Ubiquitin-conjugating enzyme E2 E1 (UBE2E1)

Ubiquitin-conjugating enzyme E2 E1 (UBE2E1) is a human enzyme of the ubiquitin-proteasome system, responsible for attaching ubiquitin from E1 to target proteins, thereby regulating protein degradation, signaling, and various cellular processes[2][3][5]. UBE2E1 participates in both E3-dependent and, in unique cases, E3-independent ubiquitination, including the monoubiquitination of specific substrates[1]. It also mediates ISGylation, the covalent attachment of ISG15, and can catalyze the formation of different polyubiquitin chain types. UBE2E1 is associated with diseases such as immunodeficiency and spinocerebellar ataxia, and its interactions are implicated in neurodegeneration and potentially oncogenic pathways through substrate regulation like PTEN and SETDB1[2][3][6]. It is classified as a member of the E2 ubiquitin-conjugating enzyme family and is essential for normal protein quality control and cellular physiology.

Other names

UBCH6UbcH6Ubiquitin carrier protein E1Ubiquitin-protein ligase E1Ubiquitin conjugating enzyme E2E 1Ubiquitin-conjugating enzyme E2E 1 (UBC4/5 homolog, yeast)Ubiquitin-conjugating enzyme E2E 1 (homologous to yeast UBC4/5)

Ubiquitin-conjugating (E2) enzyme transfers ubiquitin from E1 to substrate, either directly or with E3 ligase; can catalyze certain substrate monoubiquitination independently of E3[1][2][5].