v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress.

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.

v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress.

Curing of [URE3] protein 1; Sorting factor, central regulator of spatial protein quality control; physically and functionally interacts with chaperones to promote sorting and deposition of misfolded proteins into cytosolic compartments; involved in destabilization of [URE3] prions; CUR1 has a paralog, BTN2, that arose from the whole genome duplication.

v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol 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.

v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress.

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.

v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress.

Small heat shock protein (sHSP) with chaperone activity; forms barrel-shaped oligomers that suppress unfolded protein aggregation; involved in cytoskeleton reorganization after heat shock; protein abundance increases and forms cytoplasmic foci in response to DNA replication stress.

v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress.

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.

v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress.

[PIN(+)] prion; an infectious protein conformation that is generally an ordered protein aggregate.

v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress.

Protein 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.

v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress.

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.

v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress.

ATPase 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.

v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress.

Heat shock protein STI1; Hsp90 cochaperone; regulates spatial organization of amyloid-like proteins in the cytosol, thereby buffering the proteotoxicity caused by amyloid-like proteins; interacts with the Ssa group of the cytosolic Hsp70 chaperones and activates Ssa1p ATPase activity; interacts with Hsp90 chaperones and inhibits their ATPase activity; homolog of mammalian Hop.

v-SNARE binding protein; facilitates specific protein retrieval from a late endosome to the Golgi; modulates arginine uptake, possible role in mediating pH homeostasis between the vacuole and plasma membrane H(+)-ATPase; contributes to prion curing; preferentially expressed after severe ethanol stress.

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.

Basic leucine zipper (bZIP) transcription factor of the yAP-1 family; physically interacts with the Tup1-Cyc8 complex and recruits Tup1p to its targets; mediates pleiotropic drug resistance and salt tolerance; nuclearly localized under oxidative stress and sequestered in the cytoplasm by Lot6p under reducing conditions; CIN5 has a paralog, YAP6, that arose from the whole genome duplication.

Uncharacterized protein YOR029W; Putative protein of unknown function; conserved among S. cerevisiae strains; YOR029W is not an essential gene.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

ATPase 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.

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.

Heat shock protein STI1; Hsp90 cochaperone; regulates spatial organization of amyloid-like proteins in the cytosol, thereby buffering the proteotoxicity caused by amyloid-like proteins; interacts with the Ssa group of the cytosolic Hsp70 chaperones and activates Ssa1p ATPase activity; interacts with Hsp90 chaperones and inhibits their ATPase activity; homolog of mammalian Hop.