CALM1_HUMAN
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 03-AUG-2022, entry version 43.
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 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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42] {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 [43]
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 [44]
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 [45]
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 [46]
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 [47]
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 [48]
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 [49]
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 [50]
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 [51] {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 [52] {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 [53] {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 [54]
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 [55]
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 [56]
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 [57]
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 [58]
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 [59]
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 [60]
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 [61]
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 [62]
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 [63]
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 [64]
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 [65]
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 mediates the control of a large number of enzymes,
CC ion channels, aquaporins and other proteins through calcium-binding.
CC Among the enzymes to be stimulated by the calmodulin-calcium complex
CC are a number of protein kinases and phosphatases. Together with CCP110
CC and centrin, is involved in a genetic pathway that regulates the
CC centrosome cycle and progression through cytokinesis (PubMed:16760425).
CC Is a regulator of voltage-dependent L-type calcium channels
CC (PubMed:31454269). Mediates calcium-dependent inactivation of CACNA1C
CC (PubMed:26969752). Positively regulates calcium-activated potassium
CC channel activity of KCNN2 (PubMed:27165696). Forms a potassium channel
CC complex with KCNQ1 and regulates electrophysiological activity of the
CC channel via calcium-binding (PubMed:25441029). Acts as a sensor to
CC modulate the endoplasmic reticulum contacts with other organelles
CC mediated by VMP1:ATP2A2 (PubMed:28890335).
CC {ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:23893133,
CC ECO:0000269|PubMed:26969752, ECO:0000269|PubMed:27165696,
CC ECO:0000269|PubMed:28890335, ECO:0000269|PubMed:31454269}.
CC -!- FUNCTION: (Microbial infection) Required for Legionella pneumophila
CC SidJ glutamylase activity. {ECO:0000269|PubMed:31330532}.
CC -!- SUBUNIT: Interacts with MYO1C, MYO5A and RRAD. Interacts with MYO10 (By
CC similarity). Interacts with CEP97, CCP110, TTN/titin and SRY
CC (PubMed:9804419, PubMed:12871148, PubMed:15746192, PubMed:16760425,
CC PubMed:17719545). Interacts with USP6; the interaction is calcium
CC dependent (PubMed:16127172). Interacts with CDK5RAP2 (PubMed:20466722).
CC Interacts with SCN5A (PubMed:21167176). Interacts with RYR1
CC (PubMed:18650434). Interacts with FCHO1 (PubMed:22484487). Interacts
CC with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic
CC domains from two MIP subunits promotes MIP water channel closure
CC (PubMed:23893133). Interacts with ORAI1; this may play a role in the
CC regulation of ORAI1-mediated calcium transport (By similarity).
CC Interacts with IQCF1 (By similarity). Interacts with SYT7 (By
CC similarity). Interacts with CEACAM1 (via cytoplasmic domain); this
CC interaction is in a calcium dependent manner and reduces homophilic
CC cell adhesion through dissociation of dimer (By similarity). Interacts
CC with RYR2; regulates RYR2 calcium-release channel activity
CC (PubMed:27516456, PubMed:18650434, PubMed:26164367). 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). Interacts
CC 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). {ECO:0000250|UniProtKB:P0DP26,
CC ECO:0000250|UniProtKB:P62157, ECO:0000250|UniProtKB:P62161,
CC ECO:0000250|UniProtKB:P62204, ECO:0000269|PubMed:12485993,
CC ECO:0000269|PubMed:12577052, ECO:0000269|PubMed:12871148,
CC ECO:0000269|PubMed:15719022, ECO:0000269|PubMed:15746192,
CC ECO:0000269|PubMed:16127172, ECO:0000269|PubMed:16299511,
CC ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:17719545,
CC ECO:0000269|PubMed:18165683, ECO:0000269|PubMed:18650434,
CC ECO:0000269|PubMed:20466722, ECO:0000269|PubMed:21167176,
CC ECO:0000269|PubMed:22484487, ECO:0000269|PubMed:23109337,
CC ECO:0000269|PubMed:23607618, ECO:0000269|PubMed:23893133,
CC ECO:0000269|PubMed:25441029, 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:30021165, ECO:0000269|PubMed:30287853,
CC ECO:0000269|PubMed:31155282, 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 -!- INTERACTION:
CC P0DP23; O75874: IDH1; NbExp=7; IntAct=EBI-25817233, EBI-715695;
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 {ECO:0000269|PubMed:25441029}.
CC -!- PTM: Ubiquitination results in a strongly decreased activity.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation results in a decreased activity. {ECO:0000250}.
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://web.expasy.org/spotlight/back_issues/105";
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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_001743.5.
DR RefSeq; NP_005175.2; NM_005184.3.
DR RefSeq; NP_008819.1; NM_006888.4.
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=3-79.
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=2-77.
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=2-149.
DR PDB; 2V02; X-ray; 2.20 A; A=2-149.
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=2-80.
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; 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 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; 7SHQ; -.
DR PDBsum; 7SX3; -.
