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.[5]
^Deloulme JC, Assard N, Mbele GO, Mangin C, Kuwano R, Baudier J (November 2000). "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. PMID10913138.35302-10&rft.date=2000-11&rft_id=info:doi/10.1074/jbc.M003943200&rft_id=info:pmid/10913138&rft.aulast=Deloulme&rft.aufirst=JC&rft.au=Assard, N&rft.au=Mbele, GO&rft.au=Mangin, C&rft.au=Kuwano, R&rft.au=Baudier, J&rft_id=https://doi.org/10.1074%2Fjbc.M003943200&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">
^Yang Q, O'Hanlon D, Heizmann CW, Marks A (February 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. PMID9925766.501-9&rft.date=1999-02&rft_id=info:doi/10.1006/excr.1998.4314&rft_id=info:pmid/9925766&rft.aulast=Yang&rft.aufirst=Q&rft.au=O'Hanlon, D&rft.au=Heizmann, CW&rft.au=Marks, A&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">
^Nowotny M, Spiechowicz M, Jastrzebska B, Filipek A, Kitagawa K, Kuznicki J (July 2003). "Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and other S100 proteins". J. Biol. Chem. 278 (29): 26923–8. doi:10.1074/jbc.M211518200. PMID12746458.26923-8&rft.date=2003-07&rft_id=info:doi/10.1074/jbc.M211518200&rft_id=info:pmid/12746458&rft.aulast=Nowotny&rft.aufirst=M&rft.au=Spiechowicz, M&rft.au=Jastrzebska, B&rft.au=Filipek, A&rft.au=Kitagawa, K&rft.au=Kuznicki, J&rft_id=https://doi.org/10.1074%2Fjbc.M211518200&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">
^Sofiadis A, Dinets A, Orre LM, Branca RM, Juhlin CC, Foukakis T, Wallin G, Höög A, Hulchiy M, Zedenius J, Larsson C, Lehtiö J (October 2010). "Proteomic study of thyroid tumors reveals frequent up-regulation of the Ca2 -binding protein S100A6 in papillary thyroid carcinoma". Thyroid. 20 (10): 1067–76. doi:10.1089/thy.2009.0400. PMID20629554.1067-76&rft.date=2010-10&rft_id=info:doi/10.1089/thy.2009.0400&rft_id=info:pmid/20629554&rft.aulast=Sofiadis&rft.aufirst=A&rft.au=Dinets, A&rft.au=Orre, LM&rft.au=Branca, RM&rft.au=Juhlin, CC&rft.au=Foukakis, T&rft.au=Wallin, G&rft.au=Höög, A&rft.au=Hulchiy, M&rft.au=Zedenius, J&rft.au=Larsson, C&rft.au=Lehtiö, J&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">
Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends Biochem. Sci. 21 (4): 134–40. doi:10.1016/S0968-0004(96)80167-8. PMID8701470.134-40&rft.date=1996&rft_id=info:doi/10.1016/S0968-0004(96)80167-8&rft_id=info:pmid/8701470&rft.aulast=Schäfer&rft.aufirst=BW&rft.au=Heizmann, CW&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">
Minami H, Tokumitsu H, Mizutani A, Watanabe Y, Watanabe M, Hidaka H (1992). "Specific binding of CAP-50 to calcyclin". FEBS Lett. 305 (3): 217–9. doi:10.1016/0014-5793(92)80671-3. PMID1299619.217-9&rft.date=1992&rft_id=info:doi/10.1016/0014-5793(92)80671-3&rft_id=info:pmid/1299619&rft.aulast=Minami&rft.aufirst=H&rft.au=Tokumitsu, H&rft.au=Mizutani, A&rft.au=Watanabe, Y&rft.au=Watanabe, M&rft.au=Hidaka, H&rft_id=https://doi.org/10.1016%2F0014-5793%2892%2980671-3&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">
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. doi:10.1021/bi00157a012. PMID1384693.10258-64&rft.date=1992&rft_id=info:doi/10.1021/bi00157a012&rft_id=info:pmid/1384693&rft.aulast=Engelkamp&rft.aufirst=D&rft.au=Schäfer, BW&rft.au=Erne, P&rft.au=Heizmann, CW&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">
