Calmodulin 1

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Protein CALM1 PDB 1a29.png
Available structures
PDBHuman UniProt search: PDBe RCSB
AliasesCALM1, CALML2, CAMI, CPVT4, DD132, PHKD, caM, LQT14, Calmodulin 1, calmodulin 1 (phosphorylase kinase, delta)
External IDsHomoloGene: 134804 GeneCards: CALM1
Gene location (Human)
Chromosome 14 (human)
Chr.Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for CALM1
Genomic location for CALM1
Band14q32.11Start90,396,502 bp[1]
End90,408,261 bp[1]
RefSeq (mRNA)



RefSeq (protein)


Location (UCSC)Chr 14: 90.4 – 90.41 Mbn/a
PubMed search[2]n/a
View/Edit Human

Calmodulin 1 is a protein that in humans is encoded by the CALM1 gene.[3]


Calmodulin 1 is the archetype of the family of calcium-modulated (calmodulin) proteins of which nearly 20 members have been found. They are identified by their occurrence in the cytosol or on membranes facing the cytosol and by a high affinity for calcium. Calmodulin contains 148 amino acids and has 4 calcium-binding EF hand motifs. Its functions include roles in growth and the cell cycle as well as in signal transduction and the synthesis and release of neurotransmitters.[4]


Calmodulin 1 has been shown to interact with:


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000198668 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:". 
  3. ^ Wawrzynczak EJ, Perham RN (August 1984). "Isolation and nucleotide sequence of a cDNA encoding human calmodulin". Biochem. Int. 9 (2): 177–85. PMID 6385987. 
  4. ^ "Entrez Gene: CALM1 calmodulin 1 (phosphorylase kinase, delta)". 
  5. ^ 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 124155Freely accessible. PMID 12221128. 
  6. ^ Cifuentes E, Mataraza JM, Yoshida BA, Menon M, Sacks DB, Barrack ER, Reddy GP (Jan 2004). "Physical and functional interaction of androgen receptor with calmodulin in prostate cancer cells". Proc. Natl. Acad. Sci. U.S.A. 101 (2): 464–9. doi:10.1073/pnas.0307161101. PMC 327170Freely accessible. PMID 14695896. 
  7. ^ Li Z, Sacks DB (Feb 2003). "Elucidation of the interaction of calmodulin with the IQ motifs of IQGAP1". J. Biol. Chem. 278 (6): 4347–52. doi:10.1074/jbc.M208579200. PMID 12446675. 
  8. ^ Briggs MW, Li Z, Sacks DB (Mar 2002). "IQGAP1-mediated stimulation of transcriptional co-activation by beta-catenin is modulated by calmodulin". J. Biol. Chem. 277 (9): 7453–65. doi:10.1074/jbc.M104315200. PMID 11734550. 
  9. ^ Kutuzov MA, Solov'eva OV, Andreeva AV, Bennett N (May 2002). "Protein Ser/Thr phosphatases PPEF interact with calmodulin". Biochem. Biophys. Res. Commun. 293 (3): 1047–52. doi:10.1016/S0006-291X(02)00338-8. PMID 12051765. 
  10. ^ Numazaki M, Tominaga T, Takeuchi K, Murayama N, Toyooka H, Tominaga M (Jun 2003). "Structural determinant of TRPV1 desensitization interacts with calmodulin". Proc. Natl. Acad. Sci. U.S.A. 100 (13): 8002–6. doi:10.1073/pnas.1337252100. PMC 164702Freely accessible. PMID 12808128. 

Further reading[edit]

  • Zhang M, Yuan T (1999). "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 (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. doi:10.1023/A:1012480829618. PMID 11736632. 
  • Benaim G, Villalobo A (2002). "Phosphorylation of calmodulin. Functional implications". Eur. J. Biochem. 269 (15): 3619–31. doi:10.1046/j.1432-1033.2002.03038.x. PMID 12153558. 
  • Trudeau MC, Zagotta WN (2003). "Calcium/calmodulin modulation of olfactory and rod cyclic nucleotide-gated ion channels". J. Biol. Chem. 278 (21): 18705–8. doi:10.1074/jbc.R300001200. PMID 12626507. 

External links[edit]