CALM2

CALM2
Identifiers
Aliases	CALM2,CAMII, PHKD, PHKD2, LQT15, caM, calmodulin 2 (phosphorylase kinase, delta), calmodulin 2, CAMC, CAM1, CAMIII, CAM3, CALM, CALML2
External IDs	OMIM:114182;HomoloGene:134804;GeneCards:CALM2;OMA:CALM2 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2p21 Start 47,160,084bp End 47,176,921bp
RNA expressionpattern Bgee Human Mouse(ortholog) Top expressed in middle temporal gyrus Brodmann area 23 orbitofrontal cortex visceral pleura pons lateral nuclear group of thalamus occipital lobe germinal epithelium parietal pleura prefrontal cortex n/a More reference expression data BioGPS n/a
Gene ontology Molecular function calcium ion binding protein binding adenylate cyclase binding adenylate cyclase activator activity calcium channel inhibitor activity protein kinase binding protein domain specific binding titin binding N-terminal myristoylation domain binding protein serine/threonine kinase activator activity transmembrane transporter binding metal ion binding protein phosphatase activator activity disordered domain specific binding nitric-oxide synthase regulator activity type 3 metabotropic glutamate receptor binding phosphatidylinositol 3-kinase binding protein N-terminus binding calcium-dependent protein binding nitric-oxide synthase binding Cellular component spindle pole nucleus cytoplasm centrosome microtubule organizing center spindle cytoskeleton spindle microtubule plasma membrane voltage-gated potassium channel complex sarcomere vesicle protein-containing complex calcium channel complex myelin sheath catalytic complex growth cone synaptic vesicle membrane mitochondrial membranes neuron projection Biological process G2/M transition of mitotic cell cycle regulation of heart rate detection of calcium ion G protein-coupled receptor signaling pathway positive regulation of peptidyl-threonine phosphorylation negative regulation of peptidyl-threonine phosphorylation regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion calcium-mediated signaling substantia nigra development positive regulation of protein autophosphorylation regulation of cytokinesis positive regulation of phosphoprotein phosphatase activity positive regulation of protein dephosphorylation positive regulation of DNA binding positive regulation of cyclic-nucleotide phosphodiesterase activity response to calcium ion regulation of cardiac muscle contraction negative regulation of ryanodine-sensitive calcium-release channel activity positive regulation of ryanodine-sensitive calcium-release channel activity positive regulation of protein serine/threonine kinase activity regulation of cell communication by electrical coupling involved in cardiac conduction response to amphetamine activation of adenylate cyclase activity positive regulation of nitric-oxide synthase activity response to corticosterone regulation of ryanodine-sensitive calcium-release channel activity establishment of protein localization to membrane establishment of protein localization to mitochondrial membrane regulation of synaptic vesicle endocytosis regulation of high voltage-gated calcium channel activity regulation of synaptic vesicle exocytosis Sources:Amigo/QuickGO
Orthologs Species Human Mouse Entrez 805 n/a Ensembl ENSG00000143933 n/a UniProt P0DP31 P0DP24 n/a RefSeq (mRNA) NM_001305624 NM_001305625 NM_001305626 NM_001743 n/a RefSeq (protein) NP_059022 NP_001350598 NP_001350599 NP_008819 NP_001292553 NP_001292554 NP_001292555 NP_001734 NP_001316850 NP_001316851 NP_001316852 NP_001316853 NP_001316854 NP_001316855 NP_005175 n/a Location (UCSC) Chr 2: 47.16 – 47.18 Mb n/a PubMedsearch n/a
Wikidata
View/Edit Human

Calmodulin 2is aproteinthat in humans is encoded by theCALM2gene.A member of thecalmodulinfamily of signaling molecules, it is an intermediary between calcium ions, which act as asecond messenger,and many intracellular processes, such as the contraction ofcardiac muscle.

Clinical significance

Mutations in CALM2 are associated withcardiac arrhythmias.In particular, severalsingle-nucleotide polymorphismsof CALM2 have been reported as potential causes ofsudden infant death syndrome.Due to their heritability, CALM2 mutations can affect multiple children in a family,and the discovery of the deadly consequences of these mutations has led to challenges against the murder convictions of mothers of multiple deceased infants, as in the case ofKathleen Folbigg,acquitted after more than 20 years imprisonment, in Australia.

Interactions

CALM2 has been shown tointeractwithAKAP9.

External links

• HumanCALM2genome location andCALM2gene details page in theUCSC Genome Browser.

