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STI1 protein (Saccharomyces cerevisiae) - STRING interaction network
"STI1" - Hsp90 cochaperone, interacts with the Ssa group of the cytosolic Hsp70 chaperones and activates Ssa1p ATPase activity in Saccharomyces cerevisiae
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Known Interactions
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Predicted Interactions
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textmining
co-expression
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STI1Hsp90 cochaperone, 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; May play a role in mediating the heat shock response of some HSP70 genes. It is required for optimal growth of yeast cells at both low and high temperature (589 aa)    
Predicted Functional Partners:
HSP82
Hsp90 chaperone required for pheromone signaling and negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding and nucleotide addition; interacts with Cns1p, Cpr6p, Cpr7p, Sti1p; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dim [...] (709 aa)
     
 
  0.999
HSC82
Cytoplasmic chaperone of the Hsp90 family, 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; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction such as CNA2. Undergoes a functional cycle that is linked to its ATPase activity (By similarity). Interacts dynamically with various co-chaperones that modulate its substrate reco [...] (705 aa)
     
 
  0.999
AHA1
Co-chaperone that binds to Hsp82p and activates its ATPase activity; similar to Hch1p; expression is regulated by stresses such as heat shock; Co-chaperone that binds to the molecular chaperone HSP82 and stimulates its ATPase activity. Binding to HSP82 promotes a conformational switch in the catalytic loop of HSP82, facilitating the interaction of the catalytic ’Arg-380’ with ATP in the N- terminal nucleotide-binding domain. Although not essential, it confers thermotolerance when intracellular levels of HSP82 are limiting (350 aa)
     
 
  0.999
SSE1
ATPase that is a component of the heat shock protein Hsp90 chaperone complex; binds unfolded proteins; member of the heat shock protein 70 (HSP70) family; localized to the cytoplasm; Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures (693 aa)
     
 
  0.999
SSE2
Member of the heat shock protein 70 (HSP70) family; may be involved in protein folding; localized to the cytoplasm; highly homologous to the heat shock protein Sse1p; Has a calcium-dependent calmodulin-binding activity (693 aa)
     
 
  0.998
CPR6
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; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (371 aa)
     
 
  0.998
SIS1
Type II HSP40 co-chaperone that interacts with the HSP70 protein Ssa1p; not functionally redundant with Ydj1p due to due to substrate specificity; shares similarity with bacterial DnaJ proteins; Required for nuclear migration during mitosis. It is required for the normal initiation of translation. Might mediate the dissociation of a specific protein complex of the translation machinery. Essential for viability (352 aa)
     
 
  0.997
SBA1
Co-chaperone that binds to and regulates Hsp90 family chaperones; important for pp60v-src activity in yeast; homologous to the mammalian p23 proteins and like p23 can regulate telomerase activity; Acts as a co-chaperone (216 aa)
     
 
  0.995
HSP104
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; Required, in concert with Hsp40 (YDJ1) and Hsp70 (SSA1) and small Hsps (HSP26), for the dissociation, resolubilization and refolding of aggregates of damaged proteins after heat or other environmental stresses. Extracts proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexa [...] (908 aa)
     
 
  0.994
HCH1
Heat shock protein regulator that binds to Hsp90p and may stimulate ATPase activity; originally identified as a high-copy number suppressor of a HSP90 loss-of-function mutation; GFP-fusion protein localizes to the cytoplasm and nucleus; Co-chaperone that binds to the molecular chaperone HSP82 and stimulates its ATPase activity. Although not essential, it confers thermotolerance when intracellular levels of HSP82 are limiting (153 aa)
     
 
  0.990
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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