Substrates for peptidase M10.020: fragilysin

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
actin, aortic smooth muscle P08023 3-377 peptide-Thr66+Leu-peptide P Gly Ile Leu Thr Leu Lys Tyr Pro Moncrief et al., 1995 16655
actin, cytoplasmic 1 P60706 2-375 peptide-Gly46+Met-peptide P Val Met Val Gly Met Gly Gln Lys Moncrief et al., 1995 16654
fragilysin P54355 26-405 peptide-Cys207+Leu-peptide P Tyr Val Ile Cys Leu Arg Glu Asn Moncrief et al., 1995 16656
fragilysin P54355 26-405 peptide-Ser269+Leu-peptide P Phe Thr Ala Ser Leu Lys Ser Asn Moncrief et al., 1995 16657
Pz-peptide Pz-Pro-Leu+Gly-Pro-D-Arg N - Pz Pro Leu Gly Pro DAr - Vines & Wilkins, 2004