Cloned (Comment) | Organism |
---|---|
mutants with changed active-site residues and lacking propeptides and N-glycosylation, expressed in human embryonic kidney 293T cells | Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
D98A/D283A | mutant enzyme has no catalytic activity on either protein or synthetic substrates. In contrast with wild-type cathepsin E, the mutant enzyme is neither processed nor matured even after a 24-h chase period, but stably remains as a 46000 Da precursor | Rattus norvegicus |
N324D | N-glycosylation-deficient mutant is neither processed into a mature form nor transported to the endosomal compartement, but is stable retained in the endoplasmic reticulum without degradation | Rattus norvegicus |
N92Q | N-glycosylation-deficient mutant is neither processed into a mature form nor transported to the endosomal compartement, but is stable retained in the endoplasmic reticulum without degradation | Rattus norvegicus |
N92Q/N374D | N-glycosylation-deficient mutant is neither processed into a mature form nor transported to the endosomal compartement, but is stable retained in the endoplasmic reticulum without degradation | Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
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Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | N-glycosylation of cathepsin E plays an important role in its processing, maturation and trafficking to the appropriate destination in the cells, but is not necessarily essential for its correct folding | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
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