Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence Q13813

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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
102	meprin alpha subunit	1-2472	N		MS	Becker-Pauly et al., 2011
217	cathepsin L	215-227	N		MS	Biniossek et al., 2011
877	peptidyl-Lys metallopeptidase	1-2472	N		MS
908	peptidyl-Lys metallopeptidase	1-2472	N		MS
914	cathepsin L	910-930	N		MS	Biniossek et al., 2011
964	meprin beta subunit	1-2472	N		MS	Becker-Pauly et al., 2011
1176	calpain-1	1-2472	P			Stabach et al., 1997
1185	caspase-1	1-2472	P			Nath et al., 1996
1185	caspase-3	1-2472	P			Nath et al., 1996
1185	caspase-4	1-2472	P			Nath et al., 1996
1198	Sat peptidase	1-2472	N			Navarro-Garcia, 2004
1301	cathepsin L	1299-1313	N		MS	Biniossek et al., 2011
1301	cathepsin S	1299-1313	N		MS	Biniossek et al., 2011
1308	meprin beta subunit	1-2472	N		MS	Becker-Pauly et al., 2011
1478	caspase-3	1-2472	P	normal turnover		Wang et al., 1998
1504	meprin beta subunit	1-2472	N		MS	Becker-Pauly et al., 2011
1508	meprin alpha subunit	1-2472	N		MS	Becker-Pauly et al., 2011
1544	granzyme A	1-2472	N			Van Damme et al., 2010