3.38 A; E/F/G/H=82-148. DR PDB; 9ZRQ; EM; 2.77 A; E/F/G/H=3-148. DR AlphaFoldDB; P0DP23; -. DR EMDB; EMD-16820; -. DR EMDB; EMD-16821; -. DR EMDB; EMD-16824; -. DR EMDB; EMD-17580; -. DR EMDB; EMD-20294; -. DR EMDB; EMD-20295; -. DR EMDB; EMD-20965; -. DR EMDB; EMD-20966; -. DR EMDB; EMD-20967; -. DR EMDB; EMD-22015; -. DR EMDB; EMD-22016; -. DR EMDB; EMD-22018; -. DR EMDB; EMD-22019; -. DR EMDB; EMD-25492; -. DR EMDB; EMD-25493; -. DR EMDB; EMD-25813; -. DR EMDB; EMD-25816; -. DR EMDB; EMD-26205; -. DR EMDB; EMD-26408; -. DR EMDB; EMD-26413; -. DR EMDB; EMD-26414; -. DR EMDB; EMD-27721; -. DR EMDB; EMD-27736; -. DR EMDB; EMD-28487; -. DR EMDB; EMD-28494; -. DR EMDB; EMD-28498; -. DR EMDB; EMD-30067; -. DR EMDB; EMD-32544; -. DR EMDB; EMD-33310; -. DR EMDB; EMD-33311; -. DR EMDB; EMD-33312; -. DR EMDB; EMD-35487; -. DR EMDB; EMD-35879; -. DR EMDB; EMD-35880; -. DR EMDB; EMD-35881; -. DR EMDB; EMD-35882; -. DR EMDB; EMD-35883; -. DR EMDB; EMD-35884; -. DR EMDB; EMD-35888; -. DR EMDB; EMD-36212; -. DR EMDB; EMD-37270; -. DR EMDB; EMD-38041; -. DR EMDB; EMD-38398; -. DR EMDB; EMD-38417; -. DR EMDB; EMD-38447; -. DR EMDB; EMD-38448; -. DR EMDB; EMD-38522; -. DR EMDB; EMD-38908; -. DR EMDB; EMD-40508; -. DR EMDB; EMD-40509; -. DR EMDB; EMD-40510; -. DR EMDB; EMD-42768; -. DR EMDB; EMD-42769; -. DR EMDB; EMD-45934; -. DR EMDB; EMD-45936; -. DR EMDB; EMD-46686; -. DR EMDB; EMD-48725; -. DR EMDB; EMD-48726; -. DR EMDB; EMD-49844; -. DR EMDB; EMD-49845; -. DR EMDB; EMD-49846; -. DR EMDB; EMD-49847; -. DR EMDB; EMD-49848; -. DR EMDB; EMD-49876; -. DR EMDB; EMD-52488; -. DR EMDB; EMD-52490; -. DR EMDB; EMD-53426; -. DR EMDB; EMD-53428; -. DR EMDB; EMD-53432; -. DR EMDB; EMD-60982; -. DR EMDB; EMD-61109; -. DR EMDB; EMD-63935; -. DR EMDB; EMD-64038; -. DR EMDB; EMD-64213; -. DR EMDB; EMD-64395; -. DR EMDB; EMD-64997; -. DR EMDB; EMD-65008; -. DR EMDB; EMD-65013; -. DR EMDB; EMD-65014; -. DR EMDB; EMD-65356; -. DR EMDB; EMD-65357; -. DR EMDB; EMD-65358; -. DR EMDB; EMD-65359; -. DR EMDB; EMD-66696; -. DR EMDB; EMD-66788; -. DR EMDB; EMD-70089; -. DR EMDB; EMD-70120; -. DR EMDB; EMD-70121; -. DR EMDB; EMD-70122; -. DR EMDB; EMD-70145; -. DR EMDB; EMD-72519; -. DR EMDB; EMD-72841; -. DR EMDB; EMD-7329; -. DR EMDB; EMD-7330; -. DR EMDB; EMD-7331; -. DR EMDB; EMD-74531; -. DR EMDB; EMD-74533; -. DR EMDB; EMD-74625; -. DR EMDB; EMD-74626; -. DR EMDB; EMD-74627; -. DR EMDB; EMD-7537; -. DR EMDB; EMD-7538; -. DR EMDB; EMD-7539; -. DR EMDB; EMD-8961; -. DR EMDB; EMD-8962; -. DR EMDB; EMD-9833; -. DR EMDB; EMD-9834; -. DR EMDB; EMD-9836; -. DR EMDB; EMD-9837; -. DR EMDB; EMD-9880; -. DR EMDB; EMD-9889; -. DR MDposit; P0DP23; -. DR MDRepo; P0DP23; -. DR SASBDB; P0DP23; -. DR SMR; P0DP23; -. DR ComplexPortal; CPX-1001; Calcineurin-Calmodulin complex, gamma-R1 variant. DR ComplexPortal; CPX-1002; Calcineurin-Calmodulin complex, beta-R2 variant. DR ComplexPortal; CPX-1003; Calcineurin-Calmodulin complex, alpha-R1 variant. DR ComplexPortal; CPX-1009; Calcineurin-Calmodulin complex, beta-R1 variant. DR ComplexPortal; CPX-102; DAPK1 - calmodulin complex. DR ComplexPortal; CPX-1048; Calcineurin-Calmodulin complex, alpha-R2 variant. DR ComplexPortal; CPX-1050; Calcineurin-Calmodulin complex, gamma-R2 variant. DR ComplexPortal; CPX-1112; Calcineurin-Calmodulin-AKAP5 complex, gamma-R1 variant. DR ComplexPortal; CPX-1114; Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant. DR ComplexPortal; CPX-1116; Calcineurin-Calmodulin-AKAP5 complex, beta-R2 variant. DR ComplexPortal; CPX-1118; Calcineurin-Calmodulin-AKAP5 complex, gamma-R2 variant. DR ComplexPortal; CPX-2341; NALCN channelosome complex. DR ComplexPortal; CPX-2640; Phosphorylase kinase, muscle variant. DR ComplexPortal; CPX-674; Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant. DR ComplexPortal; CPX-902; Kv7.1 channel complex. DR ComplexPortal; CPX-9141; Silencing factor of the integrated stress response complex. DR ComplexPortal; CPX-9581; Phosphorylase kinase, liver variant. DR