Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; seamless-GFP and mCherry fusion proteins localize to the vacuole, while SWAT-GFP fusion localizes to both the endoplasmic reticulum and vacuole; suppresses toxicity of slow-folding human Z-type alpha1-antitrypsin variant associated with liver cirrhosis and emphysema.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

Processing alpha glucosidase I; ER type II integral membrane N-glycoprotein involved in assembly of cell wall beta 1,6 glucan and asparagine-linked protein glycosylation; also involved in ER protein quality control and sensing of ER stress; Belongs to the glycosyl hydrolase 63 family.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

Endoplasmic 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.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

ERAD-associated E3 ubiquitin-protein ligase HRD1; Ubiquitin-protein ligase involved in ER-associated degradation (ERAD) of misfolded proteins; upon autoubiquitination triggers retrotranslocation of misfolded proteins to cytosol for degradation; genetically linked to the unfolded protein response (UPR); regulated through association with Hrd3p; contains an H2 ring finger; likely plays a general role in targeting proteins that persistently associate with and potentially obstruct the ER-localized translocon; Belongs to the HRD1 family.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

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.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

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.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

Endoplasmic 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.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

Heat 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.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

ER degradation-enhancing alpha-mannosidase-like protein 1; Alpha-1,2-specific exomannosidase of the endoplasmic reticulum; involved in glycan trimming of both folded and misfolded glycoproteins; complexes with Pdi1p, and trims a mannose from Man8GlcNac2 glycans to generate Man7GlcNac2, an oligosaccharide signal on glycoproteins destined for ER-associated protein degradation; requires Pdi1p for stability and substrate recognition; human homolog EDEM1 can complement yeast null mutant; Belongs to the glycosyl hydrolase 47 family.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

Protein disulfide isomerase; multifunctional oxidoreductase of the ER lumen, essential for disulfide bond formation in secretory and cell-surface proteins, processing of non-native disulfide bonds; Ero1p activator; complexes with exomannosidase, Mnl1p to facilitate the recognition of misfolded glycoproteins and the trimming of glycan Man8GlcNAc2 to Man7GlcNAc2 on substrates, thereby accelerating ERAD; PDI1 has a paralog, EUG1, that arose from the whole genome duplication.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

Protein translocation protein SEC63; Essential subunit of Sec63 complex; with Sec61 complex, Kar2p/BiP and Lhs1p forms a channel competent for SRP-dependent and post-translational SRP-independent protein targeting and import into the ER; other members are Sec62p, Sec66p, and Sec72p.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

Nucleotide exchange factor for the ER lumenal Hsp70 chaperone Kar2p; required for protein translocation into the endoplasmic reticulum (ER); homolog of Yarrowia lipolytica SLS1; GrpE-like protein; Belongs to the SIL1 family.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

Member of Hsp110 subclass of the heat shock protein 70 (HSP70) family; serves as nucleotide exchange factor to load ATP onto the SSA class of cytosolic Hsp70s; may be involved in protein folding; localized to the cytoplasm; SSE2 has a paralog, SSE1, that arose from the whole genome duplication.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

Protein OS-9 homolog; ER quality-control lectin; integral subunit of the HRD ligase; participates in efficient ER retention of misfolded proteins by recognizing them and delivering them to Hrd1p; binds to glycans with terminal alpha-1,6 linked mannose on misfolded N-glycosylated proteins and participates in targeting proteins to ERAD; member of the OS-9 protein family.

Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; seamless-GFP and mCherry fusion proteins localize to the vacuole, while SWAT-GFP fusion localizes to both the endoplasmic reticulum and vacuole; suppresses toxicity of slow-folding human Z-type alpha1-antitrypsin variant associated with liver cirrhosis and emphysema.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.

Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; seamless-GFP and mCherry fusion proteins localize to the vacuole, while SWAT-GFP fusion localizes to both the endoplasmic reticulum and vacuole; suppresses toxicity of slow-folding human Z-type alpha1-antitrypsin variant associated with liver cirrhosis and emphysema.

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.

Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; seamless-GFP and mCherry fusion proteins localize to the vacuole, while SWAT-GFP fusion localizes to both the endoplasmic reticulum and vacuole; suppresses toxicity of slow-folding human Z-type alpha1-antitrypsin variant associated with liver cirrhosis and emphysema.

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.

Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; seamless-GFP and mCherry fusion proteins localize to the vacuole, while SWAT-GFP fusion localizes to both the endoplasmic reticulum and vacuole; suppresses toxicity of slow-folding human Z-type alpha1-antitrypsin variant associated with liver cirrhosis and emphysema.

Endoplasmic 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.

Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; seamless-GFP and mCherry fusion proteins localize to the vacuole, while SWAT-GFP fusion localizes to both the endoplasmic reticulum and vacuole; suppresses toxicity of slow-folding human Z-type alpha1-antitrypsin variant associated with liver cirrhosis and emphysema.

Protein disulfide isomerase; multifunctional oxidoreductase of the ER lumen, essential for disulfide bond formation in secretory and cell-surface proteins, processing of non-native disulfide bonds; Ero1p activator; complexes with exomannosidase, Mnl1p to facilitate the recognition of misfolded glycoproteins and the trimming of glycan Man8GlcNAc2 to Man7GlcNAc2 on substrates, thereby accelerating ERAD; PDI1 has a paralog, EUG1, that arose from the whole genome duplication.

Processing alpha glucosidase I; ER type II integral membrane N-glycoprotein involved in assembly of cell wall beta 1,6 glucan and asparagine-linked protein glycosylation; also involved in ER protein quality control and sensing of ER stress; Belongs to the glycosyl hydrolase 63 family.

Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast.