Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence O75390

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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
27 unknown peptidase 1-466 P NT <%Agarwal et al., 2012[]%>
34 trypsin 1 28-466 N MS Schilling & Overall, 2008
43 trypsin 1 28-466 N MS Schilling & Overall, 2008
167 matrix metallopeptidase-2 144-183 N MS Schilling & Overall, 2008
168 LAST_MAM peptidase (Limulus-type) 165-183 N MS Becker-Pauly et al., 2011
183 trypsin 1 28-466 N MS Schilling & Overall, 2008
340 trypsin 1 28-466 N MS Schilling & Overall, 2008
348 subtilisin Carlsberg 28-466 N NT Lill et al., 1984
349 subtilisin Carlsberg 28-466 N NT Lill et al., 1984
350 chymotrypsin B 28-466 P NT Lill et al., 1984
351 trypsin 1 28-466 N MS Schilling & Overall, 2008
393 trypsin 1 28-466 P NT Lill et al., 1984
393 lysyl endopeptidase (bacteria) 28-466 N NT Lill et al., 1984