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Calmodulin-2

 CALM2_HUMAN             Reviewed;         149 AA.
P0DP24; P02593; P62158; P70667; P99014; Q13942; Q53S29; Q61379; Q61380;
Q96HK3;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
10-MAY-2017, sequence version 1.
29-SEP-2021, entry version 33.
RecName: Full=Calmodulin-2 {ECO:0000312|HGNC:HGNC:1445};
Name=CALM2 {ECO:0000303|PubMed:9681195, ECO:0000312|HGNC:HGNC:1445};
Synonyms=CAM2, CAMB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2445749;
Sengupta B., Friedberg F., Detera-Wadleigh S.D.;
"Molecular analysis of human and rat calmodulin complementary DNA clones.
Evidence for additional active genes in these species.";
J. Biol. Chem. 262:16663-16670(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymphoma;
Kato S.;
"Human calmodulin cDNA.";
Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9681195; DOI=10.1016/s0143-4160(98)90028-8;
Toutenhoofd S.L., Foletti D., Wicki R., Rhyner J.A., Garcia F., Tolon R.,
Strehler E.E.;
"Characterization of the human CALM2 calmodulin gene and comparison of the
transcriptional activity of CALM1, CALM2 and CALM3.";
Cell Calcium 23:323-338(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and
4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Lung, Lymph, Placenta, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, AND METHYLATION AT
LYS-116.
TISSUE=Brain;
PubMed=7093203; DOI=10.1021/bi00539a041;
Sasagawa T., Ericsson L.H., Walsh K.A., Schreiber W.E., Fischer E.H.,
Titani K.;
"Complete amino acid sequence of human brain calmodulin.";
Biochemistry 21:2565-2569(1982).
[9]
PROTEIN SEQUENCE OF 2-31 AND 92-107, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Osteosarcoma;
Bienvenut W.V., Bensaad K., Vousden K.H.;
Submitted (FEB-2008) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 15-31; 77-107 AND 128-149, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[11]
CALCIUM-BINDING SITES.
PubMed=1474585; DOI=10.1016/0022-2836(92)90324-d;
Chattopadhyaya R., Meador W.E., Means A.R., Quiocho F.A.;
"Calmodulin structure refined at 1.7 A resolution.";
J. Mol. Biol. 228:1177-1192(1992).
[12]
INTERACTION WITH TTN.
PubMed=9804419; DOI=10.1038/27603;
Mayans O., van der Ven P.F.M., Wilm M., Mues A., Young P., Furst D.O.,
Wilmanns M., Gautel M.;
"Structural basis for activation of the titin kinase domain during
myofibrillogenesis.";
Nature 395:863-869(1998).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
ANALYSIS].
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
"Proteomic characterization of the human centrosome by protein correlation
profiling.";
Nature 426:570-574(2003).
[14]
INTERACTION WITH SRY.
PubMed=12871148; DOI=10.2174/0929866033479004;
Kelly S., Yotis J., Macris M., Harley V.;
"Recombinant expression, purification and characterisation of the HMG
domain of human SRY.";
Protein Pept. Lett. 10:281-286(2003).
[15]
INTERACTION WITH USP6.
PubMed=16127172; DOI=10.1074/jbc.m505220200;
Shen C., Ye Y., Robertson S.E., Lau A.W., Mak D.O., Chou M.M.;
"Calcium/calmodulin regulates ubiquitination of the ubiquitin-specific
protease TRE17/USP6.";
J. Biol. Chem. 280:35967-35973(2005).
[16]
INTERACTION WITH SRY.
PubMed=15746192; DOI=10.1210/me.2004-0334;
Sim H., Rimmer K., Kelly S., Ludbrook L.M., Clayton A.H., Harley V.R.;
"Defective calmodulin-mediated nuclear transport of the sex-determining
region of the Y chromosome (SRY) in XY sex reversal.";
Mol. Endocrinol. 19:1884-1892(2005).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[18]
FUNCTION, INTERACTION WITH CCP110, AND SUBCELLULAR LOCATION.
PubMed=16760425; DOI=10.1091/mbc.e06-04-0371;
Tsang W.Y., Spektor A., Luciano D.J., Indjeian V.B., Chen Z.,
Salisbury J.L., Sanchez I., Dynlacht B.D.;
"CP110 cooperates with two calcium-binding proteins to regulate cytokinesis
and genome stability.";
Mol. Biol. Cell 17:3423-3434(2006).
[19]
INTERACTION WITH CEP97 AND CCP110.
PubMed=17719545; DOI=10.1016/j.cell.2007.06.027;
Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D.;
"Cep97 and CP110 suppress a cilia assembly program.";
Cell 130:678-690(2007).
[20]
INTERACTION WITH RYR1 AND RYR2.
PubMed=18650434; DOI=10.1074/jbc.m804432200;
Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F.,
Weber D.J.;
"S100A1 and calmodulin compete for the same binding site on ryanodine
receptor.";
J. Biol. Chem. 283:26676-26683(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100 AND TYR-139, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22 AND LYS-95, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[25]
INTERACTION WITH CDK5RAP2.
PubMed=20466722; DOI=10.1074/jbc.m110.105965;
Wang Z., Wu T., Shi L., Zhang L., Zheng W., Qu J.Y., Niu R., Qi R.Z.;
"Conserved motif of CDK5RAP2 mediates its localization to centrosomes and
the Golgi complex.";
J. Biol. Chem. 285:22658-22665(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[28]
INTERACTION WITH ORAI1.
PubMed=23109337; DOI=10.1074/jbc.m112.380964;
Liu Y., Zheng X., Mueller G.A., Sobhany M., DeRose E.F., Zhang Y.,
London R.E., Birnbaumer L.;
"Crystal structure of calmodulin binding domain of orai1 in complex with
Ca2+ calmodulin displays a unique binding mode.";
J. Biol. Chem. 287:43030-43041(2012).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.m111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[30]
INTERACTION WITH FCHO1.
PubMed=22484487; DOI=10.1038/ncb2473;
Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
Tsang M., Traub L.M.;
"Distinct and separable activities of the endocytic clathrin-coat
components Fcho1/2 and AP-2 in developmental patterning.";
Nat. Cell Biol. 14:488-501(2012).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-102, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND THR-111, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[34]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[35]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[36]
INTERACTION WITH KCNQ2 AND KCNQ3.
PubMed=27564677; DOI=10.1021/acs.biochem.6b00477;
Strulovich R., Tobelaim W.S., Attali B., Hirsch J.A.;
"Structural insights into the M-channel proximal C-terminus/calmodulin
complex.";
Biochemistry 55:5353-5365(2016).
[37]
INTERACTION WITH PCP4, AND REGION.
PubMed=27876793; DOI=10.1038/ncomms13583;
Wang X., Putkey J.A.;
"PEP-19 modulates calcium binding to calmodulin by electrostatic
steering.";
Nat. Commun. 7:13583-13583(2016).
[38]
INVOLVEMENT IN LQT15, VARIANT LQT15 VAL-96, AND CHARACTERIZATION OF VARIANT
LQT15 VAL-96.
PubMed=23388215; DOI=10.1161/circulationaha.112.001216;
Crotti L., Johnson C.N., Graf E., De Ferrari G.M., Cuneo B.F., Ovadia M.,
Papagiannis J., Feldkamp M.D., Rathi S.G., Kunic J.D., Pedrazzini M.,
Wieland T., Lichtner P., Beckmann B.M., Clark T., Shaffer C., Benson D.W.,
Kaab S., Meitinger T., Strom T.M., Chazin W.J., Schwartz P.J.,
George A.L. Jr.;
"Calmodulin mutations associated with recurrent cardiac arrest in
infants.";
Circulation 127:1009-1017(2013).
[39]
INVOLVEMENT IN LQT15, VARIANTS LQT15 ILE-98; SER-98; GLU-132; HIS-134 AND
PRO-136, AND CHARACTERIZATION OF VARIANTS LQT15 ILE-98; GLU-132; HIS-134
AND PRO-136.
PubMed=24917665; DOI=10.1161/circgenetics.113.000459;
Makita N., Yagihara N., Crotti L., Johnson C.N., Beckmann B.M., Roh M.S.,
Shigemizu D., Lichtner P., Ishikawa T., Aiba T., Homfray T., Behr E.R.,
Klug D., Denjoy I., Mastantuono E., Theisen D., Tsunoda T., Satake W.,
Toda T., Nakagawa H., Tsuji Y., Tsuchiya T., Yamamoto H., Miyamoto Y.,
Endo N., Kimura A., Ozaki K., Motomura H., Suda K., Tanaka T.,
Schwartz P.J., Meitinger T., Kaeaeb S., Guicheney P., Shimizu W.,
Bhuiyan Z.A., Watanabe H., Chazin W.J., George A.L. Jr.;
"Novel calmodulin mutations associated with congenital arrhythmia
susceptibility.";
Circ. Cardiovasc. Genet. 7:466-474(2014).
[40]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[41]
VARIANT LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96, AND
INTERACTION WITH RYR2.
PubMed=26164367; DOI=10.1016/j.bbagen.2015.07.001;
Vassilakopoulou V., Calver B.L., Thanassoulas A., Beck K., Hu H.,
Buntwal L., Smith A., Theodoridou M., Kashir J., Blayney L., Livaniou E.,
Nounesis G., Lai F.A., Nomikos M.;
"Distinctive malfunctions of calmodulin mutations associated with heart
RyR2-mediated arrhythmic disease.";
Biochim. Biophys. Acta 1850:2168-2176(2015).
[42]
VARIANT LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96, AND
INTERACTION WITH RYR2.
PubMed=27516456; DOI=10.1161/circep.116.004161;
Gomez-Hurtado N., Boczek N.J., Kryshtal D.O., Johnson C.N., Sun J.,
Nitu F.R., Cornea R.L., Chazin W.J., Calvert M.L., Tester D.J.,
Ackerman M.J., Knollmann B.C.;
"Novel CPVT-Associated Calmodulin Mutation in CALM3 (CALM3-A103V) Activates
Arrhythmogenic Ca Waves and Sparks.";
Circ. Arrhythm. Electrophysiol. 9:0-0(2016).
[43]
VARIANTS LQT15 GLY-130 AND VAL-130, AND FUNCTION.
PubMed=26969752; DOI=10.1161/circgenetics.115.001323;
Boczek N.J., Gomez-Hurtado N., Ye D., Calvert M.L., Tester D.J.,
Kryshtal D.O., Hwang H.S., Johnson C.N., Chazin W.J., Loporcaro C.G.,
Shah M., Papez A.L., Lau Y.R., Kanter R., Knollmann B.C., Ackerman M.J.;
"Spectrum and Prevalence of CALM1-, CALM2-, and CALM3-Encoded Calmodulin
Variants in Long QT Syndrome and Functional Characterization of a Novel
Long QT Syndrome-Associated Calmodulin Missense Variant, E141G.";
Circ. Cardiovasc. Genet. 9:136-146(2016).
