National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory
Protein Information |
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| Protein Name | Ubiquitin conjugation factor E4 ufd-2 |
| Accession Code | Q09349 |
| Gene | ufd |
| Organism | Caenorhabditis elegans (Taxonomy: 6239) |
| Part of Reference Proteome? | Yes |
| Sequence (Length: 984) |
Description |
Position in the Nuclear Envelope |
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|---|---|---|
| Location | Location ID | Description |
| Nuclear Envelope | SL-0178 | The nuclear envelope is a membrane system which surrounds the nucleoplasm of eukaryotic cells. It is composed of the nuclear lamina, nuclear pore complexes and two nuclear membranes. The space between the two membranes is called the nuclear intermembrane space. |
| Nuclear Membrane | SL-0182 | The membrane surrounding the nucleus. This term is used when it is not known if the protein is found in or associated with the inner or outer nuclear membrane. | Membrane Topology |
| Topology | Source | Annotation Type |
| Peripheral | UniProt | Experimental Evidence {ECO:0000269|PubMed:27669035} | Assigned Ontology terms |
Description |
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|---|---|
| Acts as an E4 ubiquitin ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (PubMed:27669035). The elongation of preexisting ubiquitin chains preferentially targets ubiquitin 'Lys-29' and 'Lys-48' residues (PubMed:27669035). Also functions as an E3 ligase in conjunction with specific E1 and E2 ligases (PubMed:15294159, PubMed:27669035, PubMed:29396393). Probably by regulating protein ubiquitination at DNA damage repair sites, coordinates DNA double- strand-break repair and apoptosis in the germline (PubMed:27669035). Required for germline apoptosis in response to DNA damage downstream of cep-1 (PubMed:27669035). Involved in the resolution of DNA-repair sites by promoting the release of rad-51 from DNA damage foci (PubMed:27669035). In association with protein-ligase chn-1, acts as an E3/E4 ligase to poly-ubiquitinate lysine residues in the UCS domain of myosin chaperone unc-45 (PubMed:15294159, PubMed:29396393). By targeting myosin chaperone unc-45 for proteasomal degradation, regulates myosin assembly in body wall muscles in association with cdc- 48.1 and chn-1 (PubMed:15294159, PubMed:17369820). However, in a contrasting study, acts as an E3 ligase, independently of chn-1, to poly-ubiquitinate unc-45 without promoting unc-45 proteasomal degradation (PubMed:29396393). Instead, uses unc-45 as an adapter protein to recruit and poly-ubiquitinate unfolded myosin heavy chain B unc-54 (PubMed:29396393). {Experimental EvidencePubMed:15294159, Experimental EvidencePubMed:17369820, Experimental EvidencePubMed:27669035, Experimental EvidencePubMed:29396393}. | Assigned Ontology terms |
Interactions with other proteins (2 interactors) |
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National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory