Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P09104

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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 1-434 P NT <%Agarwal et al., 2012[]%>
29 matrix metallopeptidase-2 28-45 N MS Schilling & Overall, 2008
32 trypsin 1 2-434 N MS Schilling & Overall, 2008
38 cathepsin S 33-48 N MS Biniossek et al., 2011
38 matrix metallopeptidase-2 32-50 N MS Schilling & Overall, 2008
39 matrix metallopeptidase-2 32-50 N MS Schilling & Overall, 2008
39 elastase-2 32-50 N MS Schilling & Overall, 2008
40 LAST_MAM peptidase (Limulus-type) 37-50 N MS Becker-Pauly et al., 2011
45 glutamyl endopeptidase I 2-434 N MS Schilling & Overall, 2008
50 trypsin 1 2-434 N MS Schilling & Overall, 2008
64 trypsin 1 2-434 N MS Schilling & Overall, 2008
77 matrix metallopeptidase-2 64-89 N MS Schilling & Overall, 2008
89 trypsin 1 2-434 N MS Schilling & Overall, 2008
103 trypsin 1 2-434 N MS Schilling & Overall, 2008
105 trypsin 1 2-434 N MS Schilling & Overall, 2008
109 cathepsin L 106-120 N MS Biniossek et al., 2011
110 matrix metallopeptidase-2 105-120 N MS Schilling & Overall, 2008
120 trypsin 1 2-434 N MS Schilling & Overall, 2008
146 LAST_MAM peptidase (Limulus-type) 143-162 N MS Becker-Pauly et al., 2011
148 LAST_MAM peptidase (Limulus-type) 145-162 N MS Becker-Pauly et al., 2011
150 matrix metallopeptidase-2 143-167 N MS Schilling & Overall, 2008
150 meprin alpha subunit 147-162 N MS Becker-Pauly et al., 2011
151 cathepsin L 133-162 N MS Biniossek et al., 2011
151 cathepsin S 133-162 N MS Biniossek et al., 2011
151 matrix metallopeptidase-2 143-167 N MS Schilling & Overall, 2008
152 matrix metallopeptidase-2 143-167 N MS Schilling & Overall, 2008
161 peptidyl-Lys metallopeptidase 1-434 N MS
162 trypsin 1 2-434 N MS Schilling & Overall, 2008
167 glutamyl endopeptidase I 2-434 N MS Schilling & Overall, 2008
168 HIV-1 retropepsin 164-179 N MS Schilling & Overall, 2008
179 trypsin 1 2-434 N MS Schilling & Overall, 2008
192 peptidyl-Lys metallopeptidase 1-434 N MS
202 trypsin 1 2-434 N MS Schilling & Overall, 2008
228 trypsin 1 2-434 N MS Schilling & Overall, 2008
256 trypsin 1 2-434 N MS Schilling & Overall, 2008
262 trypsin 1 2-434 N MS Schilling & Overall, 2008
269 trypsin 1 2-434 N MS Schilling & Overall, 2008
285 trypsin 1 2-434 N MS Schilling & Overall, 2008
317 meprin alpha subunit 2-434 N MS Becker-Pauly et al., 2011
317 meprin beta subunit 2-434 N MS Becker-Pauly et al., 2011
372 trypsin 1 2-434 N MS Schilling & Overall, 2008
377 glutamyl endopeptidase I 372-394 N MS Schilling & Overall, 2008
378 meprin beta subunit 2-434 N MS Becker-Pauly et al., 2011
380 HIV-1 retropepsin 372-394 N MS Schilling & Overall, 2008
382 meprin beta subunit 379-394 N MS Becker-Pauly et al., 2011
384 cathepsin B 373-394 N MS Biniossek et al., 2011
387 matrix metallopeptidase-2 383-402 N MS Schilling & Overall, 2008
388 matrix metallopeptidase-2 383-402 N MS Schilling & Overall, 2008
394 trypsin 1 2-434 N MS Schilling & Overall, 2008
402 glutamyl endopeptidase I 2-434 N MS Schilling & Overall, 2008
432 cathepsin X 405-433 P MS Obermajer et al., 2009
433 cathepsin X 405-434 P MS Obermajer et al., 2009