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S100 calcium binding protein A3

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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: S-100, calcyclin, HAIR, S100A2, S100A4
Papers on S100A3
Age-dependent damage of hair cuticle: contribution of S100A3 protein and its citrullination.
Suzuki et al., Tokyo, Japan. In J Cosmet Dermatol, Jan 2016
S100A3 protein, located at the endocuticle, was found to be citrullinated and transformed into tetramer to improve its Ca(2+) -binding ability.
Advanced hair damage model from ultra-violet radiation in the presence of copper.
Coderch et al., Cincinnati, United States. In Int J Cosmet Sci, Oct 2015
This fragment originates from the calcium-binding protein S100A3.
S100A3 suppression inhibits in vitro and in vivo tumor growth and invasion of human castration-resistant prostate cancer cells.
Kwak et al., Seoul, South Korea. In Urology, 2015
OBJECTIVE: To investigate the role of S100A3 and the effect of S100A3 inhibition on human castration-resistant prostate cancer (CRPC) cells by using in vitro and in vivo functional assays.
Blockade of S100A3 activity inhibits murine hair growth.
Yu et al., Shanghai, China. In Genet Mol Res, 2014
S100A3 expression increased during the anagen phase and returned to normal during the telogen phase.
Role of S100A3 in human colorectal cancer and the anticancer effect of cantharidinate.
Gao et al., Changchun, China. In Exp Ther Med, 2013
In the present study, the protein expression of S100A3 was observed in a cohort of 20 patients with cancer, which indicated that S100A3 activation was involved in tumorigenesis.
Epidermal differentiation complex (locus 1q21) gene expression in head and neck cancer and normal mucosa.
Maciejewski et al., Gliwice, Poland. In Folia Histochem Cytobiol, 2013
Significant up-regulation in tumors was found for S100A11, S100A7, LCE3D, S100A3 and S100A2 genes.
Human S100A3 tetramerization propagates Ca(2+)/Zn(2+) binding states.
Izumi et al., Odawara, Japan. In Biochim Biophys Acta, 2013
The S100A3 homotetramer assembles upon citrullination of a specific symmetric Arg51 pair on its homodimer interface in human hair cuticular cells.
Purification and characterization of the human cysteine-rich S100A3 protein and its pseudo citrullinated forms expressed in insect cells.
Heizmann et al., Odawara, Japan. In Methods Mol Biol, 2012
S100A3 is a unique member of the S100 protein family with the highest cysteine content (10%).
S100 and S100 fused-type protein families in epidermal maturation with special focus on S100A3 in mammalian hair cuticles.
Heizmann et al., Odawara, Japan. In Biochimie, 2011
Epithelial Ca(2+)-regulation, which governs cornified envelope formation in the skin epidermis and hair follicles, closely coincides with the expression of S100A3, filaggrin and trichohyalin, and the post-translational modification of these proteins by Ca(2+)-dependent peptidylarginine deiminases.
Association screening in the Epidermal Differentiation Complex (EDC) identifies an SPRR3 repeat number variant as a risk factor for eczema.
Lee et al., Berlin, Germany. In J Invest Dermatol, 2011
Of these, 4 were validated in 94 eczema patients: a nonsense mutation in FLG2 (rs12568784), a stop codon mutation in LCE1D (rs41268500), a 24-bp deletion in SPRR3 (rs28989168), and a frameshift mutation in S100A3 (rs11390146).
Refined crystal structures of human Ca(2+)/Zn(2+)-binding S100A3 protein characterized by two disulfide bridges.
Kizawa et al., Naka, Japan. In J Mol Biol, 2011
One disulfide bridge is between Cys30 in the N-terminal pseudo-EF-hand and Cys68 in the C-terminal EF-hand (SS1), and another disulfide bridge attaches Cys99 in the C-terminal coil structure to Cys81 in helix IV (SS2).
Modulation of quaternary structure of S100 proteins by calcium ions.
Makhatadze et al., Troy, United States. In Biophys Chem, 2010
To this end we performed equilibrium analytical ultracentrifugation experiments for 16 S100 proteins (S100A1, S100A2, S100A3, S100A4, S100A5, S100A6, S100A7, S100A8, S100A9, S100A10, S100A11, S100A12, S100A13, S100B, S100P, and S100Z) under reducing conditions in the absence and presence of calcium ions.
Genome-wide analysis of chromosomal alterations in patients with esophageal squamous cell carcinoma exposed to tobacco and betel quid from high-risk area in India.
Kapur et al., New Delhi, India. In Mutat Res, 2010
The candidate genes located at amplified regions of chromosomes or low-level gain regions such as PLA2G5 (1p36-p34), COL11A1 (1p21), KCNK2 (1q41), S100A3 (1q21), ENAH (1q42.12),
Specific citrullination causes assembly of a globular S100A3 homotetramer: a putative Ca2+ modulator matures human hair cuticle.
Heizmann et al., Odawara, Japan. In J Biol Chem, 2008
cytoplasmic S100A3 within the cuticular layer is mostly co-localized with the type III isoform of peptidylarginine deiminase (PAD3)
In silico analysis and verification of S100 gene expression in gastric cancer.
Wang et al., Xi'an, China. In Bmc Cancer, 2007
The expression of S100A3 was further evaluated by quantitative RT-PCR.
S100 proteins in the epidermis.
Lee et al., Cleveland, United States. In J Invest Dermatol, 2004
Fourteen S100 protein genes are located within the epidermal differentiation complex on human chromosome 1q21 and 13 S100 proteins (S100A2, S100A3, S100A4, S100A6, S100A7, S100A8, S100A9, S100A10, S100A11, S100A12, S100A15, S100B, and S100P) are expressed in normal and/or diseased epidermis.
Characterization of the cysteine-rich calcium-binding S100A3 protein from human hair cuticles.
Heizmann et al., Odawara, Japan. In Biochem Biophys Res Commun, 2003
Purification and characterization of the S100A3 protein from human hair cuticles.
The crystal structure of metal-free human EF-hand protein S100A3 at 1.7-A resolution.
Heizmann et al., Zürich, Switzerland. In J Biol Chem, 2002
crystal structure of S100A3 at 1.7-A resolution
Metal-free MIRAS phasing: structure of apo-S100A3.
Grütter et al., Zürich, Switzerland. In Acta Crystallogr D Biol Crystallogr, 2002
structure was solved by MIRAS phasing
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