Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence Q9Y265

,


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
22 trypsin 1 1-456 N MS Schilling & Overall, 2008
33 trypsin 1 1-456 N MS Schilling & Overall, 2008
38 cathepsin B 34-46 N MS Biniossek et al., 2011
46 trypsin 1 1-456 N MS Schilling & Overall, 2008
57 trypsin 1 1-456 N MS Schilling & Overall, 2008
64 trypsin 1 1-456 N MS Schilling & Overall, 2008
76 trypsin 1 1-456 N MS Schilling & Overall, 2008
90 trypsin 1 1-456 N MS Schilling & Overall, 2008
107 trypsin 1 1-456 N MS Schilling & Overall, 2008
258 meprin alpha subunit 255-267 N MS Becker-Pauly et al., 2011
345 LAST_MAM peptidase (Limulus-type) 342-357 N MS Becker-Pauly et al., 2011
362 trypsin 1 1-456 N MS Schilling & Overall, 2008
372 trypsin 1 1-456 N MS Schilling & Overall, 2008
388 LAST_MAM peptidase (Limulus-type) 385-400 N MS Becker-Pauly et al., 2011
404 trypsin 1 1-456 N MS Schilling & Overall, 2008
418 trypsin 1 1-456 N MS Schilling & Overall, 2008