Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence Q13765

,

Click here to display alignment and conservation of cleavage sites of this sequence with close homologues. This will take a few moments.

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
54	meprin alpha subunit	1-125	N		MS	Becker-Pauly et al., 2011
54	meprin beta subunit	1-215	N		MS	Becker-Pauly et al., 2011
55	meprin alpha subunit	1-215	N		MS	Becker-Pauly et al., 2011
55	meprin beta subunit	1-215	N		MS	Becker-Pauly et al., 2011
56	meprin alpha subunit	1-125	N		MS	Becker-Pauly et al., 2011
56	meprin beta subunit	1-215	N		MS	Becker-Pauly et al., 2011
58	unknown peptidase	1-215	P			Van Damme et al., 2009
60	granzyme B (Homo sapiens-type)	1-215	N		MS	Van Damme et al., 2010
71	trypsin 1	1-215	N			Van Damme et al., 2009
103	HIV-1 retropepsin	100-113	N		MS	Schilling & Overall, 2008
113	trypsin 1	1-215	N		MS	Schilling & Overall, 2008
126	peptidyl-Lys metallopeptidase	1-215	N		MS
127	trypsin 1	1-215	N		MS	Schilling & Overall, 2008
141	peptidyl-Lys metallopeptidase	1-215	N		MS
195	matrix metallopeptidase-2	182-212	N		MS	Schilling & Overall, 2008
197	thrombin	182-212	N		MS	Schilling & Overall, 2008
198	matrix metallopeptidase-2	182-212	N		MS	Schilling & Overall, 2008
212	glutamyl endopeptidase I	1-215	N		MS	Schilling & Overall, 2008
214	carboxypeptidase A4	1-215	N		MS	Van Damme et al., 2010