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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

eff  -  effete

Drosophila melanogaster

Synonyms: 3527, 6535, CG7425, Dmel\CG7425, E(Pc)88D, ...
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Disease relevance of eff


High impact information on eff

  • The c-Cbl proto-oncogene is a RING family E3 that recognizes activated receptor tyrosine kinases, promotes their ubiquitination by a ubiquitin-conjugating enzyme (E2) and terminates signaling [2].
  • The pattern of telomeric associations observed in UbcD1 mutants suggests strongly that the interphase chromosomes of wild-type larval brain cells maintain a Rab1 orientation within the nucleus, with the telomeres and centromeres segregated to opposite sides of the nucleus [3].
  • The UbcD1 gene encodes a class I ubiquitin-conjugating (E2) enzyme [3].
  • UbcD1, a Drosophila ubiquitin-conjugating enzyme required for proper telomere behavior [3].
  • We therefore suggest that at least one of the targets of UbcD1 ubiquitination is a telomere-associated polypeptide that may help maintain proper chromosomal orientation during interphase [3].

Biological context of eff

  • We show here that five independent mutant alleles in the Drosophila UbcD1 gene cause frequent telomere-telomere attachments during both mitosis and male meiosis that are not seen in wild type [3].
  • By doing a precise open reading frame replacement in the yeast genome we could show that the Drosophila UbcD1 enzyme can functionally substitute for yeast UBC4 [4].
  • Here we report biochemical and genetic characterization of the Drosophila homologue of c-Cbl, a negative regulator of signal transduction with ubiquitin-protein ligase activity [5].
  • We have constructed UbcD1 mutant males carrying terminally deleted X chromosomes devoid of both HeT-A and TART sequences [6].
  • SKPa is component of a Drosophila SCF complex that functions in combination with the ubiquitin-conjugating enzyme UbcD1. skpA null mutation results in centrosome overduplication, unusual chromatin condensation, defective endoreduplication and cell-cycle progression [7].

Anatomical context of eff

  • The Drosophila seven in absentia (sina) gene is required for R7 photoreceptor cell formation during Drosophila eye development, where it functions within the Ras/Raf pathway and targets other proteins for degradation via associations with a ubiquitin-conjugating enzyme [8].
  • In vitro studies with vertebrate proteins demonstrate that the RanGAP1 associated with the nuclear pore complex is modified with small ubiquitin related modifier-1 (SUMO-1) by a ubiquitin-conjugating enzyme (E2 enzyme) [9-15] [9].

Associations of eff with chemical compounds


Physical interactions of eff


Other interactions of eff

  • Our results identify a novel function of Rpr in stimulating DIAP1 auto-ubiquitination through UBCD1, thereby promoting its degradation [11].
  • Taken together, these results suggest that Grim stimulates the poly-ubiquitination and presumably degradation of Diap1 in a novel way by binding to UbcD1 but not to the UBC domain of dBruce as an E2 [12].
  • Female sterile mutations in UbcD1, encoding an E2 ubiquitin-conjugating enzyme, have a similar effect [13].


  1. UBE2A, which encodes a ubiquitin-conjugating enzyme, is mutated in a novel X-linked mental retardation syndrome. Nascimento, R.M., Otto, P.A., de Brouwer, A.P., Vianna-Morgante, A.M. Am. J. Hum. Genet. (2006) [Pubmed]
  2. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Zheng, N., Wang, P., Jeffrey, P.D., Pavletich, N.P. Cell (2000) [Pubmed]
  3. UbcD1, a Drosophila ubiquitin-conjugating enzyme required for proper telomere behavior. Cenci, G., Rawson, R.B., Belloni, G., Castrillon, D.H., Tudor, M., Petrucci, R., Goldberg, M.L., Wasserman, S.A., Gatti, M. Genes Dev. (1997) [Pubmed]
  4. Drosophila UbcD1 encodes a highly conserved ubiquitin-conjugating enzyme involved in selective protein degradation. Treier, M., Seufert, W., Jentsch, S. EMBO J. (1992) [Pubmed]
  5. A Drosophila analogue of v-Cbl is a dominant-negative oncoprotein in vivo. Robertson, H., Hime, G.R., Lada, H., Bowtell, D.D. Oncogene (2000) [Pubmed]
  6. The role of HeT-A and TART retrotransposons in Drosophila telomere capping. Cenci, G., Siriaco, G., Gatti, M. Genetica (2003) [Pubmed]
  7. Identification of the Drosophila skpA gene as a novel target of the transcription factor DREF. Phuong Thao, D.T., Ida, H., Yoshida, H., Yamaguchi, M. Exp. Cell Res. (2006) [Pubmed]
  8. p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1. Matsuzawa, S., Takayama, S., Froesch, B.A., Zapata, J.M., Reed, J.C. EMBO J. (1998) [Pubmed]
  9. The Drosophila semushi mutation blocks nuclear import of bicoid during embryogenesis. Epps, J.L., Tanda, S. Curr. Biol. (1998) [Pubmed]
  10. A novel inflammation-induced ubiquitin E3 ligase in alveolar type II cells. Hu, Y., Nguyen, T.T., Bui, K.C., Demello, D.E., Smith, J.B. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  11. Regulation of Drosophila IAP1 degradation and apoptosis by reaper and ubcD1. Ryoo, H.D., Bergmann, A., Gonen, H., Ciechanover, A., Steller, H. Nat. Cell Biol. (2002) [Pubmed]
  12. Grim stimulates Diap1 poly-ubiquitination by binding to UbcD1. Yoo, S.J. Mol. Cells (2005) [Pubmed]
  13. Cyclin A associates with the fusome during germline cyst formation in the Drosophila ovary. Lilly, M.A., de Cuevas, M., Spradling, A.C. Dev. Biol. (2000) [Pubmed]
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