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Literature summary for 3.4.21.98 extracted from
- Quantitative proteomics identifies the membrane-associated peroxidase GPx8 as a cellular substrate of the hepatitis C virus NS3-4A protease (2014), Hepatology, 59, 423-433.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Hepacivirus C | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| peroxidase GPx8 + H2O | - |
Hepacivirus C | ? | membrane-associated peroxidase GPx8 is a cellular substrate of the hepatitis C virus NS3-4A protease. Cleavage by NS3-4A occurs at Cys11, removing the cytosolic tip of GPx8, and is observed in different experimental systems as well as in liver biopsies from patients with chronic HCV | ? |  |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | membrane-associated peroxidase GPx8 is a cellular substrate of the hepatitis C virus NS3-4A protease. GPx8 is involved in viral particle production but not in HCV entry or RNA replication | Hepacivirus C |
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Release 2023.1 (January 2023)
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