[44]
VARIANT LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96, AND
FUNCTION.
PubMed=27165696; DOI=10.1016/j.hrthm.2016.05.009;
Yu C.C., Ko J.S., Ai T., Tsai W.C., Chen Z., Rubart M., Vatta M.,
Everett T.H. IV, George A.L. Jr., Chen P.S.;
"Arrhythmogenic calmodulin mutations impede activation of small-conductance
calcium-activated potassium current.";
Heart Rhythm 13:1716-1723(2016).
-!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
ion channels, aquaporins and other proteins through calcium-binding.
Among the enzymes to be stimulated by the calmodulin-calcium complex
are a number of protein kinases and phosphatases. Together with CCP110
and centrin, is involved in a genetic pathway that regulates the
centrosome cycle and progression through cytokinesis (PubMed:16760425).
Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752).
Positively regulates calcium-activated potassium channel activity of
KCNN2 (PubMed:27165696). {ECO:0000269|PubMed:16760425,
ECO:0000269|PubMed:26969752, ECO:0000269|PubMed:27165696}.
-!- SUBUNIT: Interacts with MYO1C, MYO5A and RRAD. Interacts with MYO10 (By
similarity). Interacts with CEP97, CCP110, TTN/titin and SRY
(PubMed:9804419, PubMed:12871148, PubMed:15746192, PubMed:16760425,
PubMed:17719545). Interacts with USP6; the interaction is calcium
dependent (PubMed:16127172). Interacts with CDK5RAP2 (PubMed:20466722).
Interacts with SCN5A (By similarity). Interacts with RYR1
(PubMed:18650434). Interacts with FCHO1 (PubMed:22484487). Interacts
with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic
domains from two MIP subunits promotes MIP water channel closure (By
similarity). Interacts with ORAI1; this may play a role in the
regulation of ORAI1-mediated calcium transport (By similarity).
Interacts with IQCF1 (By similarity). Interacts with SYT7 (By
similarity). Interacts with CEACAM1 (via cytoplasmic domain); this
interaction is in a calcium dependent manner and reduces homophilic
cell adhesion through dissociation of dimer (By similarity). Interacts
with RYR2; regulates RYR2 calcium-release channel activity
(PubMed:27516456, PubMed:18650434, PubMed:26164367). Interacts with
PCP4; regulates calmodulin calcium-binding (PubMed:27876793). Interacts
with the heterotetrameric KCNQ2 and KCNQ3 channel; the interaction is
calcium-independent, constitutive and participates in the proper
assembly of a functional heterotetrameric M channel (PubMed:27564677).
{ECO:0000250|UniProtKB:P0DP23, ECO:0000250|UniProtKB:P62157,
ECO:0000250|UniProtKB:P62161, ECO:0000250|UniProtKB:P62204,
ECO:0000269|PubMed:12871148, ECO:0000269|PubMed:15746192,
ECO:0000269|PubMed:16127172, ECO:0000269|PubMed:16760425,
ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:18650434,
ECO:0000269|PubMed:20466722, ECO:0000269|PubMed:22484487,
ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:26164367,
ECO:0000269|PubMed:27516456, ECO:0000269|PubMed:27564677,
ECO:0000269|PubMed:27876793, ECO:0000269|PubMed:9804419}.
-!- INTERACTION:
P0DP24; P05067: APP; NbExp=3; IntAct=EBI-397435, EBI-77613;
P0DP24; P49407: ARRB1; NbExp=3; IntAct=EBI-397435, EBI-743313;
P0DP24; P32121: ARRB2; NbExp=3; IntAct=EBI-397435, EBI-714559;
P0DP24; Q13936: CACNA1C; NbExp=21; IntAct=EBI-397435, EBI-1038838;
P0DP24; Q9UQM7: CAMK2A; NbExp=2; IntAct=EBI-397435, EBI-1383687;
P0DP24; Q13557: CAMK2D; NbExp=5; IntAct=EBI-397435, EBI-351018;
P0DP24; O43303: CCP110; NbExp=14; IntAct=EBI-397435, EBI-1566217;
P0DP24; O15078: CEP290; NbExp=5; IntAct=EBI-397435, EBI-1811944;
P0DP24; P53355: DAPK1; NbExp=6; IntAct=EBI-397435, EBI-358616;
P0DP24; P00533: EGFR; NbExp=4; IntAct=EBI-397435, EBI-297353;
P0DP24; P25445: FAS; NbExp=4; IntAct=EBI-397435, EBI-494743;
P0DP24; P14136: GFAP; NbExp=3; IntAct=EBI-397435, EBI-744302;
P0DP24; P42858: HTT; NbExp=10; IntAct=EBI-397435, EBI-466029;
P0DP24; Q15051: IQCB1; NbExp=7; IntAct=EBI-397435, EBI-2805823;
