Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence P25705

,


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 1-553 P release of an initiating methionine MS He et al., 2006
35 mitochondrial processing peptidase beta-subunit 1-553 P release of a transit peptide MS Gevaert et al., 2003
43 mitochondrial intermediate peptidase 36-553 P release of a transit peptide MS Gevaert et al., 2003
101 matrix metallopeptidase-2 97-127 N MS Schilling & Overall, 2008
127 glutamyl endopeptidase I 44-553 N MS Schilling & Overall, 2008
139 astacin 136-149 N MS Becker-Pauly et al., 2011
139 meprin alpha subunit 136-149 N MS Becker-Pauly et al., 2011
139 LAST_MAM peptidase (Limulus-type) 136-149 N MS Becker-Pauly et al., 2011
159 caspase-3 44-553 P MS Impens et al., 2010
313 unknown peptidase 1-553 P MS Van Damme et al., 2005