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SBA1 protein (Saccharomyces cerevisiae) - STRING interaction network
"SBA1" - Co-chaperone that binds to and regulates Hsp90 family chaperones in Saccharomyces cerevisiae
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Predicted Interactions
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protein homology
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SBA1Co-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)    
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
STI1
Hsp90 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)
     
 
  0.995
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)
     
  0.995
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)
     
 
  0.986
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)
     
 
  0.983
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)
     
 
  0.935
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; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Plays a major role in negative regulation of the heat shock transcription factor (HSF) (393 aa)
     
 
  0.892
CNS1
TPR-containing co-chaperone; binds both Hsp82p (Hsp90) and Ssa1p (Hsp70) and stimulates the ATPase activity of SSA1, ts mutants reduce Hsp82p function while over expression suppresses the phenotypes of an HSP82 ts allele and a cpr7 deletion; Co-chaperone that binds to the molecular chaperones Hsp90 (HSC82 and HSP82) and Hsp70 (SSA1). Stimulates SSA1 ATPase activity, but not Hsp90 ATPase activity. Involved in only a subset of Hsp90 functions (385 aa)
     
 
  0.849
PPT1
Protein serine/threonine phosphatase with similarity to human phosphatase PP5; present in both the nucleus and cytoplasm; expressed during logarithmic growth; computational analyses suggest roles in phosphate metabolism and rRNA processing; Protein phosphatase that specifically binds to and dephosphorylates the molecular chaperone Hsp90 (HSC82 and HSP82). Dephosphorylation positively regulates the Hsp90 chaperone machinery (513 aa)
     
 
  0.837
CDC37
Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding; Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Involved in both the HOG and the PKC MAP kinase signaling cascade necessary for adaptation to stress conditions due to high osmolarity or cell wall perturbation (506 aa)
     
 
  0.835
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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