Recombinant human Ube2G1 protein (Active)

Supplementary information

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

Ube2G1 also known as ubiquitin-conjugating enzyme E2 G1 plays an important role in the ubiquitination process. This protein with a molecular mass of about 23 kDa is involved in tagging substrates with ubiquitin for proteasomal degradation—an important cellular mechanism that regulates protein levels and quality. Ube2G1 expresses in various tissues including the liver and central nervous system highlighting its broad role in maintaining cellular functions.

Biological function summary

Ube2G1's primary function supports protein homeostasis and cellular stress responses. It collaborates with E3 ubiquitin ligases in a complex to mediate the transfer of ubiquitin molecules to their targets. This activity is essential in controlling various cellular processes such as cell cycle regulation DNA repair and signal transduction. By participating in these functions Ube2G1 assures that the cellular environment remains stable and efficient.

Pathways

Ube2G1 has pivotal involvement in the ubiquitin-proteasome pathway which is significant for the regulated degradation of misfolded or damaged proteins. Additionally it interacts with components of the endoplasmic reticulum-associated degradation (ERAD) pathway working alongside proteins like Derlin-1 to eliminate faulty proteins from the ER. Through these pathways Ube2G1 contributes to cellular health by preventing protein aggregation and dysfunction.

Improper function of Ube2G1 can have serious implications for neurological conditions such as Alzheimer's disease due to the accumulation of misfolded proteins. Additionally cancer progression is linked to disruptions in protein degradation mechanisms involving Ube2G1 as it influences cell cycle and apoptosis. In cancer Ube2G1 can interact with tumor suppressor proteins like p53 affecting their stability and activity.