Substrates for peptidase S08.036: subtilisin E

Summary Alignment Sequences Sequence features Distribution Structure Literature Substrates

Peptide and protein substrates that are thought to be physiologically relevant are indicated by P. Peptide and protein substrates that are thought to be pathologically relevant are indicated by D. Peptide and protein substrates that are not physiologically relevant are indicated by N. Synthetic substrates are indicated by S. Click on the symbol to show only physiological, non-physiological or synthetic substrates, or here to display all substrates. 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 protein substrate, click on the UniProt Accession.

Substrate Uniprot Residue range Cleavage Site Cleavage type Evidence P4 P3 P2 P1 P1' P2' P3' P4' Reference CutDB MERNUM
lantibiotic subtilin P10946 1-56 peptide-Gln24+Trp-peptide P NT Ile Thr Pro Gln Trp Lys Ser Glu Corvey et al., 2003
subtilisin E P04189 30-381 peptide-Tyr106+Ala-peptide P NT Ala His Glu Tyr Ala Gln Ser Val Sone et al., 2005
Suc-Ala-Ala-Pro-Leu-NHPhNO2 Suc-Ala-Ala-Pro-Leu+NHPhNO2 S Ala Ala Pro Phe NAN - - - Sone et al., 2005
Suc-Ala-Ala-Pro-Phe-NHPhNO2 Suc-Ala-Ala-Pro-Phe+NHPhNO2 S Ala Ala Pro Phe NAN - - - Sone et al., 2005