CALM2

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Calmodulin 2 (phosphorylase kinase, delta)
PDB rendering based on 1a29.
Available structures: 1a29, 1ahr, 1ak8, 1cdl, 1cdm, 1cfc, 1cfd, 1cff, 1ckk, 1cll, 1cm1, 1cm4, 1cmf, 1cmg, 1ctr, 1deg, 1dmo, 1f70, 1f71, 1fw4, 1g4y, 1iq5, 1iwq, 1j7o, 1j7p, 1k90, 1k93, 1l7z, 1lin, 1lvc, 1mux, 1mxe, 1niw, 1nwd, 1ooj, 1pk0, 1prw, 1qiv, 1qiw, 1qs7, 1qtx, 1qx5, 1qx7, 1s26, 1sk6, 1sw8, 1sy9, 1up5, 1vrk, 1wrz, 1x02, 1xa5, 1xfu, 1xfv, 1xfw, 1xfx, 1xfy, 1xfz, 1y0v, 1y6w, 1yr5, 1yrt, 1yru, 1zot, 1zuz, 2bbm, 2bbn, 2bcx, 2be6, 2bkh, 2bki, 2col, 2dfs, 2f2o, 2f2p, 2f3y, 2f3z, 2fot, 2hf5, 2ix7, 3cln, 4cln
Identifiers
Symbol(s) CALM2; PHKD; CAMII; PHKD2
External IDs OMIM: 114182 MGI: 103250 HomoloGene: 36226
Orthologs
Human Mouse
Entrez 805 12314


Refseq NM_001743 (mRNA)
NP_001734 (protein)		 NM_007589 (mRNA)
NP_031615 (protein)
Pubmed search [1] [2]

Calmodulin 2 (phosphorylase kinase, delta), also known as CALM2, is a human gene.[1]


[edit] References

  1. ^ Entrez Gene: CALM2 Calmodulin 2 (phosphorylase kinase, delta).

[edit] Further reading

  • Zhang M, Yuan T (1999). "Molecular mechanisms of calmodulin's functional versatility.". Biochem. Cell Biol. 76 (2-3): 313–23. PMID 9923700. 
  • Gusev NB (2002). "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. PMID 11736632. 
  • Benaim G, Villalobo A (2002). "Phosphorylation of calmodulin. Functional implications.". Eur. J. Biochem. 269 (15): 3619–31. PMID 12153558. 
  • Koller M, Schnyder B, Strehler EE (1990). "Structural organization of the human CaMIII calmodulin gene.". Biochim. Biophys. Acta 1087 (2): 180–9. PMID 2223880. 
  • SenGupta B, Friedberg F, Detera-Wadleigh SD (1988). "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. 
  • Baudier J, Mochly-Rosen D, Newton A, et al. (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. PMID 3111527. 
  • Matoba R, Okubo K, Hori N, et al. (1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression.". Gene 146 (2): 199–207. PMID 8076819. 
  • Srinivas SK, Srinivas RV, Anantharamaiah GM, et al. (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, et al. (1994). "Identification of a calmodulin-binding and inhibitory peptide domain in the HIV-1 transmembrane glycoprotein.". AIDS Res. Hum. Retroviruses 9 (11): 1057–66. PMID 8312049. 
  • Berchtold MW, Egli R, Rhyner JA, et al. (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. 
  • Radding W, Pan ZQ, Hunter E, et al. (1996). "Expression of HIV-1 envelope glycoprotein alters cellular calmodulin.". Biochem. Biophys. Res. Commun. 218 (1): 192–7. PMID 8573130. 
  • Pan Z, Radding W, Zhou T, et al. (1996). "Role of calmodulin in HIV-potentiated Fas-mediated apoptosis.". Am. J. Pathol. 149 (3): 903–10. PMID 8780394. 
  • Sasaki M, Uchiyama J, Ishikawa H, et al. (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, et al. (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. 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. PMID 9242710. 
  • Miyawaki A, Llopis J, Heim R, et al. (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. PMID 9282777. 
  • Martoglio B, Graf R, Dobberstein B (1998). "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. 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. PMID 9658102. 
  • Toutenhoofd SL, Foletti D, Wicki R, et al. (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. PMID 9681195. 
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