Substrates for peptidase M48.003: farnesylated-protein converting enzyme 1

Summary Gene structure 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 22-36 peptide-farnesyl-Cys33+Val-Ile-Ala P Asp Pro Ala Cyf Val Ile Ala - Bergo & Young, 2004 17164
a-mating factor precursor mutant ({Saccharomyces cerevisiae}) peptide-farnesyl-Cys33+Ala-Met-Gln N Asp Pro Ala Cyf Ala Met Gln - Bergo & Young, 2004
Lamin-A/C P02545 1-664 peptide-Tyr646+Leu-peptide P MU Thr Arg Ser Tyr Leu Leu Gly Asn Corrigan et al., 2005
N-acetyl-S-farnesyl-Cys-protein N-acetyl-S-farnesyl-Cys+peptide N - - Ac Cyf Xaa Xaa Xaa -