PROSITE documentation PDOC51916 [for PROSITE entry PS51916]DEUBAD (DEUBiquitinase ADaptor) domain profile
Protein ubiquitination is a fundamental mechanism that affects nearly all aspects of cellular life. Deubiquitinating enzymes (DUBs) play important roles in ubiquitin (Ub) signaling by Ub cleavage from adducts. The Ub C-terminal hydrolase (UCH) family of deubiquitinases (DUBs) contains four members including UCH37 (also called ubiquitin carboxy-terminal hydrolase isozyme L5, UCHL-5) and BAP1 which share high similarity in the catalytic domain (UCH) and the C-terminal region, termed the UCH37-like domain (ULD), responsible for binding interaction partners. The ULD is important for regulation of the DUB activity of BAP1 and UCH-L5 by binding proteins with a DEUBiquitinase ADaptor (DEUBAD) domain, ASXL1 for BAP1, and RPN13 (ADRM1) and INO80G (NFRKB) for UCH-L5 [1,2,3,4,5].
The DEUBAD domain is made of eight α helices that form a helical bundle surrounding a compact hydrophobic core (see <PDB:2KR0>) [6]. It has a modular architecture with the core (α1-α4), primarily responsible for binding to ULD, and accessory elements that lead to full activation, or inhibition, of the UCH activity [7,8].
The profile we developed covers the entire DEUBAD domain.
Last update:March 2020 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Sanchez-Pulido L. Kong L. Ponting C.P. |
| Title | A common ancestry for BAP1 and Uch37 regulators. | |
| Source | Bioinformatics 28:1953-1956(2012). | |
| PubMed ID | 22645167 | |
| DOI | 10.1093/bioinformatics/bts319 |
| 2 | Authors | Jiao L. Ouyang S. Shaw N. Song G. Feng Y. Niu F. Qiu W. Zhu H. Hung L.W. Zuo X. Eleonora Shtykova V. Zhu P. Dong Y.-H. Xu R. |
| Title | Liu Z.-J. Mechanism of the Rpn13-induced activation of Uch37. | |
| Source | Protein. Cell. 5:616-630(2014). | |
| PubMed ID | 24752541 | |
| DOI | 10.1007/s13238-014-0046-z |
| 3 | Authors | Sahtoe D.D. van Dijk W.J. Ekkebus R. Ovaa H. Sixma T.K. |
| Title | BAP1/ASXL1 recruitment and activation for H2A deubiquitination. | |
| Source | Nat. Commun. 7:10292-10292(2016). | |
| PubMed ID | 26739236 | |
| DOI | 10.1038/ncomms10292 |
| 4 | Authors | Daou S. Barbour H. Ahmed O. Masclef L. Baril C. Sen Nkwe N. Tchelougou D. Uriarte M. Bonneil E. Ceccarelli D. Mashtalir N. Tanji M. Masson J.Y. Thibault P. Sicheri F. Yang H. Carbone M. Therrien M. Affar E.B. |
| Title | Monoubiquitination of ASXLs controls the deubiquitinase activity of the tumor suppressor BAP1. | |
| Source | Nat. Commun. 9:4385-4385(2018). | |
| PubMed ID | 30349006 | |
| DOI | 10.1038/s41467-018-06854-2 |
| 5 | Authors | Foglizzo M. Middleton A.J. Burgess A.E. Crowther J.M. Dobson R.C.J. Murphy J.M. Day C.L. Mace P.D. |
| Title | A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes. | |
| Source | Nat. Commun. 9:3932-3932(2018). | |
| PubMed ID | 30258054 | |
| DOI | 10.1038/s41467-018-06186-1 |
| 6 | Authors | Chen X. Lee B.-H. Finley D. Walters K.J. |
| Title | Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. | |
| Source | Mol. Cell. 38:404-415(2010). | |
| PubMed ID | 20471946 | |
| DOI | 10.1016/j.molcel.2010.04.019 |
| 7 | Authors | Sahtoe D.D. van Dijk W.J. El Oualid F. Ekkebus R. Ovaa H. Sixma T.K. |
| Title | Mechanism of UCH-L5 activation and inhibition by DEUBAD domains in RPN13 and INO80G. | |
| Source | Mol. Cell. 57:887-900(2015). | |
| PubMed ID | 25702870 | |
| DOI | 10.1016/j.molcel.2014.12.039 |
| 8 | Authors | De I. Chittock E.C. Groetsch H. Miller T.C.R. McCarthy A.A. Mueller C.W. |
| Title | Structural Basis for the Activation of the Deubiquitinase Calypso by the Polycomb Protein ASX. | |
| Source | Structure 27:528-536.e4(2019). | |
| PubMed ID | 30639226 | |
| DOI | 10.1016/j.str.2018.11.013 |
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