Anti-UBE3D antibody

Supplementary info

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

Activity summary

UBE3D also known as Ubiquitin Protein Ligase E3D is an enzyme with a molecular mass of approximately 100 kDa. This protein plays a role as a part of the ubiquitination process which marks proteins for degradation in the proteasome. UBE3D is expressed in various tissues with significant expression in the brain liver and heart. This distribution suggests it has roles in different physiological contexts possibly related to its targets for ubiquitination.

Biological function summary

UBE3D takes part in cellular protein homeostasis and regulation. It functions as an E3 ligase that tags proteins with ubiquitin an activity that usually signals these proteins for breakdown. Although not part of fully characterized complexes UBE3D likely interacts with multiple cofactors that assist in substrate recognition and ubiquitin transfer. This activity helps maintain cellular protein quality and modulate signaling pathways by controlling the abundance of key regulatory proteins.

Pathways

UBE3D is essential in the ubiquitin-proteasome system a pathway important for controlling protein turnover and degradation. This pathway ensures that damaged or misfolded proteins do not accumulate in cells thereby maintaining cellular health. UBE3D is also connected to the p53 signaling pathway through its role in regulating proteins that interact with p53 an important protein involved in cell cycle regulation and apoptosis. UBE3D therefore contributes to cell cycle control and stress responses affecting how cells react to various stimuli.

Associated diseases and disorders

UBE3D has links to neurological conditions including neurodegenerative disorders. Its dysfunction can affect protein degradation pathways leading to the buildup of proteins that could contribute to diseases such as Alzheimer's and Parkinson's. UBE3D's relation to the p53 pathway also connects it to cancer where it might influence cancer progression through its effects on protein degradation and cell cycle control. Understanding these connections could offer insights into therapeutic targets for these diseases.