Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence P27708

,


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 1-2225 P NT <%Agarwal et al., 2012[]%>
155 meprin alpha subunit 152-165 N MS Becker-Pauly et al., 2011
500 trypsin 1 2-2225 N MS Schilling & Overall, 2008
516 trypsin 1 2-2225 N MS Schilling & Overall, 2008
576 matrix metallopeptidase-2 571-592 N MS Schilling & Overall, 2008
592 trypsin 1 2-2225 N MS Schilling & Overall, 2008
789 cathepsin S 782-797 N MS Biniossek et al., 2011
1033 trypsin 1 2-2225 N MS Schilling & Overall, 2008
1048 trypsin 1 2-2225 N MS Schilling & Overall, 2008
1053 trypsin 1 2-2225 N MS Schilling & Overall, 2008
1066 trypsin 1 2-2225 N MS Schilling & Overall, 2008
1100 HtrA2 peptidase 2-2225 P Vande Walle et al., 2007
1143 caspase-3 2-2225 P normal turnover Adam-Klages et al., 1998
1371 caspase-3 2-2225 P normal turnover Adam-Klages et al., 1998
1438 cathepsin B 1435-1450 N MS Biniossek et al., 2011
1722 trypsin 1 2-2225 N MS Schilling & Overall, 2008
1731 trypsin 1 2-2225 N MS Schilling & Overall, 2008