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Calmodulin-1

 CALM1_MOUSE             Reviewed;         149 AA.
P0DP26; P02593; P62204; P70667; P99014; Q3TEH7; Q3THK5; Q3U6Z5; Q3U7C7;
Q498A3; Q61379; Q61380; Q8BNC9; Q91VQ9; Q9D6G4;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
10-MAY-2017, sequence version 1.
29-SEP-2021, entry version 37.
RecName: Full=Calmodulin-1 {ECO:0000250|UniProtKB:P0DP23};
Name=Calm1 {ECO:0000312|MGI:MGI:88251}; Synonyms=Calm, Cam, Cam1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3384819;
Bender P.K., Dedman J.R., Emerson C.P. Jr.;
"The abundance of calmodulin mRNAs is regulated in phosphorylase kinase-
deficient skeletal muscle.";
J. Biol. Chem. 263:9733-9737(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
Kato K.;
"A collection of cDNA clones with specific expression patterns in mouse
brain.";
Eur. J. Neurosci. 2:704-711(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, DBA/2J, and NOD;
TISSUE=Amnion, Bone marrow, Colon, Hippocampus, Kidney, Liver, Lung,
Mammary gland, Ovary, Placenta, Stomach, Testis, Thymus, and Tongue;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=129, C57BL/6J, and Czech II;
TISSUE=Brain, Mammary tumor, Placenta, and Spinal ganglion;
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).
[5]
PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Liver;
Bienvenut W.V.;
Submitted (JUL-2005) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 15-31; 79-87 AND 92-107, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[7]
INTERACTION WITH GIMAP4.
PubMed=16569770; DOI=10.1182/blood-2005-11-4616;
Schnell S., Demolliere C., van den Berk P., Jacobs H.;
"Gimap4 accelerates T-cell death.";
Blood 108:591-599(2006).
[8]
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100 AND SER-102, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[12]
INTERACTION WITH IQCF1.
PubMed=25380116; DOI=10.1111/andr.296;
Fang P., Xu W., Li D., Zhao X., Dai J., Wang Z., Yan X., Qin M., Zhang Y.,
Xu C., Wang L., Qiao Z.;
"A novel acrosomal protein, IQCF1, involved in sperm capacitation and the
acrosome reaction.";
Andrology 3:332-344(2015).
[13]
INTERACTION WITH SYT7.
PubMed=24569478; DOI=10.7554/elife.01524;
Liu H., Bai H., Hui E., Yang L., Evans C.S., Wang Z., Kwon S.E.,
Chapman E.R.;
"Synaptotagmin 7 functions as a Ca2+-sensor for synaptic vesicle
replenishment.";
Elife 3:E01524-E01524(2014).
[14]
INTERACTION WITH HINT1 AND HINT3.
PubMed=31088288; DOI=10.1089/ars.2019.7724;
Cortes-Montero E., Rodriguez-Munoz M., Sanchez-Blazquez P., Garzon J.;
"The Axonal Motor Neuropathy-Related HINT1 Protein Is a Zinc- and
Calmodulin-Regulated Cysteine SUMO Protease.";
Antioxid. Redox Signal. 31:503-520(2019).
[15]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-147 IN COMPLEX WITH MYO5A.
PubMed=17151196; DOI=10.1073/pnas.0609436103;
Houdusse A., Gaucher J.F., Krementsova E., Mui S., Trybus K.M., Cohen C.;
"Crystal structure of apo-calmodulin bound to the first two IQ motifs of
myosin V reveals essential recognition features.";
Proc. Natl. Acad. Sci. U.S.A. 103:19326-19331(2006).
[16] {ECO:0007744|PDB:3WFN}
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1893-1914 IN COMPLEX WITH SCN8A,
INTERACTION WITH SCN8A, AND MUTAGENESIS OF GLU-115; GLU-121; GLU-124 AND
GLU-128.
PubMed=23942337; DOI=10.1038/srep02435;
Reddy Chichili V.P., Xiao Y., Seetharaman J., Cummins T.R., Sivaraman J.;
"Structural basis for the modulation of the neuronal voltage-gated sodium
channel NaV1.6 by calmodulin.";
Sci. Rep. 3:2435-2435(2013).
-!- 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. Is a regulator of
voltage-dependent L-type calcium channels. Mediates calcium-dependent
inactivation of CACNA1C. Positively regulates calcium-activated
potassium channel activity of KCNN2. Forms a potassium channel complex
with KCNQ1 and regulates electrophysiological activity of the channel
via calcium-binding. Acts as a sensor to modulate the endomplasmic
reticulum contacts with other organelles mediated by VMP1:ATP2A2 (By
similarity). {ECO:0000250|UniProtKB:P0DP23}.
-!- SUBUNIT: Interacts with CEP97, CCP110, MYO1C, TTN/titin and SRY.
Interacts with MYO10. Interacts with RRAD (By similarity). Interacts
with USP6; the interaction is calcium dependent (By similarity).
Interacts with CDK5RAP2. Interacts with SCN5A (By similarity).
Interacts with FCHO1. Interacts with MIP in a 1:2 stoichiometry; the
interaction with the cytoplasmic domains from two MIP subunits promotes
MIP water channel closure. Interacts with ORAI1; this may play a role
in the regulation of ORAI1-mediated calcium transport (By similarity).
Interacts with RYR1 (PubMed:18650434). Interacts with MYO5A
(PubMed:17151196). Interacts with IQCF1 (PubMed:25380116). Interacts
with SYT7 (PubMed:24569478). 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:18650434). Interacts with PCP4; regulates calmodulin calcium-
binding (By similarity). 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 (By similarity). Interacts with alpha-synuclein/SNCA (By
similarity). Interacts with SLC9A1 in a calcium-dependent manner (By
similarity). In the absence of Ca(+2), interacts with GIMAP4 (via IQ
domain) (PubMed:16569770). Interacts with SCN8A; the interaction
modulates the inactivation rate of SCN8A (PubMed:23942337). Interaction
with KIF1A; the interaction is increased in presence of calcium and
increases neuronal dense core vesicles motility (By similarity).
Interacts with KCNN3 (By similarity). Interacts with KCNQ1 (via C-
terminus); forms a heterooctameric structure (with 4:4 KCNQ1:CALM
stoichiometry) in a calcium-independent manner (By similarity).
Interacts with PIK3C3; the interaction modulates PIK3C3 kinase activity
(By similarity). Interacts with HINT1; interaction increases in the
presence of calcium ions (PubMed:31088288). Interacts with HINT3
(PubMed:31088288). {ECO:0000250, ECO:0000250|UniProtKB:P0DP23,
ECO:0000250|UniProtKB:P62161, ECO:0000269|PubMed:16569770,
ECO:0000269|PubMed:17151196, ECO:0000269|PubMed:18650434,
ECO:0000269|PubMed:23942337, ECO:0000269|PubMed:24569478,
ECO:0000269|PubMed:25380116, ECO:0000269|PubMed:31088288}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
{ECO:0000250|UniProtKB:P0DP23}. Cytoplasm, cytoskeleton, spindle pole
{ECO:0000250|UniProtKB:P0DP23}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250|UniProtKB:P0DP23}.
Note=Distributed throughout the cell during interphase, but during
mitosis becomes dramatically localized to the spindle poles and the
spindle microtubules. {ECO:0000250|UniProtKB:P0DP23}.
-!- DOMAIN: The N-terminal and C-terminal lobes of CALM bind to the C-
terminus of KCNQ1 in a clamp-like conformation. Binding of CALM C-
terminus to KCNQ1 is calcium-independent but is essential for assembly
of the structure. Binding of CALM N-terminus to KCNQ1 is calcium-
dependent and regulates electrophysiological activity of the channel.
{ECO:0000250|UniProtKB:P0DP23}.
-!- PTM: Ubiquitination results in a strongly decreased activity.
{ECO:0000250}.
-!- PTM: Phosphorylation results in a decreased activity. {ECO:0000250}.
-!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
{ECO:0000250|UniProtKB:P0DP23}.
-!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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EMBL; M19381; AAA66182.1; -; mRNA.
EMBL; X61432; CAA43674.1; -; mRNA.
EMBL; AK004673; BAB23462.1; -; mRNA.
EMBL; AK013695; BAB28959.1; -; mRNA.
EMBL; AK088141; BAC40168.1; -; mRNA.
EMBL; AK150288; BAE29443.1; -; mRNA.
EMBL; AK150978; BAE30007.1; -; mRNA.
EMBL; AK151001; BAE30025.1; -; mRNA.
EMBL; AK151552; BAE30497.1; -; mRNA.
EMBL; AK151784; BAE30686.1; -; mRNA.
EMBL; AK151923; BAE30801.1; -; mRNA.
EMBL; AK151992; BAE30856.1; -; mRNA.
