Data visualization on cystic fibrosis mutations


April 2018


Students and the general public with basic scientific knowledge of genes and proteins


Dr. Andrea Gauthier


Circos, Tableau, Adobe Illustrator


11" x 17" poster, print


A novel data visualization that shows the frequencies and consequences of a subset of cystic fibrosis mutations, as well as their positions along the cystic fibrosis transmembrane conductance regulator (CFTR) protein sequence. Key amino acid residues that play an important role in CFTR protein function are also depicted in the data visualization. Data was obtained from the CFTR2 database. Future directions for this project is to make the data visualization interactive so that when the mouse hovers over each bubble plot, the CFTR mutation name and its corresponding frequency will appear in a tooltip.


  1. CFTR2 database
  2. Chin S, Yang D, Miles AJ, et al. Attenuation of Phosphorylation-dependent Activation of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) by Disease-causing Mutations at the Transmission Interface. The Journal of Biological Chemistry. 2017;292(5):1988-1999. doi:10.1074/jbc.M116.762633.
  3. Das J, Aleksandrov AA, Cui L, He L, Riordan JR, Dokholyan NV. Transmembrane helical interactions in the CFTR channel pore. Jacobs D, ed. PLoS Computational Biology. 2017;13(6):e1005594. doi:10.1371/journal.pcbi.1005594.
  4. Hwang T-C, Sheppard DN. Gating of the CFTR Cl− channel by ATP-driven nucleotide-binding domain dimerisation. The Journal of Physiology. 2009;587(Pt 10):2151-2161. doi:10.1113/jphysiol.2009.171595.
  5. Loo TW, Bartlett MC, Clarke DM. The V510D Suppressor Mutation Stabilizes ΔF508-CFTR at the Cell Surface. Biochemistry. 2010;49(30):6352-6357. doi:10.1021/bi100807h.
  6. Mense M, Vergani P, White DM, Altberg G, Nairn AC, Gadsby DC. In vivophosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer. The EMBO Journal. 2006;25(20):4728-4739. doi:10.1038/sj.emboj.7601373.