S100A6

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S100 calcium binding protein A6
File:PBB Protein S100A6 image.jpg
PDB rendering based on 1a03.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols S100A6 ; 2A9; 5B10; CABP; CACY; PRA
External IDs Template:OMIM5 Template:MGI HomoloGene7925
RNA expression pattern
File:PBB GE S100A6 217728 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

S100 calcium binding protein A6, also known as S100A6, is a human gene.[1]

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 function in stimulation of Ca2+-dependent insulin release, stimulation of prolactin secretion, and exocytosis. Chromosomal rearrangements and altered expression of this gene have been implicated in melanoma.[1]

References

  1. 1.0 1.1 "Entrez Gene: S100A6 S100 calcium binding protein A6".

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.
  • Minami H, Tokumitsu H, Mizutani A; et al. (1993). "Specific binding of CAP-50 to calcyclin". FEBS Lett. 305 (3): 217–9. PMID 1299619.
  • Engelkamp D, Schäfer BW, Erne P, Heizmann CW (1992). "S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart". Biochemistry. 31 (42): 10258–64. PMID 1384693.
  • Tomida Y, Terasawa M, Kobayashi R, Hidaka H (1993). "Calcyclin and calvasculin exist in human platelets". Biochem. Biophys. Res. Commun. 189 (3): 1310–6. PMID 1482346.
  • Filipek A, Gerke V, Weber K, Kuźnicki J (1991). "Characterization of the cell-cycle-regulated protein calcyclin from Ehrlich ascites tumor cells. Identification of two binding proteins obtained by Ca2(+)-dependent affinity chromatography". Eur. J. Biochem. 195 (3): 795–800. PMID 1999197.
  • Murphy LC, Murphy LJ, Tsuyuki D; et al. (1988). "Cloning and characterization of a cDNA encoding a highly conserved, putative calcium binding protein, identified by an anti-prolactin receptor antiserum". J. Biol. Chem. 263 (5): 2397–401. PMID 2448309.
  • Gabius HJ, Bardosi A, Gabius S; et al. (1989). "Identification of a cell cycle-dependent gene product as a sialic acid-binding protein". Biochem. Biophys. Res. Commun. 163 (1): 506–12. PMID 2775283.
  • Ferrari S, Calabretta B, deRiel JK; et al. (1987). "Structural and functional analysis of a growth-regulated gene, the human calcyclin". J. Biol. Chem. 262 (17): 8325–32. PMID 3036810.
  • Calabretta B, Battini R, Kaczmarek L; et al. (1986). "Molecular cloning of the cDNA for a growth factor-inducible gene with strong homology to S-100, a calcium-binding protein". J. Biol. Chem. 261 (27): 12628–32. PMID 3755724.
  • 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.
  • Filipek A, Wojda U (1997). "p30, a novel protein target of mouse calcyclin (S100A6)". Biochem. J. 320 ( Pt 2): 585–7. PMID 8973570.
  • Kordowska J, Stafford WF, Wang CL (1998). "Ca2+ and Zn2+ bind to different sites and induce different conformational changes in human calcyclin". Eur. J. Biochem. 253 (1): 57–66. PMID 9578461.
  • Yang Q, O'Hanlon D, Heizmann CW, Marks A (1999). "Demonstration of heterodimer formation between S100B and S100A6 in the yeast two-hybrid system and human melanoma". Exp. Cell Res. 246 (2): 501–9. doi:10.1006/excr.1998.4314. PMID 9925766.
  • Sudo T, Hidaka H (1999). "Characterization of the calcyclin (S100A6) binding site of annexin XI-A by site-directed mutagenesis". FEBS Lett. 444 (1): 11–4. PMID 10037139.
  • Deloulme JC, Assard N, Mbele GO; et al. (2001). "S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo". J. Biol. Chem. 275 (45): 35302–10. doi:10.1074/jbc.M003943200. PMID 10913138.
  • Li Y, Yang L, Cui JT; et al. (2002). "Construction of cDNA representational difference analysis based on two cDNA libraries and identification of garlic inducible expression genes in human gastric cancer cells". World J. Gastroenterol. 8 (2): 208–12. PMID 11925593.
  • Otterbein LR, Kordowska J, Witte-Hoffmann C; et al. (2002). "Crystal structures of S100A6 in the Ca(2+)-free and Ca(2+)-bound states: the calcium sensor mechanism of S100 proteins revealed at atomic resolution". Structure. 10 (4): 557–67. PMID 11937060.
  • Filipek A, Jastrzebska B, Nowotny M, Kuznicki J (2002). "CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family". J. Biol. Chem. 277 (32): 28848–52. doi:10.1074/jbc.M203602200. PMID 12042313.

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