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Appears in Networks 3

In-Edges 10

p(HGNC:PRKN) association p(HGNC:PSMD4) View Subject | View Object

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

Out-Edges 9

p(HGNC:PSMD4) association p(HGNC:PRKN) View Subject | View Object

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

p(HGNC:PSMD4) increases complex(a(MESH:Ubiquitin), p(HGNC:PSMD4)) View Subject | View Object

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

p(HGNC:PSMD4) increases complex(a(GO:"proteasome complex"), p(MESH:Proteins, pmod(Ub))) View Subject | View Object

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

p(HGNC:PSMD4) directlyIncreases complex(p(HGNC:ADRM1), p(HGNC:PSMC1), p(HGNC:PSMD4)) View Subject | View Object

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

p(HGNC:PSMD4) directlyIncreases complex(p(HGNC:PSMD4), p(HGNC:USP14)) View Subject | View Object

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

p(HGNC:PSMD4) directlyIncreases complex(p(HGNC:PSMC1), p(HGNC:PSMD4)) View Subject | View Object

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

p(HGNC:PSMD4) directlyIncreases complex(p(HGNC:PSMD2), p(HGNC:PSMD4)) View Subject | View Object

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

p(HGNC:PSMD4) directlyIncreases complex(p(HGNC:PRPS2), p(HGNC:PSMD4)) View Subject | View Object

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

p(HGNC:PSMD4) directlyIncreases complex(p(HGNC:PSMA5), p(HGNC:PSMD4)) View Subject | View Object

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

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BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.