S100A2

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S100 calcium binding protein A2
Identifiers
Symbol(s) S100A2; CAN19; MGC111539; S100L
External IDs OMIM: 176993 HomoloGene48389
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 6273 n/a
Ensembl ENSG00000196754 n/a
Uniprot P29034 n/a
Refseq NM_005978 (mRNA)
NP_005969 (protein)
n/a (mRNA)
n/a (protein)
Location Chr 1: 151.8 - 151.81 Mb n/a
Pubmed search [1] n/a

S100 calcium binding protein A2, also known as S100A2, is a human gene.

The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may have a tumor suppressor function. Chromosomal rearrangements and altered expression of this gene have been implicated in breast cancer.[1]

[edit] References

[edit] Further reading

  • Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology.". Trends Biochem. Sci. 21 (4): 134–40. PMID 8701470. 
  • Rasmussen HH, van Damme J, Puype M, et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.". Electrophoresis 13 (12): 960–9. PMID 1286667. 
  • Lee SW, Tomasetto C, Swisshelm K, et al. (1992). "Down-regulation of a member of the S100 gene family in mammary carcinoma cells and reexpression by azadeoxycytidine treatment.". Proc. Natl. Acad. Sci. U.S.A. 89 (6): 2504–8. PMID 1372446. 
  • Schäfer BW, Wicki R, Engelkamp D, et al. (1995). "Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family.". Genomics 25 (3): 638–43. PMID 7759097. 
  • Engelkamp D, Schäfer BW, Mattei MG, et al. (1993). "Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E.". Proc. Natl. Acad. Sci. U.S.A. 90 (14): 6547–51. PMID 8341667. 
  • Gimona M, Lando Z, Dolginov Y, et al. (1997). "Ca2+-dependent interaction of S100A2 with muscle and nonmuscle tropomyosins.". J. Cell. Sci. 110 ( Pt 5): 611–21. PMID 9092943. 
  • Böni R, Burg G, Doguoglu A, et al. (1997). "Immunohistochemical localization of the Ca2+ binding S100 proteins in normal human skin and melanocytic lesions.". Br. J. Dermatol. 137 (1): 39–43. PMID 9274623. 
  • Groves P, Finn BE, Kuźnicki J, Forsén S (1998). "A model for target protein binding to calcium-activated S100 dimers.". FEBS Lett. 421 (3): 175–9. PMID 9468301. 
  • Wicki R, Franz C, Scholl FA, et al. (1998). "Repression of the candidate tumor suppressor gene S100A2 in breast cancer is mediated by site-specific hypermethylation.". Cell Calcium 22 (4): 243–54. PMID 9481475. 
  • Franz C, Durussel I, Cox JA, et al. (1998). "Binding of Ca2+ and Zn2+ to human nuclear S100A2 and mutant proteins.". J. Biol. Chem. 273 (30): 18826–34. PMID 9668057. 
  • Mueller A, Bächi T, Höchli M, et al. (1999). "Subcellular distribution of S100 proteins in tumor cells and their relocation in response to calcium activation.". Histochem. Cell Biol. 111 (6): 453–9. PMID 10429967. 
  • Stradal TB, Troxler H, Heizmann CW, Gimona M (2000). "Mapping the zinc ligands of S100A2 by site-directed mutagenesis.". J. Biol. Chem. 275 (18): 13219–27. PMID 10788426. 
  • Hoyaux D, Decaestecker C, Heizmann CW, et al. (2000). "S100 proteins in Corpora amylacea from normal human brain.". Brain Res. 867 (1-2): 280–8. PMID 10837826. 
  • Deshpande R, Woods TL, Fu J, et al. (2000). "Biochemical characterization of S100A2 in human keratinocytes: subcellular localization, dimerization, and oxidative cross-linking.". J. Invest. Dermatol. 115 (3): 477–85. doi:10.1046/j.1523-1747.2000.00078.x. PMID 10951287. 
  • Nagy N, Hoyaux D, Gielen I, et al. (2002). "The Ca2+-binding S100A2 protein is differentially expressed in epithelial tissue of glandular or squamous origin.". Histol. Histopathol. 17 (1): 123–30. PMID 11813862. 
  • Kyriazanos ID, Tachibana M, Dhar DK, et al. (2002). "Expression and prognostic significance of S100A2 protein in squamous cell carcinoma of the esophagus.". Oncol. Rep. 9 (3): 503–10. PMID 11956617. 
  • Zhang T, Woods TL, Elder JT (2003). "Differential responses of S100A2 to oxidative stress and increased intracellular calcium in normal, immortalized, and malignant human keratinocytes.". J. Invest. Dermatol. 119 (5): 1196–201. doi:10.1046/j.1523-1747.2002.19520.x. PMID 12445212. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Hibi K, Fujitake S, Takase T, et al. (2004). "Identification of S100A2 as a target of the DeltaNp63 oncogenic pathway.". Clin. Cancer Res. 9 (11): 4282–5. PMID 14519656.