P0DP24; Q9H0B3: IQCN; NbExp=4; IntAct=EBI-397435, EBI-745878;
P0DP24; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-397435, EBI-1055254;
P0DP24; O95259: KCNH1; NbExp=4; IntAct=EBI-397435, EBI-2909270;
P0DP24; O95259-2: KCNH1; NbExp=8; IntAct=EBI-397435, EBI-9836801;
P0DP24; O15554: KCNN4; NbExp=2; IntAct=EBI-397435, EBI-2924473;
P0DP24; P51787-1: KCNQ1; NbExp=6; IntAct=EBI-397435, EBI-15885881;
P0DP24; A0JP07: KIAA1683; NbExp=3; IntAct=EBI-397435, EBI-10171456;
P0DP24; P02686-5: MBP; NbExp=2; IntAct=EBI-397435, EBI-15973992;
P0DP24; Q8NCR3: MFI; NbExp=3; IntAct=EBI-397435, EBI-744790;
P0DP24; Q9HD67: MYO10; NbExp=2; IntAct=EBI-397435, EBI-307061;
P0DP24; P19404: NDUFV2; NbExp=3; IntAct=EBI-397435, EBI-713665;
P0DP24; Q96PM5: RCHY1; NbExp=2; IntAct=EBI-397435, EBI-947779;
P0DP24; Q99250: SCN2A; NbExp=3; IntAct=EBI-397435, EBI-724872;
P0DP24; Q14524: SCN5A; NbExp=14; IntAct=EBI-397435, EBI-726858;
P0DP24; P37840: SNCA; NbExp=3; IntAct=EBI-397435, EBI-985879;
P0DP24; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-397435, EBI-5235340;
P0DP24; Q8WZ42: TTN; NbExp=2; IntAct=EBI-397435, EBI-681210;
P0DP24; P63104: YWHAZ; NbExp=2; IntAct=EBI-397435, EBI-347088;
P0DP24; P27884: CACNA1A; Xeno; NbExp=3; IntAct=EBI-397435, EBI-15685548;
P0DP24; Q05152: CACNA1B; Xeno; NbExp=2; IntAct=EBI-397435, EBI-15685496;
P0DP24; O35505: CACNA1C; Xeno; NbExp=2; IntAct=EBI-397435, EBI-9084208;
P0DP24; Q07652: Cacna1e; Xeno; NbExp=2; IntAct=EBI-397435, EBI-15734403;
P0DP24; P40136: cya; Xeno; NbExp=10; IntAct=EBI-397435, EBI-457011;
P0DP24; P26645: Marcks; Xeno; NbExp=2; IntAct=EBI-397435, EBI-911805;
P0DP24; Q6J8I9: MIP; Xeno; NbExp=2; IntAct=EBI-397435, EBI-15728125;
P0DP24; Q9WTI7-2: Myo1c; Xeno; NbExp=9; IntAct=EBI-397435, EBI-16129068;
P0DP24; Q9QXS1-3: Plec; Xeno; NbExp=11; IntAct=EBI-397435, EBI-16145475;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:14654843}.
Note=Distributed throughout the cell during interphase, but during
mitosis becomes dramatically localized to the spindle poles and the
spindle microtubules.
-!- PTM: Ubiquitination results in a strongly decreased activity.
{ECO:0000250}.
-!- PTM: Phosphorylation results in a decreased activity. {ECO:0000250}.
-!- DISEASE: Long QT syndrome 15 (LQT15) [MIM:616249]: A form of long QT
syndrome, a heart disorder characterized by a prolonged QT interval on
the ECG and polymorphic ventricular arrhythmias. They cause syncope and
sudden death in response to exercise or emotional stress, and can
present with a sentinel event of sudden cardiac death in infancy.
{ECO:0000269|PubMed:23388215, ECO:0000269|PubMed:24917665,
ECO:0000269|PubMed:26164367, ECO:0000269|PubMed:26969752,
ECO:0000269|PubMed:27165696, ECO:0000269|PubMed:27516456}. Note=The
disease is caused by variants affecting the gene represented in this
entry. Mutations in CALM2 are the cause of LQT15.
-!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
{ECO:0000269|PubMed:1474585}.
-!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; M19311; AAA35641.1; -; mRNA.
EMBL; D45887; BAA08302.1; -; mRNA.
EMBL; U94728; AAC83174.1; -; Genomic_DNA.
EMBL; U94725; AAC83174.1; JOINED; Genomic_DNA.
EMBL; U94726; AAC83174.1; JOINED; Genomic_DNA.
EMBL; BT009916; AAP88918.1; -; mRNA.
EMBL; CR541990; CAG46787.1; -; mRNA.
EMBL; CR542021; CAG46818.1; -; mRNA.
EMBL; AC073283; AAY24085.1; -; Genomic_DNA.
EMBL; BC003354; AAH03354.1; -; mRNA.
EMBL; BC006464; AAH06464.1; -; mRNA.
EMBL; BC008437; AAH08437.1; -; mRNA.
EMBL; BC017385; AAH17385.1; -; mRNA.
EMBL; BC018677; AAH18677.1; -; mRNA.
EMBL; BC026065; AAH26065.1; -; mRNA.
CCDS; CCDS1832.1; -.
RefSeq; NP_001292553.1; NM_001305624.1.
RefSeq; NP_001292554.1; NM_001305625.1.
RefSeq; NP_001292555.1; NM_001305626.1.
RefSeq; NP_001316851.1; NM_001329922.1.
RefSeq; NP_001734.1; NM_001743.5.
RefSeq; NP_005175.2; NM_005184.3.
RefSeq; NP_008819.1; NM_006888.4.