Tomida Y, Terasawa M, Kobayashi R, Hidaka H (1992). "Calcyclin and calvasculin exist in human platelets". Biochem. Biophys. Res. Commun. 189 (3): 1310–6. doi:10.1016/0006-291X(92)90216-8. PMID1482346.1310-6&rft.date=1992&rft_id=info:doi/10.1016/0006-291X(92)90216-8&rft_id=info:pmid/1482346&rft.aulast=Tomida&rft.aufirst=Y&rft.au=Terasawa, M&rft.au=Kobayashi, R&rft.au=Hidaka, H&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">
Gabius HJ, Bardosi A, Gabius S, Hellmann KP, Karas M, Kratzin H (1989). "Identification of a cell cycle-dependent gene product as a sialic acid-binding protein". Biochem. Biophys. Res. Commun. 163 (1): 506–12. doi:10.1016/0006-291X(89)92166-9. PMID2775283.506-12&rft.date=1989&rft_id=info:doi/10.1016/0006-291X(89)92166-9&rft_id=info:pmid/2775283&rft.aulast=Gabius&rft.aufirst=HJ&rft.au=Bardosi, A&rft.au=Gabius, S&rft.au=Hellmann, KP&rft.au=Karas, M&rft.au=Kratzin, H&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">
Ferrari S, Calabretta B, deRiel JK, Battini R, Ghezzo F, Lauret E, Griffin C, Emanuel BS, Gurrieri F, Baserga R (1987). "Structural and functional analysis of a growth-regulated gene, the human calcyclin". J. Biol. Chem. 262 (17): 8325–32. doi:10.1016/S0021-9258(18)47567-9. hdl:11380/811306. PMID3036810.8325-32&rft.date=1987&rft_id=info:hdl/11380/811306&rft_id=info:pmid/3036810&rft_id=info:doi/10.1016/S0021-9258(18)47567-9&rft.aulast=Ferrari&rft.aufirst=S&rft.au=Calabretta, B&rft.au=deRiel, JK&rft.au=Battini, R&rft.au=Ghezzo, F&rft.au=Lauret, E&rft.au=Griffin, C&rft.au=Emanuel, BS&rft.au=Gurrieri, F&rft.au=Baserga, R&rft_id=https://doi.org/10.1016%2FS0021-9258%2818%2947567-9&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">
Schäfer BW, Wicki R, Engelkamp D, Mattei MG, Heizmann CW (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. doi:10.1016/0888-7543(95)80005-7. PMID7759097.638-43&rft.date=1995&rft_id=info:doi/10.1016/0888-7543(95)80005-7&rft_id=info:pmid/7759097&rft.aulast=Schäfer&rft.aufirst=BW&rft.au=Wicki, R&rft.au=Engelkamp, D&rft.au=Mattei, MG&rft.au=Heizmann, CW&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">
Filipek A, Wojda U (1996). "p30, a novel protein target of mouse calcyclin (S100A6)". Biochem. J. 320 ( Pt 2) (Pt 2): 585–7. doi:10.1042/bj3200585. PMC1217969. PMID8973570.585-7&rft.date=1996&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1217969#id-name=PMC&rft_id=info:pmid/8973570&rft_id=info:doi/10.1042/bj3200585&rft.aulast=Filipek&rft.aufirst=A&rft.au=Wojda, U&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1217969&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">
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. doi:10.1046/j.1432-1327.1998.2530057.x. PMID9578461.57-66&rft.date=1998&rft_id=info:doi/10.1046/j.1432-1327.1998.2530057.x&rft_id=info:pmid/9578461&rft.aulast=Kordowska&rft.aufirst=J&rft.au=Stafford, WF&rft.au=Wang, CL&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">
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. PMID9925766.501-9&rft.date=1999&rft_id=info:doi/10.1006/excr.1998.4314&rft_id=info:pmid/9925766&rft.aulast=Yang&rft.aufirst=Q&rft.au=O'Hanlon, D&rft.au=Heizmann, CW&rft.au=Marks, A&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">
Deloulme JC, Assard N, Mbele GO, Mangin C, Kuwano R, Baudier J (2000). "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. PMID10913138.35302-10&rft.date=2000&rft_id=info:doi/10.1074/jbc.M003943200&rft_id=info:pmid/10913138&rft.aulast=Deloulme&rft.aufirst=JC&rft.au=Assard, N&rft.au=Mbele, GO&rft.au=Mangin, C&rft.au=Kuwano, R&rft.au=Baudier, J&rft_id=https://doi.org/10.1074%2Fjbc.M003943200&rfr_id=info:sid/en.wikipedia.org:S100A6" class="Z3988">