Literature summary for 3.4.25.1 extracted from

Aufderheide, A.; Beck, F.; Stengel, F.; Hartwig, M.; Schweitzer, A.; Pfeifer, G.; Goldberg, A.L.; Sakata, E.; Baumeister, W.; Foerster, F.
Structural characterization of the interaction of Ubp6 with the 26S proteasome (2015), Proc. Natl. Acad. Sci. USA, 112, 8626-8631 .

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Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P38624	proteasome subunit beta type-1	-

General Information

General Information	Comment	Organism
physiological function	ubiquitin C-terminal hydrolase Ubp6 binds to the regulatory particle non-ATPase (Rpn) 1 via its N-terminal ubiquitin-like domain, whereas its catalytic ubiquitin-specific protease domain is positioned variably. Addition of ubiquitin aldehyde stabilizes the binding of the ubiquitin-specific protease domain in a position where it bridges the proteasome subunits Rpn1 and the regulatory particle triple-A ATPase (Rpt) 1. The ubiquitin-specific protease domain binds to Rpt1 in the immediate vicinity of the Ubp6 active site. The catalytic triad is positioned in proximity to the mouth of the ATPase module and to the deubiquitylating enzyme Rpn11. On the proteasome side, binding of Ubp6 favors conformational switching of the 26S proteasome into an intermediate-energy conformational state, in particular upon the addition of ubiquitin aldehyde	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)