PDB; 3O77; X-ray; 2.35 A; A=45-149.
PDB; 3O78; X-ray; 2.60 A; A/B=45-149.
PDB; 5COC; X-ray; 2.67 A; A=10-78.
PDB; 5J03; X-ray; 2.00 A; B=1-149.
PDB; 5NIN; X-ray; 1.70 A; A/B=1-149.
PDB; 5VMS; EM; 3.70 A; B=1-149.
PDB; 5WSU; X-ray; 3.00 A; A/B=2-149.
PDB; 5WSV; X-ray; 2.33 A; A/C=1-147.
PDB; 6PLM; X-ray; 2.59 A; C/D=2-148.
PDB; 6S5T; EM; 4.15 A; B=1-149.
PDB; 6SZ5; X-ray; 2.23 A; A=1-149.
PDB; 6XXF; X-ray; 1.70 A; AAA=1-149.
PDB; 6Y4O; X-ray; 1.84 A; A=1-149.
PDBsum; 3O77; -.
PDBsum; 3O78; -.
PDBsum; 5COC; -.
PDBsum; 5J03; -.
PDBsum; 5NIN; -.
PDBsum; 5VMS; -.
PDBsum; 5WSU; -.
PDBsum; 5WSV; -.
PDBsum; 6PLM; -.
PDBsum; 6S5T; -.
PDBsum; 6SZ5; -.
PDBsum; 6XXF; -.
PDBsum; 6Y4O; -.
SMR; P0DP24; -.
ComplexPortal; CPX-1001; Calcineurin-Calmodulin complex, gamma-R1 variant.
ComplexPortal; CPX-1002; Calcineurin-Calmodulin complex, beta-R2 variant.
ComplexPortal; CPX-1003; Calcineurin-Calmodulin complex, alpha-R1 variant.
ComplexPortal; CPX-1009; Calcineurin-Calmodulin complex, beta-R1 variant.
ComplexPortal; CPX-102; DAPK1 - calmodulin complex.
ComplexPortal; CPX-1048; Calcineurin-Calmodulin complex, alpha-R2 variant.
ComplexPortal; CPX-1050; Calcineurin-Calmodulin complex, gamma-R2 variant.
ComplexPortal; CPX-1112; Calcineurin-Calmodulin-AKAP5 complex, gamma-R1 variant.
ComplexPortal; CPX-1114; Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant.
ComplexPortal; CPX-1116; Calcineurin-Calmodulin-AKAP5 complex, beta-R2 variant.
ComplexPortal; CPX-1118; Calcineurin-Calmodulin-AKAP5 complex, gamma-R2 variant.
ComplexPortal; CPX-674; Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant.
ComplexPortal; CPX-902; Kv7.1 channel complex.
ComplexPortal; CPX-998; Calcineurin-Calmodulin-AKAP5 complex, beta-R1 variant.
IntAct; P0DP24; 295.
BindingDB; P0DP24; -.
ChEMBL; CHEMBL4296043; -.
DrugBank; DB11093; Calcium citrate.
DrugBank; DB11348; Calcium Phosphate.
DrugBank; DB14481; Calcium phosphate dihydrate.
DrugCentral; P0DP24; -.
GlyGen; P0DP24; 1 site, 1 O-linked glycan (1 site).
iPTMnet; P0DP24; -.
BioMuta; CALM2; -.
jPOST; P0DP24; -.
MassIVE; P0DP24; -.
Antibodypedia; 53945; 69 antibodies.
DNASU; 801; -.
Ensembl; ENST00000272298; ENSP00000272298; ENSG00000143933.
GeneID; 801; -.
GeneID; 805; -.
GeneID; 808; -.
KEGG; hsa:801; -.
KEGG; hsa:805; -.
KEGG; hsa:808; -.
CTD; 801; -.
CTD; 805; -.
CTD; 808; -.
DisGeNET; 801; -.
DisGeNET; 805; -.
DisGeNET; 808; -.
GeneCards; CALM2; -.
GeneReviews; CALM2; -.
HGNC; HGNC:1445; CALM2.
HPA; ENSG00000143933; Low tissue specificity.
MalaCards; CALM2; -.
MIM; 114182; gene.
MIM; 616249; phenotype.
neXtProt; NX_P0DP24; -.
OpenTargets; ENSG00000143933; -.
OpenTargets; ENSG00000160014; -.
OpenTargets; ENSG00000198668; -.
Orphanet; 3286; Catecholaminergic polymorphic ventricular tachycardia.
Orphanet; 101016; Romano-Ward syndrome.
VEuPathDB; HostDB:ENSG00000143933; -.
OMA; DEMIREP; -.
OrthoDB; 1386217at2759; -.
PathwayCommons; P0DP24; -.
BioGRID-ORCS; 801; 3 hits in 1016 CRISPR screens.
BioGRID-ORCS; 805; 32 hits in 910 CRISPR screens.
BioGRID-ORCS; 808; 39 hits in 1011 CRISPR screens.
ChiTaRS; CALM2; human.
Pharos; P0DP24; Tclin.
PRO; PR:P0DP24; -.
Proteomes; UP000005640; Chromosome 2.
RNAct; P0DP24; protein.
ExpressionAtlas; P0DP24; baseline and differential.
GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
GO; GO:1902494; C:catalytic complex; IDA:CAFA.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0016020; C:membrane; ISS:ARUK-UCL.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
GO; GO:0030017; C:sarcomere; IDA:BHF-UCL.
GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; HDA:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
GO; GO:0010856; F:adenylate cyclase activator activity; IDA:UniProtKB.
GO; GO:0008179; F:adenylate cyclase binding; IPI:CAFA.
GO; GO:0019855; F:calcium channel inhibitor activity; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; ISS:ARUK-UCL.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
GO; GO:0031997; F:N-terminal myristoylation domain binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0072542; F:protein phosphatase activator activity; IDA:BHF-UCL.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; TAS:BHF-UCL.
GO; GO:0031432; F:titin binding; IPI:BHF-UCL.
GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
GO; GO:0005513; P:detection of calcium ion; IMP:BHF-UCL.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:1905913; P:negative regulation of calcium ion export across plasma membrane; ISS:ARUK-UCL.
GO; GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; ISS:ARUK-UCL.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; TAS:BHF-UCL.
GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:UniProtKB.
GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; IDA:BHF-UCL.
GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; TAS:BHF-UCL.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:BHF-UCL.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; TAS:BHF-UCL.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:BHF-UCL.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; TAS:BHF-UCL.
GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO; GO:0050848; P:regulation of calcium-mediated signaling; ISS:ARUK-UCL.
GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IC:BHF-UCL.
GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IC:BHF-UCL.
GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IBA:GO_Central.
GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
CDD; cd00051; EFh; 2.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13499; EF-hand_7; 2.
SMART; SM00054; EFh; 4.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 4.
PROSITE; PS50222; EF_HAND_2; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Disease variant; Isopeptide bond;
Long QT syndrome; Metal-binding; Methylation; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000269|PubMed:7093203, ECO:0000269|Ref.9,
ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
CHAIN 2..149
/note="Calmodulin-2"
/id="PRO_0000439933"
DOMAIN 8..43
/note="EF-hand 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
DOMAIN 44..79
/note="EF-hand 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
DOMAIN 81..116
/note="EF-hand 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
DOMAIN 117..149
/note="EF-hand 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
CA_BIND 21..32
/note="1"
/evidence="ECO:0000269|PubMed:1474585"
CA_BIND 57..68
/note="2"
/evidence="ECO:0000269|PubMed:1474585"
CA_BIND 94..105
/note="3"
/evidence="ECO:0000269|PubMed:1474585"
CA_BIND 130..141
/note="4"
/evidence="ECO:0000269|PubMed:1474585"
REGION 77..149
/note="Necessary and sufficient for interaction with PCP4"
/evidence="ECO:0000269|PubMed:27876793"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000269|PubMed:7093203, ECO:0000269|Ref.9,
ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
MOD_RES 22
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 45
/note="Phosphothreonine; by CaMK4"
/evidence="ECO:0000250|UniProtKB:P0DP30"
MOD_RES 82
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 95
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 100
/note="Phosphotyrosine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332"
MOD_RES 102
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
MOD_RES 111
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:24275569"
MOD_RES 116
/note="N6,N6,N6-trimethyllysine; alternate"
/evidence="ECO:0000269|PubMed:7093203,
ECO:0007744|PubMed:24129315"
MOD_RES 116
/note="N6-methyllysine; alternate"
/evidence="ECO:0007744|PubMed:24129315"
MOD_RES 139
/note="Phosphotyrosine"
/evidence="ECO:0007744|PubMed:19690332"
CROSSLNK 22
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 22
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000250|UniProtKB:P62157"
VARIANT 96
/note="D -> V (in LQT15; reduction in calcium affinity;
highly decreased calcium-dependent inactivation of L-type
calcium channel; increased action potential duration; not
changed protein abundance; not changed structure; increased
thermal stability in absence of calcium; decreased thermal