EMBL; AK152148; BAE30984.1; -; mRNA.
EMBL; AK152715; BAE31439.1; -; mRNA.
EMBL; AK152719; BAE31442.1; -; mRNA.
EMBL; AK152850; BAE31543.1; -; mRNA.
EMBL; AK152897; BAE31579.1; -; mRNA.
EMBL; AK153004; BAE31644.1; -; mRNA.
EMBL; AK153348; BAE31924.1; -; mRNA.
EMBL; AK153426; BAE31985.1; -; mRNA.
EMBL; AK153546; BAE32083.1; -; mRNA.
EMBL; AK159762; BAE35353.1; -; mRNA.
EMBL; AK160057; BAE35595.1; -; mRNA.
EMBL; AK160508; BAE35832.1; -; mRNA.
EMBL; AK161302; BAE36309.1; -; mRNA.
EMBL; AK162314; BAE36849.1; -; mRNA.
EMBL; AK166308; BAE38695.1; -; mRNA.
EMBL; AK167353; BAE39452.1; -; mRNA.
EMBL; AK168002; BAE39990.1; -; mRNA.
EMBL; AK168241; BAE40191.1; -; mRNA.
EMBL; AK168663; BAE40516.1; -; mRNA.
EMBL; AK168803; BAE40633.1; -; mRNA.
EMBL; AK169027; BAE40819.1; -; mRNA.
EMBL; AK169055; BAE40843.1; -; mRNA.
EMBL; AK169640; BAE41271.1; -; mRNA.
EMBL; BC054805; AAH54805.1; -; mRNA.
CCDS; CCDS36523.1; -.
PIR; I49567; I49567.
RefSeq; NP_001300863.1; NM_001313934.1.
RefSeq; NP_031615.1; NM_007589.5.
RefSeq; NP_031616.1; NM_007590.3.
RefSeq; NP_033920.1; NM_009790.5.
PDB; 1UP5; X-ray; 1.90 A; A/B=2-149.
PDB; 2DFS; EM; 24.00 A; B/C/D/E/F/G/N/O/P/Q/R/S=2-149.
PDB; 2IX7; X-ray; 2.50 A; A/B=3-147.
PDB; 3WFN; X-ray; 1.95 A; B/C/D/E=1-149.
PDB; 4E50; X-ray; 2.70 A; A=1-149.
PDB; 4E53; X-ray; 2.69 A; A/B=1-149.
PDB; 4HEX; X-ray; 2.00 A; A/B=1-149.
PDB; 4ZLK; X-ray; 2.50 A; B=1-149.
PDB; 7B1G; EM; 3.60 A; E=1-149.
PDB; 7CQP; X-ray; 1.90 A; B=1-78.
PDBsum; 1UP5; -.
PDBsum; 2DFS; -.
PDBsum; 2IX7; -.
PDBsum; 3WFN; -.
PDBsum; 4E50; -.
PDBsum; 4E53; -.
PDBsum; 4HEX; -.
PDBsum; 4ZLK; -.
PDBsum; 7B1G; -.
PDBsum; 7CQP; -.
SMR; P0DP26; -.
STRING; 10090.ENSMUSP00000105709; -.
ChEMBL; CHEMBL3562176; -.
iPTMnet; P0DP26; -.
MetOSite; P0DP26; -.
PhosphoSitePlus; P0DP26; -.
jPOST; P0DP26; -.
PRIDE; P0DP26; -.
ProteomicsDB; 265509; -.
Antibodypedia; 39411; 181 antibodies.
Antibodypedia; 4344; 534 antibodies.
Antibodypedia; 53945; 69 antibodies.
DNASU; 12313; -.
Ensembl; ENSMUST00000019514; ENSMUSP00000019514; ENSMUSG00000019370.
Ensembl; ENSMUST00000040440; ENSMUSP00000048857; ENSMUSG00000036438.
Ensembl; ENSMUST00000110082; ENSMUSP00000105709; ENSMUSG00000001175.
GeneID; 12313; -.
GeneID; 12314; -.
GeneID; 12315; -.
KEGG; mmu:12313; -.
KEGG; mmu:12314; -.
KEGG; mmu:12315; -.
CTD; 801; -.
CTD; 805; -.
CTD; 808; -.
MGI; MGI:88251; Calm1.
VEuPathDB; HostDB:ENSMUSG00000001175; -.
VEuPathDB; HostDB:ENSMUSG00000019370; -.
