PROSITE documentation PDOC51917
Pru (pleckstrin-like receptor for the Ub) domain profile


In eukaryotes, selective protein degradation is performed primarily by the ubiquitin-proteasome pathway, in which substrate proteins are marked by covalently attached ubiquitin chains that mediate recognition by the proteasome. Rpn13 (also called ADRM1) is a subunit of the proteasome that serves as a receptor for both ubiquitin and Uch37, one of the proteasome's three deubiquitinating enzymes. Rpn13 binds ubiquitin though a conserved amino-terminal region termed the pleckstrin-like receptor for the Ub (Pru) domain (also known as the ubiquitin-binding domain, or UBD), which binds K48-linked diubiquitin. Its carboxy-terminal DEUBAD domain (see <PDOC51916>) binds deubiquinating enzyme Uch37/UCHL5 and enhances its isopeptidase activity [1,2,3].

The Pru domain forms two contiguous, antiparallel β-sheets with a configuration similar to the pleckstrin-homology structural domain: a four-stranded twisted antiparallel β-sheet (β 1, 4-6) packs almost orthogonally against a second triple stranded β-sheet (β 7-8). Juxtaposed to the three-stranded sheet are two β-strands (β 2-3). The Pru domain forms a hydrophobic core containing conserved hydrophobic residues, which are located within β-sheets. One end of the β-sandwich is capped by a long C-terminal amphipatic α-helix (see <PDB:2R2Y>) [1,2,3].

The profile we developed covers the entire Pru domain.

Last update:

March 2020 / First entry.


Technical section

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

PRU, PS51917; Pru (pleckstrin-like receptor for ubiquitin) domain profile  (MATRIX)


1AuthorsHusnjak K. Elsasser S. Zhang N. Chen X. Randles L. Shi Y. Hofmann K. Walters K.J. Finley D. Dikic I.
TitleProteasome subunit Rpn13 is a novel ubiquitin receptor.
SourceNature 453:481-488(2008).
PubMed ID18497817

2AuthorsSchreiner P. Chen X. Husnjak K. Randles L. Zhang N. Elsasser S. Finley D. Dikic I. Walters K.J. Groll M.
TitleUbiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction.
SourceNature 453:548-552(2008).
PubMed ID18497827

3AuthorsChen 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

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)