stability in presence of calcium; significantly increased
RYR2 interaction; increased ryanodine-sensitive calcium-
release channel activity; decreased of KCNN2 calcium-
activated potassium channel activity; not changed KCNN2
expression; not changed KCNN2 location at membrane;
dbSNP:rs730882254)"
/evidence="ECO:0000269|PubMed:23388215,
ECO:0000269|PubMed:26164367, ECO:0000269|PubMed:27165696,
ECO:0000269|PubMed:27516456"
/id="VAR_073276"
VARIANT 98
/note="N -> I (in LQT15; reduction in calcium affinity;
dbSNP:rs398124647)"
/evidence="ECO:0000269|PubMed:24917665"
/id="VAR_073277"
VARIANT 98
/note="N -> S (in LQT15; the mutant has significantly
reduced calcium affinity compared to wild-type; calmodulin-
RYR2 interaction is defective at low intracellular Ca(2+)
concentrations and restored at moderate to high Ca(2+)
concentrations; increased RYR2 calcium-release channel
activity; decreased calcium-dependent inactivation of L-
type calcium channel; not changed protein abundance; not
changed structure; significantly reduced ryanodine-
sensitive calcium-release channel activity; decreased of
KCNN2 calcium-activated potassium channel activity; not
changed KCNN2 expression; not changed KCNN2 location at
membrane; dbSNP:rs398124647)"
/evidence="ECO:0000269|PubMed:24917665,
ECO:0000269|PubMed:26164367, ECO:0000269|PubMed:27165696,
ECO:0000269|PubMed:27516456"
/id="VAR_078543"
VARIANT 130
/note="D -> G (in LQT15; reduction in calcium affinity; not
changed protein abundance; not changed structure;
significantly decreased thermal stability in presence of
calcium; significantly decreased RYR2 interaction;
increased ryanodine-sensitive calcium-release channel
activity; decreased of KCNN2 calcium-activated potassium
channel activity; not changed KCNN2 expression; not changed
KCNN2 location at membrane; dbSNP:rs1573214163)"
/evidence="ECO:0000269|PubMed:23388215,
ECO:0000269|PubMed:26164367, ECO:0000269|PubMed:26969752,
ECO:0000269|PubMed:27165696"
/id="VAR_078544"
VARIANT 130
/note="D -> V (in LQT15)"
/evidence="ECO:0000269|PubMed:26969752"
/id="VAR_078262"
VARIANT 132
/note="D -> E (in LQT15; reduction in calcium affinity;
dbSNP:rs398124648)"
/evidence="ECO:0000269|PubMed:24917665"
/id="VAR_073279"
VARIANT 134
/note="D -> H (in LQT15; reduction in calcium affinity;
dbSNP:rs398124650)"
/evidence="ECO:0000269|PubMed:24917665"
/id="VAR_073280"
VARIANT 136
/note="Q -> P (in LQT15; reduction in calcium affinity;
dbSNP:rs398124649)"
/evidence="ECO:0000269|PubMed:24917665"
/id="VAR_073281"
CONFLICT 124
/note="E -> Q (in Ref. 7; AAH08437)"
/evidence="ECO:0000305"
HELIX 7..20
/evidence="ECO:0007829|PDB:6SZ5"
STRAND 25..28
/evidence="ECO:0007829|PDB:6SZ5"
HELIX 30..39
/evidence="ECO:0007829|PDB:6SZ5"
HELIX 46..54
/evidence="ECO:0007829|PDB:6SZ5"
STRAND 57..60
/evidence="ECO:0007829|PDB:6PLM"
STRAND 61..65
/evidence="ECO:0007829|PDB:6SZ5"
HELIX 66..93
/evidence="ECO:0007829|PDB:6SZ5"
STRAND 98..101
/evidence="ECO:0007829|PDB:6SZ5"
HELIX 103..112
/evidence="ECO:0007829|PDB:6SZ5"
HELIX 119..129
/evidence="ECO:0007829|PDB:6SZ5"
STRAND 131..138
/evidence="ECO:0007829|PDB:6SZ5"
HELIX 139..145
/evidence="ECO:0007829|PDB:6SZ5"
SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK


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Related Genes :
[Calm2 Cam2 CamC] Calmodulin-2
[cmk-1 K07A9.2] Calcium/calmodulin-dependent protein kinase type 1 (EC 2.7.11.17) (CaM kinase I) (CaM-KI)
[fem-2 T19C3.8] Protein phosphatase fem-2 (EC 3.1.3.16) (Ca(2+)/calmodulin-dependent protein kinase phosphatase) (CaM-kinase phosphatase) (CaMKPase) (Feminization of XX and XO animals protein 2) (Sex-determining protein fem-2)
[ckk-1 C05H8.1] Calcium/calmodulin-dependent protein kinase kinase (CaM-KK) (CaM-kinase kinase) (EC 2.7.11.17)
[Eef2k] Eukaryotic elongation factor 2 kinase (eEF-2 kinase) (eEF-2K) (EC 2.7.11.20) (Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase)
[unc-43 K11E8.1] Calcium/calmodulin-dependent protein kinase type II (CaM kinase II) (EC 2.7.11.17) (Uncoordinated protein 43)
[tax-6 cna-1 C02F4.2] Serine/threonine-protein phosphatase 2B catalytic subunit (EC 3.1.3.16) (Abnormal chemotaxis protein 6) (Calmodulin-dependent calcineurin subunit A)
[Camkk2] Calcium/calmodulin-dependent protein kinase kinase 2 (CaM-KK 2) (CaM-kinase kinase 2) (CaMKK 2) (EC 2.7.11.17) (Calcium/calmodulin-dependent protein kinase kinase beta) (CaM-KK beta) (CaM-kinase kinase beta) (CaMKK beta)
[CAMKK2 CAMKKB KIAA0787] Calcium/calmodulin-dependent protein kinase kinase 2 (CaM-KK 2) (CaM-kinase kinase 2) (CaMKK 2) (EC 2.7.11.17) (Calcium/calmodulin-dependent protein kinase kinase beta) (CaM-KK beta) (CaM-kinase kinase beta) (CaMKK beta)
