A common ancestry for BAP1 and Uch37 regulators.
basic_science · Level V
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- Record sourced from PubMed, PMID 22645167.
- Also identified by DOI 10.1093/bioinformatics/bts319.
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Abstract
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. luis.sanchezpulido@dpag.ox.ac.uk Supplementary data are available at Bioinformatics online.
Medical subject headings
- Carboxypeptidases
- Repressor Proteins
- Sequence Analysis, Protein
- Tumor Suppressor Proteins
- Ubiquitin Thiolesterase