Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P80162

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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
37 unknown peptidase 1-114 P release of a signal peptide NT Proost et al., 1993
39 dipeptidyl-peptidase IV (eukaryote) 38-114 P Ajami et al., 2008
41 matrix metallopeptidase-9 38-114 P normal turnover Van den Steen et al., 2003
42 matrix metallopeptidase-8 38-114 P conversion to two-chain form Van den Steen et al., 2003
42 matrix metallopeptidase-9 38-114 P normal turnover Van den Steen et al., 2003
43 matrix metallopeptidase-8 38-114 P Van den Steen et al., 2003
43 matrix metallopeptidase-9 38-114 P conversion to two-chain form Van den Steen et al., 2003
45 unknown peptidase 1-114 P NT <%Agarwal et al., 2012[]%>
85 lysyl endopeptidase (bacteria) 1-114 N MS
100 lysyl endopeptidase (bacteria) 1-114 N MS