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SWA2 SWA2 PRB1 PRB1 UPF3 UPF3 BTN2 BTN2 ZUO1 ZUO1 TDA3 TDA3 SSZ1 SSZ1 NMD2 NMD2 CPR7 CPR7 SUP35 SUP35 HSP104 HSP104 NAM7 NAM7 HSC82 HSC82 SIS1 SIS1 SIW14 SIW14 SSB2 SSB2 URE2 URE2 STI1 STI1 SSE1 SSE1 PUS1 PUS1 HSP82 HSP82 CUR1 CUR1 SSA2 SSA2 ARG82 ARG82 HSP26 HSP26 FES1 FES1 SUP45 SUP45 RNQ1 RNQ1 HSP42 HSP42 SSA1 SSA1
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
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SWA2Auxilin-like clathrin uncoating factor SWA2; Auxilin-like protein involved in vesicular transport; clathrin-binding protein required for uncoating of clathrin-coated vesicles. (668 aa)
PRB1Cerevisin; 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)
UPF3Component 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)
BTN2v-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)
ZUO1Zuotin; 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)
TDA3Putative 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)
SSZ1Ribosome-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)
NMD2Protein involved in the nonsense-mediated mRNA decay (NMD) pathway; interacts with Nam7p and Upf3p; involved in telomere maintenance. (1089 aa)
CPR7Peptidyl-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)
SUP35Eukaryotic 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)
HSP104Disaggregase; 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)
NAM7ATP-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)
HSC82ATP-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)
SIS1Protein 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)
SIW14Inositol phosphatase SIW14; Tyrosine phosphatase involved in actin organization and endocytosis; localized to the cytoplasm. (281 aa)
SSB2Cytoplasmic 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)
URE2Nitrogen 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)
STI1Heat 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)
SSE1ATPase 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)
PUS1tRNA: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)
HSP82ATP-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)
CUR1Curing 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)
SSA2Heat 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)
ARG82Inositol 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)
HSP26Small 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)
FES1Hsp70 (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)
SUP45Polypeptide 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)
HSP42Small 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)
SSA1Heat 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)
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
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