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SWA2 | Auxilin-like clathrin uncoating factor SWA2; Auxilin-like protein involved in vesicular transport; clathrin-binding protein required for uncoating of clathrin-coated vesicles. (668 aa) | ||||
PRB1 | Cerevisin; Vacuolar proteinase B (yscB) with H3 N-terminal endopeptidase activity; serine protease of the subtilisin family; involved in protein degradation in the vacuole and required for full protein degradation during sporulation; activity inhibited by Pbi2p; protein abundance increases in response to DNA replication stress; PRB1 has a paralog, YSP3, that arose from the whole genome duplication. (635 aa) | ||||
UPF3 | Component of the nonsense-mediated mRNA decay (NMD) pathway; along with Nam7p and Nmd2p; involved in decay of mRNA containing nonsense codons; involved in telomere maintenance; Belongs to the RENT3 family. (387 aa) | ||||
BTN2 | 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. (410 aa) | ||||
ZUO1 | Zuotin; Ribosome-associated chaperone; zuotin functions in ribosome biogenesis and as a chaperone for nascent polypeptide chains in partnership with Ssz1p and SSb1/2; contains a DnaJ domain and functions as a J-protein partner for Ssb1p and Ssb2p; human gene DNAJC2 can partially complement yeast zuo1 null mutant. (433 aa) | ||||
TDA3 | Putative oxidoreductase involved in late endosome to Golgi transport; physical and genetical interactions with Btn2p; null mutant is viable, has extended S phase, and sensitive to expression of top1-T722A allele; similar to human FOXRED1. (523 aa) | ||||
SSZ1 | Ribosome-associated complex subunit SSZ1; Hsp70 protein that interacts with Zuo1p (a DnaJ homolog); interacts with Zuo1p to form a ribosome-associated complex that binds the ribosome via the Zuo1p subunit; also involved in pleiotropic drug resistance via sequential activation of PDR1 and PDR5; binds ATP. (538 aa) | ||||
NMD2 | Protein involved in the nonsense-mediated mRNA decay (NMD) pathway; interacts with Nam7p and Upf3p; involved in telomere maintenance. (1089 aa) | ||||
CPR7 | 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. (393 aa) | ||||
SUP35 | 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(+)]. (685 aa) | ||||
HSP104 | 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. (908 aa) | ||||
NAM7 | ATP-dependent RNA helicase of the SFI superfamily; involved in nonsense mediated mRNA decay; required for efficient translation termination at nonsense codons and targeting of NMD substrates to P-bodies; binds to the small ribosomal subunit via an interaction with Rps26; forms cytoplasmic foci upon DNA replication stress. (971 aa) | ||||
HSC82 | 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. (705 aa) | ||||
SIS1 | 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. (352 aa) | ||||
SIW14 | Inositol phosphatase SIW14; Tyrosine phosphatase involved in actin organization and endocytosis; localized to the cytoplasm. (281 aa) | ||||
SSB2 | Cytoplasmic ATPase that is a ribosome-associated molecular chaperone; functions with J-protein partner Zuo1p; may be involved in the folding of newly-synthesized polypeptide chains; member of the HSP70 family; SSB2 has a paralog, SSB1, that arose from the whole genome duplication; Belongs to the heat shock protein 70 family. Ssb-type Hsp70 subfamily. (613 aa) | ||||
URE2 | 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. (354 aa) | ||||
STI1 | 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. (589 aa) | ||||
SSE1 | 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. (693 aa) | ||||
PUS1 | tRNA:pseudouridine synthase; introduces pseudouridines at positions 26-28, 34-36, 65, and 67 of tRNA; also acts on U2 snRNA; also pseudouridylates some mRNAs, and pseudouridylation level varies with growth phase; nuclear protein that appears to be involved in tRNA export; PUS1 has a paralog, PUS2, that arose from the whole genome duplication. (544 aa) | ||||
HSP82 | 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. (709 aa) | ||||
CUR1 | 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. (252 aa) | ||||
SSA2 | 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. (639 aa) | ||||
ARG82 | Inositol polyphosphate multikinase (IPMK); sequentially phosphorylates Ins(1,4,5)P3 to form Ins(1,3,4,5,6)P5; also has diphosphoinositol polyphosphate synthase activity; regulates arginine-, phosphate-, and nitrogen-responsive genes. (355 aa) | ||||
HSP26 | Small heat shock protein (sHSP) with chaperone activity; forms hollow, sphere-shaped oligomers that suppress unfolded proteins aggregation; long-lived protein that is preferentially retained in mother cells and forms cytoplasmic foci; oligomer activation requires heat-induced conformational change; also has mRNA binding activity. (214 aa) | ||||
FES1 | 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. (290 aa) | ||||
SUP45 | Polypeptide release factor (eRF1) in translation termination; mutant form acts as a recessive omnipotent suppressor; methylated by Mtq2p-Trm112p in ternary complex eRF1-eRF3-GTP; mutation of methylation site confers resistance to zymocin; has a role in cytokinesis through interaction with Mlc1p. (437 aa) | ||||
RNQ1 | [PIN(+)] prion; an infectious protein conformation that is generally an ordered protein aggregate. (405 aa) | ||||
HSP42 | 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. (375 aa) | ||||
SSA1 | 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. (642 aa) |