GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Calmodulin-3

 CALM3_MOUSE             Reviewed;         149 AA.
P0DP28; 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 35.
RecName: Full=Calmodulin-3 {ECO:0000250|UniProtKB:P0DP25};
Name=Calm3 {ECO:0000312|MGI:MGI:103249}; Synonyms=Cam3, Camc;
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=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).
[3]
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).
[4]
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.
[5]
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.
[6]
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).
[7]
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).
[8]
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).
[9]
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).
[10]
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).
[11]
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).
-!- 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. 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:P0DP25}.
-!- 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 (By
similarity). 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). {ECO:0000250|UniProtKB:P0DP25,
ECO:0000250|UniProtKB:P0DP26, ECO:0000250|UniProtKB:P62161,
ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:24569478,
ECO:0000269|PubMed:25380116}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Cytoplasm,
cytoskeleton, spindle pole. Note=Distributed throughout the cell during
interphase, but during mitosis becomes dramatically localized to the
spindle poles and the spindle microtubules. {ECO:0000250}.
-!- 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:P0DP25}.
-!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC39089.2; Type=Erroneous translation; Note=Wrong CDS prediction.; Evidence={ECO:0000305};
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; M19380; AAA66181.1; -; mRNA.
EMBL; AK083996; BAC39089.2; ALT_SEQ; mRNA.
EMBL; AK151610; BAE30549.1; -; mRNA.
EMBL; AK152754; BAE31469.1; -; mRNA.
EMBL; AK153179; BAE31782.1; -; mRNA.
EMBL; BC050926; AAH50926.1; -; mRNA.
CCDS; CCDS39789.1; -.
PIR; S37707; S37707.
RefSeq; NP_031615.1; NM_007589.5.
RefSeq; NP_031616.1; NM_007590.3.
RefSeq; NP_033920.1; NM_009790.5.
SMR; P0DP28; -.
iPTMnet; P0DP28; -.
jPOST; P0DP28; -.
ProteomicsDB; 265510; -.
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:103249; Calm3.
VEuPathDB; HostDB:ENSMUSG00000001175; -.
VEuPathDB; HostDB:ENSMUSG00000019370; -.
VEuPathDB; HostDB:ENSMUSG00000036438; -.
GeneTree; ENSGT00950000182980; -.
OMA; DEMIREP; -.
OrthoDB; 1386217at2759; -.
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; Calm3; mouse.
PRO; PR:P0DP28; -.
Proteomes; UP000000589; Chromosome 12.
Proteomes; UP000000589; Chromosome 17.
Proteomes; UP000000589; Chromosome 7.
RNAct; P0DP28; protein.
ExpressionAtlas; P0DP28; 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; ISO:MGI.
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: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; IEA:Ensembl.
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; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:1901842; P:negative regulation of high voltage-gated calcium channel activity; ISS:UniProtKB.
GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IEA:Ensembl.
GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; IEA:Ensembl.
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; IBA:GO_Central.
GO; GO:0098901; P:regulation of cardiac muscle cell action potential; ISS:UniProtKB.
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: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;
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.4"
CHAIN 2..149
/note="Calmodulin-3"
/id="PRO_0000439937"
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"
CA_BIND 57..68
/note="2"
CA_BIND 94..105
/note="3"
CA_BIND 130..141
/note="4"
REGION 77..149
/note="Necessary and sufficient for interaction with PCP4"
/evidence="ECO:0000250|UniProtKB:P0DP25"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000269|Ref.4"
MOD_RES 22
/note="N6-acetyllysine; alternate"
/evidence="ECO:0007744|PubMed:23806337"
MOD_RES 45
/note="Phosphothreonine; by CaMK4"
/evidence="ECO:0000250|UniProtKB:P0DP31"
MOD_RES 82
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P0DP25"
MOD_RES 95
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P0DP25"
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:P0DP25"
MOD_RES 116
/note="N6,N6,N6-trimethyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P0DP25"
MOD_RES 116
/note="N6-methyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P0DP25"
MOD_RES 139
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P0DP25"
CROSSLNK 22
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P0DP25"
CROSSLNK 22
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000250|UniProtKB:P62157"
CONFLICT 142
/note="F -> S (in Ref. 2; BAC39089)"
/evidence="ECO:0000305"
SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK


Related products :

