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:
a 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:
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.
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.
Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Belongs to the peroxiredoxin family. Prx5 subfamily.
Glutathione peroxidase-like peroxiredoxin HYR1; Thiol peroxidase; functions as a hydroperoxide receptor to sense intracellular hydroperoxide levels and transduce a redox signal to the Yap1p transcription factor; HYR1 has a paralog, GPX1, that arose from the whole genome duplication.
Thioredoxin-2; Cytoplasmic thioredoxin isoenzyme; part of thioredoxin system which protects cells against oxidative and reductive stress; forms LMA1 complex with Pbi2p; acts as a cofactor for Tsa1p; required for ER-Golgi transport and vacuole inheritance; with Trx1p, facilitates mitochondrial import of small Tims Tim9p, Tim10p, Tim13p by maintaining them in reduced form; abundance increases under DNA replication stress; TRX2 has a paralog, TRX1, that arose from the whole genome duplication.
Sulfiredoxin; contributes to oxidative stress resistance by reducing cysteine-sulfinic acid groups in the peroxiredoxin Tsa1p, which is formed upon exposure to oxidants; conserved in higher eukaryotes; protein abundance increases in response to DNA replication stress.
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.
Glutathione hydrolase heavy chain; Gamma-glutamyltranspeptidase; major glutathione-degrading enzyme; involved in detoxification of electrophilic xenobiotics; expression induced mainly by nitrogen starvation.
Glutathione peroxidase-like peroxiredoxin 1; Phospholipid hydroperoxide glutathione peroxidase; induced by glucose starvation that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress; GPX1 has a paralog, HYR1, that arose from the whole genome duplication.
Peroxiredoxin DOT5; Nuclear thiol peroxidase; functions as an alkyl-hydroperoxide reductase during post-diauxic growth; Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
Server load: low (16%) [HD]