IndraLab

Statements

PSMD7 affects PSMD14
13 | 20 8
PSMD14 binds PSMD7. 10 / 40
13 | 20 7
reach
"Here we describe a method for the purification of the Rpn8/Rpn11 heterodimer and ubiquitin-GC-TAMRA, a model substrate that can be used to characterize the DUB activity of Rpn11 in isolation without the need of purifying 26S proteasomes."
36350544
reach
"After transferring Zn ion to the Rpn11, we used both the Rpn11 monomer (Figure 2A) and the Rpn8-Rpn11 heterodimer (Figure 3A) structures for subsequent analysis.For the CSN5 monomer (Figure 2B), the recently solved crystal structure of CSN5 with CSN5i-3 (PDB_code: 5JOG) (Schlierf et al., 2016) was considered."
30356695
reach
"In the Rpn8-Rpn11 heterodimer, capzimin showed a bidentate coordination with Zn and a stable H-bond with side chain of Thr129 (Figure S4B)."
30356695
sparser
"This feature opens the possibility that the regulatory particle, free lid subcomplex or the heterodimer PSMD14-PSMD7 might play other physiological roles including a positive function on protein stability through deubiquitination."
36241058
biogrid
No evidence text available
25416956
biogrid
No evidence text available
19615732
biogrid
No evidence text available
19615732
reach
"Thus, we investigated whether this was an unrealistic over binding, a protein-protein complex environment would be able to reproduce the selectivity.In the heterodimeric Rpn8-Rpn11 complex, CSN5i-3 binding in the pocket was not stable (Figure 7C), the distance to zinc increases continously and eventually the ligand lost coordination with Zn (Figure 7D and Table 1) which shows that the influence of Rpn8 on the capzimin bound Rpn11 is prominent."
30356695
biogrid
No evidence text available
17323924
reach
"PSMD7 interacts with PSMD14 to activate proteasome function to regulate ubiquitinated substrate degradation."
33687056
USP15 binds PSMD14 and PSMD7. 1 / 1
| 1
sparser
"For example, USP11 has been found to interact with USP4, USP7 and USP15; and PSMD7 interacts with USP15 and PSMD14 [ xref ]."
28659380
PSMD14 binds PSME4, PSMA3, PSMB7, PSMB9, PSMC2, PSMC3, PSMC4, PSMD1, PSMD11, PSMD13, PSMD2, PSMD3, PSMD6, PSMD7, PSMD8, E6, and oncoprotein. 1 / 1
| 1
sparser
"These observations were supported by a series of analyses that demonstrated interactions between multiple α-HPV E6 oncoproteins and PSMA3, PSMC2, PSMC3, PSMD1, PSMD2, PSMD3, PSMD14, PSMD11, PSMD7, PSMC4, PSMD13, PSMD6, PSMD8, PSMB7, PSMB9 and PSME4 proteasomal subunits, while a panel of β-HPV E6 oncoproteins interacted only with a few proteasomal subunits, including PSMA3, PSMC2, PSMD1, PSMD2, PSMD3, PSMD11, and PSMD13 [ xref , xref , xref ]."
32085533