Catalog number Product name Quantity
EIAAB05212 Calml4,Calmodulin-like protein 4,Calmodulin-related,CALM-Rel,Mouse,Mus musculus
ant-342 Mouse Anti Human Calmodulin Calmodulin 20
ant-342 Mouse Anti Human Calmodulin Calmodulin 100
ant-342 Mouse Anti Human Calmodulin Calmodulin 5
MA1010 Monoclonal Anti-Calmodulin, Clone number: CM-16, Ig type: mouse IgG1, Immunogen: Preparation of purified calmodulin from Dictyostelium discoideum conjugated to KLH., Specificity: Human;chicken;rat. No 100μg/vial
LF-MA41574 Anti-Calmodulin (J4D8), Mouse Monoclonal to Calmodulin, Isotype IgG2a, Host Mouse 50
EIAAB05213 CALML5,Calmodulin-like protein 5,Calmodulin-like skin protein,CLSP,Homo sapiens,Human
pro-370 Recombinant Human Calmodulin Calmodulin 50
pro-370 Recombinant Human Calmodulin Calmodulin 10
pro-370 Recombinant Human Calmodulin Calmodulin 1mg
LF-MA50011 anti-Calmodulin (CM-16), Mouse monoclonal to Calmodulin, Isotype IgG1, Host Mouse 200 ul
EIAAB05208 CALML3,Calmodulin-like protein 3,Calmodulin-related protein NB-1,CaM-like protein,CLP,Homo sapiens,Human
orb80987 Human Calmodulin protein Calmodulin Human Recombinant full length protein expressed in E.coli, having Molecular Weight of approximately 16 kDa, the Accession number is NP_001734. For research use only 10
1740-2384 NATIVE BOVINE CALMODULIN, Product Type Purified Protein, Specificity CALMODULIN, Target Species Bovine, Host N_A, Format Purified, Isotypes , Applications E, Clone 1 mg
SCH-1740-2384 NATIVE BOVINE CALMODULIN, Product Type Purified Protein, Specificity CALMODULIN, Target Species Bovine, Host N_A, Format Purified, Isotypes , Applications E, Clone 1 mg
108334-68-5 Syntide 2 calmodulin-dependent protein Syntide 2 calmodulin-d 1g
73298-54-1 Calmodulin Calmodulin 1g
AS09 486 Antibody: Ca2+-ATPase | calmodulin-stimulated calcium-ATPase, Immunogen: KLH-conjugated synthetic peptide derived from Brassica oleracea calmodulin-stimulated calcium-ATPase P93067, Host: rabbit, poly 100
MCA5125Z MOUSE ANTI HUMAN CALMODULIN Azide free, Product Type Monoclonal Antibody, Specificity CALMODULIN, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG1, Applications IF, Clone 3F4 0.1 mg
EIAAB05237 Calmodulin-regulated spectrin-associated protein 1-like protein 1,Calmodulin-regulated spectrin-associated protein 2,CAMSAP1L1,CAMSAP2,Homo sapiens,Human,KIAA1078
EIAAB05236 Calmodulin-regulated spectrin-associated protein 1-like protein 1,Calmodulin-regulated spectrin-associated protein 2,Camsap1l1,Camsap2,Kiaa1078,Mouse,Mus musculus
orb70537 Calmodulin Dependent Protein Kinase 2-g (345-358) peptide This is Calmodulin Dependent Protein Kinase 2-g (345-358) peptide. For research use only. 1 mg
orb71484 Calmodulin-Dependent Protein Kinase 2 (281-309) peptide This is Calmodulin-Dependent Protein Kinase 2 (281-309) peptide. For research use only. 1 mg
orb70539 Calmodulin-Dependent Protein Kinase 2 (281-289) peptide This is Calmodulin-Dependent Protein Kinase 2 (281-289) peptide. For research use only. 1 mg
orb71485 Calmodulin-Dependent Protein Kinase 2 (290-309) peptide This is Calmodulin-Dependent Protein Kinase 2 (290-309) peptide. For research use only. 1 mg
Pathways :
WP164: Glutathione metabolism
WP1545: miRNAs involved in DDR
WP497: Urea cycle and metabolism of amino groups
WP1349: Wnt Signaling Pathway
WP1388: Glycogen Metabolism
WP104: Alanine and aspartate metabolism
WP1379: Diurnally regulated genes with circadian orthologs
WP436: Glycogen Metabolism
WP537: Translation Factors
WP822: Diurnally regulated genes with circadian orthologs
WP2349: vitamin B3 (niacin), NAD and NADP biosynthesis pathway
WP2087: miRNA regulation of DNA Damage Response
WP1346: IL-7 Signaling Pathway
WP426: Urea cycle and metabolism of amino groups
WP1039: Glutathione metabolism
WP730: Glutathione and one carbon metabolism
WP2344: vitamin B6 (pyridoxine, pyridoxal, pyridoxamine) biosynthesis and salvage pathway
WP1322: IL-6 Signaling Pathway
WP270: Tryptophan metabolism
WP394: RNA interference and miRNA
WP240: Alanine and aspartate metabolism
WP562: Circadian Exercise
WP79: Tryptophan metabolism
WP387: IL-6 signaling Pathway
WP1530: miRNA regulation of DNA Damage Response

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)

Bibliography :
[34558042] Bioinformatics analysis of key genes and potential mechanism in cadmium-induced breast cancer progression.
[34349506] Sputum Protein Biomarkers in Airway Diseases: A Pilot Study.
[33281552] Krüppel-Like Factors 9 and 13 Block Axon Growth by Transcriptional Repression of Key Components of the cAMP Signaling Pathway.
[32071822] RNA-sequencing analysis of the effect of luteolin on methamphetamine-induced hepatotoxicity in rats: a preliminary study.
[30816530] In silico analysis identified miRNA‑based therapeutic agents against glioblastoma multiforme.
[28765142] A retained intron in the 3'-UTR of mRNA mediates its Staufen2- and activity-dependent localization to neuronal dendrites.
[26483802] ROS-mediated enhanced transcription of CYP38 promotes the plant tolerance to high light stress by suppressing GTPase activation of PsbO2.
[25625560] Melatonin improves experimental colitis with sleep deprivation.
[25396734] Comprehensive analysis of the association of EGFR, CALM3 and SMARCD1 gene polymorphisms with BMD in Caucasian women.
[25206881] Chronic neuroprotective effects of low concentration lithium on SH-SY5Y cells: possible involvement of stress proteins and gene expression.