Ubiquitin-conjugating enzyme E2 C (UBE2C) (UBE2C)

Ubiquitin-conjugating enzyme E2 C (UBE2C) is a critical regulator of the cell cycle, specifically facilitating the transition from metaphase to anaphase. It functions as an E2 enzyme that works in conjunction with the Anaphase-Promoting Complex/Cyclosome (APC/C) to ubiquitinate and trigger the degradation of key mitotic regulators, such as cyclin B1 and securin (UniProt P22567). In many human malignancies, UBE2C is significantly overexpressed, which leads to uncontrolled cell proliferation and genomic instability (PMID: 30106350). Consequently, high levels of UBE2C mRNA and protein are frequently used as prognostic biomarkers for poor clinical outcomes in cancers like breast, lung, and gastric carcinoma (PMID: 25103498). From a therapeutic perspective, UBE2C is an attractive target; its activity can be inhibited by small molecules like NSC697923, which covalently binds to its active site, or its expression can be silenced using RNA interference (RNAi) technologies (PMID: 21460847). Targeting UBE2C aims to arrest the cell cycle in mitosis, thereby inducing apoptosis in cancer cells.

Other names

UBCH10Ubiquitin-conjugating enzyme E2CdJ447F3.2

Inhibition of the ubiquitin-conjugating activity by targeting the active site cysteine residue, or degradation of mRNA transcripts via RNA interference.