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Calmodulin-3

 CALM3_HUMAN             Reviewed;         149 AA.
P0DP25; 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 39.
RecName: Full=Calmodulin-3 {ECO:0000312|HGNC:HGNC:1449};
Name=CALM3 {ECO:0000312|HGNC:HGNC:1449};
Synonyms=CALML2, CAM3, CAMC, CAMIII;
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=3182832;
Fischer R., Koller M., Flura M., Mathews S., Strehler-Page M.A., Krebs J.,
Penniston J.T., Carafoli E., Strehler E.E.;
"Multiple divergent mRNAs code for a single human calmodulin.";
J. Biol. Chem. 263:17055-17062(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
PubMed=2223880; DOI=10.1016/0167-4781(90)90203-e;
Koller M., Schnyder B., Strehler E.E.;
"Structural organization of the human CaMIII calmodulin gene.";
Biochim. Biophys. Acta 1087:180-189(1990).
[3]
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
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).
[6]
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).
[7]
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.
[8]
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.
[9]
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).
[10]
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).
[11]
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).
[12]
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).
[13]
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).
[14]
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).
[15]
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).
[16]
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).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
INTERACTION 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).
[35]
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).
[36]
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).
[37]
INVOLVEMENT IN LQT16, AND VARIANT LQT16 GLY-130.
PubMed=25460178; DOI=10.1016/j.hrthm.2014.10.035;
Reed G.J., Boczek N.J., Etheridge S.P., Ackerman M.J.;
"CALM3 mutation associated with long QT syndrome.";
Heart Rhythm 12:419-422(2015).
[38]
INVOLVEMENT IN CPVT6, VARIANT CPVT6 VAL-103, CHARACTERIZATION OF VARIANT
CPVT6 VAL-103, 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).
[39]
INVOLVEMENT IN LQT16, VARIANTS LQT16 GLY-130 AND LYS-141, CHARACTERIZATION
OF VARIANT LQT16 LYS-141, AND FUNCTION.
PubMed=31454269; DOI=10.1161/circgen.119.002581;
Wren L.M., Jimenez-Jaimez J., Al-Ghamdi S., Al-Aama J.Y., Bdeir A.,
Al-Hassnan Z.N., Kuan J.L., Foo R.Y., Potet F., Johnson C.N., Aziz M.C.,
Carvill G.L., Kaski J.P., Crotti L., Perin F., Monserrat L., Burridge P.W.,
Schwartz P.J., Chazin W.J., Bhuiyan Z.A., George A.L. Jr.;
"Genetic mosaicism in calmodulinopathy.";
Circ. Genom. Precis. Med. 12:375-385(2019).
-!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
ion channels, aquaporins and other proteins through calcium-binding. Is
a regulator of voltage-dependent L-type calcium channels
(PubMed:31454269). 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. {ECO:0000250|UniProtKB:P0DP23,
ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:31454269}.
-!- 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). 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:27516456,
ECO:0000269|PubMed:27564677, ECO:0000269|PubMed:27876793,
ECO:0000269|PubMed:9804419}.
-!- 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: Ventricular tachycardia, catecholaminergic polymorphic, 6
(CPVT6) [MIM:618782]: An arrhythmogenic disorder characterized by
stress-induced, bidirectional ventricular tachycardia that may
degenerate into cardiac arrest and cause sudden death. Patients present
with recurrent syncope, seizures, or sudden death after physical
activity or emotional stress. CPVT6 inheritance is autosomal dominant.
{ECO:0000269|PubMed:27516456}. Note=The disease may be caused by
variants affecting the gene represented in this entry.
-!- DISEASE: Long QT syndrome 16 (LQT16) [MIM:618782]: An autosomal
dominant 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:25460178,
ECO:0000269|PubMed:31454269}. Note=The disease is caused by variants
affecting the gene represented in this entry.
-!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
{ECO:0000269|PubMed:1474585}.
-!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA36839.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; J04046; AAA51918.1; -; mRNA.
EMBL; X52606; CAA36839.1; ALT_SEQ; Genomic_DNA.
EMBL; X52607; CAA36839.1; JOINED; Genomic_DNA.
EMBL; X52608; CAA36839.1; JOINED; Genomic_DNA.
EMBL; BT006855; AAP35501.1; -; mRNA.
EMBL; AC093503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC005137; AAH05137.1; -; mRNA.
CCDS; CCDS33061.1; -.
CCDS; CCDS86782.1; -.
RefSeq; NP_001316851.1; NM_001329922.1.
RefSeq; NP_001316852.1; NM_001329923.1.
RefSeq; NP_001316853.1; NM_001329924.1.
RefSeq; NP_001316854.1; NM_001329925.1.
RefSeq; NP_001316855.1; NM_001329926.1.
RefSeq; NP_001734.1; NM_001743.5.
RefSeq; NP_005175.2; NM_005184.3.
