Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence P62829

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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
15	trypsin 1	1-140	N		MS	Schilling & Overall, 2008
19	cathepsin B	16-35	N		MS	Biniossek et al., 2011
23	cathepsin L	16-35	N		MS	Biniossek et al., 2011
23	cathepsin S	16-35	N		MS	Biniossek et al., 2011
23	cathepsin B	16-35	N		MS	Biniossek et al., 2011
35	trypsin 1	1-140	N		MS	Schilling & Overall, 2008
43	trypsin 1	1-140	N		MS	Schilling & Overall, 2008
51	trypsin 1	1-140	N		MS	Schilling & Overall, 2008
53	LAST_MAM peptidase (Limulus-type)	50-77	N		MS	Becker-Pauly et al., 2011
58	meprin beta subunit	55-67	N		MS	Becker-Pauly et al., 2011
59	matrix metallopeptidase-2	51-67	N		MS	Schilling & Overall, 2008
59	glutamyl endopeptidase I	51-67	N		MS	Schilling & Overall, 2008
66	trypsin 1	1-140	N		MS	Schilling & Overall, 2008
67	trypsin 1	1-140	N		MS	Schilling & Overall, 2008
99	cathepsin S	92-109	N		MS	Biniossek et al., 2011