STRING protein interaction network
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
PRX1Mitochondrial peroxiredoxin with thioredoxin peroxidase activity; has a role in reduction of hydroperoxides; reactivation requires Trr2p and glutathione; induced during respiratory growth and oxidative stress; phosphorylated; protein abundance increases in response to DNA replication stress (261 aa)    
Predicted Functional Partners:
ER associated glutathione S-transferase; capable of homodimerization; glutathione transferase for Yvc1p vacuolar cation channel; expression induced during the diauxic shift and throughout stationary phase; functional overlap with Gtt2p, Grx1p, and Grx2p
Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress
Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p
Ras-related protein SEC4; Rab family GTPase; essential for vesicle-mediated exocytic secretion and autophagy; associates with the exocyst component Sec15p and may regulate polarized delivery of transport vesicles to the exocyst at the plasma membrane
Glutaredoxin-2, mitochondrial; Cytoplasmic glutaredoxin; thioltransferase, glutathione-dependent disulfide oxidoreductase involved in maintaining redox state of target proteins, also exhibits glutathione peroxidase activity, expression induced in response to stress; GRX2 has two in-frame start codons resulting in a shorter isoform that is retained in the cytosol and a longer form translocated to the mitochondrial matrix; GRX2 has a paralog, GRX1, that arose from the whole genome duplication
Cys-Gly metallodipeptidase DUG1; Cys-Gly metallo-di-peptidase; forms a complex with Dug2p and Dug3p to degrade glutathione (GSH) and other peptides containing a gamma-glu-X bond in an alternative pathway to GSH degradation by gamma-glutamyl transpeptidase (Ecm38p); human homolog CNDP2 can complement yeast dug1 mutant
Putative ribokinase; Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily
Protein PBDC1 homolog; Protein of unknown function; may interact with ribosomes, based on co-purification experiments; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm; protein abundance increases in response to DNA replication stress; Belongs to the PBDC1 family
Nitrogen catabolite repression transcriptional regulator; inhibits GLN3 transcription in good nitrogen source; role in sequestering Gln3p and Gat1p to the cytoplasm; has glutathione peroxidase activity and can mutate to acquire GST activity; self-assembly under limited nitrogen conditions creates [URE3] prion and releases catabolite repression
Cytosolic catalase T; has a role in protection from oxidative damage by hydrogen peroxide
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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