RPN10 cDNA ORF clone, Saccharomyces cerevisiae S288C

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII.
Johnston M, Andrews S, Brinkman R, Cooper J, Ding H, Dover J, Du Z, Favello A, Fulton L, Gattung S
Science (New York, N.Y.)265(5181)2077-82(1994 Sep)

Genetic, bioinformatics, biochemical and biophysical data show that attraction between this alpha1-conjugated ubiquitin and the HECT ubiquitin-binding patch pulls the alpha1-helix out of the interface, thereby promoting trimerization. Strikingly, trimerization renders the ubiquitin ligase inactive.
Title: Ubiquitylation-dependent oligomerization regulates activity of Nedd4 ligases.

functional yeast proteasomes have the capacity to associate and dissociate with Rpn10 and that Rpn10 monoubiquitination decreases the Rpn10-proteasome and Rpn10-Dsk2 associations.
Title: Rpn10 monoubiquitination orchestrates the association of the ubiquilin-type DSK2 receptor with the proteasome.

Mutations in this disordered region promote ubiquitin chain extension of Rpn10.
Title: An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination.

X-ray analysis revealed that these crystals of Rpn10 belonged to the monoclinic system C2, with unit-cell parameters a = 107.3, b = 49.7, c = 81.3 A, alpha = gamma = 90.0, beta = 130.5 degrees
Title: Purification and crystallization of mono-ubiquitylated ubiquitin receptor Rpn10.

On the basis of the mutual positions of Rpn10 and Rpn13, we propose a model for polyubiquitin binding to the 26S proteasome
Title: Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy.