Recombinant Human Ube2G2 protein (His tag)

Supplementary information

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

Ube2G2 also known as Ubiquitin-conjugating enzyme E2 G2 is involved in the ubiquitin-proteasome pathway. This enzyme functions by facilitating the transfer of ubiquitin from E1 activating enzymes to target proteins marking them for degradation. It has a molecular mass of approximately 21 kDa and is expressed in various tissues with noticeable presence in the heart and skeletal muscle. The activity of Ube2G2 is essential for maintaining protein homeostasis in cells.

Biological function summary

Ube2G2 interacts as a part of the ubiquitin-conjugating system forming complexes with E3 ligases like gp78. These complexes determine substrate specificity and enhance the degradation of misfolded or damaged proteins. The function of Ube2G2 in protein degradation is important for cellular processes including cell cycle regulation and stress responses. The enzyme therefore contributes to maintaining cellular integrity by preventing the accumulation of nonfunctional proteins.

Pathways

Ube2G2 plays an integral role in the endoplasmic reticulum-associated degradation (ERAD) pathway which orchestrates the removal of defective proteins from the endoplasmic reticulum. Ube2G2 collaborates with the E3 ligase gp78 and these together facilitate the ubiquitination and subsequent proteasomal degradation of target substrates. Additionally Ube2G2 influences calcium-related signaling pathways impacting cellular calcium homeostasis.

Ube2G2's dysfunction is linked with neurological disorders and cancer. Impairments in Ube2G2 activity may lead to defective ERAD contributing to neurodegenerative disorders through the accumulation of toxic protein aggregates. In cancer altered Ube2G2 expression affects the degradation of oncogenic proteins implicating it in tumorigenesis. In these contexts its interaction with proteins like gp78 becomes significant in understanding how cellular degradation pathways are disrupted.