PEP4 protein (Saccharomyces cerevisiae) - STRING interaction network
"PEP4" - Vacuolar aspartyl protease (proteinase A), required for the posttranslational precursor maturation of vacuolar proteinases in Saccharomyces cerevisiae
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Predicted Interactions
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Gene Fusion
PEP4Vacuolar aspartyl protease (proteinase A), required for the posttranslational precursor maturation of vacuolar proteinases; important for protein turnover after oxidative damage; synthesized as a zymogen, self-activates; Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself (405 aa)    
Predicted Functional Partners:
Vacuolar carboxypeptidase Y (proteinase C, CPY); broad-specificity C-terminal exopeptidase involved in non-specific protein degradation in the vacuole; member of the serine carboxypeptidase family; Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1’ position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (532 aa)
Vacuolar proteinase B (yscB), a serine protease of the subtilisin family; involved in protein degradation in the vacuole and required for full protein degradation during sporulation; activity inhibited by Pbi2p; Vacuolar proteinase B involved in protein degradation in the vacuole. Among other substrates, acts on carboxypeptidase Y (cpY/PRC1) to activate it by processing its Pro-peptide. Required for meiosis and spore formation, and for optimal survival in stationary phase (635 aa)
Subtilisin-like protease (proprotein convertase), a calcium-dependent serine protease involved in the activation of proproteins of the secretory pathway; Processing of precursors of alpha-factors and killer toxin (814 aa)
Cytoplasmic proteinase A (Pep4p) inhibitor, dependent on Pbs2p and Hog1p protein kinases for osmotic induction; intrinsically unstructured, N-terminal half becomes ordered in the active site of proteinase A upon contact; Specific and potent inhibitor for yeast aspartic protease A (yscA). The proteinase acts as a folding template stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity (68 aa)
Orotidine-5’-phosphate (OMP) decarboxylase, catalyzes the sixth enzymatic step in the de novo biosynthesis of pyrimidines, converting OMP into uridine monophosphate (UMP); converts 5-FOA into 5-fluorouracil, a toxic compound (267 aa)
Type I transmembrane sorting receptor for multiple vacuolar hydrolases; cycles between the late-Golgi and prevacuolar endosome-like compartments; Functions as a sorting receptor in the Golgi compartment required for the intracellular sorting and delivery of soluble vacuolar proteins, like carboxypeptidase Y (CPY) and proteinase A. May execute multiple rounds of sorting by cycling between the late Golgi and a prevacuolar endosome-like compartment. Binds the Golgi-modified P2 form of CPY, and this interaction is dependent on the presence of an intact CPY vacuolar protein sorting signal (1579 aa)
Mitochondrial aminopeptidase; cleaves the N termini of at least 38 imported proteins after cleavage by the mitochondrial processing peptidase (MPP), thereby increasing their stability; member of the aminopeptidase P family; Aminopeptidase which cleaves preprotein intermediates that carry destabilizing N-ter amino acid residues after the mitochondrial processing peptidase (MPP) cleavage site and is thus critical for stabilization of the mitochondrial proteome (511 aa)
Repressible vacuolar alkaline phosphatase; regulated by levels of Pi and by Pho4p, Pho9p, Pho80p, Pho81p and Pho85p; dephosphorylates phosphotyrosyl peptides; contributes to NAD+ metabolism by producing nicotinamide riboside from NMN; Phosphatase with broad substrate specificity. A truncated (soluble) version of the protein is responsible for the production of (E,E)-farnesol from (E,E)-farnesyl diphosphate. Acts as a fructose-2,6-bisphosphate 6-phosphatase (PubMed-1848184) (566 aa)
Beta-isopropylmalate dehydrogenase (IMDH), catalyzes the third step in the leucine biosynthesis pathway; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate (364 aa)
ATPase required for vesicular transport between ER and Golgi, the ’priming’ step in homotypic vacuole fusion, autophagy, and protein secretion; releases Sec17p from SNAP complexes; has similarity to mammalian NSF; Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin (758 aa)
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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