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HCH1 protein (Saccharomyces cerevisiae) - STRING interaction network
"HCH1" - Heat shock protein regulator that binds to Hsp90p and may stimulate ATPase activity in Saccharomyces cerevisiae
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Predicted Interactions
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HCH1Heat 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)    
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)
     
 
  0.992
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)
     
 
  0.990
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)
     
 
  0.985
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)
     
 
  0.935
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)
     
 
  0.914
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)
     
 
  0.898
SEC13
Component of the Nup84 nuclear pore sub-complex, the Sec13p-Sec31p complex of the COPII vesicle coat, and the SEA (Seh1-associated) complex; required for vesicle formation in ER to Golgi transport and nuclear pore complex organization; the Nup84 sub /.../x has a role in transcription elongation; Functions as a component of the nuclear pore complex (NPC) and the COPII coat. It is one of 5 proteins constituting the COPII coat, which is involved in anterograde (ER to Golgi) double- membrane transport vesicle formation. First the small GTPase SAR1, activated by and binding to the integral [...] (297 aa)
     
      0.753
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)
     
 
0.731
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)
     
   
  0.730
TEF4
Gamma subunit of translational elongation factor eEF1B, stimulates the binding of aminoacyl-tRNA (AA-tRNA) to ribosomes by releasing eEF1A (Tef1p/Tef2p) from the ribosomal complex; Subunit of the eukaryotic elongation factor 1 complex (eEF1). Probably plays a role in anchoring the complex to other cellular components (By similarity) (412 aa)
     
 
  0.712
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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