Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence Q15459

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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
51 matrix metallopeptidase-2 48-68 N MS Schilling & Overall, 2008
68 glutamyl endopeptidase I 1-793 N MS Schilling & Overall, 2008
105 trypsin 1 1-793 N MS Schilling & Overall, 2008
115 trypsin 1 1-793 N MS Schilling & Overall, 2008
151 glutamyl endopeptidase I 144-168 N MS Schilling & Overall, 2008
168 trypsin 1 1-793 N MS Schilling & Overall, 2008
414 matrix metallopeptidase-2 399-424 N MS Schilling & Overall, 2008
424 trypsin 1 1-793 N MS Schilling & Overall, 2008
456 meprin alpha subunit 1-793 N MS Becker-Pauly et al., 2011
456 meprin beta subunit 1-793 N MS Becker-Pauly et al., 2011
475 meprin alpha subunit 472-488 N MS Becker-Pauly et al., 2011
503 unknown peptidase P MS Mahrus et al., 2008
515 LAST_MAM peptidase (Limulus-type) 512-531 N MS Becker-Pauly et al., 2011
522 cathepsin G 511-531 N MS Schilling & Overall, 2008
523 cathepsin L 512-531 N MS Biniossek et al., 2011
531 trypsin 1 1-793 N MS Schilling & Overall, 2008
612 matrix metallopeptidase-2 607-625 N MS Schilling & Overall, 2008
616 LAST_MAM peptidase (Limulus-type) 613-625 N MS Becker-Pauly et al., 2011
625 trypsin 1 1-793 N MS Schilling & Overall, 2008
670 meprin beta subunit 1-793 N MS Becker-Pauly et al., 2011
677 meprin alpha subunit 1-793 N MS Becker-Pauly et al., 2011
686 trypsin 1 1-793 N MS Schilling & Overall, 2008
699 trypsin 1 1-793 N MS Schilling & Overall, 2008