Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

Allantoate permease; ureidosuccinate permease; also transports dipeptides, though with lower affinity than for allantoate and ureidosuccinate; expression is constitutive but sensitive to nitrogen catabolite repression; Belongs to the major facilitator superfamily. Allantoate permease family.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Enzyme that catalyzes the fourth step in the histidine pathway; Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

ATP-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.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

Disaggregase; 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.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

ATP-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.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

Cell 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.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

Eukaryotic 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(+)].

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

Orotidine-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.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

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.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

Mitochondrial 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.

Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family.

Hsp70/Hsp90 co-chaperone CNS1; TPR-containing co-chaperone; binds both Hsp82p (Hsp90) and Ssa1p (Hsp70); stimulates ATPase activity of Ssa1p; ts mutants reduce Hsp82p function, overexpression suppresses phenotypes of HSP82 ts allele and cpr7 deletion; human homolog TTC4 complements yeast cns1 mutant; Belongs to the TTC4 family.

Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family.

Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily.

Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family.

Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds to Hsp82p and contributes to chaperone activity; plays a role in determining prion variants.

Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family.

Hsp70 (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.

Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family.

Hsp90 co-chaperone HCH1; Heat shock protein regulator; binds to Hsp90p and may stimulate ATPase activity; originally identified as a high-copy number suppressor of a HSP90 loss-of-function mutation; role in regulating Hsp90 inhibitor drug sensitivity; GFP-fusion protein localizes to the cytoplasm and nucleus; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family.

Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family.

ATP-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.

Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family.

Trimeric heat shock transcription factor; activates multiple genes in response to highly diverse stresses; recognizes variable heat shock elements (HSEs) consisting of inverted NGAAN repeats; monitors translational status of cell through an RQC (Ribosomal Quality Control)-mediated translation-stress signal; involved in diauxic shift; posttranslationally regulated; human homolog HSF1 with linker region mutations can complement yeast hsf1 mutant; Belongs to the HSF family.

Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family.

Disaggregase; 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.

Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family.

ATP-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.

Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family.

Protein serine/threonine phosphatase; regulates Hsp90 chaperone by affecting its ATPase and cochaperone binding activities; has similarity to human phosphatase PP5; present in both the nucleus and cytoplasm; expressed during logarithmic growth; Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily.