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LYS2 LYS2 SSA1 SSA1 SSA3 SSA3 HSP26 HSP26 FES1 FES1 LEU2 LEU2 TRP1 TRP1 SUP35 SUP35 SMT3 SMT3 URA3 URA3 SSA4 SSA4 TDH3 TDH3 TDH1 TDH1 TDH2 TDH2 SSA2 SSA2 HSP104 HSP104 HSP60 HSP60 HSC82 HSC82 SIS1 SIS1 YDJ1 YDJ1 KAR1 KAR1 HSP10 HSP10 ADE2 ADE2 HIS3 HIS3 ULP1 ULP1 SSE1 SSE1 HSP82 HSP82
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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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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
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gene co-occurrence
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LYS2Alpha aminoadipate reductase; catalyzes the reduction of alpha-aminoadipate to alpha-aminoadipate 6-semialdehyde, which is the fifth step in biosynthesis of lysine; activation requires posttranslational phosphopantetheinylation by Lys5p; Belongs to the ATP-dependent AMP-binding enzyme family. (1392 aa)
SSA1Heat shock protein SSA1; ATPase involved in protein folding and NLS-directed nuclear transport; member of HSP70 family; required for ubiquitin-dependent degradation of short-lived proteins; forms chaperone complex with Ydj1p; localized to nucleus, cytoplasm, cell wall; 98% identical to paralog Ssa2p with different functional specificity in propagation of yeast [URE3] prions, vacuolar-mediated degradations of gluconeogenesis enzymes; general targeting factor of Hsp104p to prion fibrils. (642 aa)
SSA3Heat shock protein SSA3; ATPase involved in protein folding and the response to stress; plays a role in SRP-dependent cotranslational protein-membrane targeting and translocation; member of the heat shock protein 70 (HSP70) family; localized to the cytoplasm; SSA3 has a paralog, SSA4, that arose from the whole genome duplication. (649 aa)
HSP26Small heat shock protein (sHSP) with chaperone activity; forms hollow, sphere-shaped oligomers that suppress unfolded proteins aggregation; long-lived protein that is preferentially retained in mother cells and forms cytoplasmic foci; oligomer activation requires heat-induced conformational change; also has mRNA binding activity. (214 aa)
FES1Hsp70 (Ssa1p) nucleotide exchange factor; required for the release of misfolded proteins from the Hsp70 system to the Ub-proteasome machinery for destruction; cytosolic homolog of Sil1p, which is the nucleotide exchange factor for BiP (Kar2p) in the endoplasmic reticulum; protein abundance increases in response to DNA replication stress. (290 aa)
LEU2Beta-isopropylmalate dehydrogenase (IMDH); catalyzes the third step in the leucine biosynthesis pathway; can additionally catalyze the conversion of beta-ethylmalate into alpha-ketovalerate; Belongs to the isocitrate and isopropylmalate dehydrogenases family. (364 aa)
TRP1Phosphoribosylanthranilate isomerase; catalyzes the third step in tryptophan biosynthesis; in 2004, the sequence of TRP1 from strain S228C was updated by changing the previously annotated internal STOP (TAA) to serine (TCA); enhances vegetative growth at low and high temperatures when used as an auxotrophic marker in strains such as W303. (224 aa)
SUP35Eukaryotic peptide chain release factor GTP-binding subunit; Translation termination factor eRF3; has a role in mRNA deadenylation and decay; altered protein conformation creates the [PSI(+)] prion that modifies cellular fitness, alters translational fidelity by affecting reading frame selection, and results in a nonsense suppressor phenotype; many stress-response genes are repressed in the presence of [PSI(+)]. (685 aa)
SMT3Ubiquitin-like protein of the SUMO family; conjugated to lysine residues of target proteins; associates with transcriptionally active genes; regulates chromatid cohesion, chromosome segregation, APC-mediated proteolysis, DNA replication and septin ring dynamics; human homolog SUMO1 can complement yeast null mutant. (101 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)
SSA4Heat shock protein that is highly induced upon stress; plays a role in SRP-dependent cotranslational protein-membrane targeting and translocation; member of the HSP70 family; cytoplasmic protein that concentrates in nuclei upon starvation; SSA4 has a paralog, SSA3, that arose from the whole genome duplication. (642 aa)
TDH3Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), isozyme 3; involved in glycolysis and gluconeogenesis; tetramer that catalyzes the reaction of glyceraldehyde-3-phosphate to 1,3 bis-phosphoglycerate; detected in the cytoplasm and cell wall; GAPDH-derived antimicrobial peptides secreted by S. cerevisiae are active against a wide variety of wine-related yeasts and bacteria; binds AU-rich RNA. (332 aa)