DR PDBsum; 7SX4; -.
DR AlphaFoldDB; P0DP23; -.
DR SASBDB; P0DP23; -.
DR SMR; P0DP23; -.
DR IntAct; P0DP23; 5.
DR MINT; P0DP23; -.
DR STRING; 9606.ENSP00000272298; -.
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; 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; DB01023; Felodipine.
DR DrugBank; DB04841; Flunarizine.
DR DrugBank; DB00623; Fluphenazine.
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 PeptideAtlas; P0DP23; -.
DR PRIDE; P0DP23; -.
DR Antibodypedia; 4344; 533 antibodies from 34 providers.
DR DNASU; 801; -.
DR Ensembl; ENST00000356978.9; ENSP00000349467.4; ENSG00000198668.14.
DR GeneID; 801; -.
DR GeneID; 805; -.
DR GeneID; 808; -.
DR KEGG; hsa:801; -.
DR KEGG; hsa:805; -.
DR KEGG; hsa:808; -.
DR MANE-Select; ENST00000272298.12; ENSP00000272298.7; NM_001743.6; NP_001734.1.
DR MANE-Select; ENST00000291295.14; ENSP00000291295.8; NM_005184.4; NP_005175.2.
DR MANE-Select; ENST00000356978.9; ENSP00000349467.4; NM_006888.6; NP_008819.1.
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 neXtProt; NX_P0DP23; -.
DR OpenTargets; ENSG00000143933; -.
DR OpenTargets; ENSG00000160014; -.
DR OpenTargets; ENSG00000198668; -.
DR Orphanet; 3286; Catecholaminergic polymorphic ventricular tachycardia.
DR Orphanet; 101016; Romano-Ward syndrome.
DR VEuPathDB; HostDB:ENSG00000198668; -.
DR eggNOG; KOG0027; Eukaryota.
DR OMA; SCDRHPP; -.
DR OrthoDB; 1386217at2759; -.
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 SignaLink; P0DP23; -.
DR SIGNOR; P0DP23; -.
DR BioGRID-ORCS; 801; 10 hits in 1080 CRISPR screens.
DR BioGRID-ORCS; 805; 35 hits in 960 CRISPR screens.
DR BioGRID-ORCS; 808; 45 hits in 1080 CRISPR screens.
DR ChiTaRS; CALM1; human.
DR Pharos; P0DP23; Tclin.
DR PRO; PR:P0DP23; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P0DP23; protein.
DR Bgee; ENSG00000198668; Expressed in lateral nuclear group of thalamus and 209 other tissues.
DR ExpressionAtlas; P0DP23; baseline and differential.
DR GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
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; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
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: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:0008179; F:adenylate cyclase binding; IPI:CAFA.
DR GO; GO:0019855; F:calcium channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0031997; F:N-terminal myristoylation domain binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
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; TAS:BHF-UCL.
DR GO; GO:0031432; F:titin binding; IPI:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; IDA:UniProtKB.
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:0000086; P:G2/M transition of mitotic cell cycle; IEA:Ensembl.
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:0010801; P:negative regulation of peptidyl-threonine phosphorylation; TAS:BHF-UCL.
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:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; IDA:BHF-UCL.
DR GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; TAS:BHF-UCL.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:BHF-UCL.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; TAS:BHF-UCL.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:BHF-UCL.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; TAS:BHF-UCL.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; 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; IC:BHF-UCL.
DR GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IC: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 InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
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:0007744|PDB:1CLL, ECO:0007744|PDB:5J03"
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:0007744|PDB:1CLL, ECO:0007744|PDB:5J03"
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:0007744|PDB:1CLL, ECO:0007744|PDB:5J03"
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:0007744|PDB:1CLL, ECO:0007744|PDB:5J03"
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:0007744|PDB:1CLL, ECO:0007744|PDB:5J03"
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:0007744|PDB:1CLL, ECO:0007744|PDB:5J03"
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:0007744|PDB:1CLL, ECO:0007744|PDB:5J03"
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:0007744|PDB:1CLL, ECO:0007744|PDB:5J03"
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:0007744|PDB:1CLL, ECO:0007744|PDB:5J03"
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:0007744|PDB:1CLL, ECO:0007744|PDB:5J03"
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; calmodulin-
FT RYR2 interaction is defective at low intracellular Ca(2+)
FT concentrations and restored at moderate to high Ca(2+)
FT concentrations; increased RYR2 calcium-release channel
FT activity; decreased KCNN2 calcium-activated potassium
FT channel activity; not changed KCNN2 expression; not changed
FT KCNN2 location at membrane; 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 /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 /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 voltage-
FT gated calcium channel activity; impaired regulation of
FT 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:4DJC"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2M0J"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:4DJC"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:4DJC"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:4DJC"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:4LZX"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:4DJC"
FT HELIX 66..93
FT /evidence="ECO:0007829|PDB:4DJC"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1WRZ"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:4DJC"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:4DJC"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4LZX"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:4DJC"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4DCK"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:4DJC"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:4DJC"
SQ SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK
