Searches of the MEROPS database
Display Known Cleavages for a Protein
Please enter a UniProt accession (eg P05067):
Sequence P29966
,
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 |
|---|
| 1 |
unknown peptidase |
1-332 |
P |
|
NT |
<%Agarwal et al., 2012[]%> |
| 11 |
trypsin 1 |
2-332 |
N |
|
MS |
Schilling & Overall, 2008 |
| 30 |
trypsin 1 |
2-332 |
N |
|
MS |
Schilling & Overall, 2008 |
| 40 |
trypsin 1 |
2-332 |
N |
|
MS |
Schilling & Overall, 2008 |
| 55 |
trypsin 1 |
2-332 |
N |
|
MS |
Schilling & Overall, 2008 |
| 85 |
matrix metallopeptidase-2 |
69-105 |
N |
|
MS |
Schilling & Overall, 2008 |
| 86 |
peptidyl-Lys metallopeptidase |
1-332 |
N |
|
MS |
|
| 87 |
trypsin 1 |
2-332 |
N |
|
MS |
Schilling & Overall, 2008 |
| 92 |
matrix metallopeptidase-2 |
87-105 |
N |
|
MS |
Schilling & Overall, 2008 |
| 94 |
LAST_MAM peptidase (Limulus-type) |
91-105 |
N |
|
MS |
Becker-Pauly et al., 2011 |
| 104 |
peptidyl-Lys metallopeptidase |
1-332 |
N |
|
MS |
|
| 105 |
trypsin 1 |
2-332 |
N |
|
MS |
Schilling & Overall, 2008 |
| 124 |
meprin beta subunit |
121-137 |
N |
|
MS |
Becker-Pauly et al., 2011 |
| 137 |
trypsin 1 |
2-332 |
N |
|
MS |
Schilling & Overall, 2008 |
| 152 |
trypsin 1 |
2-332 |
N |
|
MS |
Schilling & Overall, 2008 |
| 153 |
trypsin 1 |
2-332 |
N |
|
MS |
Schilling & Overall, 2008 |
| 165 |
cathepsin B |
2-332 |
P |
normal turnover |
|
Spizz & Blackshear, 1997 |
| 165 |
trypsin 1 |
2-332 |
N |
|
MS |
Schilling & Overall, 2008 |
| 168 |
cathepsin B |
2-332 |
P |
normal turnover |
|
Spizz & Blackshear, 1997 |
| 172 |
trypsin 1 |
2-332 |
N |
|
MS |
Schilling & Overall, 2008 |
| 173 |
lysyl endopeptidase (bacteria) |
1-332 |
N |
|
MS |
|
| 176 |
trypsin 1 |
2-332 |
N |
|
MS |
Schilling & Overall, 2008 |
| 193 |
trypsin 1 |
2-332 |
N |
|
MS |
Schilling & Overall, 2008 |
| 227 |
glutamyl endopeptidase I |
193-256 |
N |
|
MS |
Schilling & Overall, 2008 |
| 241 |
cathepsin S |
194-256 |
N |
|
MS |
Biniossek et al., 2011 |
| 241 |
glutamyl endopeptidase I |
193-256 |
N |
|
MS |
Schilling & Overall, 2008 |
| 242 |
cathepsin S |
194-256 |
N |
|
MS |
Biniossek et al., 2011 |
| 242 |
cathepsin G |
193-256 |
N |
|
MS |
Schilling & Overall, 2008 |
| 243 |
cathepsin S |
239-256 |
N |
|
MS |
Biniossek et al., 2011 |
| 256 |
trypsin 1 |
2-332 |
N |
|
MS |
Schilling & Overall, 2008 |
