Ubiquitin-conjugating enzyme E2 L5 (UBE2L5)

Ubiquitin-conjugating enzyme E2 L5 (UBE2L5) is a member of the E2 family of enzymes, which play a central role in the ubiquitination pathway. UBE2L5 catalyzes the transfer of ubiquitin from E1 (activating enzymes) to substrate proteins, usually in concert with an E3 (ligase), marking them for proteasomal degradation or altering their cellular function. This enzyme is predicted to participate in K11-linked ubiquitination and is primarily active in the nucleus. An important paralog is UBE2L3. UBE2L5 is part of the overall ubiquitin-proteasome system that regulates protein turnover and quality control in cells. There are no well-documented direct disease roles, interacting drugs, or safety concerns specifically associated with UBE2L5 as of current knowledge.

Other names

UBE2L5Ubiquitin-protein ligase L5UBCH7N2UBE2L5Pubiquitin-conjugating enzyme E2 L5ubiquitin-protein ligase L5

Conjugation of ubiquitin to substrate proteins (via interaction with E1 and E3 enzymes)