General 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.

3-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.

General 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.

Protein component of the small (40S) ribosomal subunit; least basic of non-acidic ribosomal proteins; phosphorylated in vivo; essential for viability; homologous to mammalian ribosomal protein S5 and bacterial S7.

General 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.

Serine/threonine-protein kinase SCH9; AGC family protein kinase; functional ortholog of mammalian S6 kinase; phosphorylated by Tor1p and required for TORC1-mediated regulation of ribosome biogenesis, translation initiation, and entry into G0 phase; involved in transactivation of osmostress-responsive genes; regulates G1 progression, cAPK activity and nitrogen activation of the FGM pathway; integrates nutrient signals and stress signals from sphingolipids to regulate lifespan.

General 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.

Alpha subunit of the translation initiation factor eIF2; eIF2 is involved in identification of the start codon; phosphorylation of Ser51 is required for regulation of translation by inhibiting the exchange of GDP for GTP; protein abundance increases in response to DNA replication stress.

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.

12 kDa heat shock protein; Plasma membrane protein involved in maintaining membrane organization; involved in maintaining organization during stress conditions; induced by heat shock, oxidative stress, osmostress, stationary phase, glucose depletion, oleate and alcohol; protein abundance increased in response to DNA replication stress and dietary restriction; regulated by the HOG and Ras-Pka pathways; required for dietary restriction-induced lifespan extension.

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.

30 kDa heat shock protein; Negative regulator of the H(+)-ATPase Pma1p; stress-responsive protein; hydrophobic plasma membrane localized; induced by heat shock, ethanol treatment, weak organic acid, glucose limitation, and entry into stationary phase; Belongs to the archaeal/bacterial/fungal opsin 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.

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.

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.

3-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.

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.

Protein serine/threonine kinase; essential for cell wall remodeling during growth; localized to sites of polarized growth and the mother-daughter bud neck; homolog of the alpha, beta, and gamma isoforms of mammalian protein kinase C (PKC).

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.

Protein component of the small (40S) ribosomal subunit; has apurinic/apyrimidinic (AP) endonuclease activity; essential for viability; nascent Rps3p is bound by specific chaperone Yar1p during translation; homologous to mammalian ribosomal protein S3 and bacterial S3.

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.

Serine/threonine-protein kinase SCH9; AGC family protein kinase; functional ortholog of mammalian S6 kinase; phosphorylated by Tor1p and required for TORC1-mediated regulation of ribosome biogenesis, translation initiation, and entry into G0 phase; involved in transactivation of osmostress-responsive genes; regulates G1 progression, cAPK activity and nitrogen activation of the FGM pathway; integrates nutrient signals and stress signals from sphingolipids to regulate lifespan.

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.

Heat 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.

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.

Heat 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.

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.

Heat 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.

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.

Alpha subunit of the translation initiation factor eIF2; eIF2 is involved in identification of the start codon; phosphorylation of Ser51 is required for regulation of translation by inhibiting the exchange of GDP for GTP; protein abundance increases in response to DNA replication stress.

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.

Serine/threonine-protein kinase YPK2/YKR2; Protein kinase similar to S/T protein kinase Ypk1p; functionally redundant with YPK1 at the genetic level; participates in a signaling pathway required for optimal cell wall integrity; involved in the TORC-dependent phosphorylation of ribosomal proteins Rps6a/b (S6); human homolog SGK2 can complement a ypk1 ypk2 double mutant.

12 kDa heat shock protein; Plasma membrane protein involved in maintaining membrane organization; involved in maintaining organization during stress conditions; induced by heat shock, oxidative stress, osmostress, stationary phase, glucose depletion, oleate and alcohol; protein abundance increased in response to DNA replication stress and dietary restriction; regulated by the HOG and Ras-Pka pathways; required for dietary restriction-induced lifespan extension.

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.

12 kDa heat shock protein; Plasma membrane protein involved in maintaining membrane organization; involved in maintaining organization during stress conditions; induced by heat shock, oxidative stress, osmostress, stationary phase, glucose depletion, oleate and alcohol; protein abundance increased in response to DNA replication stress and dietary restriction; regulated by the HOG and Ras-Pka pathways; required for dietary restriction-induced lifespan extension.

30 kDa heat shock protein; Negative regulator of the H(+)-ATPase Pma1p; stress-responsive protein; hydrophobic plasma membrane localized; induced by heat shock, ethanol treatment, weak organic acid, glucose limitation, and entry into stationary phase; Belongs to the archaeal/bacterial/fungal opsin family.

12 kDa heat shock protein; Plasma membrane protein involved in maintaining membrane organization; involved in maintaining organization during stress conditions; induced by heat shock, oxidative stress, osmostress, stationary phase, glucose depletion, oleate and alcohol; protein abundance increased in response to DNA replication stress and dietary restriction; regulated by the HOG and Ras-Pka pathways; required for dietary restriction-induced lifespan extension.

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.

12 kDa heat shock protein; Plasma membrane protein involved in maintaining membrane organization; involved in maintaining organization during stress conditions; induced by heat shock, oxidative stress, osmostress, stationary phase, glucose depletion, oleate and alcohol; protein abundance increased in response to DNA replication stress and dietary restriction; regulated by the HOG and Ras-Pka pathways; required for dietary restriction-induced lifespan extension.

3-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.