Searches of the MEROPS database
Display Known Cleavages for a Protein
Please enter a UniProt accession (eg P05067):
Sequence P04632
,
Click here to display alignment and conservation of cleavage sites of this sequence with close homologues. This will take a few moments.
Peptide and protein substrates that are thought to be physiologically relevant are indicated by P. Peptide and protein substrates that are not physiologically relevant are indicated by N. How cleavage sites have been identified are indicated by the following evidence codes: NT = N-terminal sequencing, MS = mass spectroscopy, MU = mutation, CS = consensus sequence, LC = liquid chromatography. To see all annotated cleavages for a peptidase, click on the peptidase name.
| Cleavage Site | Peptidase | Residue range | Cleavage type | Description | Evidence | Reference |
|---|---|---|---|---|---|---|
| 33 | cathepsin S | 10-60 | N | MS | Biniossek et al., 2011 | |
| 34 | cathepsin L | 10-60 | N | MS | Biniossek et al., 2011 | |
| 34 | cathepsin S | 10-60 | N | MS | Biniossek et al., 2011 | |
| 38 | cathepsin L | 28-65 | N | MS | Biniossek et al., 2011 | |
| 64 | matrix metallopeptidase-2 | 60-84 | N | MS | Schilling & Overall, 2008 | |
| 84 | trypsin 1 | 1-268 | N | MS | Schilling & Overall, 2008 | |
| 89 | LAST peptidase (Limulus-type) | 86-99 | N | MS | Becker-Pauly et al., 2011 | |
| 99 | trypsin 1 | 1-268 | N | MS | Schilling & Overall, 2008 |
