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AHA1 protein (Saccharomyces cerevisiae) - STRING interaction network
"AHA1" - Co-chaperone that binds to Hsp82p and activates its ATPase activity in Saccharomyces cerevisiae
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Known Interactions
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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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AHA1Co-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)    
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)
     
 
  0.999
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)
     
 
  0.998
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)
     
 
  0.997
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)
     
 
  0.986
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)
     
 
  0.944
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)
     
 
  0.924
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)
     
 
  0.893
GCN1
Positive regulator of the Gcn2p kinase activity, forms a complex with Gcn20p; proposed to stimulate Gcn2p activation by an uncharged tRNA; Acts as a positive activator of the GCN2 protein kinase activity in response to amino acid starvation (PubMed-8497269, PubMed-24333428). Component of the GCN1-GCN20 complex that forms a complex with GCN2 on translating ribosomes; during this process, GCN1 seems to act as a chaperone to facilitate delivery of uncharged tRNAs that enter the A site of ribosomes to the tRNA- binding domain of GCN2, and hence stimulating GCN2 kinase activity (PubMed-7621 [...] (2672 aa)
       
 
  0.804
MBF1
Transcriptional coactivator that bridges the DNA-binding region of Gcn4p and TATA-binding protein Spt15p; suppressor of frameshift mutations; Transcriptional coactivator that stimulates GCN4- dependent transcriptional activity by bridging the DNA-binding region of GCN4 and TBP (SPT15), thereby recruiting TBP to GCN4- bound promoters (151 aa)
     
   
  0.801
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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