Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence Q14697

,


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
28 unknown peptidase 1-944 P NT <%Agarwal et al., 2012[]%>
100 trypsin 1 29-944 N MS Schilling & Overall, 2008
109 trypsin 1 29-944 N MS Schilling & Overall, 2008
133 trypsin 1 29-944 N MS Schilling & Overall, 2008
148 trypsin 1 29-944 N MS Schilling & Overall, 2008
173 trypsin 1 29-944 N MS Schilling & Overall, 2008
182 trypsin 1 29-944 N MS Schilling & Overall, 2008
257 cathepsin S 238-267 N MS Biniossek et al., 2011
257 LAST_MAM peptidase (Limulus-type) 254-267 N MS Becker-Pauly et al., 2011
343 cathepsin L 338-354 N MS Biniossek et al., 2011
343 cathepsin S 338-354 N MS Biniossek et al., 2011
343 cathepsin B 338-354 N MS Biniossek et al., 2011
465 cathepsin L 463-472 N MS Biniossek et al., 2011
465 cathepsin S 463-492 N MS Biniossek et al., 2011
602 trypsin 1 29-944 N MS Schilling & Overall, 2008
610 trypsin 1 29-944 N MS Schilling & Overall, 2008
615 cathepsin L 611-627 N MS Biniossek et al., 2011
615 cathepsin S 611-627 N MS Biniossek et al., 2011
691 cathepsin L 685-698 N MS Biniossek et al., 2011