Ubiquitin-conjugating enzyme E2 J2 (UBE2J2)

Ubiquitin-conjugating enzyme E2 J2 (UBE2J2) is an ER-associated E2 class enzyme that catalyzes the covalent attachment of ubiquitin to proteins as part of the ubiquitin-proteasome system[1][3][5]. It primarily participates in endoplasmic reticulum-associated degradation (ERAD), working in concert with specific E3 ligases, such as mK3, to facilitate the clearance of misfolded or unassembled membrane and secretory proteins from the ER[1]. Unlike canonical E2s, UBE2J2 can catalyze ubiquitination on both lysine and hydroxylated amino acids (serine, threonine), frequently forming K48-linked ubiquitin chains that target substrates for proteasomal degradation[1]. Its function is essential for protein homeostasis, and dysregulation of UBE2J2 can lead to impaired ERAD, contributing to ER stress and associated diseases[3][4]. UBE2J2 is considered a therapeutic target due to its central role in regulated protein degradation, but specific modulators, biomarkers, or approved drugs are not currently described in publicly available data[3][4][5].

Other names

UBE2J2NCUBE2NCUBE-2Ubc6pE2 ubiquitin-conjugating enzyme J2Non-canonical ubiquitin-conjugating enzyme 2PRO2121UBC6yeast UBC6 homolog

Catalyzes the transfer of ubiquitin from the E1 activating enzyme to target proteins, working with E3 ligases; initiates ubiquitin chain assembly (such as K48-linked chains). Facilitates the degradation of misfolded or excess proteins in the ER.