Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence P05386

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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	1-114	P		NT	<%Agarwal et al., 2012[]%>
9	matrix metallopeptidase-2	6-33	N		MS	Schilling & Overall, 2008
19	LAST_MAM peptidase (Limulus-type)	16-33	N		MS	Becker-Pauly et al., 2011
20	HIV-1 retropepsin	1-33	N		MS	Schilling & Overall, 2008
20	glutamyl endopeptidase I	1-114	N		MS	Schilling & Overall, 2008
32	peptidyl-Lys metallopeptidase	1-114	N		MS
33	trypsin 1	1-114	N		MS	Schilling & Overall, 2008
48	peptidyl-Lys metallopeptidase	1-114	N		MS
49	trypsin 1	1-114	N		MS	Schilling & Overall, 2008
52	cathepsin S	50-61	N		MS	Biniossek et al., 2011
61	cathepsin B	50-83	N		MS	Biniossek et al., 2011
64	cathepsin L	50-85	N		MS	Biniossek et al., 2011
64	cathepsin B	50-83	N		MS	Biniossek et al., 2011
66	cathepsin L	50-92	N		MS	Biniossek et al., 2011
70	matrix metallopeptidase-2	49-92	N		MS	Schilling & Overall, 2008
72	cathepsin B	50-83	N		MS	Biniossek et al., 2011
73	cathepsin L	50-93	N		MS	Biniossek et al., 2011
73	cathepsin B	50-92	N		MS	Biniossek et al., 2011
78	cathepsin L	50-92	N		MS	Biniossek et al., 2011
92	trypsin 1	1-114	N		MS	Schilling & Overall, 2008