Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P26640

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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	1-1264	P		NT	<%Agarwal et al., 2012[]%>
122	trypsin 1	2-1264	N		MS	Schilling & Overall, 2008
137	trypsin 1	2-1264	N		MS	Schilling & Overall, 2008
215	matrix metallopeptidase-2	201-229	N		MS	Schilling & Overall, 2008
217	cathepsin L	202-229	N		MS	Biniossek et al., 2011
229	trypsin 1	2-1264	N		MS	Schilling & Overall, 2008
321	matrix metallopeptidase-2	303-334	N		MS	Schilling & Overall, 2008
334	trypsin 1	2-1264	N		MS	Schilling & Overall, 2008
423	lysyl endopeptidase (bacteria)	1-1264	N		MS
491	granzyme B (Homo sapiens-type)	2-1264	N		MS	Van Damme et al., 2010
769	trypsin 1	2-1264	N		MS	Schilling & Overall, 2008
777	trypsin 1	2-1264	N		MS	Schilling & Overall, 2008
884	matrix metallopeptidase-2	865-901	N		MS	Schilling & Overall, 2008
901	trypsin 1	2-1264	N		MS	Schilling & Overall, 2008
1229	elastase-2	1222-1242	N		MS	Schilling & Overall, 2008
1242	trypsin 1	2-1264	N		MS	Schilling & Overall, 2008
1263	carboxypeptidase A4	2-1264	N		MS	Van Damme et al., 2010