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Calmodulin-2

 CALM2_RAT               Reviewed;         149 AA.
P0DP30; P02593; P62161; P70667; P99014; Q61379; Q61380;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
10-MAY-2017, sequence version 1.
29-SEP-2021, entry version 33.
RecName: Full=Calmodulin-2 {ECO:0000250|UniProtKB:P0DP24};
Name=Calm2 {ECO:0000312|RGD:2258};
Synonyms=Cam2, Camb, CaMII {ECO:0000303|PubMed:2527998};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2445749;
Sengupta B., Friedberg F., Detera-Wadleigh S.D.;
"Molecular analysis of human and rat calmodulin complementary DNA clones.
Evidence for additional active genes in these species.";
J. Biol. Chem. 262:16663-16670(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3037336; DOI=10.1128/mcb.7.5.1873-1880.1987;
Nojima H., Kishi K., Sokabe H.;
"Multiple calmodulin mRNA species are derived from two distinct genes.";
Mol. Cell. Biol. 7:1873-1880(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SHR;
PubMed=2527998; DOI=10.1016/0022-2836(89)90388-4;
Nojima H.;
"Structural organization of multiple rat calmodulin genes.";
J. Mol. Biol. 208:269-282(1989).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
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 2-149, ACETYLATION AT ALA-2, AND METHYLATION AT
LYS-116.
TISSUE=Testis;
PubMed=201628;
Dedman J.R., Jackson R.L., Schreiber W.E., Means A.R.;
"Sequence homology of the Ca2+-dependent regulator of cyclic nucleotide
phosphodiesterase from rat testis with other Ca2+-binding proteins.";
J. Biol. Chem. 253:343-346(1978).
[6]
PROTEIN SEQUENCE OF 15-31; 79-87 AND 92-107, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
Lubec G., Chen W.-Q., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[7]
INTERACTION WITH CEACAM1.
PubMed=8576129; DOI=10.1074/jbc.271.3.1393;
Edlund M., Blikstad I., Obrink B.;
"Calmodulin binds to specific sequences in the cytoplasmic domain of C-CAM
and down-regulates C-CAM self-association.";
J. Biol. Chem. 271:1393-1399(1996).
[8]
PHOSPHORYLATION AT THR-45.
PubMed=12392717; DOI=10.1016/s0003-9861(02)00514-3;
Ishida A., Kameshita I., Okuno S., Kitani T., Fujisawa H.;
"Phosphorylation of calmodulin by Ca2+/calmodulin-dependent protein kinase
IV.";
Arch. Biochem. Biophys. 407:72-82(2002).
[9]
INTERACTION WITH RRAD.
PubMed=18056528; DOI=10.1161/circulationaha.107.707257;
Chang L., Zhang J., Tseng Y.-H., Xie C.-Q., Ilany J., Bruning J.C., Sun Z.,
Zhu X., Cui T., Youker K.A., Yang Q., Day S.M., Kahn C.R., Chen Y.E.;
"Rad GTPase deficiency leads to cardiac hypertrophy.";
Circulation 116:2976-2983(2007).
[10]
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
Lubec G., Chen W.-Q.;
Submitted (FEB-2007) to UniProtKB.
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100 AND SER-102, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14 different rat
organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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. Mediates calcium-
dependent inactivation of CACNA1C. Positively regulates calcium-
activated potassium channel activity of KCNN2.
{ECO:0000250|UniProtKB:P62158}.
-!- SUBUNIT: Interacts with CEP97, CCP110, TTN/titin and SRY (By
similarity). Interacts with MYO5A and RRAD (PubMed:18056528). Interacts
with USP6; the interaction is calcium dependent (By similarity).
Interacts with CDK5RAP2 (By similarity). Interacts with SCN5A (By
similarity). Interacts with RYR1 (By similarity). Interacts with FCHO1
(By similarity). 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 SYT7 (By similarity). Interacts with
MYO10 and MYO1C (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
(PubMed:8576129). Interacts with RYR2; regulates RYR2 calcium-release
channel activity (By similarity). 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:P0DP24, ECO:0000250|UniProtKB:P0DP29,
ECO:0000250|UniProtKB:P62157, ECO:0000250|UniProtKB:P62158,
ECO:0000250|UniProtKB:P62204, ECO:0000269|PubMed:18056528,
ECO:0000269|PubMed:8576129}.
