A common ancestry for BAP1 and Uch37 regulators

Luis Sanchez-Pulido, Lesheng Kong, Chris P Ponting

Research output: Contribution to journalArticlepeer-review

Abstract

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.

CONTACT: luis.sanchezpulido@dpag.ox.ac.uk

SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.

Original languageEnglish
Pages (from-to)1953-6
Number of pages4
JournalBioinformatics
Volume28
Issue number15
DOIs
Publication statusPublished - 1 Aug 2012

Keywords

  • Animals
  • Carboxypeptidases
  • Computational Biology
  • DNA-Binding Proteins
  • Humans
  • Membrane Glycoproteins
  • Repressor Proteins
  • Sequence Analysis, Protein
  • Sequence Homology, Amino Acid
  • Tumor Suppressor Proteins
  • Ubiquitin Thiolesterase

Fingerprint

Dive into the research topics of 'A common ancestry for BAP1 and Uch37 regulators'. Together they form a unique fingerprint.

Cite this