Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P01011

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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
23	unknown peptidase	1-95	P	release of a signal peptide	NT	Lindmark et al., 1989
25	unknown peptidase	1-423	P		NT	<%Agarwal et al., 2012[]%>
37	glutamyl endopeptidase I	24-423	P
41	clostripain	24-423	N
41	trypsin 1	24-423	P	normal turnover
381	elastase-2	24-423	P	normal turnover
383	cathepsin D	24-423	P	normal turnover		Pimenta et al., 2000
383	staphopain C	24-423	N		NT	Wladyka et al., 2011
383	granzyme M	24-423	P			Mahrus et al., 2004
383	kallikrein-related peptidase 2	24-423	P			Mikolajczyk et al., 1999
384	staphopain C	24-423	N		NT	Wladyka et al., 2011
384	aureolysin	24-423	N			Potempa & Travis, 2004
384	matrix metallopeptidase-1	24-423	P			Mast et al., 1991
384	serralysin	24-423	P
385	cathepsin D	24-423	P	normal turnover		Pimenta et al., 2000
385	pseudolysin	24-423	N
385	matrix metallopeptidase-8	24-423	P		NT	Desrochers et al., 1992
385	matrix metallopeptidase-3	24-423	P			Mast et al., 1991
385	matrix metallopeptidase-13	24-423	P	springing of a trap mechanism		Leeman et al., 2002
386	cathepsin D	24-423	P	normal turnover		Pimenta et al., 2000
386	staphopain C	24-423	N		NT	Wladyka et al., 2011
387	seaprose (Aspergillus melleus)	24-423	P		NT	Korzus et al., 1994