ComplexPortal; CPX-998; Calcineurin-Calmodulin-AKAP5 complex, beta-R1 variant. DR CORUM; P0DP23; -. DR FunCoup; P0DP23; 3752. DR IntAct; P0DP23; 92. DR MINT; P0DP23; -. DR NDEx; IQUERY-CP-CALM1; 48 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000291295; -. DR BindingDB; P0DP23; -. DR ChEMBL; CHEMBL6093; -. DR DrugBank; DB08039; (3Z)-N,N-DIMETHYL-2-OXO-3-(4,5,6,7-TETRAHYDRO-1H-INDOL-2-YLMETHYLIDENE)-2,3-DIHYDRO-1H-INDOLE-5-SULFONAMIDE. DR DrugBank; DB14511; Acetate. DR DrugBank; DB01429; Aprindine. DR DrugBank; DB01244; Bepridil. DR DrugBank; DB01373; Calcium. DR DrugBank; DB11093; Calcium citrate. DR DrugBank; DB13800; Calcium levulinate. DR DrugBank; DB11348; Calcium Phosphate. DR DrugBank; DB14481; Calcium phosphate dihydrate. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB00527; Cinchocaine. DR DrugBank; DB02868; Deacetoxyvinzolidine. DR DrugBank; DB04209; Dequalinium. DR DrugBank; DB01023; Felodipine. DR DrugBank; DB04841; Flunarizine. DR DrugBank; DB00623; Fluphenazine. DR DrugBank; DB01218; Halofantrine. DR DrugBank; DB00753; Isoflurane. DR DrugBank; DB00836; Loperamide. DR DrugBank; DB01065; Melatonin. DR DrugBank; DB08231; Myristic acid. DR DrugBank; DB04513; N-(6-Aminohexyl)-5-Chloro-1-Naphthalenesulfonamide. DR DrugBank; DB00622; Nicardipine. DR DrugBank; DB01115; Nifedipine. DR DrugBank; DB00850; Perphenazine. DR DrugBank; DB00925; Phenoxybenzamine. DR DrugBank; DB01100; Pimozide. DR DrugBank; DB04825; Prenylamine. DR DrugBank; DB01069; Promethazine. DR DrugBank; DB03900; tert-butanol. DR DrugBank; DB00831; Trifluoperazine. DR DrugBank; DB03977; Trimethyllysine. DR DrugCentral; P0DP23; -. DR MoonDB; P0DP23; Predicted. DR GlyGen; P0DP23; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P0DP23; -. DR MetOSite; P0DP23; -. DR PhosphoSitePlus; P0DP23; -. DR BioMuta; CALM1; -. DR jPOST; P0DP23; -. DR MassIVE; P0DP23; -. DR PaxDb; 9606-ENSP00000291295; -. DR PeptideAtlas; P0DP23; -. DR Pumba; P0DP23; -. DR Antibodypedia; 4344; 519 antibodies from 36 providers. DR DNASU; 801; -. DR Ensembl; ENST00000272298.12; ENSP00000272298.7; ENSG00000143933.21. DR Ensembl; ENST00000291295.14; ENSP00000291295.8; ENSG00000160014.18. DR Ensembl; ENST00000356978.9; ENSP00000349467.4; ENSG00000198668.15. DR Ensembl; ENST00000596362.1; ENSP00000472141.1; ENSG00000160014.18. DR Ensembl; ENST00000866717.1; ENSP00000536776.1; ENSG00000160014.18. DR GeneID; 801; -. DR GeneID; 805; -. DR GeneID; 808; -. DR KEGG; hsa:801; -. DR KEGG; hsa:805; -. DR KEGG; hsa:808; -. DR MANE-Select; ENST00000356978.9; ENSP00000349467.4; NM_006888.6; NP_008819.1. DR AGR; HGNC:1442; -. DR AGR; HGNC:1445; -. DR AGR; HGNC:1449; -. DR CTD; 801; -. DR CTD; 805; -. DR CTD; 808; -. DR DisGeNET; 801; -. DR DisGeNET; 805; -. DR DisGeNET; 808; -. DR GeneCards; CALM1; -. DR GeneReviews; CALM1; -. DR HGNC; HGNC:1442; CALM1. DR HPA; ENSG00000198668; Low tissue specificity. DR MalaCards; CALM1; -. DR MIM; 114180; gene. DR MIM; 614916; phenotype. DR MIM; 616247; phenotype. DR OpenTargets; ENSG00000143933; -. DR OpenTargets; ENSG00000160014; -. DR OpenTargets; ENSG00000198668; -. DR Orphanet; 727192; Calmodulin-related isolated congenital long QT syndrome. DR Orphanet; 3286; Catecholaminergic polymorphic ventricular tachycardia. DR VEuPathDB; HostDB:ENSG00000198668; -. DR eggNOG; KOG0027; Eukaryota. DR GeneTree; ENSGT00950000182980; -. DR InParanoid; P0DP23; -. DR OMA; ARKMKEC; -. DR OrthoDB; 9924840at2759; -. DR PAN-GO; P0DP23; 8 GO annotations based on evolutionary models. DR PathwayCommons; P0DP23; -. DR Reactome; R-HSA-111932; CaMK IV-mediated phosphorylation of CREB. DR Reactome; R-HSA-111933; Calmodulin induced events. DR Reactome; R-HSA-111957; Cam-PDE 1 activation. DR Reactome; R-HSA-111997; CaM pathway. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane. DR Reactome; R-HSA-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation. DR Reactome; R-HSA-163615; PKA activation. DR Reactome; R-HSA-180024; DARPP-32 events. DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol. DR Reactome; R-HSA-2025928; Calcineurin activates NFAT. DR Reactome; R-HSA-203615; eNOS activation. DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis. DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade. DR Reactome; R-HSA-2672351; Stimuli-sensing channels. DR Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization. DR Reactome; R-HSA-4086398; Ca2+ pathway. DR Reactome; R-HSA-418359; Reduction of cytosolic Ca++ levels. DR Reactome; R-HSA-425561; Sodium/Calcium exchangers. DR Reactome; R-HSA-438066; Unblocking of NMDA receptors, glutamate binding and activation. DR Reactome; R-HSA-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase. DR Reactome; R-HSA-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde. DR Reactome; R-HSA-442982; Ras activation upon Ca2+ influx through NMDA receptor. DR Reactome; R-HSA-445355; Smooth Muscle Contraction. DR Reactome; R-HSA-451308; Activation of Ca-permeable Kainate Receptor. DR Reactome; R-HSA-5210891; Uptake and function of anthrax toxins. DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability. DR Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation. DR Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation. DR Reactome; R-HSA-5578775; Ion homeostasis. DR Reactome; R-HSA-5607763; CLEC7A (Dectin-1) induces NFAT activation. DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs. DR Reactome; R-HSA-5627123; RHO GTPases activate PAKs. DR Reactome; R-HSA-5673000; RAF activation. DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade. DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants. DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions. DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF. DR Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis). DR Reactome; R-HSA-8876725; Protein methylation. DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling. DR Reactome; R-HSA-9022535; Loss of phosphorylation of MECP2 at T308. DR Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity. DR Reactome; R-HSA-936837; Ion transport by P-type ATPases. DR Reactome; R-HSA-9617324; Negative regulation of NMDA receptor-mediated neuronal transmission. DR Reactome; R-HSA-9619229; Activation of RAC1 downstream of NMDARs. DR Reactome; R-HSA-9619483; Activation of AMPK downstream of NMDARs. DR Reactome; R-HSA-9620244; Long-term potentiation. DR Reactome; R-HSA-9648002; RAS processing. DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants. DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants. DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis. DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers. DR Reactome; R-HSA-9856530; High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells. DR Reactome; R-HSA-9948001; CASP4 inflammasome assembly. DR Reactome; R-HSA-9956593; Enterobacterial factors antagonize host defense. DR SignaLink; P0DP23; -. DR SIGNOR; P0DP23; -. DR Agora; ENSG00000198668; -. DR BioGRID-ORCS; 801; 10 hits in 1158 CRISPR screens. DR BioGRID-ORCS; 805; 38 hits in 1009 CRISPR screens. DR BioGRID-ORCS; 808; 46 hits in 1159 CRISPR screens. DR ChiTaRS; CALM1; human. DR EvolutionaryTrace; P0DP23; -. DR Pharos; P0DP23; Tclin. DR PRO; PR:P0DP23; -. DR Proteomes; UP000005640; Chromosome 14. DR Proteomes; UP000005640; Chromosome 19. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P0DP23; protein. DR Bgee; ENSG00000198668; Expressed in lateral nuclear group of thalamus and 211 other cell types or tissues. DR ExpressionAtlas; P0DP23; baseline and differential. DR GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL. DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl. DR GO; GO:1902494; C:catalytic complex; IDA:CAFA. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0043209; C:myelin sheath; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB. DR GO; GO:0099523; C:presynaptic cytosol; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA. DR GO; GO:0030017; C:sarcomere; IDA:BHF-UCL. DR GO; GO:0097225; C:sperm midpiece; IEA:Ensembl. DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB. DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB. DR GO; GO:0031982; C:vesicle; HDA:UniProtKB. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl. DR GO; GO:0010856; F:adenylate cyclase activator activity; IDA:UniProtKB. DR GO; GO:0019855; F:calcium channel inhibitor activity; IDA:UniProtKB. DR GO; GO:0005246; F:calcium channel regulator activity; IDA:BHF-UCL. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl. DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL. DR GO; GO:0072542; F:protein phosphatase activator activity; IDA:BHF-UCL. DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB. DR GO; GO:0031432; F:titin binding; IPI:BHF-UCL. DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL. DR GO; GO:0016240; P:autophagosome membrane docking; IDA:UniProtKB. DR GO; GO:0097720; P:calcineurin-mediated signaling; IDA:BHF-UCL. DR GO; GO:0035458; P:cellular response to interferon-beta; IDA:UniProt. DR GO; GO:0071346; P:cellular response to type II interferon; IDA:UniProt. DR GO; GO:0005513; P:detection of calcium ion; IMP:BHF-UCL. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:UniProtKB. DR GO; GO:0060291; P:long-term synaptic potentiation; TAS:BHF-UCL. DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IDA:UniProtKB. DR GO; GO:1905913; P:negative regulation of calcium ion export across plasma membrane; IEA:Ensembl. DR GO; GO:1901842; P:negative regulation of high voltage-gated calcium channel activity; IMP:UniProtKB. DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:UniProtKB. DR GO; GO:0140056; P:organelle localization by membrane tethering; IDA:UniProtKB. DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:UniProt. DR GO; GO:0140238; P:presynaptic endocytosis; IEA:Ensembl. DR GO; GO:0098901; P:regulation of cardiac muscle cell action potential; IMP:UniProtKB. DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL. DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IDA:BHF-UCL. DR GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IDA:BHF-UCL. DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB. DR GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL. DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL. DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IDA:UniProtKB. DR GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL. DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB. DR CDD; cd00051; EFh; 2. DR DisProt; DP02013; -. DR FunFam; 1.10.238.10:FF:000527; Calmodulin-3; 1. DR Gene3D; 1.10.238.10; EF-hand; 3. DR IDEAL; IID00706; -. DR InterPro; IPR050230; CALM/Myosin/TropC-like. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR PANTHER; PTHR23048:SF0; CALMODULIN LIKE 3; 1. DR PANTHER; PTHR23048; MYOSIN LIGHT CHAIN 1, 3; 1. DR Pfam; PF13499; EF-hand_7; 2. DR PRINTS; PR00450; RECOVERIN. DR SMART; SM00054; EFh; 4. DR SUPFAM; SSF47473; EF-hand; 1. DR PROSITE; PS00018; EF_HAND_1; 4. DR PROSITE; PS50222; EF_HAND_2; 4. DR PDBsum; 12DK; -. DR PDBsum; 1CDL; -. DR PDBsum; 1CLL; -. DR PDBsum; 1CTR; -. DR PDBsum; 1IWQ; -. DR PDBsum; 1J7O; -. DR PDBsum; 1J7P; -. DR PDBsum; 1K90; -. DR PDBsum; 1K93; -. DR PDBsum; 1L7Z; -. DR PDBsum; 1LVC; -. DR PDBsum; 1NKF; -. DR PDBsum; 1PK0; -. DR PDBsum; 1S26; -. DR PDBsum; 1SK6; -. DR PDBsum; 1SW8; -. DR PDBsum; 1UP5; -. DR PDBsum; 1WRZ; -. DR PDBsum; 1XFU; -. DR PDBsum; 1XFV; -. DR PDBsum; 1XFW; -. DR PDBsum; 1XFX; -. DR PDBsum; 1XFY; -. DR PDBsum; 1XFZ; -. DR PDBsum; 1Y6W; -. DR PDBsum; 1YR5; -. DR PDBsum; 1YRT; -. DR PDBsum; 1YRU; -. DR PDBsum; 1ZOT; -. DR PDBsum; 1ZUZ; -. DR PDBsum; 2BE6; -. DR PDBsum; 2F3Y; -. DR PDBsum; 2F3Z; -. DR PDBsum; 2HF5; -. DR PDBsum; 2I08; -. DR PDBsum; 2JZI; -. DR PDBsum; 2K0E; -. DR PDBsum; 2K0F; -. DR PDBsum; 2K0J; -. DR PDBsum; 2K61; -. DR PDBsum; 2KNE; -. DR PDBsum; 2KUG; -. DR PDBsum; 2KUH; -. DR PDBsum; 2L53; -. DR PDBsum; 2L7L; -. DR PDBsum; 2LGF; -. DR PDBsum; 2LL6; -. DR PDBsum; 2LL7; -. DR PDBsum; 