Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P62701

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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 1-263 P NT <%Agarwal et al., 2012[]%>
15 peptidyl-Lys metallopeptidase 1-263 N MS
21 granzyme B (Homo sapiens-type) 1-263 P MS Van Damme et al., 2009
21 granzyme B, rodent-type 1-263 N MS Van Damme et al., 2009
52 peptidyl-Lys metallopeptidase 1-263 N MS
85 matrix metallopeptidase-2 77-100 N MS Schilling & Overall, 2008
87 LAST_MAM peptidase (Limulus-type) 84-100 N MS Becker-Pauly et al., 2011
91 meprin alpha subunit 88-100 N MS Becker-Pauly et al., 2011
99 chymotrypsin A (cattle-type) 2-263 N MS Schilling & Overall, 2008
100 trypsin 1 2-263 N MS Schilling & Overall, 2008
117 granzyme B (Homo sapiens-type) 2-263 N MS Plasman et al., 2011
127 trypsin 1 2-263 N Van Damme et al., 2009
133 peptidyl-Lys metallopeptidase 1-263 N MS
154 peptidyl-Lys metallopeptidase 1-263 N MS
155 trypsin 1 2-263 N MS Schilling & Overall, 2008
163 HIV-1 retropepsin 155-174 N MS Schilling & Overall, 2008
168 trypsin 1 2-263 N MS Schilling & Overall, 2008
174 trypsin 1 2-263 N MS Schilling & Overall, 2008
203 cathepsin L 201-211 N MS Biniossek et al., 2011
242 lysyl endopeptidase (bacteria) 1-263 N MS