The enzymes of the ubiquitylation pathway play a pivotal role in a number of cellular processes including regulated and targeted proteosomal degradation of substrate proteins. Three classes of enzymes are involved in the process of ubiquitylation; activating enzymes (E1s), conjugating enzymes (E2s) and protein ligases (E3s). UBE2C is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Townsley et al. (1997). UBE2C shares 85% and 61% homology with frog and clam sequences respectively, and contains a 30 amino acid N-terminal extension. UBE2C binds APC11 and APC2 resulting in their autoubiquitylation and proteosomal degradation, a switch in the APC complex which causes sister chromatid separation and exit from mitosis (Rape and Kirschner, 2004; Tang et al., 2001). UBE2C has also been identified as a molecular marker useful in non small cell lung carcinoma (NSCLC) prognosis (Kadara et al., 2009).
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Tang Z, Li B, Bharadwaj R, Zhu H, Ozkan E, Hakala K, Deisenhofer J, Yu H (2001) APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex. Mol Biol Cell 12, 3839-51.
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