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. Author manuscript; available in PMC: 2013 May 1.
Published in final edited form as: Prog Neurobiol. 2011 Nov 23;97(2):239–257. doi: 10.1016/j.pneurobio.2011.11.006

Figure 1.

Figure 1

Functional domains and posttranslational modifications of ATXN3. A) ATXN3 contains a N-terminal DUB catalytic domain (Josephin domain, JD) centered on residues Q9, C14, H119, and N134 (red), two Ub-binding sites, and two nuclear export signals (NES77 and NES141). The C-terminal region of ATXN3 contains 2 or 3 UIMs (depending on the isoform), the polyQ tract (Qn), and the NLS. ATXN3 is mono-ubiquitinated primarily at residue K117 and phosphorylated at residues S111, S236, S256, S340, and S352. B) Solution structure of JD (PDB: 1YZB) highlighting the catalytic residues (red) and critical residues of Ub-binding sites (blue). Ub-binding site 1 (I77Q78) resides near the catalytic pocket while Ub-binding site 2 (W87) resides on the opposite side, separated from site 1 by a helical hairpin (hh). The main ATXN3 mono-ubiquitination site, K117 (green), also localizes near the catalytic cleft.