Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Sequence Q16576

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	Evidence	Reference
1	unknown peptidase	1-425	P	NT	<%Agarwal et al., 2012[]%>
4	trypsin 1	1-425	N	MS	Schilling & Overall, 2008
14	trypsin 1	1-425	N	MS	Schilling & Overall, 2008
45	cathepsin B	26-58	N	MS	Biniossek et al., 2011
67	cathepsin L	59-82	N	MS	Biniossek et al., 2011
67	cathepsin S	59-79	N	MS	Biniossek et al., 2011
67	cathepsin B	58-78	N	MS	Biniossek et al., 2011
68	cathepsin S	59-82	N	MS	Biniossek et al., 2011
93	cathepsin S	83-105	N	MS	Biniossek et al., 2011
98	LAST_MAM peptidase (Limulus-type)	95-113	N	MS	Becker-Pauly et al., 2011
134	cathepsin L	131-142	N	MS	Biniossek et al., 2011
142	trypsin 1	1-425	N	MS	Schilling & Overall, 2008
154	elastase-2	142-171	N	MS	Schilling & Overall, 2008
155	trypsin 1	1-425	N	MS	Schilling & Overall, 2008
171	trypsin 1	1-425	N	MS	Schilling & Overall, 2008
201	elastase-2	196-211	N	MS	Schilling & Overall, 2008
211	trypsin 1	1-425	N	MS	Schilling & Overall, 2008
295	trypsin 1	1-425	N	MS	Schilling & Overall, 2008
303	trypsin 1	1-425	N	MS	Schilling & Overall, 2008
313	cathepsin L	309-321	N	MS	Biniossek et al., 2011
360	meprin beta subunit	357-375	N	MS	Becker-Pauly et al., 2011
366	HIV-1 retropepsin	348-375	N	MS	Schilling & Overall, 2008
375	trypsin 1	1-425	N	MS	Schilling & Overall, 2008