S100 calcium-binding protein A3 (S100A3) is a protein that in humans is encoded by the S100A3gene.[1][2]
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 has the highest content of cysteines of all S100 proteins, has a high affinity for Zinc, and is highly expressed in human hair cuticle. The precise function of this protein is unknown.[2]
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Föhr UG, Heizmann CW, Engelkamp D, et al. (1995). "Purification and cation binding properties of the recombinant human S100 calcium-binding protein A3, an EF-hand motif protein with high affinity for zinc". J. Biol. Chem. 270 (36): 21056–61. doi:10.1074/jbc.270.36.21056. PMID7673133.
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. doi:10.1016/0888-7543(95)80005-7. PMID7759097.
Kizawa K, Uchiwa H, Murakami U (1996). "Highly-expressed S100A3, a calcium-binding protein, in human hair cuticle". Biochim. Biophys. Acta. 1312 (2): 94–8. doi:10.1016/0167-4889(96)00023-7. PMID8672544.
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. doi:10.1111/j.1365-2133.1997.tb03698.x. PMID9274623.
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. doi:10.1016/S0014-5793(97)01535-4. PMID9468301.
Ridinger K, Ilg EC, Niggli FK, et al. (1999). "Clustered organization of S100 genes in human and mouse". Biochim. Biophys. Acta. 1448 (2): 254–63. doi:10.1016/S0167-4889(98)00137-2. PMID9920416.
Fritz G, Heizmann CW, Kroneck PM (1999). "Probing the structure of the human Ca2+- and Zn2+-binding protein S100A3: spectroscopic investigations of its transition metal ion complexes, and three-dimensional structural model". Biochim. Biophys. Acta. 1448 (2): 264–76. doi:10.1016/S0167-4889(98)00138-4. PMID9920417.
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. doi:10.1016/S0006-8993(00)02393-3. PMID10837826.
Fritz G, Mittl PR, Vasak M, et al. (2002). "The crystal structure of metal-free human EF-hand protein S100A3 at 1.7-A resolution". J. Biol. Chem. 277 (36): 33092–8. doi:10.1074/jbc.M200574200. PMID12045193.
Mittl PR, Fritz G, Sargent DF, et al. (2003). "Metal-free MIRAS phasing: structure of apo-S100A3". Acta Crystallogr. D. 58 (Pt 8): 1255–61. doi:10.1107/S0907444902008430. PMID12136135.
Kizawa K, Troxler H, Kleinert P, et al. (2003). "Characterization of the cysteine-rich calcium-binding S100A3 protein from human hair cuticles". Biochem. Biophys. Res. Commun. 299 (5): 857–62. doi:10.1016/S0006-291X(02)02744-4. PMID12470658.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID16189514.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID16710414.