Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q9R0P9 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
kidney | the enzyme is found in tubular and parietal cells of the kidney and is expressed de novo in injured podocytes. Constitutive UCH-L1 expression in tubulointerstitial and glomerular cells | Mus musculus | - |
podocyte | the enzyme is found in tubular and parietal cells of the kidney and is expressed de novo in injured podocytes | Mus musculus | - |
Synonyms | Comment | Organism |
---|---|---|
ubiquitin C-terminal hydrolase L1 | - |
Mus musculus |
UCH-L1 | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
malfunction | UCH-L1-deficient mice develop proteinuria, without gross changes in glomerular morphology. Tubular cells, endothelial cells, and podocytes show signs of stress with an accumulation of oxidative modified and polyubiquitinated proteins. Mechanistically, abnormal protein accumulation results from an altered proteasome abundance leading to decreased proteasomal activity. UCH-L1-deficient mice exhibit an exacerbated course of disease with increased tubulointerstitial and glomerular damage, acute renal failure, and death, the latter most likely a result of general neurologic impairment | Mus musculus |
metabolism | the enzyme is required for regulated protein degradation through the ubiquitin proteasome system in kidney | Mus musculus |
physiological function | major deubiquitinating enzyme of the nervous system and associated with the development of neurodegenerative diseases | Mus musculus |
physiological function | the enzyme is required for regulated protein degradation in the kidney by controlling proteasome abundance | Mus musculus |