Ubiquitin-conjugating enzyme E2 J1 (UBE2J1)

Ubiquitin-conjugating enzyme E2 J1 (UBE2J1) is a tail-anchored E2 enzyme embedded in the ER membrane, functioning as a critical mediator of ER-associated degradation (ERAD). It partners with specific E3 ligases (such as HRD1, RNF26, RNF133) to catalyze the transfer of ubiquitin to misfolded or regulatory substrates, targeting them for degradation via the proteasome. UBE2J1 is essential in processes including maintaining protein quality control in the ER, facilitating recovery from ER stress, antigen presentation, and spermatogenesis. Pathologically, loss or dysregulation of UBE2J1 activity has been implicated in antiandrogen-resistant prostate cancer, defective spermatogenesis leading to male infertility, and increased susceptibility to certain infections. Although no approved drugs currently target UBE2J1 directly, modulation of its activity may represent a promising therapeutic strategy for cancers and other proteinopathies[1][2][3][4].

Other names

HSPC153HSPC205HSU93243NCUBE-1NCUBE1UBC6Ubc6pCGI-76UBC6EYeast ubiquitin conjugating enzyme UBC6 homolog ENon-canonical ubiquitin-conjugating enzyme 1HSUBC6e

Drugs or molecules that target UBE2J1 generally modulate ubiquitination and degradation of specific proteins (e.g., restoring androgen receptor ubiquitination in prostate cancer therapy)[1][3].