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SSB1 protein (Saccharomyces cerevisiae) - STRING interaction network
"SSB1" - Cytoplasmic ATPase that is a ribosome-associated molecular chaperone, functions with J-protein partner Zuo1p in Saccharomyces cerevisiae
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Predicted Interactions
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SSB1Cytoplasmic ATPase that is a ribosome-associated molecular chaperone, functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p; May aid in the passage of the nascent polypeptide chain through the ribosome channel into the cytosol. Such an interaction could be crucial for continuous transport of the polypeptide; could serve to prevent the nascent polypeptide from interfering with translation by clogging the ribosome channel (613 aa)    
Predicted Functional Partners:
YDJ1
Type I HSP40 co-chaperone involved in regulation of the HSP90 and HSP70 functions; involved in protein translocation across membranes; member of the DnaJ family; Probably involved in mitochondrial protein import. Is also required for efficient translocation of pre-pro-alpha-factor. Involved in heme regulation of HAP1, as a component of the high- molecular-weight (HMC) complex (409 aa)
 
  0.981
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)
     
 
  0.974
HLJ1
Co-chaperone for Hsp40p, anchored in the ER membrane; with its homolog Ydj1p promotes ER-associated protein degradation (ERAD) of integral membrane substrates; similar to E. coli DnaJ (224 aa)
 
  0.973
MGE1
Mitochondrial matrix cochaperone, acts as a nucleotide release factor for Ssc1p in protein translocation and folding; also acts as cochaperone for Ssq1p in folding of Fe-S cluster proteins; homolog of E. coli GrpE; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of SSC1 to substrate proteins and the association of SSC1 with TIM44 (228 aa)
   
 
  0.967
SCJ1
One of several homologs of bacterial chaperone DnaJ, located in the ER lumen where it cooperates with Kar2p to mediate maturation of proteins; Regulates protein folding in the endoplasmic reticulum lumen. Probably acts as a J-protein for the Hsp70-type chaperone KAR2 by stimulating its ATP-dependent reaction cycle and initiating folding reactions. Also involved in the endoplasmic reticulum-associated degradation (ERAD) process. Cooperates with KAR2 and another J-protein JEM1 to facilitate the export of ERAD substrates to the cytoplasm by maintaining them in a translocation-competent st [...] (377 aa)
 
  0.965
MDJ1
Co-chaperone that stimulates HSP70 protein Ssc1p ATPase activity; involved in protein folding/refolding in the mitochodrial matrix; required for proteolysis of misfolded proteins; member of the HSP40 (DnaJ) family of chaperones; Plays a role in mitochondrial biogenesis and protein folding (511 aa)
 
  0.963
XDJ1
Putative chaperone, homolog of E. coli DnaJ, closely related to Ydj1p; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies (459 aa)
 
  0.962
APJ1
Putative chaperone of the HSP40 (DNAJ) family; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; Putative chaperone involved in protein folding. Interferes with propagation of [PSI+] prion when overproduced (528 aa)
 
  0.957
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)
   
  0.953
SWA2
Auxilin-like protein involved in vesicular transport; clathrin-binding protein required for uncoating of clathrin-coated vesicles; Cofactor for the uncoating of clathrin-coated vesicles (CCVs) by Hsp70-type chaperones (SSA1/2/3 and SSB1/2). Coat disassembly is important for fusion of vesicles with target membranes and for recycling components of clathrin coats to the cytoplasm for further rounds of vesicle formation. Binds to assembled clathrin and recruits the ATP-activated chaperone to CCVs. Stimulates the ATPase activity of the clathrin-associated Hsp70-type chaperone SSA1, which th [...] (668 aa)
       
 
  0.953
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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