PROSITE documentation PDOC50271
Zinc finger UBP-type profile


The UBP-type zinc finger was first isolated in some members of a subfamily of deubiquitinating enzyme, the ubiquitin-specific processing protease (UBP) (see <PDOC00750>). HDAC6 UBP-type zinc finger has been shown to interact with ubiquitin [1,2]. Like with other ubiquitin binding domain (UBD) the interaction with ubiquitin is moderate or even weak. In addition, several UBD families have members that do not interact with ubiquitin at all, which emphasis that binding domains that are identified by similarity searches should be experimentally verified [3].

Some proteins containing an UBP-type zinc finger are listed below:

  • BRCA1-associated protein 2 (BRAP2). It binds the nuclear localization signal of BRCA1.
  • Animal histone deacetylase 6 (HDAC6). An atypical deacetylase that contains two functional catalytic domains. HDAC6 shuttles in and out of the cell nucleus. In the cytoplasm it is part of a multiprotein complex involved in the control of protein ubiquitination.
  • Various eukaryotic deubiquitinating enzymes of the UBP subfamily.
  • A small family of uncharacterized bacterial proteins found in Actinobacteria, Proteobacteria, Cyanobacteria and Acidobacteria.

The profile we developed covers the whole UBP-type zinc finger.


The UBP-type zinc finger is also known as the PAZ domain, but this name describes another domain in the literature (see <PDOC50821>).

Last update:

April 2021 / Profile revised.


Technical section

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

ZF_UBP, PS50271; Zinc finger UBP-type profile  (MATRIX)


1AuthorsSeigneurin-Berny D. Verdel A. Curtet S. Lemercier C. Garin J. Rousseaux S. Khochbin S.
TitleIdentification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways.
SourceMol. Cell. Biol. 21:8035-8044(2001).
PubMed ID11689694

2AuthorsHook S.S. Orian A. Cowley S.M. Eisenman R.N.
TitleHistone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes.
SourceProc. Natl. Acad. Sci. U.S.A. 99:13425-13430(2002).
PubMed ID12354939

3AuthorsHicke L. Schubert H.L. Hill C.P.
TitleUbiquitin-binding domains.
SourceNat. Rev. Mol. Cell Biol. 6:610-621(2005).
PubMed ID16064137

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)