Substrates for peptidase M48.001: Ste24 peptidase

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
A-mating factor precursor P34165 1-36 peptide-farnesyl-Cys33+Val-Ile-Ala P Asp Pro Ala Cyf Val Ile Ala - Boyartchuk et al., 1997 17162
A-mating factor precursor P34165 1-33 peptide-Thr7+Ala-peptide P Ser Thr Ala Thr Ala Ala Pro Lys Schmidt & Michaelis, 2004 17163
a-mating factor precursor mutant ({Saccharomyces cerevisiae}) peptide-farnesyl-Cys33+Ala-Met-Gln N Asp Pro Ala Cyf Ala Met Gln - Boyartchuk & Rine, 1998
N-acetyl-S-farnesyl-Cys-Val-Ile-Met N-acetyl-S-farnesyl-Cys+Val-Ile-Met N - - Ac Cyf Val Ile Met -
prelamin-A/C P48678 1-665 peptide-Cys662+Ser-Ile-Met P AB Ser Gln Asn Cys Ser Ile Met - Bergo et al., 2002
Ydj1p E7QK08 1-409 peptide-Cys406+Ala-Ser-Gln P CS Gly Val Gln Cys Ala Ser Gln - Trueblood et al., 2000