Further reading

• Zhang M, Yuan T (1998). "Molecular mechanisms of calmodulin's functional versatility".Biochemistry and Cell Biology.76(2–3): 313–323.doi:10.1139/bcb-76-2-3-313.PMID9923700.
• Gusev NB (October 2001). "Some properties of caldesmon and calponin and the participation of these proteins in regulation of smooth muscle contraction and cytoskeleton formation".Biochemistry. Biokhimiia.66(10): 1112–1121.doi:10.1023/A:1012480829618.PMID11736632.S2CID310781.
• Benaim G, Villalobo A (August 2002)."Phosphorylation of calmodulin. Functional implications".European Journal of Biochemistry.269(15): 3619–3631.doi:10.1046/j.1432-1033.2002.03038.x.hdl:10261/79981.PMID12153558.
• Koller M, Schnyder B, Strehler EE (October 1990). "Structural organization of the human CaMIII calmodulin gene".Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression.1087(2): 180–189.doi:10.1016/0167-4781(90)90203-e.PMID2223880.
• Baudier J, Mochly-Rosen D, Newton A, Lee SH, Koshland DE, Cole RD (May 1987). "Comparison of S100b protein with calmodulin: interactions with melittin and microtubule-associated tau proteins and inhibition of phosphorylation of tau proteins by protein kinase C".Biochemistry.26(10): 2886–2893.doi:10.1021/bi00384a033.PMID3111527.
• Matoba R, Okubo K, Hori N, Fukushima A, Matsubara K (September 1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression".Gene.146(2): 199–207.doi:10.1016/0378-1119(94)90293-3.PMID8076819.
• Srinivas SK, Srinivas RV, Anantharamaiah GM, Compans RW, Segrest JP (October 1993)."Cytosolic domain of the human immunodeficiency virus envelope glycoproteins binds to calmodulin and inhibits calmodulin-regulated proteins".The Journal of Biological Chemistry.268(30): 22895–22899.doi:10.1016/S0021-9258(18)41610-9.PMID8226798.
• Miller MA, Mietzner TA, Cloyd MW, Robey WG, Montelaro RC (November 1993). "Identification of a calmodulin-binding and inhibitory peptide domain in the HIV-1 transmembrane glycoprotein".AIDS Research and Human Retroviruses.9(11): 1057–1066.doi:10.1089/aid.1993.9.1057.PMID8312049.
• Radding W, Pan ZQ, Hunter E, Johnston P, Williams JP, McDonald JM (January 1996). "Expression of HIV-1 envelope glycoprotein alters cellular calmodulin".Biochemical and Biophysical Research Communications.218(1): 192–197.doi:10.1006/bbrc.1996.0034.PMID8573130.
• Pan Z, Radding W, Zhou T, Hunter E, Mountz J, McDonald JM (September 1996)."Role of calmodulin in HIV-potentiated Fas-mediated apoptosis".The American Journal of Pathology.149(3): 903–910.PMC1865159.PMID8780394.
• Sasaki M, Uchiyama J, Ishikawa H, Matsushita S, Kimura G, Nomoto K, Koga Y (October 1996)."Induction of apoptosis by calmodulin-dependent intracellular Ca2+ elevation in CD4+ cells expressing gp 160 of HIV".Virology.224(1): 18–24.doi:10.1006/viro.1996.0502.PMID8862395.
• Brigino E, Haraguchi S, Koutsonikolis A, Cianciolo GJ, Owens U, Good RA, Day NK (April 1997)."Interleukin 10 is induced by recombinant HIV-1 Nef protein involving the calcium/calmodulin-dependent phosphodiesterase signal transduction pathway".Proceedings of the National Academy of Sciences of the United States of America.94(7): 3178–3182.Bibcode:1997PNAS...94.3178B.doi:10.1073/pnas.94.7.3178.PMC20342.PMID9096366.
• Minakami R, Jinnai N, Sugiyama H (August 1997)."Phosphorylation and calmodulin binding of the metabotropic glutamate receptor subtype 5 (mGluR5) are antagonistic in vitro".The Journal of Biological Chemistry.272(32): 20291–20298.doi:10.1074/jbc.272.32.20291.PMID9242710.
• Miyawaki A, Llopis J, Heim R, McCaffery JM, Adams JA, Ikura M, Tsien RY (August 1997)."Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin".Nature.388(6645): 882–887.doi:10.1038/42264.PMID9278050.S2CID13745050.
• Malvoisin E, Wild F (August 1997). "Inhibition of HIV-1, HIV-2 and SIV envelope glycoprotein-mediated cell fusion by calmodulin".Virus Research.50(2): 119–127.doi:10.1016/S0168-1702(97)00060-9.PMID9282777.
• Martoglio B, Graf R, Dobberstein B (November 1997)."Signal peptide fragments of preprolactin and HIV-1 p-gp160 interact with calmodulin".The EMBO Journal.16(22): 6636–6645.doi:10.1093/emboj/16.22.6636.PMC1170268.PMID9362478.
• Ishikawa H, Sasaki M, Noda S, Koga Y (August 1998)."Apoptosis induction by the binding of the carboxyl terminus of human immunodeficiency virus type 1 gp160 to calmodulin".Journal of Virology.72(8): 6574–6580.doi:10.1128/JVI.72.8.6574-6580.1998.PMC109834.PMID9658102.
• Toutenhoofd SL, Foletti D, Wicki R, Rhyner JA, Garcia F, Tolon R, Strehler EE (May 1998). "Characterization of the human CALM2 calmodulin gene and comparison of the transcriptional activity of CALM1, CALM2 and CALM3".Cell Calcium.23(5): 323–338.doi:10.1016/S0143-4160(98)90028-8.PMID9681195.