IndraLab

Statements

PSMD7 affects PSMD14
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PSMD14 binds PSMD7. 10 / 81
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"The third DEP, PSMD7 (Rpn8), is part of the Rpn8-Rpn11 heterodimer with a function in removal of polyubiquitin tags before protein degradation in the proteasome 30 ."
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"A proteasomal subunit in close proximity to the Rpn8-Rpn11 heterodimer is PSMD13 (Rpn9), which showed a trend towards upregulation (fold change = 4.2; p = 0.07)."
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"A possible explanation for this finding is that SMK-24 may have bound effectively to the purified recombinant Rpn11/Rpn8 heterodimer, but not to endogenous Rpn11 in the greater structure of the 26S proteasome."
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"Proteasome 26S subunit, non-ATPase 7 (PSMD7, Rpn8, Mov34), an ATP-independent component of the 19S regulatory subunit, forms the heterodimers with PSMD14 as a functional complex which is extremely critical for degradation of ubiquitinated substrate with the proteasome [ xref ]."
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"PSMD7 interacts with PSMD14 to activate proteasome function to regulate ubiquitinated substrate degradation."
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"The Rpn11/Rpn8 heterodimer was expressed and purified as previously described ."
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"PSMD7 interacts with PSMD14 to activate proteasome function to regulate ubiquitinated substrate degradation."
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"The yeast RPN11/RPN8 complex, which is comparable to the human PSMD14/PSMD7 complex, has previously been reported to hydrolyse all isopeptide-linked diubiquitins ."
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"The RPN11/RPN8 complex is reported to process all linkages, however the catalytic efficiency for the processing of Lys11-linked diUb is two times higher as for Lys48-linked diUb and four times higher as for Lys63-linked diUb ."
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"Indeed, the minimal DUB-component complex of PSMD14 corresponds to the obligate PSMD14-PSMD7 heterodimers [ 18 , 26 ]."
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PSMD7 binds USP15 and PSMD14. 1 / 1
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"For example, USP11 has been found to interact with USP4, USP7 and USP15; and PSMD7 interacts with USP15 and PSMD14 [ xref ]."
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PSMD14 binds PSMD7 and 19S. 1 / 1
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"Therefore, it is now important to define whether this non-canonical function of PSMD14 on autophagy is either related to the free the heterodimer PSMD14-PSMD7, lid subcomplex or 19S RP ( Fig. 1 )."
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PSMD14 binds PSMD7 and Lys11. 1 / 1
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"These observed differences in hydrolysis rates between those reported for individual chains and the ones we found in the mixture containing all linkages may indicate that the presence of certain diUb linkages can lead to a change in hydrolysis rates of other linkages.Another interesting finding is the high preference of the metallo-DUB RPN11/RPN8 complex for Lys11 diUb."
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E6 binds oncoprotein, PSMA3, PSMC2, PSMC3, PSMD1, PSMD2, PSMD3, PSMD14, PSMD11, PSMD7, PSMC4, PSMD13, PSMD6, PSMD8, PSMB7, PSMB9, and PSME4. 1 / 1
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"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 ]."
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19S affects PSMD7
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PSMD14 binds PSMD7 and 19S. 1 / 1
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"Therefore, it is now important to define whether this non-canonical function of PSMD14 on autophagy is either related to the free the heterodimer PSMD14-PSMD7, lid subcomplex or 19S RP ( Fig. 1 )."
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