2LQC; -. DR PDBsum; 2LQP; -. DR PDBsum; 2LV6; -. DR PDBsum; 2M0J; -. DR PDBsum; 2M0K; -. DR PDBsum; 2M55; -. DR PDBsum; 2MG5; -. DR PDBsum; 2N27; -. DR PDBsum; 2N6A; -. DR PDBsum; 2N77; -. DR PDBsum; 2N8J; -. DR PDBsum; 2R28; -. DR PDBsum; 2V01; -. DR PDBsum; 2V02; -. DR PDBsum; 2VAY; -. DR PDBsum; 2W73; -. DR PDBsum; 2WEL; -. DR PDBsum; 2X0G; -. DR PDBsum; 2Y4V; -. DR PDBsum; 3BYA; -. DR PDBsum; 3DVE; -. DR PDBsum; 3DVJ; -. DR PDBsum; 3DVK; -. DR PDBsum; 3DVM; -. DR PDBsum; 3EVV; -. DR PDBsum; 3EWT; -. DR PDBsum; 3EWV; -. DR PDBsum; 3G43; -. DR PDBsum; 3HR4; -. DR PDBsum; 3J41; -. DR PDBsum; 3O77; -. DR PDBsum; 3O78; -. DR PDBsum; 3OXQ; -. DR PDBsum; 3SUI; -. DR PDBsum; 3UCT; -. DR PDBsum; 3UCW; -. DR PDBsum; 3UCY; -. DR PDBsum; 4BW7; -. DR PDBsum; 4BW8; -. DR PDBsum; 4BYF; -. DR PDBsum; 4DCK; -. DR PDBsum; 4DJC; -. DR PDBsum; 4GOW; -. DR PDBsum; 4JPZ; -. DR PDBsum; 4JQ0; -. DR PDBsum; 4L79; -. DR PDBsum; 4LZX; -. DR PDBsum; 4M1L; -. DR PDBsum; 4OVN; -. DR PDBsum; 4Q57; -. DR PDBsum; 4Q5U; -. DR PDBsum; 4UMO; -. DR PDBsum; 4UPU; -. DR PDBsum; 4V0C; -. DR PDBsum; 5COC; -. DR PDBsum; 5DBR; -. DR PDBsum; 5DOW; -. DR PDBsum; 5DSU; -. DR PDBsum; 5GGM; -. DR PDBsum; 5I0I; -. DR PDBsum; 5J03; -. DR PDBsum; 5J8H; -. DR PDBsum; 5JQA; -. DR PDBsum; 5JTH; -. DR PDBsum; 5K7L; -. DR PDBsum; 5K8Q; -. DR PDBsum; 5OEO; -. DR PDBsum; 5TP5; -. DR PDBsum; 5TP6; -. DR PDBsum; 5V02; -. DR PDBsum; 5V03; -. DR PDBsum; 5V7X; -. DR PDBsum; 5WBX; -. DR PDBsum; 5WC5; -. DR PDBsum; 6B8L; -. DR PDBsum; 6B8M; -. DR PDBsum; 6B8N; -. DR PDBsum; 6B8P; -. DR PDBsum; 6B8Q; -. DR PDBsum; 6BUT; -. DR PDBsum; 6C1D; -. DR PDBsum; 6C1G; -. DR PDBsum; 6C1H; -. DR PDBsum; 6CNM; -. DR PDBsum; 6CNN; -. DR PDBsum; 6CNO; -. DR PDBsum; 6DAD; -. DR PDBsum; 6DAE; -. DR PDBsum; 6DAF; -. DR PDBsum; 6DAH; -. DR PDBsum; 6E2F; -. DR PDBsum; 6E2G; -. DR PDBsum; 6EEB; -. DR PDBsum; 6FEG; -. DR PDBsum; 6FEH; -. DR PDBsum; 6GDK; -. DR PDBsum; 6GDL; -. DR PDBsum; 6HCS; -. DR PDBsum; 6HR1; -. DR PDBsum; 6JI8; -. DR PDBsum; 6JII; -. DR PDBsum; 6JIU; -. DR PDBsum; 6JIY; -. DR PDBsum; 6JRS; -. DR PDBsum; 6JV2; -. DR PDBsum; 6K4K; -. DR PDBsum; 6K4L; -. DR PDBsum; 6K4R; -. DR PDBsum; 6M2W; -. DR PDBsum; 6M7H; -. DR PDBsum; 6MUD; -. DR PDBsum; 6MUE; -. DR PDBsum; 6N5W; -. DR PDBsum; 6O5G; -. DR PDBsum; 6OS4; -. DR PDBsum; 6PAW; -. DR PDBsum; 6PBX; -. DR PDBsum; 6PBY; -. DR PDBsum; 6TV7; -. DR PDBsum; 6U39; -. DR PDBsum; 6U3A; -. DR PDBsum; 6U3B; -. DR PDBsum; 6U3D; -. DR PDBsum; 6UZZ; -. DR PDBsum; 6V00; -. DR PDBsum; 6V01; -. DR PDBsum; 6X32; -. DR PDBsum; 6X33; -. DR PDBsum; 6X35; -. DR PDBsum; 6X36; -. DR PDBsum; 6XXX; -. DR PDBsum; 6XY3; -. DR PDBsum; 6XYR; -. DR PDBsum; 6Y4P; -. DR PDBsum; 6Y94; -. DR PDBsum; 6Y95; -. DR PDBsum; 6YA9; -. DR PDBsum; 6YNS; -. DR PDBsum; 6YNU; -. DR PDBsum; 6ZBI; -. DR PDBsum; 7AUG; -. DR PDBsum; 7BF1; -. DR PDBsum; 7BF2; -. DR PDBsum; 7KL5; -. DR PDBsum; 7L8V; -. DR PDBsum; 7PSZ; -. DR PDBsum; 7PU9; -. DR PDBsum; 7SHQ; -. DR PDBsum; 7SX3; -. DR PDBsum; 7SX4; -. DR PDBsum; 7T2Q; -. DR PDBsum; 7TCI; -. DR PDBsum; 7TCP; -. DR PDBsum; 7TZC; -. DR PDBsum; 7U9T; -. DR PDBsum; 7UA3; -. DR PDBsum; 7UA4; -. DR PDBsum; 7VMB; -. DR PDBsum; 7VUO; -. DR PDBsum; 7VUR; -. DR PDBsum; 7VUS; -. DR PDBsum; 7VUT; -. DR PDBsum; 7VUU; -. DR PDBsum; 7VVD; -. DR PDBsum; 7VVH; -. DR PDBsum; 7WJI; -. DR PDBsum; 7WR3; -. DR PDBsum; 7WR4; -. DR PDBsum; 7WR5; -. DR PDBsum; 7WZS; -. DR PDBsum; 7XN4; -. DR PDBsum; 7XN5; -. DR PDBsum; 7XN6; -. DR PDBsum; 7ZRP; -. DR PDBsum; 7ZRQ; -. DR PDBsum; 8AHS; -. DR PDBsum; 8B6Q; -. DR PDBsum; 8BFG; -. DR PDBsum; 8DGH; -. DR PDBsum; 8DGK; -. DR PDBsum; 8DUJ; -. DR PDBsum; 8DVE; -. DR PDBsum; 8EOW; -. DR PDBsum; 8EP0; -. DR PDBsum; 8EP1; -. DR PDBsum; 8FNY; -. DR PDBsum; 8FO6; -. DR PDBsum; 8GM4; -. DR PDBsum; 8GM5; -. DR PDBsum; 8IJK; -. DR PDBsum; 8J00; -. DR PDBsum; 8J01; -. DR PDBsum; 8J02; -. DR PDBsum; 8J03; -. DR PDBsum; 8J04; -. DR PDBsum; 8J05; -. DR PDBsum; 8J07; -. DR PDBsum; 8JFK; -. DR PDBsum; 8ODZ; -. DR PDBsum; 8OE0; -. DR PDBsum; 8OE4; -. DR PDBsum; 8PB1; -. DR PDBsum; 8SIK; -. DR PDBsum; 8SIM; -. DR PDBsum; 8SIN; -. DR PDBsum; 8UXL; -. DR PDBsum; 8UXM; -. DR PDBsum; 8W4U; -. DR PDBsum; 8X43; -. DR PDBsum; 8XJI; -. DR PDBsum; 8XKH; -. DR PDBsum; 8XLF; -. DR PDBsum; 8XLH; -. DR PDBsum; 8XO1; -. DR PDBsum; 8XYA; -. DR PDBsum; 8XYB; -. DR PDBsum; 8Y40; -. DR PDBsum; 9CUI; -. DR PDBsum; 9CUK; -. DR PDBsum; 9D9Z; -. DR PDBsum; 9E17; -. DR PDBsum; 9EL6; -. DR PDBsum; 9HXW; -. DR PDBsum; 9IXZ; -. DR PDBsum; 9J38; -. DR PDBsum; 9JQI; -. DR PDBsum; 9K8W; -. DR PDBsum; 9K8X; -. DR PDBsum; 9KUI; -. DR PDBsum; 9KUO; -. DR PDBsum; 9KUU; -. DR PDBsum; 9KUZ; -. DR PDBsum; 9KV1; -. DR PDBsum; 9KV9; -. DR PDBsum; 9KVB; -. DR PDBsum; 9KVO; -. DR PDBsum; 9MVW; -. DR PDBsum; 9MXD; -. DR PDBsum; 9MY3; -. DR PDBsum; 9MY4; -. DR PDBsum; 9NVN; -. DR PDBsum; 9NVO; -. DR PDBsum; 9NVP; -. DR PDBsum; 9NVQ; -. DR PDBsum; 9NVR; -. DR PDBsum; 9NWE; -. DR PDBsum; 9O48; -. DR PDBsum; 9O51; -. DR PDBsum; 9O52; -. DR PDBsum; 9O53; -. DR PDBsum; 9O5O; -. DR PDBsum; 9OCW; -. DR PDBsum; 9PCQ; -. DR PDBsum; 9PQH; -. DR PDBsum; 9PQI; -. DR PDBsum; 9QWS; -. DR PDBsum; 9QWU; -. DR PDBsum; 9QX0; -. DR PDBsum; 9U7F; -. DR PDBsum; 9UC8; -. DR PDBsum; 9UJ4; -. DR PDBsum; 9UPG; -. DR PDBsum; 9VEC; -. DR PDBsum; 9VEI; -. DR PDBsum; 9VEN; -. DR PDBsum; 9VEO; -. DR PDBsum; 9VU9; -. DR PDBsum; 9VUA; -. DR PDBsum; 9VUB; -. DR PDBsum; 9VUC; -. DR PDBsum; 9WD8; -. DR PDBsum; 9XB9; -. DR PDBsum; 9XED; -. DR PDBsum; 9Y5Q; -. DR PDBsum; 9YDZ; -. DR PDBsum; 9ZPO; -. DR PDBsum; 9ZPT; -. DR PDBsum; 9ZRK; -. DR PDBsum; 9ZRL; -. DR PDBsum; 9ZRQ; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Calcium; Cell projection; Cilium; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; Disease variant; Flagellum; KW Host-virus interaction; Isopeptide bond; Long QT syndrome; Metal-binding; KW Methylation; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712" FT CHAIN 2..149 FT /note="Calmodulin-1" FT /id="PRO_0000439932" FT DOMAIN 8..43 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 44..79 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 81..116 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 117..149 FT /note="EF-hand 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT REGION 77..149 FT /note="Necessary and sufficient for interaction with PCP4" FT /evidence="ECO:0000269|PubMed:27876793" FT BINDING 21 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, FT ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, FT ECO:0007744|PDB:5J03" FT BINDING 23 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, FT ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, FT ECO:0007744|PDB:5J03" FT BINDING 25 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, FT ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, FT ECO:0007744|PDB:5J03" FT BINDING 27 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, FT ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, FT ECO:0007744|PDB:5J03" FT BINDING 32 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, FT ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, FT ECO:0007744|PDB:5J03" FT BINDING 57 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, FT ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, FT ECO:0007744|PDB:5J03" FT BINDING 59 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, FT ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, FT ECO:0007744|PDB:5J03" FT BINDING 61 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, FT ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, FT ECO:0007744|PDB:5J03" FT BINDING 63 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, FT ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, FT ECO:0007744|PDB:5J03" FT BINDING 68 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, FT ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, FT ECO:0007744|PDB:5J03" FT BINDING 94 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, FT ECO:0000269|PubMed:29724949, ECO:0000269|PubMed:40328314, FT ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03, FT ECO:0007744|PDB:6CNN, ECO:0007744|PDB:6CNO, FT ECO:0007744|PDB:9D9Z, ECO:0007744|PDB:9NWE" FT BINDING 96 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, FT ECO:0000269|PubMed:29724949, ECO:0000269|PubMed:40328314, FT ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03, FT ECO:0007744|PDB:6CNN, ECO:0007744|PDB:6CNO, FT ECO:0007744|PDB:9D9Z, ECO:0007744|PDB:9NWE" FT BINDING 98 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, FT ECO:0000269|PubMed:29724949, ECO:0000269|PubMed:40328314, FT ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03, FT ECO:0007744|PDB:6CNN, ECO:0007744|PDB:6CNO, FT ECO:0007744|PDB:9D9Z, ECO:0007744|PDB:9NWE" FT BINDING 100 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, FT ECO:0000269|PubMed:29724949, ECO:0000269|PubMed:40328314, FT ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03, FT ECO:0007744|PDB:6CNN, ECO:0007744|PDB:6CNO, FT ECO:0007744|PDB:9D9Z, ECO:0007744|PDB:9NWE" FT BINDING 105 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, FT ECO:0000269|PubMed:29724949, ECO:0000269|PubMed:40328314, FT ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03, FT ECO:0007744|PDB:6CNN, ECO:0007744|PDB:6CNO, FT ECO:0007744|PDB:9D9Z, ECO:0007744|PDB:9NWE" FT BINDING 130 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, FT ECO:0000269|PubMed:40328314, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:5J03, ECO:0007744|PDB:9D9Z, FT ECO:0007744|PDB:9NWE" FT BINDING 132 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, FT ECO:0000269|PubMed:40328314, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:5J03, ECO:0007744|PDB:9D9Z, FT ECO:0007744|PDB:9NWE" FT BINDING 134 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, FT ECO:0000269|PubMed:40328314, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:5J03, ECO:0007744|PDB:9D9Z, FT ECO:0007744|PDB:9NWE" FT BINDING 136 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, FT ECO:0000269|PubMed:40328314, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:5J03, ECO:0007744|PDB:9D9Z, FT ECO:0007744|PDB:9NWE" FT BINDING 141 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, FT ECO:0000269|PubMed:40328314, ECO:0007744|PDB:1CLL, FT ECO:0007744|PDB:5J03, ECO:0007744|PDB:9D9Z, FT ECO:0007744|PDB:9NWE" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712" FT MOD_RES 22 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 45 FT /note="Phosphothreonine; by CaMK4" FT /evidence="ECO:0000250|UniProtKB:P0DP29" FT MOD_RES 82 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 95 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 100 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 102 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 111 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 116 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:7093203, FT ECO:0007744|PubMed:24129315" FT MOD_RES 116 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 139 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19690332" FT CROSSLNK 22 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 22 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P62157" FT VARIANT 54 FT /note="N -> I (in CPVT4; increased RYR2 calcium-release FT channel activity; not changed calcium-dependent FT inactivation of L-type calcium channel; not changed protein FT abundance; not changed structure; not changed thermal FT stability both in the absence and presence of calcium; no FT effect on the calcium binding affinity; significantly FT increased binding of RYR2; increased ryanodine-sensitive FT calcium-release channel activity; decreased of KCNN2 FT calcium-activated potassium channel activity; not changed FT KCNN2 expression; not changed KCNN2 location at membrane; FT dbSNP:rs267607276)" FT /evidence="ECO:0000269|PubMed:23040497, FT ECO:0000269|PubMed:26164367, ECO:0000269|PubMed:27165696, FT ECO:0000269|PubMed:27516456" FT /id="VAR_069222" FT