Anti-USP19 antibody

Supplementary info

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

Activity summary

USP19 also known as Ubiquitin Specific Peptidase 19 is an enzyme with deubiquitinating activity. It belongs to the family of cysteine proteases and has a molecular mass of approximately 150 kDa. This protein's primary function involves the removal of ubiquitin from specific protein substrates regulating their degradation and maintaining protein homeostasis. USP19 is expressed in multiple tissues including skeletal muscle heart and brain indicating its widespread physiological roles.

Biological function summary

The regulation of protein turnover and cellular stress responses involves USP19. As a standalone enzyme it participates independently rather than as part of a larger protein complex. By deubiquitinating target proteins USP19 influences their stability and function affecting a variety of cellular processes such as protein synthesis cell cycle progression and stress response through modulation of ubiquitin chains on substrates.

Pathways

The modulation of protein degradative pathways involves USP19 specifically impacting the ubiquitin-proteasome system (UPS) and chaperone-mediated autophagy (CMA). It interacts with key proteins in these pathways such as ubiquitin-conjugating enzymes and proteasomal subunits to maintain cellular homeostasis. By regulating pathways like UPS USP19 plays a role in controlling protein quality and preventing aggregation which is critical for cell function.

Associated diseases and disorders

The dysregulation of protein degradation mechanisms implicates USP19 in conditions such as muscle atrophy and neurodegenerative diseases. Abnormal activity of USP19 associates with disorders like Parkinson’s disease where it may interact with proteins such as Parkin affecting the ubiquitination balance. Studies on USP19 continue to explore its potential as a therapeutic target for treating these conditions.