Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence P27824

,


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
20 unknown peptidase 1-592 P NT <%Agarwal et al., 2012[]%>
41 glutamyl endopeptidase I 4-57 N MS Schilling & Overall, 2008
57 trypsin 1 21-592 N MS Schilling & Overall, 2008
68 glutamyl endopeptidase I 61-77 N MS Schilling & Overall, 2008
77 trypsin 1 21-592 N MS Schilling & Overall, 2008
361 glutamyl endopeptidase I 359-380 N MS Schilling & Overall, 2008
370 astacin 367-380 N MS Becker-Pauly et al., 2011
380 trypsin 1 21-592 N MS Schilling & Overall, 2008
389 meprin beta subunit 386-400 N MS Becker-Pauly et al., 2011
448 LAST_MAM peptidase (Limulus-type) 445-459 N MS Becker-Pauly et al., 2011
558 LAST_MAM peptidase (Limulus-type) 555-573 N MS Becker-Pauly et al., 2011