Searches of the MEROPS database
Display Known Cleavages for a Protein
Please enter a UniProt accession (eg P05067):
Sequence P02687
,
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 |
| 14 |
ADAM17 peptidase |
1-169 |
P |
|
|
Chesneau et al., 2003 |
| 16 |
calpain-1 |
1-169 |
P |
|
|
Tsubata & Takahashi, 1989 |
| 16 |
calpain-2 |
1-169 |
P |
|
|
Tsubata & Takahashi, 1989 |
| 16 |
ADAM28 peptidase (mouse-type) |
1-169 |
P |
|
|
Blobel, 2004 |
| 16 |
ADAM10 peptidase |
1-169 |
P |
|
|
Chesneau et al., 2003 |
| 16 |
ADAM19 peptidase |
1-169 |
P |
|
|
Chesneau et al., 2003 |
| 16 |
ADAM17 peptidase |
1-169 |
P |
|
|
Chesneau et al., 2003 |
| 16 |
ADAM28 peptidase (Homo sapiens-type) |
1-169 |
N |
|
|
Howard et al., 2001 |
| 36 |
cathepsin D |
1-169 |
P |
normal turnover |
|
Whitaker & Seyer, 1979 |
| 42 |
cathepsin D |
1-169 |
P |
normal turnover |
|
Whitaker & Seyer, 1979 |
| 42 |
angiotensin-converting enzyme peptidase unit 2 |
1-169 |
N |
|
|
Amour et al., 1999 |
| 62 |
ADAM28 peptidase (mouse-type) |
1-169 |
P |
|
|
Blobel, 2004 |
| 62 |
ADAM10 peptidase |
1-169 |
P |
|
|
Chesneau et al., 2003 |
| 63 |
ADAM17 peptidase |
1-169 |
P |
|
|
Chesneau et al., 2003 |
| 68 |
calpain-1 |
1-169 |
P |
|
|
Tsubata & Takahashi, 1989 |
| 68 |
calpain-2 |
1-169 |
P |
|
|
Tsubata & Takahashi, 1989 |
| 71 |
ADAM28 peptidase (mouse-type) |
1-169 |
P |
|
|
Blobel, 2004 |
| 71 |
ADAM8 peptidase |
1-169 |
P |
|
|
Schlomann et al., 2002 |
| 71 |
ADAM10 peptidase |
1-169 |
P |
|
|
Chesneau et al., 2003 |
| 71 |
ADAM19 peptidase |
1-169 |
P |
|
|
Chesneau et al., 2003 |
| 71 |
ADAM28 peptidase (Homo sapiens-type) |
1-169 |
N |
|
|
Howard et al., 2001 |
| 73 |
ADAM19 peptidase |
1-169 |
P |
|
|
Chesneau et al., 2003 |
| 88 |
cathepsin D |
1-169 |
P |
normal turnover |
|
Whitaker & Seyer, 1979 |
| 88 |
angiotensin-converting enzyme peptidase unit 2 |
1-169 |
N |
|
|
Amour et al., 1999 |
| 88 |
ADAM17 peptidase |
1-169 |
P |
|
|
Chesneau et al., 2003 |
| 91 |
cathepsin D |
1-169 |
P |
normal turnover |
|
Whitaker & Seyer, 1979 |
| 93 |
calpain-1 |
1-169 |
P |
|
|
Tsubata & Takahashi, 1989 |
| 93 |
calpain-2 |
1-169 |
P |
|
|
Tsubata & Takahashi, 1989 |
| 96 |
calpain-1 |
1-169 |
P |
|
|
Tsubata & Takahashi, 1989 |
| 96 |
calpain-2 |
1-169 |
P |
|
|
Tsubata & Takahashi, 1989 |
| 106 |
ADAM28 peptidase (mouse-type) |
1-169 |
P |
|
|
Blobel, 2004 |
| 106 |
ADAM28 peptidase (Homo sapiens-type) |
1-169 |
N |
|
|
Howard et al., 2001 |
| 110 |
ADAM19 peptidase |
1-169 |
P |
|
|
Chesneau et al., 2003 |
| 135 |
ADAM19 peptidase |
1-169 |
P |
|
|
Chesneau et al., 2003 |