VEuPathDB; HostDB:ENSMUSG00000036438; -.
eggNOG; KOG0027; Eukaryota.
OMA; DEMIREP; -.
OrthoDB; 1386217at2759; -.
Reactome; R-MMU-111932; CaMK IV-mediated phosphorylation of CREB.
Reactome; R-MMU-111933; Calmodulin induced events.
Reactome; R-MMU-111957; Cam-PDE 1 activation.
Reactome; R-MMU-114608; Platelet degranulation.
Reactome; R-MMU-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
Reactome; R-MMU-163615; PKA activation.
Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-MMU-2025928; Calcineurin activates NFAT.
Reactome; R-MMU-203615; eNOS activation.
Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
Reactome; R-MMU-2672351; Stimuli-sensing channels.
Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-MMU-4086398; Ca2+ pathway.
Reactome; R-MMU-418359; Reduction of cytosolic Ca++ levels.
Reactome; R-MMU-425561; Sodium/Calcium exchangers.
Reactome; R-MMU-438066; Unblocking of NMDA receptors, glutamate binding and activation.
Reactome; R-MMU-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
Reactome; R-MMU-445355; Smooth Muscle Contraction.
Reactome; R-MMU-451308; Activation of Ca-permeable Kainate Receptor.
Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
Reactome; R-MMU-5578775; Ion homeostasis.
Reactome; R-MMU-5607763; CLEC7A (Dectin-1) induces NFAT activation.
Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
Reactome; R-MMU-5673000; RAF activation.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
Reactome; R-MMU-8876725; Protein methylation.
Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
Reactome; R-MMU-936837; Ion transport by P-type ATPases.
Reactome; R-MMU-9619229; Activation of RAC1 downstream of NMDARs.
Reactome; R-MMU-9648002; RAS processing.
BioGRID-ORCS; 12313; 4 hits in 65 CRISPR screens.
BioGRID-ORCS; 12314; 1 hit in 60 CRISPR screens.
BioGRID-ORCS; 12315; 1 hit in 63 CRISPR screens.
ChiTaRS; Calm1; mouse.
PRO; PR:P0DP26; -.
Proteomes; UP000000589; Chromosome 12.
Proteomes; UP000000589; Chromosome 17.
Proteomes; UP000000589; Chromosome 7.
RNAct; P0DP26; protein.
ExpressionAtlas; P0DP26; baseline and differential.
GO; GO:0034704; C:calcium channel complex; IEA:Ensembl.
GO; GO:1902494; C:catalytic complex; IEA:Ensembl.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030426; C:growth cone; ISO:MGI.
GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl.
GO; GO:0043209; C:myelin sheath; IDA:CAFA.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0030017; C:sarcomere; IEA:Ensembl.
GO; GO:0005876; C:spindle microtubule; IEA:Ensembl.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
GO; GO:0008076; C:voltage-gated potassium channel complex; IGI:MGI.
GO; GO:0010856; F:adenylate cyclase activator activity; IEA:Ensembl.
GO; GO:0008179; F:adenylate cyclase binding; ISO:MGI.
GO; GO:0019855; F:calcium channel inhibitor activity; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
GO; GO:0031997; F:N-terminal myristoylation domain binding; IEA:Ensembl.
GO; GO:0050998; F:nitric-oxide synthase binding; ISO:MGI.
GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISO:MGI.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0072542; F:protein phosphatase activator activity; IEA:Ensembl.
GO; GO:0031432; F:titin binding; IEA:Ensembl.
GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
GO; GO:0031800; F:type 3 metabotropic glutamate receptor binding; ISO:MGI.
GO; GO:0007190; P:activation of adenylate cyclase activity; IEA:Ensembl.
GO; GO:0016240; P:autophagosome membrane docking; ISS:UniProtKB.
GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
GO; GO:0005513; P:detection of calcium ion; IEA:Ensembl.
GO; GO:0090151; P:establishment of protein localization to mitochondrial membrane; IEA:Ensembl.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:MGI.
GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; ISS:UniProtKB.
GO; GO:1901842; P:negative regulation of high voltage-gated calcium channel activity; IEA:Ensembl.
GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISS:UniProtKB.
GO; GO:0140056; P:organelle localization by membrane tethering; ISS:UniProtKB.
GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; IEA:Ensembl.
GO; GO:0043388; P:positive regulation of DNA binding; IDA:MGI.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IEA:Ensembl.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IEA:Ensembl.
