| First Author | Yasugi T | Year | 1996 |
| Journal | Nucleic Acids Res | Volume | 24 |
| Issue | 11 | Pages | 2005-10 |
| PubMed ID | 8668529 | Mgi Jnum | J:46869 |
| Mgi Id | MGI:1202179 | Doi | 10.1093/nar/24.11.2005 |
| Citation | Yasugi T, et al. (1996) Identification of the structural and functional human homolog of the yeast ubiquitin conjugating enzyme UBC9. Nucleic Acids Res 24(11):2005-10 |
| abstractText | Ubiquitin conjugating enzymes (UBCs) are a family of proteins directly involved in ubiquitination of proteins. Ubiquitination is known to be involved in control of a variety of cellular processes, including cell proliferation, through the targeting of key regulatory proteins for degradation. The ubc9 gene of the yeast Saccharomyces cerevisiae (Scubc9) is an essential gene which is required for cell cycle progression and is involved in the degradation of S phase and M phase cyclins. We have identified a human homolog of Scubc9 (termed hubc9) using the two hybrid screen for proteins that interact with the human papillomavirus type 16 E1 replication protein. The hubc9 encoded protein shares a very high degree of amino acid sequence similarity with ScUBC9 and with the homologous hus5+ gene product of Schizosaccharomyces pombe. Genetic complementation experiments in a S.cerevisiae ubc9ts mutant reveal that hUBC9 can substitute for the function of ScUBC9 required for cell cycle progression. |