TDH1Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), isozyme 1; involved in glycolysis and gluconeogenesis; tetramer that catalyzes the reaction of glyceraldehyde-3-phosphate to 1,3 bis-phosphoglycerate; detected in the cytoplasm and cell wall; protein abundance increases in response to DNA replication stress; GAPDH-derived antimicrobial peptides secreted by S. cerevisiae are active against a wide variety of wine-related yeasts and bateria. (332 aa)
TDH2Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), isozyme 2; involved in glycolysis and gluconeogenesis; tetramer that catalyzes reaction of glyceraldehyde-3-phosphate to 1,3 bis-phosphoglycerate; detected in cytoplasm and cell wall; protein abundance increases in response to DNA replication stress; GAPDH-derived antimicrobial peptides are active against a wide variety of wine-related yeasts and bateria; TDH2 has a paralog, TDH3, that arose from the whole genome duplication. (332 aa)
SSA2Heat shock protein SSA2; HSP70 family ATP-binding protein; involved in protein folding, vacuolar import of proteins; required for ubiquitin-dependent degradation of short-lived proteins; associated with chaperonin-containing T-complex; 98% identical to paralog Ssa1p with distinct functional specificity in propagation of yeast [URE3] prions and vacuolar-mediated degradation of gluconeogenesis enzymes; binds tRNA, has role in tRNA nuclear import during starvation. (639 aa)
HSP104Disaggregase; heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate previously denatured, aggregated proteins; responsive to stresses including: heat, ethanol, and sodium arsenite; involved in [PSI+] propagation; protein becomes more abundant and forms cytoplasmic foci in response to DNA replication stress; potentiated Hsp104p variants decrease TDP-43 proteotoxicity by eliminating its cytoplasmic aggregation; Belongs to the ClpA/ClpB family. (908 aa)
HSP60Heat shock protein 60, mitochondrial; Tetradecameric mitochondrial chaperonin; required for ATP-dependent folding of precursor polypeptides and complex assembly; prevents aggregation and mediates protein refolding after heat shock; role in mtDNA transmission; phosphorylated. (572 aa)
HSC82ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication. (705 aa)
SIS1Protein SIS1; Type II HSP40 co-chaperone that interacts with the HSP70 protein Ssa1p; shuttles between cytosol and nucleus; mediates delivery of misfolded proteins into the nucleus for degradation; involved in proteasomal degradation of misfolded cytosolic proteins; protein abundance increases in response to DNA replication stress; polyQ aggregates sequester Sis1p and interfere with clearance of misfolded proteins; similar to bacterial DnaJ proteins and mammalian DnaJB1. (352 aa)
YDJ1Mitochondrial protein import protein MAS5; Type I HSP40 co-chaperone; involved in regulation of HSP90 and HSP70 functions; acts as an adaptor that helps Rsp5p recognize cytosolic misfolded proteins for ubiquitination after heat shock; critical for determining cell size at Start as a function of growth rate; involved in protein translocation across membranes; member of the DnaJ family; chimeric protein in which human p58IPK J domain replaces yeast Ydj1p J domain can complement yeast ydj1 mutant. (409 aa)
KAR1Cell division control protein KAR1; Protein involved in karyogamy and spindle pole body duplication; involved in karyogamy during mating; involved in spindle pole body duplication during mitosis; localizes to the half-bridge of the spindle pole body; interacts with Spc72p during karyogamy; also interacts with Cdc31p; essential gene. (433 aa)
HSP1010 kDa heat shock protein, mitochondrial; Mitochondrial matrix co-chaperonin; inhibits the ATPase activity of Hsp60p, a mitochondrial chaperonin; involved in protein folding and sorting in the mitochondria; 10 kD heat shock protein with similarity to E. coli groES. (106 aa)
ADE2Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine. (571 aa)
HIS3Imidazoleglycerol-phosphate dehydratase; catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p. (220 aa)
ULP1Ubiquitin-like-specific protease 1; Protease that specifically cleaves Smt3p protein conjugates; required for cell cycle progression; associates with nucleoporins and may interact with septin rings during telophase; sequestered to the nucleolus under stress conditions. (621 aa)
SSE1ATPase component of heat shock protein Hsp90 chaperone complex; serves as nucleotide exchange factor to load ATP onto the SSA class of cytosolic Hsp70s; plays a role in prion propagation and determining prion variants; binds unfolded proteins; member of Hsp110 subclass of HSP70 proteins; deletion results in spindle elongation in S phase; SSE1 has a paralog, SSE2, that arose from the whole genome duplication. (693 aa)
HSP82ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication. (709 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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