-!- 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:0000269|PubMed:12392717}.
-!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
{ECO:0000250|UniProtKB:P0DP24}.
-!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; M19312; AAA40862.1; -; mRNA.
EMBL; M17069; AAA40863.1; -; mRNA.
EMBL; X13833; CAA32062.1; -; Genomic_DNA.
EMBL; X13834; CAA32062.1; JOINED; Genomic_DNA.
EMBL; X13835; CAA32062.1; JOINED; Genomic_DNA.
EMBL; BC058485; AAH58485.1; -; mRNA.
RefSeq; NP_036650.1; NM_012518.3.
RefSeq; NP_059022.1; NM_017326.3.
RefSeq; NP_114175.1; NM_031969.2.
PDB; 6ALE; X-ray; 2.50 A; R=5-148.
PDBsum; 6ALE; -.
SMR; P0DP30; -.
iPTMnet; P0DP30; -.
jPOST; P0DP30; -.
PRIDE; P0DP30; -.
Ensembl; ENSRNOT00000022603; ENSRNOP00000022603; ENSRNOG00000016770.
Ensembl; ENSRNOT00000064679; ENSRNOP00000063822; ENSRNOG00000004060.
GeneID; 24242; -.
GeneID; 24244; -.
GeneID; 50663; -.
KEGG; rno:24242; -.
KEGG; rno:24244; -.
KEGG; rno:50663; -.
CTD; 801; -.
CTD; 805; -.
CTD; 808; -.
RGD; 2258; Calm2.
OMA; RTCPSHL; -.
OrthoDB; 1386217at2759; -.
PRO; PR:P0DP30; -.
Proteomes; UP000002494; Chromosome 1.
Proteomes; UP000002494; Chromosome 6.
ExpressionAtlas; P0DP30; baseline and differential.
GO; GO:0034704; C:calcium channel complex; ISO:RGD.
GO; GO:1902494; C:catalytic complex; ISO:RGD.
GO; GO:0005813; C:centrosome; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0030426; C:growth cone; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0043209; C:myelin sheath; IDA:CAFA.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; ISO:RGD.
GO; GO:0030017; C:sarcomere; ISO:RGD.
GO; GO:0005876; C:spindle microtubule; ISO:RGD.
GO; GO:0000922; C:spindle pole; ISO:RGD.
GO; GO:0031982; C:vesicle; IEA:Ensembl.
GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD.
GO; GO:0010856; F:adenylate cyclase activator activity; ISO:RGD.
GO; GO:0008179; F:adenylate cyclase binding; IDA:RGD.
GO; GO:0019855; F:calcium channel inhibitor activity; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:RGD.
GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
GO; GO:0031997; F:N-terminal myristoylation domain binding; ISO:RGD.
GO; GO:0050998; F:nitric-oxide synthase binding; IDA:RGD.
GO; GO:0030235; F:nitric-oxide synthase regulator activity; IDA:RGD.
GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; ISO:RGD.
GO; GO:0047485; F:protein N-terminus binding; IDA:RGD.
GO; GO:0072542; F:protein phosphatase activator activity; ISO:RGD.
GO; GO:0031432; F:titin binding; ISO:RGD.
GO; GO:0044325; F:transmembrane transporter binding; IDA:RGD.
GO; GO:0007190; P:activation of adenylate cyclase activity; IDA:RGD.
GO; GO:0016240; P:autophagosome membrane docking; ISO:RGD.
GO; GO:0019722; P:calcium-mediated signaling; IMP:RGD.
GO; GO:0005513; P:detection of calcium ion; ISO:RGD.
GO; GO:0090150; P:establishment of protein localization to membrane; IMP:CAFA.
GO; GO:0090151; P:establishment of protein localization to mitochondrial membrane; IMP:CAFA.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:RGD.
GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; ISO:RGD.
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; ISO:RGD.
GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISS:UniProtKB.
