Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P26038

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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
1 unknown peptidase 1-577 P NT <%Agarwal et al., 2012[]%>
15 HIV-1 retropepsin 8-27 N MS Schilling & Overall, 2008
27 trypsin 1 2-577 N MS Schilling & Overall, 2008
35 trypsin 1 2-577 N MS Schilling & Overall, 2008
40 trypsin 1 2-577 N MS Schilling & Overall, 2008
53 trypsin 1 2-577 N MS Schilling & Overall, 2008
83 trypsin 1 2-577 N MS Schilling & Overall, 2008
100 trypsin 1 2-577 N MS Schilling & Overall, 2008
145 matrix metallopeptidase-2 140-159 N MS Schilling & Overall, 2008
146 matrix metallopeptidase-2 140-159 N MS Schilling & Overall, 2008
159 glutamyl endopeptidase I 2-577 N MS Schilling & Overall, 2008
237 trypsin 1 2-577 N MS Schilling & Overall, 2008
246 trypsin 1 2-577 N MS Schilling & Overall, 2008
263 trypsin 1 2-577 N MS Schilling & Overall, 2008
273 trypsin 1 2-577 N MS Schilling & Overall, 2008
395 meprin alpha subunit 2-577 N MS Becker-Pauly et al., 2011
395 meprin beta subunit 2-577 N MS Becker-Pauly et al., 2011
438 trypsin 1 2-577 N MS Schilling & Overall, 2008
448 trypsin 1 2-577 N MS Schilling & Overall, 2008
451 HIV-1 retropepsin 2-577 N pathological turnover Ott et al., 1996
523 trypsin 1 2-577 N MS Schilling & Overall, 2008
533 trypsin 1 2-577 N MS Schilling & Overall, 2008