Substrates for peptidase S01.253: halystase

Summary Alignment 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	P4	P3	P2	P1	P1'	P2'	P3'	P4'	Reference	CutDB
fibrinogen alpha chain	P02671	36-866	peptide-Arg510+His-peptide	P	Asp	Gly	Phe	Arg	His	Arg	His	Pro	Matsui et al., 1998	24439
fibrinogen beta chain	P02675	45-491	peptide-Arg87+Lys-peptide	P	Lys	Val	Glu	Arg	Lys	Ala	Pro	Asp	Matsui et al., 1998
fibrinogen beta chain	P02675	45-491	peptide-Arg72+Ala-peptide	P	Gly	Gly	Tyr	Arg	Ala	Arg	Pro	Ala	Matsui et al., 1998	24438
H-kininogen	P01044	19-644	peptide-Lys379+Arg-peptide	P	Ser	Leu	Met	Lys	Arg	Pro	Pro	Gly	Matsui et al., 1998	24441
H-kininogen	P01044	19-644	peptide-Arg388+Ser-peptide	P	Ser	Pro	Phe	Arg	Ser	Val	Gln	Val	Matsui et al., 1998	24442
Pro-Phe-Arg-NHMec			Pro-Phe-Arg+NHMec	S	-	Pro	Phe	Arg	AMC	-	-	-	Matsui et al., 1998