Biology:CALM2
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Short description: Protein-coding gene in the species Homo sapiens
![]() Generic protein structure example |
Calmodulin 2 is a protein that in humans is encoded by the CALM2 gene.[1][2]
Clinical significance
Mutations in CALM2 are associated to cardiac arrhythmias.[3]
Interactions
CALM2 has been shown to interact with AKAP9.[4][5]
See also
References
- ↑ "Entrez Gene: CALM2 Calmodulin 2 (phosphorylase kinase, delta)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=805.
- ↑ "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. December 1987. doi:10.1016/S0021-9258(18)49306-4. PMID 2445749.
- ↑ "Novel calmodulin mutations associated with congenital arrhythmia susceptibility". Circ Cardiovasc Genet 7 (4): 466–74. 2014. doi:10.1161/CIRCGENETICS.113.000459. PMID 24917665.
- ↑ "Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex". Mol. Biol. Cell 13 (9): 3235–45. Sep 2002. doi:10.1091/mbc.E02-02-0112. PMID 12221128.
- ↑ "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. May 1993. doi:10.1006/geno.1993.1211. PMID 8314583.
External links
- Human CALM2 genome location and CALM2 gene details page in the UCSC Genome Browser.
Further reading
- "Molecular mechanisms of calmodulin's functional versatility". Biochem. Cell Biol. 76 (2–3): 313–23. 1998. doi:10.1139/bcb-76-2-3-313. PMID 9923700.
- "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. 2001. doi:10.1023/A:1012480829618. PMID 11736632.
- "Phosphorylation of calmodulin. Functional implications". Eur. J. Biochem. 269 (15): 3619–31. 2002. doi:10.1046/j.1432-1033.2002.03038.x. PMID 12153558. https://digital.csic.es/bitstream/10261/79981/1/Phosphorylation%20of%20calmodulin.pdf.
- "Structural organization of the human CaMIII calmodulin gene". Biochim. Biophys. Acta 1087 (2): 180–9. 1990. doi:10.1016/0167-4781(90)90203-e. PMID 2223880.
- "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. 1987. doi:10.1021/bi00384a033. PMID 3111527.
- "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression". Gene 146 (2): 199–207. 1994. doi:10.1016/0378-1119(94)90293-3. PMID 8076819.
- "Cytosolic domain of the human immunodeficiency virus envelope glycoproteins binds to calmodulin and inhibits calmodulin-regulated proteins". J. Biol. Chem. 268 (30): 22895–9. 1993. doi:10.1016/S0021-9258(18)41610-9. PMID 8226798.
- "Identification of a calmodulin-binding and inhibitory peptide domain in the HIV-1 transmembrane glycoprotein". AIDS Res. Hum. Retroviruses 9 (11): 1057–66. 1993. doi:10.1089/aid.1993.9.1057. PMID 8312049.
- "Expression of HIV-1 envelope glycoprotein alters cellular calmodulin". Biochem. Biophys. Res. Commun. 218 (1): 192–7. 1996. doi:10.1006/bbrc.1996.0034. PMID 8573130.
- "Role of calmodulin in HIV-potentiated Fas-mediated apoptosis". Am. J. Pathol. 149 (3): 903–10. 1996. PMID 8780394.
- "Induction of apoptosis by calmodulin-dependent intracellular Ca2+ elevation in CD4+ cells expressing gp 160 of HIV". Virology 224 (1): 18–24. 1996. doi:10.1006/viro.1996.0502. PMID 8862395.
- "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. 1997. doi:10.1073/pnas.94.7.3178. PMID 9096366.
- "Phosphorylation and calmodulin binding of the metabotropic glutamate receptor subtype 5 (mGluR5) are antagonistic in vitro". J. Biol. Chem. 272 (32): 20291–8. 1997. doi:10.1074/jbc.272.32.20291. PMID 9242710.
- "Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin". Nature 388 (6645): 882–7. 1997. doi:10.1038/42264. PMID 9278050.
- "Inhibition of HIV-1, HIV-2 and SIV envelope glycoprotein-mediated cell fusion by calmodulin". Virus Res. 50 (2): 119–27. 1997. doi:10.1016/S0168-1702(97)00060-9. PMID 9282777.
- "Signal peptide fragments of preprolactin and HIV-1 p-gp160 interact with calmodulin". EMBO J. 16 (22): 6636–45. 1997. doi:10.1093/emboj/16.22.6636. PMID 9362478.
- "Apoptosis induction by the binding of the carboxyl terminus of human immunodeficiency virus type 1 gp160 to calmodulin". J. Virol. 72 (8): 6574–80. 1998. doi:10.1128/JVI.72.8.6574-6580.1998. PMID 9658102.
- "Characterization of the human CALM2 calmodulin gene and comparison of the transcriptional activity of CALM1, CALM2 and CALM3". Cell Calcium 23 (5): 323–38. 1998. doi:10.1016/S0143-4160(98)90028-8. PMID 9681195.