EDE1/YBL047C Summary Help

EDE1 BASIC INFORMATION

Standard Name EDE1 1
Systematic Name YBL047C
Alias BUD15 2
Feature Type ORF, Verified
Description Key endocytic protein involved in a network of interactions with other endocytic proteins, binds membranes in a ubiquitin-dependent manner, may also bind ubiquitinated membrane-associated proteins (1, 3 and see Summary Paragraph)
Name Description EH Domains and Endocytosis 1
GO Annotations All EDE1 GO evidence and references
    View Computational GO annotations for EDE1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Mutant Phenotype All EDE1 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions EDE1 All interactions details and references
68 total interaction(s) for 48 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 19
  • Affinity Capture-RNA: 2
  • Biochemical Activity: 9
  • Co-crystal Structure: 1
  • Co-localization: 1
  • Reconstituted Complex: 2
  • Two-hybrid: 8

Genetic Interactions
  • Phenotypic Suppression: 1
  • Synthetic Growth Defect: 4
  • Synthetic Lethality: 20
  • Synthetic Rescue: 1

Sequence Information
ChrII:132043 to 127898 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 2004-07-16 | Sequence: 1997-01-28
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..4146 132043..127898 2004-07-16 1997-01-28
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000000143

EDE1 RESOURCES

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SGD ORF map
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Expression Summary histogram

SUMMARY PARAGRAPH for EDE1

Ede1p is a key endocytic protein that exhibits a cortical patch membrane localization pattern, and is involved in a network of interactions with other endocytic proteins that localize to membranes. Ede1p comprises a multimodular domain structure including three EH domains, a proline-rich region, coiled coils, and a ubiquitin-associated domain (UBA) (3, 1). The UBA binds membranes in a ubiquitin-dependent manner, and this recruitment of Ede1p to membranes is inhibited by free ubiquitin. Ede1p may also bind ubiquitinated membrane-associated proteins. Both deletion of EDE1 and inactivation of the Ent1p ubiquitin interaction motif are required for a significant endocytic defect (3).

Last updated: 2004-03-28

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for EDE1]

1) Gagny B, et al.  (2000) A novel EH domain protein of Saccharomyces cerevisiae, Ede1p, involved in endocytosis. J Cell Sci 113 ( Pt 18)():3309-19
2) Ni L and Snyder M  (2001) A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae. Mol Biol Cell 12(7):2147-70
3) Aguilar RC, et al.  (2003) The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions. J Biol Chem 278(12):10737-43