RefSeq; NP_008819.1; NM_006888.4.
PDB; 5COC; X-ray; 2.67 A; A=7-78.
PDB; 5J03; X-ray; 2.00 A; B=1-149.
PDB; 6K67; X-ray; 1.95 A; B/D=9-81.
PDB; 7BYL; EM; 2.50 A; B/D/F/H=1-149.
PDB; 7BYM; EM; 3.10 A; B/D/F/H=1-149.
PDB; 7BYN; EM; 3.30 A; B/D/F/H=1-149.
PDB; 7CR3; EM; 3.60 A; C/E/F/H=1-149.
PDB; 7CR4; EM; 3.90 A; C/E/G/H=1-149.
PDB; 7CR7; EM; 3.70 A; C/E/F/H=1-149.
PDBsum; 5COC; -.
PDBsum; 5J03; -.
PDBsum; 6K67; -.
PDBsum; 7BYL; -.
PDBsum; 7BYM; -.
PDBsum; 7BYN; -.
PDBsum; 7CR3; -.
PDBsum; 7CR4; -.
PDBsum; 7CR7; -.
SMR; P0DP25; -.
BindingDB; P0DP25; -.
DrugBank; DB11093; Calcium citrate.
DrugBank; DB11348; Calcium Phosphate.
DrugBank; DB14481; Calcium phosphate dihydrate.
DrugCentral; P0DP25; -.
GlyGen; P0DP25; 1 site, 1 O-linked glycan (1 site).
iPTMnet; P0DP25; -.
MetOSite; P0DP25; -.
BioMuta; CALM3; -.
EPD; P0DP25; -.
jPOST; P0DP25; -.
MassIVE; P0DP25; -.
PRIDE; P0DP25; -.
Antibodypedia; 39411; 181 antibodies.
DNASU; 801; -.
Ensembl; ENST00000291295; ENSP00000291295; ENSG00000160014.
Ensembl; ENST00000596362; ENSP00000472141; ENSG00000160014.
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; CALM3; -.
HGNC; HGNC:1449; CALM3.
HPA; ENSG00000160014; Tissue enhanced (brain).
MalaCards; CALM3; -.
MIM; 114183; gene.
MIM; 618782; phenotype.
neXtProt; NX_P0DP25; -.
OpenTargets; ENSG00000143933; -.
OpenTargets; ENSG00000160014; -.
OpenTargets; ENSG00000198668; -.
Orphanet; 3286; Catecholaminergic polymorphic ventricular tachycardia.
Orphanet; 101016; Romano-Ward syndrome.
VEuPathDB; HostDB:ENSG00000160014; -.
GeneTree; ENSGT00950000182980; -.
OMA; HQIEFDE; -.
OrthoDB; 1386217at2759; -.
PathwayCommons; P0DP25; -.
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; CALM3; human.
Pharos; P0DP25; Tclin.
PRO; PR:P0DP25; -.
Proteomes; UP000005640; Chromosome 19.
RNAct; P0DP25; protein.
ExpressionAtlas; P0DP25; 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; TAS:UniProtKB.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl.
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:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
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:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
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:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
GO; GO:0030235; F:nitric-oxide synthase regulator activity; IEA:Ensembl.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl.
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:0031800; F:type 3 metabotropic glutamate receptor binding; IEA:Ensembl.
GO; GO:0007190; P:activation of adenylate cyclase activity; IEA:Ensembl.
GO; GO:0005513; P:detection of calcium ion; IMP:BHF-UCL.
GO; GO:0090151; P:establishment of protein localization to mitochondrial membrane; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:1901842; P:negative regulation of high voltage-gated calcium channel activity; IMP:UniProtKB.
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; ISS:BHF-UCL.
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:0051000; P:positive regulation of nitric-oxide synthase activity; 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; IEA:Ensembl.
GO; GO:0098901; P:regulation of cardiac muscle cell action potential; IMP:UniProtKB.
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:1900242; P:regulation of synaptic vesicle endocytosis; IEA:Ensembl.
GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
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.7,
ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
CHAIN 2..149
/note="Calmodulin-3"
/id="PRO_0000439934"
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.7,
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:P0DP31"
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 103
/note="A -> V (in CPVT6; decreased calcium-binding
affinity; not changed binding to RYR2; increased RYR2
calcium-release channel activity; decreased calcium-
dependent inactivation of L-type calcium channel; not
changed action potential duration)"
/evidence="ECO:0000269|PubMed:27516456"
/id="VAR_078261"
VARIANT 130
/note="D -> G (in LQT16)"
/evidence="ECO:0000269|PubMed:25460178,
ECO:0000269|PubMed:31454269"
/id="VAR_083815"
VARIANT 141
/note="E -> K (in LQT16; loss-of-function variant causing
impaired negative regulation of high voltage-gated calcium
channel activity; impaired regulation of cardiac muscle
cell action potential; decreased calcium ion binding)"
/evidence="ECO:0000269|PubMed:31454269"
/id="VAR_083816"
HELIX 9..20
/evidence="ECO:0007829|PDB:6K67"
STRAND 26..28
/evidence="ECO:0007829|PDB:7BYL"
HELIX 30..39
/evidence="ECO:0007829|PDB:6K67"
HELIX 46..54
/evidence="ECO:0007829|PDB:6K67"
STRAND 61..64
/evidence="ECO:0007829|PDB:6K67"
HELIX 66..76
/evidence="ECO:0007829|PDB:6K67"
HELIX 80..92
/evidence="ECO:0007829|PDB:7BYL"
STRAND 98..102
/evidence="ECO:0007829|PDB:7BYL"
HELIX 103..112
/evidence="ECO:0007829|PDB:7BYL"
STRAND 113..115
/evidence="ECO:0007829|PDB:7BYL"
HELIX 119..128
/evidence="ECO:0007829|PDB:7BYL"
STRAND 133..138
/evidence="ECO:0007829|PDB:7BYL"
HELIX 139..146
/evidence="ECO:0007829|PDB:7BYL"
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 :
[Camsap3 Kiaa1543] Calmodulin-regulated spectrin-associated protein 3 (Marshalin) (Protein Nezha)
[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)
[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)
[Camk2d Kiaa4163] Calcium/calmodulin-dependent protein kinase type II subunit delta (CaM kinase II subunit delta) (CaMK-II subunit delta) (EC 2.7.11.17)
[calA camA DDB_G0279407] Calmodulin (CaM)
[PPP3CC CALNA3 CNA3] Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calcineurin, testis-specific catalytic subunit) (Calmodulin-dependent calcineurin A subunit gamma isoform)
[PDE1C] Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C (Cam-PDE 1C) (3',5'-cyclic-AMP phosphodiesterase) (EC 3.1.4.-) (3',5'-cyclic-GMP phosphodiesterase) (EC 3.1.4.35) (Hcam3)
[PPP3CB CALNA2 CALNB CNA2] Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit beta isoform) (CNA beta)
[PPP3CA CALNA CNA] Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit alpha isoform)
[Ppp3ca Calna] Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit alpha isoform) (CNA alpha)
[Pde1c] Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C (Cam-PDE 1C) (3',5'-cyclic-AMP phosphodiesterase) (EC 3.1.4.-) (3',5'-cyclic-GMP phosphodiesterase) (EC 3.1.4.35)
[Pde1c] Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C (Cam-PDE 1C) (3',5'-cyclic-AMP phosphodiesterase) (EC 3.1.4.-) (3',5'-cyclic-GMP phosphodiesterase) (EC 3.1.4.35)
[Ppp3cb Calnb] Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit beta isoform) (CNA beta)
[Ppp3cc Calnc] Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calcineurin, testis-specific catalytic subunit) (Calmodulin-dependent calcineurin A subunit gamma isoform)
[CALM3 CALML2 CAM3 CAMC CAMIII] Calmodulin-3
[PPP3CA] Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit alpha isoform)
[Ppp3ca Calna] Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit alpha isoform)
[CCAMK DMI3 MTR_8g043970] Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase DMI-3 (EC 2.7.11.17) (CCaMK DMI3) (MtCCaMK) (Protein DOES NOT MAKE INFECTIONS 3)
[Ppp3cb] Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit beta isoform) (CNA beta)
[Calm3 Cam3 Camc CaMIII] Calmodulin-3
[CRK3 CaMK4 CK At2g46700 T3A4.8] CDPK-related kinase 3 (AtCRK3) (EC 2.7.11.1) (Calcium/calmodulin-dependent protein kinase 4) (AtCK)
[CAMK1G CLICK3 VWS1] Calcium/calmodulin-dependent protein kinase type 1G (EC 2.7.11.17) (CaM kinase I gamma) (CaM kinase IG) (CaM-KI gamma) (CaMKI gamma) (CaMKIG) (CaMK-like CREB kinase III) (CLICK III)
[Calm3 Cam3 Camc] Calmodulin-3
[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)
[PDE1B PDE1B1 PDES1B] Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B (Cam-PDE 1B) (EC 3.1.4.17) (63 kDa Cam-PDE)
[cmd-1 T21H3.3] Calmodulin (CaM)
[PDE1A] Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A (Cam-PDE 1A) (EC 3.1.4.17) (61 kDa Cam-PDE) (hCam-1)
[Pde1b Pde1b1] Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B (Cam-PDE 1B) (EC 3.1.4.17) (63 kDa Cam-PDE)
[Pde1a] Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A (Cam-PDE 1A) (EC 3.1.4.17) (61 kDa Cam-PDE)
[CNA1 CMP1 YLR433C L9753.6] Serine/threonine-protein phosphatase 2B catalytic subunit A1 (EC 3.1.3.16) (Calcineurin A1) (Calmodulin-binding protein 1)

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