Calmodulin 1

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Calmodulin 1 (phosphorylase kinase, delta)
Protein CALM1 PDB 1a29.png
PDB rendering based on 1a29.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CALM1 ; CALML2; CAMI; CPVT4; DD132; PHKD; caM
External IDs OMIM114180 MGI88251 HomoloGene134804 ChEMBL: 6093 GeneCards: CALM1 Gene
EC number 2.7.11.19
Orthologs
Species Human Mouse
Entrez 801 640703
Ensembl ENSG00000143933 ENSMUSG00000001175
UniProt P62158 P62204
RefSeq (mRNA) NM_001166106 NM_009790
RefSeq (protein) NP_008819 NP_033920
Location (UCSC) Chr 14:
90.86 – 90.87 Mb
Chr 12:
101.44 – 101.45 Mb
PubMed search [1] [2]

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

Function[edit]

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.[2]

Interactions[edit]

Calmodulin 1 has been shown to interact with:

References[edit]

  1. ^ Wawrzynczak EJ, Perham RN (August 1984). "Isolation and nucleotide sequence of a cDNA encoding human calmodulin". Biochem. Int. 9 (2): 177–85. PMID 6385987. 
  2. ^ "Entrez Gene: CALM1 calmodulin 1 (phosphorylase kinase, delta)". 
  3. ^ 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. 
  4. ^ Cifuentes E, Mataraza JM, Yoshida BA, Menon M, Sacks DB, Barrack ER et al. (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 327170. PMID 14695896. 
  5. ^ 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. 
  6. ^ 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. 
  7. ^ 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. 
  8. ^ 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 164702. 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]