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GLR1 GLR1 DUG2 DUG2 YFH1 YFH1 YCF1 YCF1 GRX2 GRX2 GCG1 GCG1 DUG1 DUG1 GTO1 GTO1 TRX2 TRX2 GTT1 GTT1 GSH1 GSH1 OXP1 OXP1 ECM4 ECM4 GTT2 GTT2 ECM38 ECM38 GLO1 GLO1 GTO3 GTO3 DUG3 DUG3 GSH2 GSH2
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
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GLR1Cytosolic 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. (483 aa)
DUG2Probable di- and tripeptidase DUG2; Component of glutamine amidotransferase (GATase II); forms a complex with 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). (878 aa)
YFH1Frataxin homolog intermediate form; Mitochondrial matrix iron chaperone; oxidizes and stores iron; interacts with Isu1p to promote Fe-S cluster assembly; mutation results in multiple Fe/S-dependent enzyme deficiencies; human frataxin homolog FXN is mutated in Friedrich's ataxia; human FTL gene can complement yeast yfh1 null mutant. (174 aa)
YCF1Metal resistance protein YCF1; Vacuolar glutathione S-conjugate transporter; ABC-C transporter of the ATP-binding cassette family; required for vacuole fusion; forms stable complexes with vacuole fusion machinery; regulates Vam7p recruitment to vacuoles; role in detoxifying metals (Cd, Hg, As); transports GSSG that is not immediately reduced in cytosol to vacuole; transports unconjugated bilirubin, selenodigluthatione, oxidized glutathione; similar to human cystic fibrosis protein CFTR; Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily. (1515 aa)
GRX2Glutaredoxin-2; 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. (143 aa)
GCG1Glutathione-specific gamma-glutamylcyclotransferase; Gamma-glutamyl cyclotransferase; cleaves the gamma-glutamyl bond of glutathione to yield 5-oxoproline and a Cys-Gly dipeptide; similar to mammalian pro-apoptotic protein ChaC1; expression of mouse ChaC1 in yeast increases apoptosis; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm and nucleus; periodically expressed during the metabolic cycle. (232 aa)
DUG1Cys-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. (481 aa)
GTO1Glutathione S-transferase omega-like 1; Omega-class glutathione transferase; induced under oxidative stress; putative peroxisomal localization. (356 aa)
TRX2Thioredoxin-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. (104 aa)
GTT1ER 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. (234 aa)
GSH1Glutamate--cysteine ligase; Gamma glutamylcysteine synthetase; catalyzes the first step in glutathione (GSH) biosynthesis; expression induced by oxidants, cadmium, and mercury; protein abundance increases in response to DNA replication stress; Belongs to the glutamate--cysteine ligase type 3 family. (678 aa)
OXP15-oxoprolinase; enzyme is ATP-dependent and functions as a dimer; similar to mouse Oplah gene; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm; protein abundance increases in response to DNA replication stress. (1286 aa)
ECM4Glutathione S-transferase omega-like 2; S-glutathionyl-(chloro)hydroquinone reductase (GS-HQR); glutathione transferase involved in cell-surface biosynthesis and architecture; catalyzes glutathione (GSH)-dependent reduction of GS-trichloro-p-hydroquinone to trichloro-p-hydroquinone; expression upregulated upon exposure to genotoxic agents, such as methyl methanesulfonate, cisplatin and bleomycin; not an essential gene; similar to YGR154C; green fluorescent protein (GFP)-fusion protein localizes to cytoplasm; Belongs to the GST superfamily. Omega family. (370 aa)
GTT2Glutathione S-transferase capable of homodimerization; functional overlap with Gtt2p, Grx1p, and Grx2p; protein abundance increases in response to DNA replication stress; Belongs to the GST superfamily. (233 aa)
ECM38Glutathione hydrolase heavy chain; Gamma-glutamyltranspeptidase; major glutathione-degrading enzyme; involved in detoxification of electrophilic xenobiotics; expression induced mainly by nitrogen starvation. (660 aa)
GLO1Lactoylglutathione lyase; Monomeric glyoxalase I; catalyzes the detoxification of methylglyoxal (a by-product of glycolysis) via condensation with glutathione to produce S-D-lactoylglutathione; expression regulated by methylglyoxal levels and osmotic stress. (326 aa)
GTO3Glutathione S-transferase omega-like 3; Omega class glutathione transferase; putative cytosolic localization. (366 aa)
DUG3Component of glutamine amidotransferase (GATase II); forms a complex with Dug2p 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). (357 aa)
GSH2Glutathione synthetase; catalyzes the ATP-dependent synthesis of glutathione (GSH) from gamma-glutamylcysteine and glycine; induced by oxidative stress and heat shock. (491 aa)
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
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