Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P62826

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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 1-216 P NT <%Agarwal et al., 2012[]%>
4 cathepsin S 2-12 N MS Biniossek et al., 2011
12 trypsin 1 2-216 N MS Schilling & Overall, 2008
23 trypsin 1 2-216 N MS Schilling & Overall, 2008
28 lysyl endopeptidase (bacteria) 1-216 N MS
41 cathepsin B 39-50 N MS Biniossek et al., 2011
42 cathepsin B 39-50 N MS Biniossek et al., 2011
46 cathepsin L 39-53 N MS Biniossek et al., 2011
46 cathepsin S 39-53 N MS Biniossek et al., 2011
59 elastase-2 56-71 N MS Schilling & Overall, 2008
60 trypsin 1 2-216 N MS Schilling & Overall, 2008
71 trypsin 1 2-216 N MS Schilling & Overall, 2008
107 matrix metallopeptidase-2 104-119 N MS Schilling & Overall, 2008
110 trypsin 1 2-216 N MS Schilling & Overall, 2008
113 glutamyl endopeptidase I 110-123 N MS Schilling & Overall, 2008
119 chymotrypsin A (cattle-type) 2-216 N MS Schilling & Overall, 2008
123 trypsin 1 2-216 N MS Schilling & Overall, 2008
142 trypsin 1 2-216 N MS Schilling & Overall, 2008
151 peptidyl-Lys metallopeptidase 1-216 N MS
152 trypsin 1 2-216 N MS Schilling & Overall, 2008