Summary: To reveal how the polycomb repressive–deubiquitinase (PR–DUB) complex controls substrate selection specificity, we undertook a detailed computational sequence analysis of its components: additional sex combs like 1 (ASXL1) and BRCA1-associated protein 1 (BAP1) proteins. This led to the discovery of two previously unrecognized domains in ASXL1: a forkhead (winged-helix) DNA-binding domain and a deubiquitinase adaptor domain shared with two regulators of ubiquitin carboxyl-terminal hydrolase 37 (Uch37), namely adhesion regulating molecule 1 (ADRM1) and nuclear factor related to kappaB (NFRKB). Our analysis demonstrates a common ancestry for BAP1 and Uch37 regulators in PR–DUB, INO80 chromatin remodelling and proteosome complexes.#R##N##R##N#Contact: luis.sanchezpulido@dpag.ox.ac.uk#R##N##R##N#Supplementary information: Supplementary data are available at Bioinformatics online.
['Luis Sanchez-Pulido', 'Lesheng Kong', 'Chris P. Ponting']
A common ancestry for BAP1 and Uch37 regulators