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Gene Review

S100A11  -  S100 calcium binding protein A11

Gallus gallus

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Disease relevance of S100A11


High impact information on S100A11


Biological context of S100A11


Anatomical context of S100A11


Associations of S100A11 with chemical compounds

  • Our data suggests that, like S100A1 and S100B, S100A11 might have a role in the regulation of membrane activities, probably in relation to Ca(2+) fluxes in skeletal muscle cells [4].

Other interactions of S100A11

  • Computer aided homology analysis revealed that calgizzarin exhibits a 43.2% homology to S-100 alpha, 38.6% to S-100 beta and 40.0% to annexin II light chain, p10 [3].

Analytical, diagnostic and therapeutic context of S100A11


  1. Molecular cloning and expression of avian smooth muscle S100A11 (calgizzarin, S100C). Schönekess, B.O., Walsh, M.P. Biochem. Cell Biol. (1997) [Pubmed]
  2. Purification, characterization, and partial sequence analysis of a newly identified EF-hand type 13-kDa Ca(2+)-binding protein from smooth muscle and non-muscle tissues. Todoroki, H., Kobayashi, R., Watanabe, M., Minami, H., Hidaka, H. J. Biol. Chem. (1991) [Pubmed]
  3. Molecular cloning and sequencing of a cDNA clone encoding a new calcium binding protein, named calgizzarin, from rabbit lung. Watanabe, M., Ando, Y., Todoroki, H., Minami, H., Hidaka, H. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  4. Subcellular localization of S100A11 (S100C, calgizzarin) in developing and adult avian skeletal muscles. Arcuri, C., Giambanco, I., Bianchi, R., Donato, R. Biochim. Biophys. Acta (2002) [Pubmed]
  5. Characterization of the Ca2+-binding properties of calgizzarin (S100C) isolated from chicken gizzard smooth muscle. Allen, B.G., Durussel, I., Walsh, M.P., Cox, J.A. Biochem. Cell Biol. (1996) [Pubmed]
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