| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 5.6.2.7 | cytoplasm | - |
Mammalia | 5737 | - |
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.6.2.7 | Mammalia | - |
- |
- |
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.6.2.7 | Dbp5 | - |
Mammalia |
| 5.6.2.7 | DEAD-box RNA helicase Dbp5 | - |
Mammalia |
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.6.2.7 | metabolism | Dbp5 aids shuttling RNAs from export to translation, process overview, modelling. Dbp5 participates in cytoplasmic mRNA quality control | Mammalia |
| 5.6.2.7 | additional information | the N-terminal extension of Dbp5 is able to fold in-or outward of the helicase core, therefore allowing or disrupting the formation of the catalytic center of the enzyme. While nucleotide-free Dbp5 exhibits an open conformation, the binding of ATP leads to the inward folding of the N-terminal extension. The association of mRNA and the cofactor Gle1-IP6 induces the displacement of the N-terminal extension and closure of the cleft between the helicase domains, resulting in the formation of the catalytic center. Dbp5-ADP is recycled at the NPC by the nucleoporin Nup159, resulting in the release of ADP and positioning the helicase for the next remodeling event. Reaction mechanism and mechanism of ranslocation of ribosomal subunits, overview | Mammalia |
| 5.6.2.7 | physiological function | in order to prevent mRNPs from reentering the nucleus, it is important to establish a distinct export directionality. This is facilitated by the DEAD-box RNA helicase Dbp5/Rat8, which remodels mRNP complexes at the cytoplasmic side of the NPC. Dbp5 is involved in the export of ribosomal subunits. Key function for Dbp5 in translation termination, which identifies this helicase as a master regulator of mRNA expression. At the cytoplasmic site of the nuclear pore complex, the export receptor is displaced by the action of the DEAD-box RNA helicase Dbp5. Subsequent quality control of the open reading frame requires translation. Involvement of Dbp5 in cytoplasmic no-go-and non-stop decay | Mammalia |