Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P08708

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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 1-135 P NT <%Agarwal et al., 2012[]%>
19 lysyl endopeptidase (bacteria) 1-135 N MS
32 lysyl endopeptidase (bacteria) 1-135 N MS
33 trypsin 1 2-135 N MS Schilling & Overall, 2008
35 meprin beta subunit 32-45 N MS Becker-Pauly et al., 2011
44 trypsin 1 2-135 N MS Schilling & Overall, 2008
48 peptidyl-Lys metallopeptidase 1-135 N MS
49 trypsin 1 2-135 N MS Schilling & Overall, 2008
51 cathepsin B 50-59 N MS Biniossek et al., 2011
58 peptidyl-Lys metallopeptidase 1-135 N MS
59 trypsin 1 2-135 N MS Schilling & Overall, 2008
91 granzyme B (Homo sapiens-type) 2-135 N MS Van Damme et al., 2010
92 cathepsin K 88-107 N MS Schilling & Overall, 2008
92 granzyme B (Homo sapiens-type) 2-135 N MS Van Damme et al., 2010
107 trypsin 1 2-135 N MS Schilling & Overall, 2008
110 glutamyl endopeptidase I 107-129 N MS Schilling & Overall, 2008
116 matrix metallopeptidase-2 110-135 N MS Schilling & Overall, 2008
129 trypsin 1 2-135 N MS Schilling & Overall, 2008