Substrates for peptidase S9G.103: PofibS endopeptidase (Philodryas olfersii)

Summary Distribution 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
Ac-Phe-Arg-NHPhNO2 Ac-Phe-Arg+NHPhNO2 S - Ac Phe Arg NAN - - - Mandelbaum et al., 2004
alcohol dehydrogenase P00334 1-256 peptide-Lys8+Asn-peptide N NT Leu Thr Asn Lys Asn Val Ile Phe Thatcher et al., 1979
alcohol dehydrogenase P00334 1-256 peptide-Lys29+Arg-peptide N NT Glu Leu Leu Lys Arg Asp Leu Lys Thatcher et al., 1979
alcohol dehydrogenase P00334 1-256 peptide-Lys33+Asn-peptide N NT Arg Asp Leu Lys Asn Leu Val Ile Thatcher et al., 1979
insulin B-chain (oxidized) P01317 25-54 Phe-Val-Asn-Gln-His-Leu-Cya-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Tyr-Leu-Val-Cya-Gly-Glu-Arg+Gly-Phe-Phe-Tyr-Thr-Pro-Lys-Ala N Cya Gly Glu Arg Gly Phe Phe Tyr Mandelbaum et al., 2004