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:
[email protected]
Supplementary information:
Supplementary data are available at Bioinformatics online.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Carboxypeptidases / genetics
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Carboxypeptidases / metabolism*
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Computational Biology / methods
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism
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Humans
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Intracellular Signaling Peptides and Proteins
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Membrane Glycoproteins / genetics
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Membrane Glycoproteins / metabolism
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Repressor Proteins / genetics
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Repressor Proteins / metabolism*
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Sequence Analysis, Protein / methods*
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Sequence Homology, Amino Acid
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Tumor Suppressor Proteins / genetics
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Tumor Suppressor Proteins / metabolism*
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Ubiquitin Thiolesterase / genetics
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Ubiquitin Thiolesterase / metabolism*
Substances
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ADRM1 protein, human
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ASXL1 protein, human
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BAP1 protein, human
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DNA-Binding Proteins
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Intracellular Signaling Peptides and Proteins
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Membrane Glycoproteins
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NFRKB protein, human
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Repressor Proteins
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Tumor Suppressor Proteins
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Carboxypeptidases
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UCHL5 protein, human
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Ubiquitin Thiolesterase