GO; GO:0140056; P:organelle localization by membrane tethering; ISO:RGD.
GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; ISO:RGD.
GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:RGD.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:RGD.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:RGD.
GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; ISO:RGD.
GO; GO:0050848; P:regulation of calcium-mediated signaling; IEA:Ensembl.
GO; GO:0098901; P:regulation of cardiac muscle cell action potential; ISO:RGD.
GO; GO:0055117; P:regulation of cardiac muscle contraction; ISO:RGD.
GO; GO:0032465; P:regulation of cytokinesis; ISO:RGD.
GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
GO; GO:1901841; P:regulation of high voltage-gated calcium channel activity; IMP:RGD.
GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:RGD.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IDA:RGD.
GO; GO:1901339; P:regulation of store-operated calcium channel activity; IC:RGD.
GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IMP:CAFA.
GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:CAFA.
GO; GO:0001975; P:response to amphetamine; IEP:RGD.
GO; GO:0051592; P:response to calcium ion; ISO:RGD.
GO; GO:0051412; P:response to corticosterone; IEP:RGD.
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|PubMed:201628, ECO:0000269|Ref.10"
CHAIN 2..149
/note="Calmodulin-2"
/id="PRO_0000439939"
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:P0DP24"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000269|PubMed:201628, ECO:0000269|Ref.10"
MOD_RES 22
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P0DP24"
MOD_RES 45
/note="Phosphothreonine; by CaMK4"
/evidence="ECO:0000269|PubMed:12392717"
MOD_RES 82
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P0DP24"
MOD_RES 95
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P0DP24"
MOD_RES 100
/note="Phosphotyrosine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 102
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
MOD_RES 111
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P0DP24"
MOD_RES 116
/note="N6,N6,N6-trimethyllysine; alternate"
/evidence="ECO:0000269|PubMed:201628"
MOD_RES 116
/note="N6-methyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P0DP24"
MOD_RES 139
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P0DP24"
CROSSLNK 22
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P0DP24"
CROSSLNK 22
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000250|UniProtKB:P62157"
HELIX 7..20
/evidence="ECO:0007829|PDB:6ALE"
STRAND 25..28
/evidence="ECO:0007829|PDB:6ALE"
HELIX 30..39
/evidence="ECO:0007829|PDB:6ALE"
HELIX 46..56
/evidence="ECO:0007829|PDB:6ALE"
STRAND 58..65
/evidence="ECO:0007829|PDB:6ALE"
HELIX 66..74
/evidence="ECO:0007829|PDB:6ALE"
HELIX 83..91
/evidence="ECO:0007829|PDB:6ALE"
STRAND 97..102
/evidence="ECO:0007829|PDB:6ALE"
HELIX 103..110
/evidence="ECO:0007829|PDB:6ALE"
HELIX 119..129
/evidence="ECO:0007829|PDB:6ALE"
STRAND 133..138
/evidence="ECO:0007829|PDB:6ALE"
HELIX 139..147
/evidence="ECO:0007829|PDB:6ALE"
SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK


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

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[33951696] Circular RNA circ_0010729 Knockdown Attenuates Oxygen-Glucose Deprivation-Induced Human Cardiac Myocytes Injury by miR-338-3p/CALM2 Axis.
[33788723] Targeting CALM2 Inhibits Hepatocellular Carcinoma Growth and Metastasis by Suppressing E2F5-mediated Cell Cycle Progression.
[33173240] HLA-J, a Non-Pseudogene as a New Prognostic Marker for Therapy Response and Survival in Breast Cancer.
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[31628181] Protein Kinase C and Calmodulin Serve As Calcium Sensors for Calcium-Stimulated Endocytosis at Synapses.
[31602204] Smoking alters the evolutionary trajectory of non-small cell lung cancer.
[31429119] lncRNA GAS5 regulates myocardial infarction by targeting the miR-525-5p/CALM2 axis.
[30713075] Dynamic Interactions of Plant CNGC Subunits and Calmodulins Drive Oscillatory Ca Channel Activities.
[27881195] The involvement of RUNX2 and SPARC genes in the bacterial chondronecrosis with osteomyelitis in broilers.