Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence P01149

,


Click here to display alignment and conservation of cleavage sites of this sequence with close homologues.  This will take a few moments.

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
19 unknown peptidase 1-165 P CS Liang et al., 2003
85 kexin 20-165 N CS Bader et al., 2008
87 dipeptidyl aminopeptidase A 85-105 P Misumi & Ikehara, 2004
89 dipeptidyl aminopeptidase A 87-105 P Misumi & Ikehara, 2004
95 barrierpepsin 90-102 P normal turnover MacKay et al., 1992
95 leulysin 90-102 P NT Okada et al., 1987
104 kexin 20-165 P Fuller, 2004
108 dipeptidyl aminopeptidase A 106-125 P Misumi & Ikehara, 2004
110 dipeptidyl aminopeptidase A 108-125 P Misumi & Ikehara, 2004
125 kexin 20-165 P Fuller, 2004
131 unknown peptidase 1-165 P NT <%Agarwal et al., 2012[]%>
144 kex carboxypeptidase 20-144 P Remington, 2004
145 kex carboxypeptidase 20-145 P Remington, 2004
152 unknown peptidase 1-165 P NT <%Agarwal et al., 2012[]%>