Substrates for peptidase S51.001: dipeptidase E

Summary Alignment Tree 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
Asp-Gly-Gly Asp+Gly-Gly N - - - Asp Gly Gly - - Miller, 2004
Asp-Leu Asp+Leu N - - - Asp Leu - - - Miller, 2004
Asp-NHPhNO2 Asp+NHPhNO2 S - - - Asp NAN - - - Miller, 2004
Asp-Phe-NH2 Asp+Phe-NH2 N - - - Asp Phe NH2 - - Miller, 2004
Asp-Phe-NHPhNO2 Asp+Phe-NHPhNO2 S - - - Asp Phe NAN - - Miller, 2004
Asp-Phe-OMe Asp+Phe-NH2 N - - - Asp Phe OMe - - Miller, 2004
aspartyl-amino acid Asp+Xaa N - - - Asp Xaa - - - Miller, 2004