Recombinant Human UBE2J2 protein

Supplementary information

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

UBE2J2 also known as UBC6e is an E2 ubiquitin-conjugating enzyme with a molecular mass of around 35 kDa. It is involved in the ubiquitination process transferring ubiquitin from an E1 activating enzyme to a substrate often marking the substrate for degradation by the proteasome. UBE2J2 localizes primarily in the endoplasmic reticulum (ER) membrane but you can also find it distributed in other cellular membranes.

Biological function summary

The ubiquitin-conjugating enzyme UBE2J2 plays a role in protein quality control helping in the ER-associated degradation (ERAD) pathway. This process is important for maintaining cellular homeostasis by degrading misfolded or improperly assembled proteins. UBE2J2 may function in conjunction with other proteins like E3 ligases to form a complete complex required for the ubiquitination and subsequent degradation of target proteins.

Pathways

The enzyme UBE2J2 integrates with the ERAD pathway a significant component of the protein degradation system in cells. It also interacts with the ubiquitin-proteasome pathway which is important for degrading unwanted and misfolded proteins. UBE2J2 has shown interaction with several E3 ligases such as Hrd1 which facilitates the transfer of ubiquitin onto target substrates. This integration ensures the quality control of proteins within the ER.

Mutations or dysregulations in UBE2J2 can contribute to neurodegenerative diseases like Parkinson's disease due to its role in protein degradation. The impaired function and accumulation of misfolded proteins can exacerbate these conditions. Additionally cancer research has shown that overexpression of UBE2J2 might be linked to tumor progression such as in hepatocellular carcinoma. Its connection with proteins like p53 is critical as p53 is known to be a tumor suppressor and its regulation can be influenced by UBE2J2 activity.