CALM2

CALM2
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	2VAY, 1Y6W, 4JPZ, 3UCY, 1WRZ, 4G28, 1ZOT, 1YRT, 1IQ5, 1CDL, 2LL6, 3HR4, 4BW7, 4BW8, 1YR5, 4J9Y, 4LZX, 1L7Z, 1ZUZ, 2BE6, 2V01, 1XFV, 2M55, 1CTR, 2I08, 2MG5, 2R28, 3O77, 4UPU, 2L7L, 2K0F, 2M0K, 4V0C, 1SW8, 2WEL, 3DVK, 2M0J, 3DVM, 2KUH, 1K90, 1K93, 4G27, 1CLL, 2KUG, 1XFX, 4DJC, 2LQC, 2LQP, 4L79, 2W73, 2LV6, 1NKF, 2JZI, 3UCT, 4GOW, 1J7O, 1PK0, 4Q5U, 2V02, 3BYA, 4Q57, 2KNE, 1YRU, 2Y4V, 2L53, 2F3Y, 3O78, 1LVC, 4M1L, 2K0E, 1S26, 4DCK, 1XFW, 3SUI, 2X0G, 3EWV, 1XFY, 2LL7, 4OVN, 3J41, 2BKI, 1SK6, 3DVJ, 3UCW, 2LGF, 4UMO, 3DVE, 4JQ0, 3OXQ, 2K61, 1XFU, 3SJQ, 2K0J, 4BYF, 1J7P, 3G43, 3EWT, 4J9Z, 1XFZ, 2F3Z, 1IWQ, 2N6A, 2HF5, 2N27, 4ZLK, 5COC
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
Gene location (Human)
Chr.	Chromosome 19 (human)[1]
End	47,176,921 bp[1]
Gene ontology
Molecular function	• calcium ion binding; • GO:0001948 protein binding; • calcium channel inhibitor activity; • protein kinase binding; • titin binding; • protein serine/threonine kinase activator activity; • ion channel binding; • metal ion binding; • protein phosphatase activator activity; • adenylate cyclase binding; • disordered domain specific binding; • Ras guanyl-nucleotide exchange factor activity; • inositol-1,4,5-trisphosphate 3-kinase activity; • ligand-gated ion channel activity; • adenylate cyclase activator activity; • protein domain specific binding; • nitric-oxide synthase regulator activity; • type 3 metabotropic glutamate receptor binding; • N-terminal myristoylation domain binding; • phosphatidylinositol 3-kinase binding; • protein N-terminus binding; • calcium-dependent protein binding; • nitric-oxide synthase binding;
Cellular component	• cytoplasm; • cytosol; • calcium channel complex; • extracellular region; • spindle microtubule; • neuron projection; • cytoskeleton; • cell nucleus; • centrosome; • voltage-gated potassium channel complex; • extracellular exosome; • spindle pole; • growth cone; • cell membrane; • spindle; • sarcomere; • nucleoplasm; • vesicle; • postsynaptic density; • catalytic complex; • microtubule organizing center; • synaptic vesicle membrane; • mitochondrial membranes; • macromolecular complex; • myelin;
Biological process	• muscle contraction; • response to amphetamine; • positive regulation of protein serine/threonine kinase activity; • detection of calcium ion; • Fc-epsilon receptor signaling pathway; • positive regulation of phosphoprotein phosphatase activity; • G2/M transition of mitotic cell cycle; • regulation of high voltage-gated calcium channel activity; • positive regulation of DNA binding; • substantia nigra development; • positive regulation of protein dephosphorylation; • inositol phosphate metabolic process; • positive regulation of nitric-oxide synthase activity; • glycogen catabolic process; • positive regulation of cyclic-nucleotide phosphodiesterase activity; • G-protein coupled receptor signaling pathway; • regulation of cytokinesis; • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; • regulation of rhodopsin mediated signaling pathway; • response to corticosterone; • negative regulation of peptidyl-threonine phosphorylation; • activation of adenylate cyclase activity; • regulation of heart rate; • positive regulation of ryanodine-sensitive calcium-release channel activity; • response to calcium ion; • regulation of ryanodine-sensitive calcium-release channel activity; • regulation of nitric-oxide synthase activity; • platelet degranulation; • negative regulation of ryanodine-sensitive calcium-release channel activity; • MAPK cascade; • positive regulation of peptidyl-threonine phosphorylation; • positive regulation of protein autophosphorylation; • regulation of cardiac muscle contraction; • regulation of cell communication by electrical coupling involved in cardiac conduction; • regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; • calcium-mediated signaling; • ion transmembrane transport; • Wnt signaling pathway, calcium modulating pathway; • positive regulation of GTPase activity; • protein methylation; • establishment of protein localization to membrane; • establishment of protein localization to mitochondrial membrane; • regulation of synaptic vesicle endocytosis; • regulation of synaptic vesicle exocytosis;
	Sources:Amigo / QuickGO
Orthologs
	805
	n/a
	ENSG00000143933
	n/a
	P0DP23; P0DP25
	n/a
	NM_001305624; NM_001305625; NM_001305626; NM_001743
	n/a
NP_001292553; NP_001292554; NP_001292555; NP_001734; NP_001316850;
	NP_001316851; NP_001316852; NP_001316853; NP_001316854; NP_001316855; NP_005175; NP_008819; NP_001350598; NP_001350599; NP_008819
	n/a
	Wikidata
View/Edit Human

Calmodulin 2 is a protein that in humans is encoded by the CALM2 gene.[3][4]

Clinical significance

Mutations in CALM2 are associated to cardiac arrhythmias.[5]

Interactions

CALM2 has been shown to interact with AKAP9.[6][7]

References

GRCh38: Ensembl release 89: ENSG00000143933 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: CALM2 Calmodulin 2 (phosphorylase kinase, delta)".
SenGupta B, Friedberg F, Detera-Wadleigh SD (December 1987). "Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species". J. Biol. Chem. 262 (34): 16663–70. PMID 2445749.
Makita N, Yagihara N, Crotti L, Johnson CN, Beckmann BM, Roh MS, Shigemizu D, Lichtner P, Ishikawa T, Aiba T, Homfray T, Behr ER, Klug D, Denjoy I, Mastantuono E, Theisen D, Tsunoda T, Satake W, Toda T, Nakagawa H, Tsuji Y, Tsuchiya T, Yamamoto H, Miyamoto Y, Endo N, Kimura A, Ozaki K, Motomura H, Suda K, Tanaka T, Schwartz PJ, Meitinger T, Kääb S, Guicheney P, Shimizu W, Bhuiyan ZA, Watanabe H, Chazin WJ, George AL (2014). "Novel calmodulin mutations associated with congenital arrhythmia susceptibility". Circ Cardiovasc Genet. 7 (4): 466–74. doi:10.1161/CIRCGENETICS.113.000459. PMC 4140998. PMID 24917665.
Takahashi M, Yamagiwa A, Nishimura T, Mukai H, Ono Y (Sep 2002). "Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex". Mol. Biol. Cell. 13 (9): 3235–45. doi:10.1091/mbc.E02-02-0112. PMC 124155. PMID 12221128.
Berchtold MW, Egli R, Rhyner JA, Hameister H, Strehler EE (May 1993). "Localization of the human bona fide calmodulin genes CALM1, CALM2, and CALM3 to chromosomes 14q24-q31, 2p21.1-p21.3, and 19q13.2-q13.3". Genomics. 16 (2): 461–5. doi:10.1006/geno.1993.1211. PMID 8314583.

External links

Human CALM2 genome location and CALM2 gene details page in the UCSC Genome Browser.

