Background
The enzymes of the ubiquitylation pathway play a pivotal role in a number of cellular processes including regulated and targeted proteasomal 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). UBE2G1 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Watanabe et al. (1996). UBE2G1 shares 74% sequence identity with UBC7 from C. elegans and a high degree of homology with UBC7 from other species. Expression of UBE2G1 and a helix-loop-helix transcription factor and member of the MYC/MAX superfamily (ROX/MNT) is decreased in medullablastoma tumours. Haploinsufficiency of the human 17p13.3 region is associated with 35% to 50% of medullablastomas, indicating the presence of one or more tumour suppressor genes which have not yet been identified (Cvekl et al., 2004)
References
Cvekl A, Jr., Zavadil J, Birshtein BK, Grotzer MA, Cvekl A (2004) Analysis of transcripts from 17p13.3 in medulloblastoma suggests ROX/MNT as a potential tumour suppressor gene. Eur J Cancer 40, 2525-32.
Watanabe TK, Kawai A, Fujiwara T, Maekawa H, Hirai Y, Nakamura Y, Takahashi E (1996) Molecular cloning of UBE2G, encoding a human skeletal muscle-specific ubiquitin-conjugating enzyme homologous to UBC7 of C. elegans. Cytogenet Cell Genet 74, 146-8.