p(HGNC:PSMD4)

Entity

Name

PSMD4

Namespace

hgnc

Namespace Version

20180906

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Indeed, it has been reported that Parkin associates with the RPN10 (S5a) subunit of the 26S proteasome (Sakata et al., 2003) PubMed:14556719

Indeed, it has been reported that Parkin associates with the RPN10 (S5a) subunit of the 26S proteasome (Sakata et al., 2003) PubMed:14556719

Two ubiquitin binding subunits of the 19S RP have been identified, Rpn10 (S5a in mammalian cells) and Rpt5 (S6'); however, their essential role and mode of action have not been discerned PubMed:14556719

First, ubiquitinated proteins are docked to the proteasome through receptors associated to the 19S [67,68], including the proteasome proteins Rpn10 (proteasome regulatory particle base subunit; also known as Psmd4 – proteasome 26S subunit, non- ATPase, 4) and Rpn13 (also known as Adrm1, adhesion regulating molecule 1), that bind to the poly-ubiquitin chains [69,70]. PubMed:24457024

Similarly, three components of the proteasome regulatory particle (PSMD4, PSMC1, and ADRM1) clustered together, as did the two subunits of the prefoldin complex, PFDN2 and PFDN5 (Figure 5A) PubMed:25036637

RPN1 interacted strongly with four BAG proteins and with the ubiquitin ligase CHIP. This was in contrast to the three other subunits (RPN10, RPN13, and RPT2) that primarily interacted with other proteasome subunits (Figures 5I, 5J, and S4E) PubMed:25036637

RPN1 interacted strongly with four BAG proteins and with the ubiquitin ligase CHIP. This was in contrast to the three other subunits (RPN10, RPN13, and RPT2) that primarily interacted with other proteasome subunits (Figures 5I, 5J, and S4E) PubMed:25036637

RPN1 interacted strongly with four BAG proteins and with the ubiquitin ligase CHIP. This was in contrast to the three other subunits (RPN10, RPN13, and RPT2) that primarily interacted with other proteasome subunits (Figures 5I, 5J, and S4E) PubMed:25036637

RPN1 interacted strongly with four BAG proteins and with the ubiquitin ligase CHIP. This was in contrast to the three other subunits (RPN10, RPN13, and RPT2) that primarily interacted with other proteasome subunits (Figures 5I, 5J, and S4E) PubMed:25036637

RPN1 interacted strongly with four BAG proteins and with the ubiquitin ligase CHIP. This was in contrast to the three other subunits (RPN10, RPN13, and RPT2) that primarily interacted with other proteasome subunits (Figures 5I, 5J, and S4E) PubMed:25036637