Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence O14737

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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	1-125	P		NT	<%Agarwal et al., 2012[]%>
22	meprin alpha subunit	2-125	N		MS	Becker-Pauly et al., 2011
22	meprin beta subunit	2-125	N		MS	Becker-Pauly et al., 2011
40	trypsin 1	2-125	N		MS	Schilling & Overall, 2008
53	trypsin 1	2-125	N		MS	Schilling & Overall, 2008
53	thrombin	49-65	N		MS	Schilling & Overall, 2008
65	glutamyl endopeptidase I	2-125	N		MS	Schilling & Overall, 2008
68	trypsin 1	2-125	N		MS	Schilling & Overall, 2008
71	glutamyl endopeptidase I	68-79	N		MS	Schilling & Overall, 2008
79	trypsin 1	2-125	N		MS	Schilling & Overall, 2008
86	trypsin 1	2-125	N		MS	Schilling & Overall, 2008
88	meprin alpha subunit	85-98	N		MS	Becker-Pauly et al., 2011
88	meprin beta subunit	85-98	N		MS	Becker-Pauly et al., 2011
97	lysyl endopeptidase (bacteria)	1-125	N		MS
98	trypsin 1	2-125	N		MS	Schilling & Overall, 2008