Zhang M, Yuan T (1998). "Molecular mechanisms of calmodulin's functional versatility". Biochem. Cell Biol. 76 (2–3): 313–23. doi:10.1139/bcb-76-2-3-313. PMID 9923700.
Gusev NB (2001). "Some properties of caldesmon and calponin and the participation of these proteins in regulation of smooth muscle contraction and cytoskeleton formation". Biochemistry Mosc. 66 (10): 1112–21. doi:10.1023/A:1012480829618. PMID 11736632.
Benaim G, Villalobo A (2002). "Phosphorylation of calmodulin. Functional implications" (PDF). Eur. J. Biochem. 269 (15): 3619–31. doi:10.1046/j.1432-1033.2002.03038.x. PMID 12153558.
Koller M, Schnyder B, Strehler EE (1990). "Structural organization of the human CaMIII calmodulin gene". Biochim. Biophys. Acta. 1087 (2): 180–9. doi:10.1016/0167-4781(90)90203-e. PMID 2223880.
Baudier J, Mochly-Rosen D, Newton A, Lee SH, Koshland DE, Cole RD (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): 2886–93. doi:10.1021/bi00384a033. PMID 3111527.
Matoba R, Okubo K, Hori N, Fukushima A, Matsubara K (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. PMID 8076819.
Srinivas SK, Srinivas RV, Anantharamaiah GM, Compans RW, Segrest JP (1993). "Cytosolic domain of the human immunodeficiency virus envelope glycoproteins binds to calmodulin and inhibits calmodulin-regulated proteins". J. Biol. Chem. 268 (30): 22895–9. PMID 8226798.
Miller MA, Mietzner TA, Cloyd MW, Robey WG, Montelaro RC (1993). "Identification of a calmodulin-binding and inhibitory peptide domain in the HIV-1 transmembrane glycoprotein". AIDS Res. Hum. Retroviruses. 9 (11): 1057–66. doi:10.1089/aid.1993.9.1057. PMID 8312049.
Radding W, Pan ZQ, Hunter E, Johnston P, Williams JP, McDonald JM (1996). "Expression of HIV-1 envelope glycoprotein alters cellular calmodulin". Biochem. Biophys. Res. Commun. 218 (1): 192–7. doi:10.1006/bbrc.1996.0034. PMID 8573130.
Pan Z, Radding W, Zhou T, Hunter E, Mountz J, McDonald JM (1996). "Role of calmodulin in HIV-potentiated Fas-mediated apoptosis". Am. J. Pathol. 149 (3): 903–10. PMC 1865159. PMID 8780394.
Sasaki M, Uchiyama J, Ishikawa H, Matsushita S, Kimura G, Nomoto K, Koga Y (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. PMID 8862395.
Brigino E, Haraguchi S, Koutsonikolis A, Cianciolo GJ, Owens U, Good RA, Day NK (1997). "Interleukin 10 is induced by recombinant HIV-1 Nef protein involving the calcium/calmodulin-dependent phosphodiesterase signal transduction pathway". Proc. Natl. Acad. Sci. U.S.A. 94 (7): 3178–82. doi:10.1073/pnas.94.7.3178. PMC 20342. PMID 9096366.
Minakami R, Jinnai N, Sugiyama H (1997). "Phosphorylation and calmodulin binding of the metabotropic glutamate receptor subtype 5 (mGluR5) are antagonistic in vitro". J. Biol. Chem. 272 (32): 20291–8. doi:10.1074/jbc.272.32.20291. PMID 9242710.
Miyawaki A, Llopis J, Heim R, McCaffery JM, Adams JA, Ikura M, Tsien RY (1997). "Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin". Nature. 388 (6645): 882–7. doi:10.1038/42264. PMID 9278050.
Malvoisin E, Wild F (1997). "Inhibition of HIV-1, HIV-2 and SIV envelope glycoprotein-mediated cell fusion by calmodulin". Virus Res. 50 (2): 119–27. doi:10.1016/S0168-1702(97)00060-9. PMID 9282777.
Martoglio B, Graf R, Dobberstein B (1997). "Signal peptide fragments of preprolactin and HIV-1 p-gp160 interact with calmodulin". EMBO J. 16 (22): 6636–45. doi:10.1093/emboj/16.22.6636. PMC 1170268. PMID 9362478.
Ishikawa H, Sasaki M, Noda S, Koga Y (1998). "Apoptosis induction by the binding of the carboxyl terminus of human immunodeficiency virus type 1 gp160 to calmodulin". J. Virol. 72 (8): 6574–80. PMC 109834. PMID 9658102.
Toutenhoofd SL, Foletti D, Wicki R, Rhyner JA, Garcia F, Tolon R, Strehler EE (1998). "Characterization of the human CALM2 calmodulin gene and comparison of the transcriptional activity of CALM1, CALM2 and CALM3". Cell Calcium. 23 (5): 323–38. doi:10.1016/S0143-4160(98)90028-8. PMID 9681195.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000143933 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Entrez Gene: CALM2 Calmodulin 2 (phosphorylase kinase, delta)".

[pmid2445749-4] SenGupta B, Friedberg F, Detera-Wadleigh SD (December 1987). "Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species". J. Biol. Chem. 262 (34): 16663–70. PMID 2445749.

[5] Makita N, Yagihara N, Crotti L, Johnson CN, Beckmann BM, Roh MS, Shigemizu D, Lichtner P, Ishikawa T, Aiba T, Homfray T, Behr ER, Klug D, Denjoy I, Mastantuono E, Theisen D, Tsunoda T, Satake W, Toda T, Nakagawa H, Tsuji Y, Tsuchiya T, Yamamoto H, Miyamoto Y, Endo N, Kimura A, Ozaki K, Motomura H, Suda K, Tanaka T, Schwartz PJ, Meitinger T, Kääb S, Guicheney P, Shimizu W, Bhuiyan ZA, Watanabe H, Chazin WJ, George AL (2014). "Novel calmodulin mutations associated with congenital arrhythmia susceptibility". Circ Cardiovasc Genet. 7 (4): 466–74. doi:10.1161/CIRCGENETICS.113.000459. PMC 4140998. PMID 24917665.

[pmid12221128-6] Takahashi M, Yamagiwa A, Nishimura T, Mukai H, Ono Y (Sep 2002). "Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex". Mol. Biol. Cell. 13 (9): 3235–45. doi:10.1091/mbc.E02-02-0112. PMC 124155. PMID 12221128.

[pmid8314583-7] Berchtold MW, Egli R, Rhyner JA, Hameister H, Strehler EE (May 1993). "Localization of the human bona fide calmodulin genes CALM1, CALM2, and CALM3 to chromosomes 14q24-q31, 2p21.1-p21.3, and 19q13.2-q13.3". Genomics. 16 (2): 461–5. doi:10.1006/geno.1993.1211. PMID 8314583.

CALM2

Clinical significance

Interactions

See also

References

External links

Further reading