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TPI1 TPI1 EUG1 EUG1 GCN4 GCN4 SCJ1 SCJ1 ERO1 ERO1 SFP1 SFP1 SRX1 SRX1 LHS1 LHS1 YKL069W YKL069W KAR2 KAR2 SUC2 SUC2 CTT1 CTT1 URA3 URA3 PGK1 PGK1 GCN2 GCN2
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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
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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TPI1Triose phosphate isomerase, abundant glycolytic enzyme; mRNA half-life is regulated by iron availability; transcription is controlled by activators Reb1p, Gcr1p, and Rap1p through binding sites in the 5' non-coding region; inhibition of Tpi1p activity by PEP (phosphoenolpyruvate) stimulates redox metabolism in respiring cells; E104D mutation in human homolog TPI1 causes a rare autosomal disease; human TPI1 can complement yeast null mutant. (248 aa)
EUG1Protein disulfide-isomerase EUG1; Protein disulfide isomerase of the endoplasmic reticulum lumen; EUG1 has a paralog, PDI1, that arose from the whole genome duplication; function overlaps with that of Pdi1p; may interact with nascent polypeptides in the ER. (517 aa)
GCN4General control protein GCN4; bZIP transcriptional activator of amino acid biosynthetic genes; activator responds to amino acid starvation; expression is tightly regulated at both the transcriptional and translational levels; Belongs to the bZIP family. GCN4 subfamily. (281 aa)
SCJ1DnaJ-related protein SCJ1; One of several homologs of bacterial chaperone DnaJ; located in the ER lumen where it cooperates with Kar2p to mediate maturation of proteins. (377 aa)
ERO1Endoplasmic oxidoreductin-1; Thiol oxidase required for oxidative protein folding in the ER; essential for maintaining ER redox balance; feedback regulated via reduction and oxidation of regulatory bonds; reduced Pdi1p activates Ero1p by direct reduction of Ero1p regulatory bonds; depletion of thiol substrates and accumulation of oxidized Pdi1p results in inactivation of Ero1p by both Pdi1p-mediated oxidation and autonomous oxidation of Ero1p regulatory bonds; ero1-1 mutation complemented by human ERO1L. (563 aa)
SFP1Transcription factor SFP1; Regulates transcription of ribosomal protein and biogenesis genes; regulates response to nutrients and stress, G2/M transitions during mitotic cell cycle and DNA-damage response, and modulates cell size; regulated by TORC1 and Mrs6p; sequence of zinc finger, ChIP localization data, and protein-binding microarray (PBM) data, and computational analyses suggest it binds DNA directly at highly active RP genes and indirectly through Rap1p at others; can form the [ISP+] prion. (683 aa)
SRX1Sulfiredoxin; 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. (127 aa)
LHS1Heat shock protein 70 homolog LHS1; Molecular chaperone of the endoplasmic reticulum lumen; involved in polypeptide translocation and folding; nucleotide exchange factor for the ER lumenal Hsp70 chaperone Kar2p; regulated by the unfolded protein response pathway. (881 aa)
YKL069WMethionine-R-sulfoxide reductase; reduces the R enantiomer of free Met-SO, in contrast to Ycl033Cp which reduces Met-R-SO in a peptide linkage; has a role in protection against oxidative stress; relative distribution to the nucleus increases upon DNA replication stress. (180 aa)
KAR2Endoplasmic reticulum chaperone BiP; ATPase involved in protein import into the ER; also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p. (682 aa)
SUC2Invertase; sucrose hydrolyzing enzyme; a secreted, glycosylated form is regulated by glucose repression, and an intracellular, nonglycosylated enzyme is produced constitutively. (532 aa)
CTT1Cytosolic catalase T; has a role in protection from oxidative damage by hydrogen peroxide. (562 aa)
URA3Orotidine-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)
PGK13-phosphoglycerate kinase; catalyzes transfer of high-energy phosphoryl groups from the acyl phosphate of 1,3-bisphosphoglycerate to ADP to produce ATP; key enzyme in glycolysis and gluconeogenesis. (416 aa)
GCN2eIF-2-alpha kinase GCN2; Protein kinase; phosphorylates the alpha-subunit of translation initiation factor eIF2 (Sui2p) in response to starvation; activated by uncharged tRNAs and the Gcn1p-Gcn20p complex; contributes to DNA damage checkpoint control. (1659 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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