Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence Q96AE4

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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 1-644 P NT <%Agarwal et al., 2012[]%>
13 cathepsin B 2-32 N MS Biniossek et al., 2011
101 meprin alpha subunit 2-644 N MS Becker-Pauly et al., 2011
101 meprin beta subunit 2-644 N MS Becker-Pauly et al., 2011
102 meprin beta subunit 2-644 N MS Becker-Pauly et al., 2011
128 meprin alpha subunit 2-644 N MS Becker-Pauly et al., 2011
128 meprin beta subunit 2-644 N MS Becker-Pauly et al., 2011
146 trypsin 1 1-644 N MS Schilling & Overall, 2008
161 trypsin 1 1-644 N MS Schilling & Overall, 2008
221 cathepsin L 219-236 N MS Biniossek et al., 2011
223 cathepsin L 219-236 N MS Biniossek et al., 2011
223 cathepsin S 219-236 N MS Biniossek et al., 2011
224 LAST_MAM peptidase (Limulus-type) 221-236 N MS Becker-Pauly et al., 2011
271 trypsin 1 1-644 N MS Schilling & Overall, 2008
284 trypsin 1 1-644 N MS Schilling & Overall, 2008
377 meprin beta subunit 373-387 N MS Becker-Pauly et al., 2011
448 cathepsin L 441-464 N MS Biniossek et al., 2011
574 LAST_MAM peptidase (Limulus-type) 571-584 N MS Becker-Pauly et al., 2011
584 trypsin 1 1-644 N MS Schilling & Overall, 2008
591 trypsin 1 1-644 N MS Schilling & Overall, 2008