Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P04181

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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
3	YMXG peptidase	1-25	N			Kitada et al., 2007
8	YMXG peptidase	1-25	N			Kitada et al., 2007
9	YMXG peptidase	1-25	N			Kitada et al., 2007
12	YMXG peptidase	1-25	N			Kitada et al., 2007
17	mitochondrial processing peptidase beta-subunit	1-25	P	release of a transit peptide	NT	Kitada et al., 2007
25	unknown peptidase	1-439	P		NT	<%Agarwal et al., 2012[]%>
35	cathepsin S	33-46	N		MS	Biniossek et al., 2011
120	cathepsin S	114-129	N		MS	Biniossek et al., 2011
279	HIV-1 retropepsin	274-292	N		MS	Schilling & Overall, 2008
280	LAST_MAM peptidase (Limulus-type)	277-292	N		MS	Becker-Pauly et al., 2011
281	glutamyl endopeptidase I	274-292	N		MS	Schilling & Overall, 2008
282	meprin alpha subunit	279-292	N		MS	Becker-Pauly et al., 2011
292	trypsin 1	26-439	N		MS	Schilling & Overall, 2008