Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence P30050

,

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
6	unknown peptidase	1-165	P		MS	Van Damme et al., 2005
16	trypsin 1	1-165	N		MS	Schilling & Overall, 2008
19	meprin beta subunit	16-31	N		MS	Becker-Pauly et al., 2011
31	trypsin 1	1-165	N		MS	Schilling & Overall, 2008
40	trypsin 1	1-165	N		MS	Schilling & Overall, 2008
43	meprin alpha subunit	1-165	N		MS	Becker-Pauly et al., 2011
43	meprin beta subunit	1-165	N		MS	Becker-Pauly et al., 2011
61	lysyl endopeptidase (bacteria)	1-165	N		MS
67	trypsin 1	1-165	N		MS	Schilling & Overall, 2008
72	cathepsin L	68-83	N		MS	Biniossek et al., 2011
83	trypsin 1	1-165	N		MS	Schilling & Overall, 2008
137	cathepsin B	131-146	N		MS	Biniossek et al., 2011