Human JOSD1 knockout HEK-293T cell lysate

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

JOSD1 also known as Josephin domain-containing protein 1 functions as a deubiquitinating enzyme. It specifically removes ubiquitin from protein substrates which regulates protein degradation localization and activity in cells. The protein mass is approximately 45 kDa. JOSD1 is expressed in various tissues with significant levels seen in the brain liver and kidney. By modulating the ubiquitination status of substrates JOSD1 influences cellular processes like signal transduction and response to stress.

Biological function summary

This protein modifies the stability and activity of other proteins by removing ubiquitin molecules. It acts as part of a larger deubiquitinase complex which interacts with protein networks to maintain cellular homeostasis. Through its enzyme activity JOSD1 contributes to the regulation of processes such as protein quality control and cell cycle progression.

Pathways

Scientists have placed JOSD1 in the ubiquitin-proteasome system an important pathway responsible for protein turnover in cells. It has connections with other proteins like USP7 and USP9X in this pathway reflecting its coordination role in protein deubiquitination. JOSD1 also participates in the endoplasmic reticulum-associated degradation (ERAD) pathway helping to eliminate misfolded proteins important for maintaining protein folding homeostasis within the cell.

Associated diseases and disorders

Abnormal activity of JOSD1 can connect to neurodegenerative disorders such as Alzheimer's disease where protein misfolding and aggregation play significant roles. JOSD1's interaction with proteins like tau and amyloid precursor protein suggests its potential to influence disease progression. Additionally research associates JOSD1 with liver cancer where dysregulated ubiquitin signaling may contribute to tumor development and progression.