IndraLab

Statements

YOD1 is ubiquitinated. 10 / 10
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"In this study, we observed TRIM54 binds and increases ubiquitination of YOD1 ( xref )."
38042492
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"The ubiquitination of YOD1 at lysine 213/257 is a novel observation that is not reported previously."
36182100
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"Further, through immunoprecipitation studies, we identified that TRIM54 regulates inflammation in TDSCs by binding to and ubiquitinating YOD1."
38042492
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"Both YOD1 and USP21 are ubiquitinated."
37743467
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"Since TRIM54 is an ubiquitinating enzyme, we wanted to assess if it binds and increases the ubiquitination of YOD1."
38042492
sparser
"Initially, we overexpressed TRIM54 and observed an increase in ubiquitination of endogenous YOD1 protein in HEK 293T cells ( xref A )."
38042492
sparser
"Initially, we observed that indeed ubiquitination of YOD1 increases in the presence of TRIM54, however presence of deubiquitinase 3 significantly decreased this ubiquitination ( xref C )."
38042492
sparser
"Our findings that injury rapidly caused a differential ubiquitination and activation of the ER-associated DUBs YOD1 and ATXN3 indicated that this change in ubiquitination pattern might directly regulate protein activity."
36182100
sparser
"Hence, based on these results, it is evident that TRIM54 binds to and ubiquitinates YOD1 protein."
38042492
sparser
"Co-IP studies confirmed that TRIM54 binds and regulates YOD1 ubiquitination ( xref )."
38042492