EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.4.22.B30 | ATP synthase beta + H2O |
- |
Mus musculus |
? |
- |
? |
| 3.4.22.B30 | ATP synthase beta + H2O |
- |
Rattus norvegicus |
? |
- |
? |
| 3.4.22.B30 | FITC-casein + H2O |
in the presence of CaCl2 |
Oryctolagus cuniculus |
FITC + casein |
- |
? |
| 3.4.22.B30 | FITC-casein + H2O |
in the presence of CaCl2 |
Rattus norvegicus |
FITC + casein |
- |
? |
| 3.4.22.B30 | more |
DAP13 (13 kDa differentiation-associated protein) is not hydrolyzed by calpain 10 in the presence of CaCl2 |
Oryctolagus cuniculus |
? |
- |
? |
| 3.4.22.B30 | more |
DAP13 (13 kDa differentiation-associated protein) is not hydrolyzed by calpain 10 in the presence of CaCl2 |
Rattus norvegicus |
? |
- |
? |
| 3.4.22.B30 | more |
mitochondrial calpain 10 is required for cell viability. Calpain 10 levels specifically decrease in aging human kidney tissue when renal function decreases, suggesting that calpain 10 is required for renal function and is a biomarker of the aging kidney |
Homo sapiens |
? |
- |
? |
| 3.4.22.B30 | more |
mitochondrial calpain 10 is required for cell viability. Calpain 10 levels specifically decrease in aging rat kidney tissue when renal function decreases, suggesting that calpain 10 is required for renal function and is a biomarker of the aging kidney |
Rattus norvegicus |
? |
- |
? |
| 3.4.22.B30 | more |
mitochondrial calpain 10 is required for cell viability. Calpain 10 levels specifically decreases in aging mouse kidney tissue when renal function decreases, suggesting that calpain 10 is required for renal function and is a biomarker of the aging kidney |
Mus musculus |
? |
- |
? |
| 3.4.22.B30 | more |
none of the calpain-10 proteins purified from different sources has putative proteolytic activity under in vitro conditions when examined using different peptide substrates, including more than 70 in vitro translated, radiolabeled oligopeptides. Calpain-10 may require a special intracellular localization or interacting partner(s) to acquire proteolytic activity, or it may functions by interacting with other proteins rather than through its proteolytic activity |
Homo sapiens |
? |
- |
? |
