Alpha-mannosidase; Vacuolar alpha mannosidase; involved in free oligosaccharide (fOS) degradation; delivered to the vacuole in a novel pathway separate from the secretory 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.

Alpha-mannosidase; Vacuolar alpha mannosidase; involved in free oligosaccharide (fOS) degradation; delivered to the vacuole in a novel pathway separate from the secretory pathway.

Degradation in the endoplasmic reticulum protein 1; ER membrane protein that promotes export of misfolded polypeptides; required for ER-associated protein degradation of misfolded or unassembled proteins; initiates export of aberrant polypeptides from ER lumen by threading them into ER membrane and routing them to Hrd1p for ubiquitination; function normally requires N-terminal acetylation by NatB; N- and C- termini protrude into cytoplasm; similar to Dfm1p; homolog of mammalian derlin-1.

Alpha-mannosidase; Vacuolar alpha mannosidase; involved in free oligosaccharide (fOS) degradation; delivered to the vacuole in a novel pathway separate from the secretory pathway.

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.

Alpha-mannosidase; Vacuolar alpha mannosidase; involved in free oligosaccharide (fOS) degradation; delivered to the vacuole in a novel pathway separate from the secretory pathway.

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.

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.

Alpha-mannosidase; Vacuolar alpha mannosidase; involved in free oligosaccharide (fOS) degradation; delivered to the vacuole in a novel pathway separate from the secretory 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.

Degradation in the endoplasmic reticulum protein 1; ER membrane protein that promotes export of misfolded polypeptides; required for ER-associated protein degradation of misfolded or unassembled proteins; initiates export of aberrant polypeptides from ER lumen by threading them into ER membrane and routing them to Hrd1p for ubiquitination; function normally requires N-terminal acetylation by NatB; N- and C- termini protrude into cytoplasm; similar to Dfm1p; homolog of mammalian derlin-1.

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.

ERAD-associated E3 ubiquitin-protein ligase component HRD3; ER membrane protein that plays a central role in ERAD; forms HRD complex with Hrd1p and ER-associated protein degradation (ERAD) determinants that engages in lumen to cytosol communication and coordination of ERAD events; Belongs to the sel-1 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.

Conserved ER protein translocation channel; essential subunit of Sec61 complex (Sec61p, Sbh1p, and Sss1p); forms channel for SRP-dependent protein import; with Sec63 complex allows SRP-independent protein import into ER; involved in posttranslational soluble protein import into the ER, ERAD of soluble substrates, and misfolded soluble protein export from the ER.

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.

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.

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.

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.

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.

Degradation in the endoplasmic reticulum protein 1; ER membrane protein that promotes export of misfolded polypeptides; required for ER-associated protein degradation of misfolded or unassembled proteins; initiates export of aberrant polypeptides from ER lumen by threading them into ER membrane and routing them to Hrd1p for ubiquitination; function normally requires N-terminal acetylation by NatB; N- and C- termini protrude into cytoplasm; similar to Dfm1p; homolog of mammalian derlin-1.

Alpha-mannosidase; Vacuolar alpha mannosidase; involved in free oligosaccharide (fOS) degradation; delivered to the vacuole in a novel pathway separate from the secretory pathway.

Degradation in the endoplasmic reticulum protein 1; ER membrane protein that promotes export of misfolded polypeptides; required for ER-associated protein degradation of misfolded or unassembled proteins; initiates export of aberrant polypeptides from ER lumen by threading them into ER membrane and routing them to Hrd1p for ubiquitination; function normally requires N-terminal acetylation by NatB; N- and C- termini protrude into cytoplasm; similar to Dfm1p; homolog of mammalian derlin-1.

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.