Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence P07205

,


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 1-417 P NT <%Agarwal et al., 2012[]%>
63 matrix metallopeptidase-2 57-75 N MS Schilling & Overall, 2008
74 peptidyl-Lys metallopeptidase 1-417 N MS
75 trypsin 1 2-417 N MS Schilling & Overall, 2008
87 matrix metallopeptidase-2 84-98 N MS Schilling & Overall, 2008
90 peptidyl-Lys metallopeptidase 1-417 N MS
91 cathepsin B 84-105 N MS Biniossek et al., 2011
98 glutamyl endopeptidase I 2-417 N MS Schilling & Overall, 2008
113 astacin 110-123 N MS Becker-Pauly et al., 2011
151 cathepsin L 147-164 N MS Biniossek et al., 2011
151 thrombin 148-164 N MS Schilling & Overall, 2008
156 trypsin 1 2-417 N MS Schilling & Overall, 2008
164 glutamyl endopeptidase I 2-417 N MS Schilling & Overall, 2008
171 trypsin 1 2-417 N MS Schilling & Overall, 2008
372 cathepsin L 366-382 N MS Biniossek et al., 2011
391 matrix metallopeptidase-2 388-406 N MS Schilling & Overall, 2008
393 cathepsin L 389-406 N MS Biniossek et al., 2011
393 cathepsin S 389-403 N MS Biniossek et al., 2011
393 cathepsin B 389-406 N MS Biniossek et al., 2011
394 cathepsin B 389-406 N MS Biniossek et al., 2011
394 elastase-2 388-406 N MS Schilling & Overall, 2008
406 trypsin 1 2-417 N MS Schilling & Overall, 2008