Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence Q32P51

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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
20 matrix metallopeptidase-2 15-31 N MS Schilling & Overall, 2008
31 trypsin 1 1-320 N MS Schilling & Overall, 2008
35 glutamyl endopeptidase I 31-52 N MS Schilling & Overall, 2008
52 trypsin 1 1-320 N MS Schilling & Overall, 2008
109 elastase-2 107-122 N MS Schilling & Overall, 2008
122 trypsin 1 1-320 N MS Schilling & Overall, 2008
129 peptidyl-Lys metallopeptidase 1-320 N MS
143 peptidyl-Lys metallopeptidase 1-320 N MS
150 HIV-1 retropepsin 146-161 N MS Schilling & Overall, 2008
151 elastase-2 146-161 N MS Schilling & Overall, 2008
161 trypsin 1 1-320 N MS Schilling & Overall, 2008
248 cathepsin L 226-266 N MS Biniossek et al., 2011
262 glutamyl endopeptidase I 261-277 N MS Schilling & Overall, 2008
277 trypsin 1 1-320 N MS Schilling & Overall, 2008