Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence B2RPK0

,


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
1 unknown peptidase 1-211 P NT <%Agarwal et al., 2012[]%>
11 peptidyl-Lys metallopeptidase 1-211 N MS
16 granzyme B (Homo sapiens-type) 2-211 N MS Van Damme et al., 2010
27 peptidyl-Lys metallopeptidase 1-211 N MS
111 peptidyl-Lys metallopeptidase 1-211 N MS
112 lysyl endopeptidase (bacteria) 1-211 N MS
113 peptidyl-Lys metallopeptidase 1-211 N MS
126 peptidyl-Lys metallopeptidase 1-211 N MS
127 peptidyl-Lys metallopeptidase 1-211 N MS
128 trypsin 1 1-211 N MS Schilling & Overall, 2008
130 cathepsin K 128-146 N MS Schilling & Overall, 2008
131 matrix metallopeptidase-2 128-146 N MS Schilling & Overall, 2008
131 glutamyl endopeptidase I 128-146 N MS Schilling & Overall, 2008
140 peptidyl-Lys metallopeptidase 1-211 N MS
146 trypsin 1 1-211 N MS Schilling & Overall, 2008
147 trypsin 1 1-211 N MS Schilling & Overall, 2008