PROSITE documentation PDOC51283
DUSP domain profile


Deubiquitinating enzymes (DUB) form a large family of cysteine protease that can deconjugate ubiquitin or ubiquitin-like proteins (see <PDOC00271>) from ubiquitin-conjugated proteins. All DUBs contain a catalytic domain surrounded by one or more subdomains, some of which contribute to target recognition. The ~120-residue DUSP (domain present in ubiquitin-specific proteases) domain is one of these specific subdomains. Single or tandem DUSP domains are located both N- and C-terminal to the ubiquitin carboxyl-terminal hydrolase catalytic core domain (see <PDOC00750>) [1].

The DUSP domain displays a tripod-like AB3 fold with a three-helix bundle and a three-stranded anti-parallel β-sheet ressembling the legs and seat of the tripod (see <PDB:1W6V>). Conserved residues are predominantly involved in hydrophobic packing interactions within the three α-helices. The most conserved DUSP residues, forming the PGPI motif, are flanked by two long loops that vary both in length and sequence. The PGPI motif packs against the three-helix bundle and is highly ordered [1].

Some proteins known to contain a DUSP domain are listed below:

  • Mammalian ubiquitin carboxyl-terminal hydrolase 4 (USP4) (EC
  • Mammalian ubiquitin carboxyl-terminal hydrolase 11 (USP11) (EC
  • Mammalian ubiquitin carboxyl-terminal hydrolase 15 (USP15) (EC
  • Mammalian ubiquitin carboxyl-terminal hydrolase 20 (USP20) (EC
  • Mammalian ubiquitin carboxyl-terminal hydrolase 32 (USP32) (EC
  • Vertebrate ubiquitin carboxyl-terminal hydrolase 33 (USP33) (EC
  • Vertebrate ubiquitin carboxyl-terminal hydrolase 48 (USP48) (EC

The profile we developed covers the entire DUSP domain.

Last update:

December 2006 / First entry.


Technical section

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

DUSP, PS51283; DUSP domain profile  (MATRIX)


1Authorsde Jong R.N. AB E. Diercks T. Truffault V. Daniels M. Kaptein R. Folkers G.E.
TitleSolution structure of the human ubiquitin-specific protease 15 DUSP domain.
SourceJ. Biol. Chem. 281:5026-5031(2006).
PubMed ID16298993

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