GO; GO:0098901; P:regulation of cardiac muscle cell action potential; IEA:Ensembl.
GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:Ensembl.
GO; GO:0032465; P:regulation of cytokinesis; IEA:Ensembl.
GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IEA:Ensembl.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; ISS:UniProtKB.
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:0051412; P:response to corticosterone; IEA:Ensembl.
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; Isopeptide bond; Metal-binding; Methylation;
Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000269|Ref.5"
CHAIN 2..149
/note="Calmodulin-1"
/id="PRO_0000439935"
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:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
CA_BIND 57..68
/note="2"
/evidence="ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
CA_BIND 94..105
/note="3"
/evidence="ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
CA_BIND 130..141
/note="4"
/evidence="ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK"
REGION 77..149
/note="Necessary and sufficient for interaction with PCP4"
/evidence="ECO:0000250|UniProtKB:P0DP23"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000269|Ref.5"
MOD_RES 22
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 45
/note="Phosphothreonine; by CaMK4"
/evidence="ECO:0000250|UniProtKB:P0DP29"
MOD_RES 82
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P0DP23"
MOD_RES 95
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P0DP23"
MOD_RES 100
/note="Phosphotyrosine"
/evidence="ECO:0007744|PubMed:18034455,
ECO:0007744|PubMed:21183079"
MOD_RES 102
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 111
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P0DP23"
MOD_RES 116
/note="N6,N6,N6-trimethyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P0DP23"
MOD_RES 116
/note="N6-methyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P0DP23"
MOD_RES 139
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P0DP23"
CROSSLNK 22
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P0DP23"
CROSSLNK 22
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000250|UniProtKB:P62157"
MUTAGEN 115
/note="E->A: Decreases interaction with SCN8A in the
absence of calcium."
/evidence="ECO:0000269|PubMed:23942337"
MUTAGEN 121
/note="E->A: Decreases interaction with SCN8A in the
absence of calcium."
/evidence="ECO:0000269|PubMed:23942337"
MUTAGEN 124
/note="E->A: Decreases interaction with SCN8A in the
absence of calcium."
/evidence="ECO:0000269|PubMed:23942337"
MUTAGEN 128
/note="E->A: Decreases interaction with SCN8A in the
absence of calcium."
/evidence="ECO:0000269|PubMed:23942337"
CONFLICT 26
/note="G -> N (in Ref. 1; AAA66182)"
/evidence="ECO:0000305"
CONFLICT 55
/note="E -> V (in Ref. 3; BAE41271)"
/evidence="ECO:0000305"
CONFLICT 69
/note="F -> L (in Ref. 3; BAE40191)"
/evidence="ECO:0000305"
CONFLICT 82
/note="S -> G (in Ref. 3; BAE31439/BAE31644/BAE31442)"
/evidence="ECO:0000305"
CONFLICT 126
/note="I -> T (in Ref. 3; BAE31579)"
/evidence="ECO:0000305"
CONFLICT 143
/note="V -> L (in Ref. 3; BAB28959)"
/evidence="ECO:0000305"
HELIX 2..4
/evidence="ECO:0007829|PDB:3WFN"
HELIX 7..19
/evidence="ECO:0007829|PDB:3WFN"
STRAND 22..29
/evidence="ECO:0007829|PDB:3WFN"
HELIX 30..32
/evidence="ECO:0007829|PDB:3WFN"
HELIX 33..39
/evidence="ECO:0007829|PDB:3WFN"
HELIX 46..54
/evidence="ECO:0007829|PDB:3WFN"
STRAND 63..65
/evidence="ECO:0007829|PDB:3WFN"
HELIX 66..93
/evidence="ECO:0007829|PDB:3WFN"
STRAND 98..102
/evidence="ECO:0007829|PDB:3WFN"
HELIX 103..112
/evidence="ECO:0007829|PDB:3WFN"
STRAND 113..115
/evidence="ECO:0007829|PDB:3WFN"
HELIX 119..128
/evidence="ECO:0007829|PDB:3WFN"
STRAND 131..133
/evidence="ECO:0007829|PDB:4E53"
STRAND 136..138
/evidence="ECO:0007829|PDB:3WFN"
HELIX 139..146
/evidence="ECO:0007829|PDB:3WFN"
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 :
[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)
[cya cyaA BP0760] Bifunctional hemolysin/adenylate cyclase (AC-HLY) (ACT) (Cyclolysin) [Cleaved into: Calmodulin-sensitive adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase); Hemolysin]
