Biology:S100A6
Generic protein structure example |
S100 calcium-binding protein A6 (S100A6) is a protein that in humans is encoded by the S100A6 gene.[1]
Function
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]
Interactions
S100A6 has been shown to interact with S100B[2][3] and SUGT1.[4]
Pathology
S100A6 to be reported as possible diagnostic marker of papillary thyroid carcinoma.[5]
References
- ↑ 1.0 1.1 "Entrez Gene: S100A6 S100 calcium binding protein A6". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6277.
- ↑ "S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo". J. Biol. Chem. 275 (45): 35302–10. November 2000. doi:10.1074/jbc.M003943200. PMID 10913138.
- ↑ "Demonstration of heterodimer formation between S100B and S100A6 in the yeast two-hybrid system and human melanoma". Exp. Cell Res. 246 (2): 501–9. February 1999. doi:10.1006/excr.1998.4314. PMID 9925766.
- ↑ "Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and other S100 proteins". J. Biol. Chem. 278 (29): 26923–8. July 2003. doi:10.1074/jbc.M211518200. PMID 12746458.
- ↑ "Proteomic study of thyroid tumors reveals frequent up-regulation of the Ca2+ -binding protein S100A6 in papillary thyroid carcinoma". Thyroid 20 (10): 1067–76. October 2010. doi:10.1089/thy.2009.0400. PMID 20629554.
Further reading
- "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends Biochem. Sci. 21 (4): 134–40. 1996. doi:10.1016/S0968-0004(96)80167-8. PMID 8701470.
- "Specific binding of CAP-50 to calcyclin". FEBS Lett. 305 (3): 217–9. 1992. doi:10.1016/0014-5793(92)80671-3. PMID 1299619.
- "S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart". Biochemistry 31 (42): 10258–64. 1992. doi:10.1021/bi00157a012. PMID 1384693.
- "Calcyclin and calvasculin exist in human platelets". Biochem. Biophys. Res. Commun. 189 (3): 1310–6. 1992. doi:10.1016/0006-291X(92)90216-8. PMID 1482346.
- "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. 1991. doi:10.1111/j.1432-1033.1991.tb15768.x. PMID 1999197.
- "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. 1988. doi:10.1016/S0021-9258(18)69220-8. PMID 2448309.
- "Identification of a cell cycle-dependent gene product as a sialic acid-binding protein". Biochem. Biophys. Res. Commun. 163 (1): 506–12. 1989. doi:10.1016/0006-291X(89)92166-9. PMID 2775283.
- "Structural and functional analysis of a growth-regulated gene, the human calcyclin". J. Biol. Chem. 262 (17): 8325–32. 1987. doi:10.1016/S0021-9258(18)47567-9. PMID 3036810.
- "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. 1986. doi:10.1016/S0021-9258(18)67137-6. PMID 3755724.
- "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. 1995. doi:10.1016/0888-7543(95)80005-7. PMID 7759097.
- "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. 1993. doi:10.1073/pnas.90.14.6547. PMID 8341667. Bibcode: 1993PNAS...90.6547E.
- "p30, a novel protein target of mouse calcyclin (S100A6)". Biochem. J. 320 ( Pt 2) (Pt 2): 585–7. 1996. doi:10.1042/bj3200585. PMID 8973570.
- "Ca2+ and Zn2+ bind to different sites and induce different conformational changes in human calcyclin". Eur. J. Biochem. 253 (1): 57–66. 1998. doi:10.1046/j.1432-1327.1998.2530057.x. PMID 9578461.
- "Demonstration of heterodimer formation between S100B and S100A6 in the yeast two-hybrid system and human melanoma". Exp. Cell Res. 246 (2): 501–9. 1999. doi:10.1006/excr.1998.4314. PMID 9925766.
- "Characterization of the calcyclin (S100A6) binding site of annexin XI-A by site-directed mutagenesis". FEBS Lett. 444 (1): 11–4. 1999. doi:10.1016/S0014-5793(99)00014-9. PMID 10037139.
- "S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo". J. Biol. Chem. 275 (45): 35302–10. 2000. doi:10.1074/jbc.M003943200. PMID 10913138.
- "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. 2002. doi:10.3748/wjg.v8.i2.208. PMID 11925593.
- "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. 2002. doi:10.1016/S0969-2126(02)00740-2. PMID 11937060.
- "CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family". J. Biol. Chem. 277 (32): 28848–52. 2002. doi:10.1074/jbc.M203602200. PMID 12042313.
Original source: https://en.wikipedia.org/wiki/S100A6.
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