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PROSITE documentation PDOC51916

DEUBAD (DEUBiquitinase ADaptor) domain profile





Description

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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Technical section

PROSITE method (with tools and information) covered by this documentation:

DEUBAD, PS51916; DEUBAD (DEUBiquitinase ADaptor) domain profile  (MATRIX)


References

1AuthorsSanchez-Pulido L. Kong L. Ponting C.P.
TitleA common ancestry for BAP1 and Uch37 regulators.
SourceBioinformatics 28:1953-1956(2012).
PubMed ID22645167
DOI10.1093/bioinformatics/bts319

2AuthorsJiao 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. Liu Z.-J.
TitleMechanism of the Rpn13-induced activation of Uch37.
SourceProtein. Cell. 5:616-630(2014).
PubMed ID24752541
DOI10.1007/s13238-014-0046-z

3AuthorsSahtoe D.D. van Dijk W.J. Ekkebus R. Ovaa H. Sixma T.K.
TitleBAP1/ASXL1 recruitment and activation for H2A deubiquitination.
SourceNat. Commun. 7:10292-10292(2016).
PubMed ID26739236
DOI10.1038/ncomms10292

4AuthorsDaou 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.
TitleMonoubiquitination of ASXLs controls the deubiquitinase activity of the tumor suppressor BAP1.
SourceNat. Commun. 9:4385-4385(2018).
PubMed ID30349006
DOI10.1038/s41467-018-06854-2

5AuthorsFoglizzo M. Middleton A.J. Burgess A.E. Crowther J.M. Dobson R.C.J. Murphy J.M. Day C.L. Mace P.D.
TitleA bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes.
SourceNat. Commun. 9:3932-3932(2018).
PubMed ID30258054
DOI10.1038/s41467-018-06186-1

6AuthorsChen X. Lee B.-H. Finley D. Walters K.J.
TitleStructure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2.
SourceMol. Cell. 38:404-415(2010).
PubMed ID20471946
DOI10.1016/j.molcel.2010.04.019

7AuthorsSahtoe D.D. van Dijk W.J. El Oualid F. Ekkebus R. Ovaa H. Sixma T.K.
TitleMechanism of UCH-L5 activation and inhibition by DEUBAD domains in RPN13 and INO80G.
SourceMol. Cell. 57:887-900(2015).
PubMed ID25702870
DOI10.1016/j.molcel.2014.12.039

8AuthorsDe I. Chittock E.C. Groetsch H. Miller T.C.R. McCarthy A.A. Mueller C.W.
TitleStructural Basis for the Activation of the Deubiquitinase Calypso by the Polycomb Protein ASX.
SourceStructure 27:528-536.e4(2019).
PubMed ID30639226
DOI10.1016/j.str.2018.11.013



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