S100A6

From Wikipedia, the free encyclopedia

S100 calcium binding protein A6

PDB rendering based on 1a03.

Available structures: 1a03, 1cnp, 1jwd, 1k8u, 1k96, 1k9k, 1k9p, 2cnp

Identifiers

Symbol(s)

S100A6; 2A9; 5B10; CABP; CACY; PRA

External IDs

OMIM: 114110 MGI: 1339467 HomoloGene: 7925

Gene ontology
Molecular Function:	• calcium ion binding • growth factor activity • zinc ion binding • protein homodimerization activity • S100 beta binding • calcium-dependent protein binding
Cellular Component:	• ruffle • nucleus • nuclear envelope • cytoplasm
Biological Process:	• regulation of progression through cell cycle • cell cycle • signal transduction • cell-cell signaling • axonogenesis • cell proliferation • positive regulation of fibroblast proliferation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_014624 (mRNA)
NP_055439 (protein)

NM_011313 (mRNA)
NP_035443 (protein)

Location

Chr 1: 151.77 - 151.78 Mb

Chr 3: 90.7 - 90.7 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: S100A6 S100 calcium binding protein A6.

[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.
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.