[cya pXO1-122 BXA0141 GBAA_pXO1_0142] Calmodulin-sensitive adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (Anthrax edema toxin adenylate cyclase component) (Edema factor) (EF)
[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)
[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)
[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 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)
[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)
[Aspm Calmbp1 Sha1] Abnormal spindle-like microcephaly-associated protein homolog (Calmodulin-binding protein Sha1) (Calmodulin-binding protein 1) (Spindle and hydroxyurea checkpoint abnormal protein)
[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)
[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)
[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)
[Camk2n1] Calcium/calmodulin-dependent protein kinase II inhibitor 1 (calcium/calmodulin-dependent protein kinase II inhibitor alpha) (CaM-KIINalpha) (CaMKIINalpha)
[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)
[CML24 TCH2 At5g37770 K22F20.1] Calcium-binding protein CML24 (Calmodulin-like protein 24) (Touch-induced calmodulin-related protein 2)
[Camk2a] Calcium/calmodulin-dependent protein kinase type II subunit alpha (CaM kinase II subunit alpha) (CaMK-II subunit alpha) (EC 2.7.11.17)
[Camk2b Camk2d] Calcium/calmodulin-dependent protein kinase type II subunit beta (CaM kinase II subunit beta) (CaMK-II subunit beta) (EC 2.7.11.17)
[Camk1] Calcium/calmodulin-dependent protein kinase type 1 (EC 2.7.11.17) (CaM kinase I) (CaM-KI) (CaM kinase I alpha) (CaMKI-alpha)
[ADCY1] Adenylate cyclase type 1 (EC 4.6.1.1) (ATP pyrophosphate-lyase 1) (Adenylate cyclase type I) (Adenylyl cyclase 1) (AC1) (Ca(2+)/calmodulin-activated adenylyl cyclase)
[CAMK1] Calcium/calmodulin-dependent protein kinase type 1 (EC 2.7.11.17) (CaM kinase I) (CaM-KI) (CaM kinase I alpha) (CaMKI-alpha)
[PDE1B PDE1B1 PDES1B] Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B (Cam-PDE 1B) (EC 3.1.4.17) (63 kDa Cam-PDE)
[CALM1 CALM CAM CAM1] Calmodulin-1
[Gap43 Basp2] Neuromodulin (Axonal membrane protein GAP-43) (Calmodulin-binding protein P-57) (Growth-associated protein 43)
[Pde1b Pde1b1] Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B (Cam-PDE 1B) (EC 3.1.4.17) (63 kDa Cam-PDE)
[Adcy1] Adenylate cyclase type 1 (EC 4.6.1.1) (ATP pyrophosphate-lyase 1) (Adenylate cyclase type I) (Adenylyl cyclase 1) (Ca(2+)/calmodulin-activated adenylyl cyclase)
[CNA1 CMP1 YLR433C L9753.6] Serine/threonine-protein phosphatase 2B catalytic subunit A1 (EC 3.1.3.16) (Calcineurin A1) (Calmodulin-binding protein 1)
[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)
[Camk1] Calcium/calmodulin-dependent protein kinase type 1 (EC 2.7.11.17) (CaM kinase I) (CaM-KI) (CaM kinase I alpha) (CaMKI-alpha)

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[34572507] Subtype Differences in the Interaction of HIV-1 Matrix with Calmodulin: Implications for Biological Functions.
[34338988] CALM1 rs3179089 polymorphism might contribute to coronary artery disease susceptibility in Chinese male: a case-control study.
[33616872] Astrocyte Intracellular Caand TrkB Signaling in the Hippocampus Could Be Involved in the Beneficial Behavioral Effects of Antidepressant Treatment.
[33563308] Genetic markers of osteoarthritis: early diagnosis in susceptible Pakistani population.
[33546420] Tribbles Pseudokinase 2 (TRIB2) Regulates Expression of Binding Partners in Bovine Granulosa Cells.
[33280702] Effects of brain tissue section processing and storage time on gene expression.
[33233425] ACE2 Interaction Networks in COVID-19: A Physiological Framework for Prediction of Outcome in Patients with Cardiovascular Risk Factors.
[32625180] Molecular Analysis of S-morphology Aflatoxin Producers From the United States Reveals Previously Unknown Diversity and Two New Taxa.
[32522888] Elimination of long 3'-UTR mRNA isoform by CRISPR-Cas9 gene editing impairs dorsal root ganglion development and hippocampal neuron activation in mice.