[Camkk2 Kiaa0787] Calcium/calmodulin-dependent protein kinase kinase 2 (CaM-KK 2) (CaM-kinase kinase 2) (CaMKK 2) (EC 2.7.11.17) (Calcium/calmodulin-dependent protein kinase kinase beta) (CaM-KK beta) (CaM-kinase kinase beta) (CaMKK beta)
[CAMTA3 CMTA3 SARD3 SR1 At2g22300 T26C19.4] Calmodulin-binding transcription activator 3 (AtCAMTA3) (Ethylene-induced calmodulin-binding protein 1) (EICBP1) (Ethylene-induced calmodulin-binding protein a) (EICBP.a) (Protein SAR-DEFICIENT 3) (Signal-responsive protein 1) (AtSR1)
[CAMTA2 CMTA2 SR4 At5g64220 MSJ1.6] Calmodulin-binding transcription activator 2 (AtCAMTA2) (AtER66) (Ethylene-induced calmodulin-binding protein c) (EICBP.c) (Signal-responsive protein 4) (AtSR4)
[CAMTA1 CMTA1 SR2 At5g09410 T5E8.210] Calmodulin-binding transcription activator 1 (AtCAMTA1) (Ethylene-induced calmodulin-binding protein b) (EICBP.b) (Signal-responsive protein 2) (AtSR2)
[CRK1 CaMK3 CBK3 At2g41140 T3K9.9] CDPK-related kinase 1 (AtCRK1) (EC 2.7.11.1) (Calcium/calmodulin-dependent protein kinase 3) (Calmodulin-binding protein kinase 3) (AtCBK3) (CaM-binding protein kinase 3)
[CML24 TCH2 At5g37770 K22F20.1] Calcium-binding protein CML24 (Calmodulin-like protein 24) (Touch-induced calmodulin-related protein 2)
[Camk2n1] Calcium/calmodulin-dependent protein kinase II inhibitor 1 (calcium/calmodulin-dependent protein kinase II inhibitor alpha) (CaM-KIINalpha) (CaMKIINalpha)
[Camkk1] Calcium/calmodulin-dependent protein kinase kinase 1 (CaM-KK 1) (CaM-kinase kinase 1) (CaMKK 1) (EC 2.7.11.17) (CaM-kinase IV kinase) (Calcium/calmodulin-dependent protein kinase kinase alpha) (CaM-KK alpha) (CaM-kinase kinase alpha) (CaMKK alpha)
[Camkk1 Camkk] Calcium/calmodulin-dependent protein kinase kinase 1 (CaM-KK 1) (CaM-kinase kinase 1) (CaMKK 1) (EC 2.7.11.17) (CaM-kinase IV kinase) (Calcium/calmodulin-dependent protein kinase kinase alpha) (CaM-KK alpha) (CaM-kinase kinase alpha) (CaMKK alpha)
[CAMKK1 CAMKKA] Calcium/calmodulin-dependent protein kinase kinase 1 (CaM-KK 1) (CaM-kinase kinase 1) (CaMKK 1) (EC 2.7.11.17) (CaM-kinase IV kinase) (Calcium/calmodulin-dependent protein kinase kinase alpha) (CaM-KK alpha) (CaM-kinase kinase alpha) (CaMKK alpha)
[cmkA AN2412] Calcium/calmodulin-dependent protein kinase cmkA (CMPK) (EC 2.7.11.17) (Multifunctional calcium/calmodulin-dependent protein kinase) (ACMPK) (CaMK)
[Calm1 Calm Cam Cam1] Calmodulin-1
[cmd-1 T21H3.3] Calmodulin (CaM)
[CAMRLK MEE62 At5g45800 MRA19.24] Calmodulin-binding receptor kinase CaMRLK (EC 2.7.11.1) (Calmodulin-binding receptor-like kinase) (AtCaMRLK) (Protein MATERNAL EFFECT EMBRYO ARREST 62)
[Calm3 Cam3 Camc] Calmodulin-3
[CAMK1 Os03g0366200 LOC_Os03g25070] Calcium/calmodulin-dependent serine/threonine-protein kinase 1 (EC 2.7.11.17) (Calcium/calmodulin-binding serine/threonine-protein kinase) (CaM-binding protein kinase) (OsCBK)
[CAMSAP2 CAMSAP1L1 KIAA1078] Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)
[Camsap2 Camsap1l1 Kiaa1078] Calmodulin-regulated spectrin-associated protein 2 (Calmodulin-regulated spectrin-associated protein 1-like protein 1)
[CAM GSPATT00015825001] Calmodulin (CaM)
[calA camA DDB_G0279407] Calmodulin (CaM)
[CAMK2B CAM2 CAMK2 CAMKB] Calcium/calmodulin-dependent protein kinase type II subunit beta (CaM kinase II subunit beta) (CaMK-II subunit beta) (EC 2.7.11.17)

Bibliography :
[34604066] Calmodulin 2 Facilitates Angiogenesis and Metastasis of Gastric Cancer STAT3/HIF-1A/VEGF-A Mediated Macrophage Polarization.
[33951696] Circular RNA circ_0010729 Knockdown Attenuates Oxygen-Glucose Deprivation-Induced Human Cardiac Myocytes Injury by miR-338-3p/CALM2 Axis.
[33788723] Targeting CALM2 Inhibits Hepatocellular Carcinoma Growth and Metastasis by Suppressing E2F5-mediated Cell Cycle Progression.
[33173240] HLA-J, a Non-Pseudogene as a New Prognostic Marker for Therapy Response and Survival in Breast Cancer.
[32724216] Identification of the novel bacterial blight resistance gene Xa46(t) by mapping and expression analysis of the rice mutant H120.
[31628181] Protein Kinase C and Calmodulin Serve As Calcium Sensors for Calcium-Stimulated Endocytosis at Synapses.
[31602204] Smoking alters the evolutionary trajectory of non-small cell lung cancer.
[31429119] lncRNA GAS5 regulates myocardial infarction by targeting the miR-525-5p/CALM2 axis.
[30713075] Dynamic Interactions of Plant CNGC Subunits and Calmodulins Drive Oscillatory Ca Channel Activities.
[27881195] The involvement of RUNX2 and SPARC genes in the bacterial chondronecrosis with osteomyelitis in broilers.