Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence Q15029

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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
148	matrix metallopeptidase-2	142-158	N		MS	Schilling & Overall, 2008
158	trypsin 1	1-972	N		MS	Schilling & Overall, 2008
180	matrix metallopeptidase-2	172-198	N		MS	Schilling & Overall, 2008
198	chymotrypsin A (cattle-type)	1-972	N		MS	Schilling & Overall, 2008
383	cathepsin B	380-394	N		MS	Biniossek et al., 2011
498	cathepsin S	496-508	N		MS	Biniossek et al., 2011
499	cathepsin B	496-508	N		MS	Biniossek et al., 2011
547	matrix metallopeptidase-2	543-561	N		MS	Schilling & Overall, 2008
561	trypsin 1	1-972	N		MS	Schilling & Overall, 2008
573	glutamyl endopeptidase I	569-581	N		MS	Schilling & Overall, 2008
581	trypsin 1	1-972	N		MS	Schilling & Overall, 2008
793	glutamyl endopeptidase I	790-803	N		MS	Schilling & Overall, 2008
803	trypsin 1	1-972	N		MS	Schilling & Overall, 2008
918	cathepsin L	915-931	N		MS	Biniossek et al., 2011
954	meprin alpha subunit	951-963	N		MS	Becker-Pauly et al., 2011
954	LAST_MAM peptidase (Limulus-type)	951-963	N		MS	Becker-Pauly et al., 2011