Substrates for peptidase S15.001: Xaa-Pro dipeptidyl-peptidase

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
Ala-Ala-NHPhNO2 Ala-Ala+NHPhNO2 S - - Ala Ala NAN - - - Jobin et al., 2005
Ala-Pro-NHPhNO2 Ala-Pro+NHPhNO2 S - - Ala Pro NAN - - -
Ala-Pro-NHPhNO2 Ala-Pro+NHPhNO2 S - - Ala Pro NAN - - - Jobin et al., 2005
Arg-Pro-NHPhNO2 Arg-Pro+NHPhNO2 S - - Arg Pro NAN - - - Jobin et al., 2005
Asp-Pro-NHPhNO2 Asp-Pro+NHPhNO2 S - - Asp Pro NAN - - - Jobin et al., 2005
Gly-Pro-Ile Gly-Pro+Ile N - - Gly Pro Ile - - - Enzyme Nomenclature, 1992
Gly-Pro-NHPhNO2 Gly-Pro+NHPhNO2 S - - Gly Pro NAN - - - Jobin et al., 2005
Lys-Ala-NHPhNO2 Lys-Ala+NHPhNO2 S - - Lys Ala NAN - - - Jobin et al., 2005
Phe-Pro-Gly-Pro-Ile Phe-Pro+Gly-Pro-Ile N - - Phe Pro Gly Pro Ile - Enzyme Nomenclature, 1992
Tyr-Pro-Phe-Pro-Gly-Pro-Ile Tyr-Pro+Phe-Pro-Gly-Pro-Ile N - - Tyr Pro Phe Pro Gly Pro Enzyme Nomenclature, 1992