Substrates for peptidase M12.190: ammodytase

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
Fibrinogen alpha chain	P02671	36-866	Peptide-Glu441+Leu-Peptide	P	NT	Gly	Asp	Lys	Glu	Leu	Arg	Thr	Gly	Leonardi et al., 2007
Fibrinogen alpha chain	P02671	36-866	Peptide-Glu539+Phe-Peptide	P	NT	Met	Leu	Gly	Glu	Phe	Val	Ser	Glu	Leonardi et al., 2007
Fibrinogen beta chain	P02675	45-491	Peptide-Pro48+Leu-Peptide	P	NT	Gly	His	Arg	Pro	Leu	Asp	Lys	Lys	Leonardi et al., 2007
Fibrinogen beta chain	P02675	45-491	Peptide-Lys52+Arg-Peptide	P	NT	Leu	Asp	Lys	Lys	Arg	Glu	Glu	Ala	Leonardi et al., 2007
insulin B chain (oxidized)	P01308	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	NT	Phe	Val	Asn	Gln	His	Leu	Cys	Gly	Leonardi et al., 2007
insulin B chain (oxidized)	P01308	25-54	Peptide-Tyr40+Leu-Peptide	N	NT	Glu	Ala	Leu	Tyr	Leu	Val	Cys	Gly	Leonardi et al., 2007