Substrates for peptidase M07.001: snapalysin

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
furylacryloyl-Ala-Phe-NH2 (FAAFA) furylacryloyl-Ala+Phe-NH2 S - - FA Ala Phe NH2 - - Inouye et al., 2007
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 Val Glu Ala Leu Tyr Leu Val Cya Kurisu et al., 1997
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 Gly Glu Arg Gly Phe Phe Tyr Thr Kurisu et al., 1997
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 Glu Arg Gly Phe Phe Tyr Thr Pro Kurisu et al., 1997