Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence Q29040

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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
296	thermolysin	1-595	N			Thole et al., 1995
297	stem bromelain	1-595	N			Thole et al., 1995
297	thermolysin	1-595	N			Thole et al., 1995
300	ficin	1-595	N			Thole et al., 1995
301	stem bromelain	1-595	N			Thole et al., 1995
302	ficin	1-595	N			Thole et al., 1995
302	lysyl endopeptidase (bacteria)	1-595	N			Thole et al., 1995
303	lysyl endopeptidase (bacteria)	1-595	N			Thole et al., 1995
309	ficin	1-595	N			Thole et al., 1995
309	thermolysin	1-595	N			Thole et al., 1995
328	chymotrypsin A (cattle-type)	1-595	N			Thole et al., 1995
336	thermolysin	1-595	N			Thole et al., 1995
416	lysyl endopeptidase (bacteria)	1-595	N			Thole et al., 1995
465	thermolysin	1-595	N			Thole et al., 1995
466	chymotrypsin A (cattle-type)	1-595	N			Thole et al., 1995
467	ficin	1-595	N			Thole et al., 1995
467	trypsin 1	1-595	N			Thole et al., 1995
467	lysyl endopeptidase (bacteria)	1-595	N			Thole et al., 1995
472	lysyl endopeptidase (bacteria)	1-595	N			Thole et al., 1995
529	lysyl endopeptidase (bacteria)	1-595	N			Thole et al., 1995
531	trypsin 1	1-595	N			Thole et al., 1995
531	lysyl endopeptidase (bacteria)	1-595	N			Thole et al., 1995