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CPR6 protein (Saccharomyces cerevisiae) - STRING interaction network
"CPR6" - Peptidyl-prolyl cis-trans isomerase 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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CPR6Peptidyl-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)    
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)
     
 
  0.998
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)
     
 
  0.997
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)
   
 
  0.994
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)
     
 
  0.983
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)
   
 
  0.940
PRP4
Splicing factor, component of the U4/U6-U5 snRNP complex; Involved in RNA splicing. Is required for the association of U4/U6 snRNP with U5 snRNP in an early step of spliceosome assembly (465 aa)
     
 
  0.921
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)
     
 
  0.920
SSA1
ATPase involved in protein folding and nuclear localization signal (NLS)-directed nuclear transport; member of heat shock protein 70 (HSP70) family; forms a chaperone complex with Ydj1p; localized to the nucleus, cytoplasm, and cell wall; 98% identi /.../th Ssa2p, but subtle differences between the two proteins provide functional specificity with respect to propagation of yeast [URE3] prions and vacuolar-mediated degradations of gluconeogenesis enzymes; May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functio [...] (642 aa)
   
 
  0.892
HSP78
Oligomeric mitochondrial matrix chaperone; cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; able to prevent the aggregation of misfolded proteins as well as resolubilize protein aggregates; Required, in concert with mitochondrial Hsp70 (SSC1), for the dissociation, resolubilization and refolding of aggregates of damaged proteins in the mitochondrial matrix after heat stress. May extract proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by the Hsp [...] (811 aa)
   
 
  0.885
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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