VARIANT 90 FT /note="F -> L (in LQT14; significantly decreased of KCNN2 FT calcium-activated potassium channel activity; not changed FT KCNN2 expression; not changed KCNN2 location at membrane; FT decreased thermal stability in presence of calcium ions; FT decreased interaction with RYR2; dbSNP:rs730882253)" FT /evidence="ECO:0000269|PubMed:24076290, FT ECO:0000269|PubMed:25036739, ECO:0000269|PubMed:27165696" FT /id="VAR_073275" FT VARIANT 98 FT /note="N -> S (in CPVT4; the mutant has significantly FT reduced calcium affinity compared to wild-type; FT calmodulin-RYR2 interaction is defective at low FT intracellular Ca(2+) concentrations and restored at FT moderate to high Ca(2+) concentrations; increased RYR2 FT calcium-release channel activity; decreased KCNN2 FT calcium-activated potassium channel activity; not changed FT KCNN2 expression; not changed KCNN2 location at membrane; FT dbSNP:rs267607277)" FT /evidence="ECO:0000269|PubMed:23040497, FT ECO:0000269|PubMed:26164367, ECO:0000269|PubMed:27165696, FT ECO:0000269|PubMed:27516456" FT /id="VAR_078541" FT VARIANT 130 FT /note="D -> G (in LQT14; reduction in calcium affinity; not FT changed protein abundance; not changed structure; FT significantly decreased thermal stability in presence of FT calcium; significantly decreased RYR2 interaction; FT increased ryanodine-sensitive calcium-release channel FT activity; decreased of KCNN2 calcium-activated potassium FT channel activity; not changed KCNN2 expression; not changed FT KCNN2 location at membrane; dbSNP:rs730882252)" FT /evidence="ECO:0000269|PubMed:23388215, FT ECO:0000269|PubMed:26164367, ECO:0000269|PubMed:27165696" FT /id="VAR_078542" FT VARIANT 141 FT /note="E -> G (in LQT14; decreased calcium affinity; loss FT of CACNA1C calcium-dependent-inactivation; no effect on FT intracellular RYR2-mediated calcium release; FT dbSNP:rs1887120112)" FT /evidence="ECO:0000269|PubMed:26969752" FT /id="VAR_078263" FT VARIANT 141 FT /note="E -> V (in LQT14; loss-of-function variant causing FT impaired negative regulation of high voltage-gated calcium FT channel activity; impaired regulation of cardiac muscle FT cell action potential; decreased calcium ion binding; FT dbSNP:rs1887120112)" FT /evidence="ECO:0000269|PubMed:31454269" FT /id="VAR_083814" FT VARIANT 142 FT /note="F -> L (in LQT14; reduction in calcium affinity; not FT changed protein abundance; not changed structure; FT significantly decreased thermal stability in presence of FT calcium; no effect on RYR2 interaction; significantly FT reduced ryanodine-sensitive calcium-release channel FT activity; impaired negative regulation of high FT voltage-gated calcium channel activity; impaired regulation FT of cardiac muscle cell action potential; dbSNP:rs1085307479 FT and dbSNP:rs199744595)" FT /evidence="ECO:0000269|PubMed:23388215, FT ECO:0000269|PubMed:26164367, ECO:0000269|PubMed:26969752, FT ECO:0000269|PubMed:28158429" FT /id="VAR_073282" FT HELIX 2..4 FT /evidence="ECO:0007829|PDB:4DJC" FT HELIX 7..20 FT /evidence="ECO:0007829|PDB:7BF1" FT STRAND 21..23 FT /evidence="ECO:0007829|PDB:2M0J" FT STRAND 25..28 FT /evidence="ECO:0007829|PDB:7BF1" FT HELIX 30..39 FT /evidence="ECO:0007829|PDB:7BF1" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:8J05" FT HELIX 46..56 FT /evidence="ECO:0007829|PDB:7BF1" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:4LZX" FT STRAND 61..65 FT /evidence="ECO:0007829|PDB:7BF1" FT HELIX 66..93 FT /evidence="ECO:0007829|PDB:7BF1" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:1WRZ" FT STRAND 98..101 FT /evidence="ECO:0007829|PDB:7BF1" FT HELIX 103..113 FT /evidence="ECO:0007829|PDB:7BF1" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:4LZX" FT HELIX 119..129 FT /evidence="ECO:0007829|PDB:7BF1" FT STRAND 131..138 FT /evidence="ECO:0007829|PDB:7BF1" FT HELIX 139..147 FT /evidence="ECO:0007829|PDB:7BF1" SQ SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64; MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK //