Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P17225

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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
2	caspase-3	1-527	N		MS	Demon et al., 2009
2	caspase-7	1-527	N		MS	Demon et al., 2009
7	granzyme B (Homo sapiens-type)	1-527	N			Van Damme et al., 2009
7	granzyme B, rodent-type	1-527	P			Van Damme et al., 2009
14	trypsin 1	1-527	N			Van Damme et al., 2009
97	cathepsin E	1-527	P		MS	Impens et al., 2010
112	matrix metallopeptidase-2	1-527	N		MS	auf dem Keller et al., 2010
163	cathepsin E	1-527	P		MS	Impens et al., 2010
166	unknown peptidase	1-527	P			Van Damme et al., 2009
171	caspase-3	1-527	N		MS	Demon et al., 2009
171	caspase-7	1-527	N		MS	Demon et al., 2009
173	unknown peptidase	1-527	P			Van Damme et al., 2009
174	unknown peptidase	1-527	P			Van Damme et al., 2009
184	trypsin 1	1-527	N			Van Damme et al., 2009
328	matrix metallopeptidase-2	1-527	N		MS	auf dem Keller et al., 2010
337	cathepsin D	1-527	P		MS	Impens et al., 2010
337	cathepsin E	1-527	P		MS	Impens et al., 2010
338	cathepsin E	1-527	P		MS	Impens et al., 2010
355	cathepsin D	1-527	P		MS	Impens et al., 2010
355	cathepsin E	1-527	P		MS	Impens et al., 2010
356	cathepsin E	1-527	P		MS	Impens et al., 2010