Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence Q02878

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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 1-288 P NT <%Agarwal et al., 2012[]%>
90 astacin 87-100 N MS Becker-Pauly et al., 2011
90 meprin alpha subunit 87-100 N MS Becker-Pauly et al., 2011
91 cathepsin B 88-100 N MS Biniossek et al., 2011
114 granzyme A 1-288 N Van Damme et al., 2010
123 granzyme A 1-288 N Van Damme et al., 2010
141 trypsin 1 2-288 N MS Schilling & Overall, 2008
156 trypsin 1 2-288 N MS Schilling & Overall, 2008
192 trypsin 1 2-288 N MS Schilling & Overall, 2008
200 trypsin 1 2-288 N MS Schilling & Overall, 2008
226 trypsin 1 2-288 N MS Schilling & Overall, 2008
229 meprin alpha subunit 2-288 N MS Becker-Pauly et al., 2011
233 meprin beta subunit 2-288 N MS Becker-Pauly et al., 2011
234 meprin alpha subunit 2-288 N MS Becker-Pauly et al., 2011
234 meprin beta subunit 2-288 N MS Becker-Pauly et al., 2011
234 LAST_MAM peptidase (Limulus-type) 231-246 N MS Becker-Pauly et al., 2011
237 trypsin 1 2-288 N MS Schilling & Overall, 2008
262 trypsin 1 2-288 N MS Schilling & Overall, 2008
272 trypsin 1 2-288 N MS Schilling & Overall, 2008
275 cathepsin G 272-285 N MS Schilling & Overall, 2008
277 HIV-1 retropepsin 272-285 N MS Schilling & Overall, 2008
285 trypsin 1 2-288 N MS Schilling & Overall, 2008