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SIS1 protein (Saccharomyces cerevisiae) - STRING interaction network
"SIS1" - Type II HSP40 co-chaperone that interacts with the HSP70 protein Ssa1p in Saccharomyces cerevisiae
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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SIS1Type 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)    
Predicted Functional Partners:
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)
   
 
  0.999
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)
 
  0.999
SSA2
ATP binding protein involved in protein folding and vacuolar import of proteins; member of heat shock protein 70 (HSP70) family; associated with the chaperonin-containing T-complex; present in the cytoplasm, vacuolar membrane and cell wall; 98% iden /.../with Ssa1p, 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 funct [...] (639 aa)
 
  0.999
KAR2
ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis (682 aa)
 
  0.998
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)
     
 
  0.997
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)
   
 
  0.997
SSA4
Heat shock protein that is highly induced upon stress; plays a role in SRP-dependent cotranslational protein-membrane targeting and translocation; member of the HSP70 family; cytoplasmic protein that concentrates in nuclei upon starvation (642 aa)
 
  0.994
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)
   
  0.991
SSA3
ATPase involved in protein folding and the response to stress; plays a role in SRP-dependent cotranslational protein-membrane targeting and translocation; member of the heat shock protein 70 (HSP70) family; localized to the cytoplasm (649 aa)
 
  0.991
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)
   
  0.989
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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