Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P26641

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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	1-437	P		NT	<%Agarwal et al., 2012[]%>
32	cathepsin L	31-41	N		MS	Biniossek et al., 2011
33	LAST peptidase (Limulus-type)	30-45	N		MS	Becker-Pauly et al., 2011
33	LAST_MAM peptidase (Limulus-type)	30-45	N		MS	Becker-Pauly et al., 2011
64	caspase-6	2-437	P			Klaiman et al., 2008
105	caspase-6	2-437	P			Klaiman et al., 2008
137	trypsin 1	2-437	N		MS	Schilling & Overall, 2008
147	trypsin 1	2-437	N		MS	Schilling & Overall, 2008
149	trypsin 1	2-437	N		MS	Schilling & Overall, 2008
156	trypsin 1	2-437	N		MS	Schilling & Overall, 2008
263	meprin beta subunit	2-437	N		MS	Becker-Pauly et al., 2011
264	caspase-6	2-437	P			Klaiman et al., 2008
266	meprin beta subunit	2-437	N		MS	Becker-Pauly et al., 2011
285	trypsin 1	2-437	N		MS	Schilling & Overall, 2008
295	trypsin 1	2-437	N		MS	Schilling & Overall, 2008
401	trypsin 1	2-437	N		MS	Schilling & Overall, 2008
414	trypsin 1	2-437	N		MS	Schilling & Overall, 2008
418	cathepsin B	415-428	N		MS	Biniossek et al., 2011
418	meprin beta subunit	415-428	N		MS	Becker-Pauly et al., 2011
428	trypsin 1	2-437	N		MS	Schilling & Overall, 2008