Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P63038

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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
26 unknown peptidase 1-573 P NT <%Agarwal et al., 2012[]%>
46 cathepsin E 27-573 P MS Impens et al., 2010
47 cathepsin D 27-573 P MS Impens et al., 2010
49 caspase-1 27-573 P normal turnover MS Lamkanfi et al., 2008
49 matrix metallopeptidase-2 27-573 N MS auf dem Keller et al., 2010
100 caspase-1 27-573 P normal turnover MS Lamkanfi et al., 2008
203 caspase-3 27-573 N MS Demon et al., 2009
203 caspase-7 27-573 N MS Demon et al., 2009
253 matrix metallopeptidase-2 27-573 N MS Prudova et al., 2010
279 caspase-3 27-573 N MS Demon et al., 2009
279 caspase-7 27-573 N MS Demon et al., 2009
299 matrix metallopeptidase-2 27-573 N MS auf dem Keller et al., 2010
404 cathepsin D 27-573 P MS Impens et al., 2010
404 cathepsin E 27-573 P MS Impens et al., 2010
411 cathepsin E 27-573 P MS Impens et al., 2010
435 cathepsin E 27-573 P MS Impens et al., 2010
513 cathepsin D 27-573 P MS Impens et al., 2010
513 cathepsin E 27-573 P MS Impens et al., 2010
531 caspase-3 27-573 N MS Demon et al., 2009
531 caspase-7 27-573 N MS Demon et al., 2009
537 matrix metallopeptidase-2 27-573 N MS Kleifeld et al., 2010