Sequence and domain structure of ASPP2.

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Sequence and domain structure of ASPP2. Sequence and domain structure of ASPP2. (A) Protein sequence alignment of ASPP2 and previously identified FIH-1 substrates (Cockman et al., 2009; Coleman and Ratcliffe, 2009). (B) Protein sequence alignment of previously identified FIH-1 substrates for aspartyl and histidinyl hydroxylation (Yang et al., 2011a; Yang et al., 2011b). (C) Alignment of ASPP peptides used in this study. Potential and actual hydroxylation sites are indicated by asterisks. Alignments were created using the CLCbio sequence viewer, version 6 (http://www.clcbio.com/). (D) Schematic diagram of the domain structure of ASPP2, iASPP, HIF-1α and the protein fragments or peptides used in this study. All expressed fragments and peptides are shown according to their position in the full length protein. N-terminal protein tags are indicated. His, histidine tag; GST, GST tag; Ub, ubiquitin-like fold; Pro, proline-rich region; ARD, ankyrin repeat domain; SH3, Src-homology 3 domain; bHLH, basic helix-loop-helix domain; PAS, Per-Arnt-Sim domain; ODD, oxygen-dependent degradation domain; NTAD, N-terminal transactivation domain; CTAD, C-terminal transactivation domain. Kirsten Janke et al. J Cell Sci 2013;126:2629-2640 © 2013. Published by The Company of Biologists Ltd