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FB:eff

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Contents

Species (Taxon ID) Drosophila melanogaster (fruit fly) (taxon:7227)
Gene Name(s) eff ( synonyms: 3527, 6535, CG7425, E(Pc)88D, EFF, Eff, Effete, SS3-3, Suppressor of GMR-sina 3-3, UBC4, UBCD-1, UBCD1, Ubc-D1, UbcD, UbcD1, Ubiquitin conjugating enzyme 1, anon-WO0118547.343, effette, fs(3)01295, l(3)01462, l(3)j2C8, l(3)s1782, mei68, meiotic 68, ms(3)01295, ms(3)1, ms(3)3, ms(3)88D, ms(3)neo2, ms(3)ry1, ms(3)ry3, ubcD1 )
Protein Name(s) effete,
External Links
FB FBgn0011217

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0001745

compound eye morphogenesis

FB:FBrf0100609
PMID:9475739[1]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0001751

compound eye photoreceptor cell differentiation

FB:FBrf0155951
PMID:12215542[2]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0004842

ubiquitin-protein ligase activity

FB:FBrf0055959
PMID:1310935[3]

IGI: Inferred from Genetic Interaction

SGD:S000000286
SGD:S000002466

F

From FB

GO:0004842

ubiquitin-protein ligase activity

FB:FBrf0055959
PMID:1310935[3]

ISS: Inferred from Sequence or Structural Similarity

SGD:S000000286

F

From FB

GO:0004842

ubiquitin-protein ligase activity

FB:FBrf0055959
PMID:1310935[3]

ISS: Inferred from Sequence or Structural Similarity

SGD:S000002466

F

From FB

GO:0004842

ubiquitin-protein ligase activity

FB:FBrf0123869

NAS: Non-traceable Author Statement

F

From FB

GO:0004842

ubiquitin-protein ligase activity

FB:FBrf0167429
PMID:14644196[4]

TAS: Traceable Author Statement

F

From FB

GO:0005515

protein binding

FB:FBrf0098364
PMID:9267026[5]

IPI: Inferred from Physical Interaction

FB:FBgn0003410

F

From FB

GO:0005875

microtubule associated complex

FB:FBrf0204649
PMID:18433294[6]

IDA: Inferred from Direct Assay

C

From FB

GO:0006511

ubiquitin-dependent protein catabolic process

FB:FBrf0055959
PMID:1310935[3]

IGI: Inferred from Genetic Interaction

SGD:S000000286
SGD:S000002466

P

From FB

GO:0007067

mitosis

FB:FBrf0093291
PMID:9106658[7]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0007140

male meiosis

FB:FBrf0093291
PMID:9106658[7]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0007286

spermatid development

FB:FBrf0064394
PMID:8244010[8]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0008054

cyclin catabolic process

FB:FBrf0209346
PMID:19906849[9]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0016322

neuron remodeling

FB:FBrf0195405
PMID:16880123[10]

IDA: Inferred from Direct Assay

P

From FB

GO:0016567

protein ubiquitination

FB:FBrf0055959
PMID:1310935[3]

ISS: Inferred from Sequence or Structural Similarity

SGD:S000000286

P

From FB

GO:0016567

protein ubiquitination

FB:FBrf0055959
PMID:1310935[3]

ISS: Inferred from Sequence or Structural Similarity

SGD:S000002466

P

From FB

GO:0016567

protein ubiquitination

FB:FBrf0167429
PMID:14644196[4]

TAS: Traceable Author Statement

P

From FB

GO:0016567

protein ubiquitination

FB:FBrf0209346
PMID:19906849[9]

IDA: Inferred from Direct Assay

P

From FB

GO:0022008

neurogenesis

FB:FBrf0214431

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0030718

germ-line stem cell maintenance

FB:FBrf0209346
PMID:19906849[9]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0031647

regulation of protein stability

FB:FBrf0209346
PMID:19906849[9]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0045676

regulation of R7 cell differentiation

FB:FBrf0155951
PMID:12215542[2]

IGI: Inferred from Genetic Interaction

FB:FBgn0003410

P

From FB

GO:0048132

female germ-line stem cell division

FB:FBrf0209346
PMID:19906849[9]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0048477

oogenesis

FB:FBrf0132360
PMID:11131529[11]

TAS: Traceable Author Statement

P

From FB

GO:0051276

chromosome organization

FB:FBrf0093291
PMID:9106658[7]

IMP: Inferred from Mutant Phenotype

P

From FB


Notes

References

See Help:References for how to manage references in GONUTS.
  1. Neufeld TP et al. (1998) A genetic screen to identify components of the sina signaling pathway in Drosophila eye development. Genetics 148: 277-86 PubMed GONUTS page
  2. 2.0 2.1 Li S et al. (2002) Phyllopod acts as an adaptor protein to link the sina ubiquitin ligase to the substrate protein tramtrack. Mol Cell Biol 22: 6854-65 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 3.5 Treier M et al. (1992) Drosophila UbcD1 encodes a highly conserved ubiquitin-conjugating enzyme involved in selective protein degradation. EMBO J 11: 367-72 PubMed GONUTS page
  4. 4.0 4.1 Bergmann A et al. (2003) Regulators of IAP function: coming to grips with the grim reaper. Curr Opin Cell Biol 15: 717-24 PubMed GONUTS page
  5. Tang AH et al. (1997) PHYL acts to down-regulate TTK88, a transcriptional repressor of neuronal cell fates, by a SINA-dependent mechanism. Cell 90: 459-67 PubMed GONUTS page
  6. Hughes JR et al. (2008) A microtubule interactome: complexes with roles in cell cycle and mitosis. PLoS Biol 6: e98 PubMed GONUTS page
  7. 7.0 7.1 7.2 Cenci G et al. (1997) UbcD1, a Drosophila ubiquitin-conjugating enzyme required for proper telomere behavior. Genes Dev 11: 863-75 PubMed GONUTS page
  8. Castrillon DH et al. (1993) Toward a molecular genetic analysis of spermatogenesis in Drosophila melanogaster: characterization of male-sterile mutants generated by single P element mutagenesis. Genetics 135: 489-505 PubMed GONUTS page
  9. 9.0 9.1 9.2 9.3 9.4 Chen D et al. (2009) Effete-mediated degradation of Cyclin A is essential for the maintenance of germline stem cells in Drosophila. Development 136: 4133-42 PubMed GONUTS page
  10. Kuo CT et al. (2006) Identification of E2/E3 ubiquitinating enzymes and caspase activity regulating Drosophila sensory neuron dendrite pruning. Neuron 51: 283-90 PubMed GONUTS page
  11. Deng W & Lin H (2001) Asymmetric germ cell division and oocyte determination during Drosophila oogenesis. Int Rev Cytol 203: 93-138 PubMed GONUTS page
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