Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P18124

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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
8 peptidyl-Lys metallopeptidase 1-248 N MS
9 trypsin 1 1-248 N MS Schilling & Overall, 2008
19 trypsin 1 1-248 N MS Schilling & Overall, 2008
77 granzyme A 1-248 N Van Damme et al., 2010
88 trypsin 1 1-248 N MS Schilling & Overall, 2008
94 trypsin 1 1-248 N MS Schilling & Overall, 2008
134 trypsin 1 1-248 N MS Schilling & Overall, 2008
148 trypsin 1 1-248 N MS Schilling & Overall, 2008
166 trypsin 1 1-248 N MS Schilling & Overall, 2008
177 trypsin 1 1-248 N MS Schilling & Overall, 2008
180 peptidyl-Lys metallopeptidase 1-248 N MS
198 peptidyl-Lys metallopeptidase 1-248 N MS
202 trypsin 1 1-248 N MS Schilling & Overall, 2008
203 glutamyl endopeptidase I 202-212 N MS Schilling & Overall, 2008
212 trypsin 1 1-248 N MS Schilling & Overall, 2008
229 cathepsin L 224-242 N MS Biniossek et al., 2011
229 cathepsin S 224-242 N MS Biniossek et al., 2011
229 cathepsin K 223-242 N MS Schilling & Overall, 2008
229 LAST_MAM peptidase (Limulus-type) 226-242 N MS Becker-Pauly et al., 2011
229 glutamyl endopeptidase I 223-242 N MS Schilling & Overall, 2008
230 astacin 227-242 N MS Becker-Pauly et al., 2011
231 LAST_MAM peptidase (Limulus-type) 228-242 N MS Becker-Pauly et al., 2011
242 trypsin 1 1-248 N MS Schilling & Overall, 2008