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HSP90B1 protein (human) - STRING interaction network
"HSP90B1" - Endoplasmin in Homo sapiens
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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
filled nodes:
some 3D structure is known or predicted
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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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HSP90B1Endoplasmin; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity; Belongs to the heat shock protein 90 family (803 aa)    
Predicted Functional Partners:
CALR
Calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity) (417 aa)
     
  0.999
HSPA5
78 kDa glucose-regulated protein; Plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate (By similarity); Belongs to the heat shock protein 70 family (654 aa)
     
  0.999
P4HB
Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...] (508 aa)
     
  0.998
PDIA6
Protein disulfide-isomerase A6; May function as a chaperone that inhibits aggregation of misfolded proteins. Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling. May also regulate the UPR via the EIF2AK3 UPR sensor. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin; Protein disulfide isomerases (492 aa)
     
  0.997
HYOU1
Hypoxia up-regulated protein 1; Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding; Belongs to the heat shock protein 70 family (999 aa)
     
  0.995
DNAJC3
DnaJ homolog subfamily C member 3; Involved in the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress. Acts as a negative regulator of the EIF2AK4/GCN2 kinase activity by preventing the phosphorylation of eIF-2-alpha at ’Ser-52’ and hence attenuating general protein synthesis under ER stress, hypothermic and amino acid starving stress conditions (By similarity). Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2 [...] (504 aa)
     
  0.995
PRKCSH
Glucosidase 2 subunit beta; Regulatory subunit of glucosidase II; EF-hand domain containing (535 aa)
     
  0.994
PDIA4
Protein disulfide-isomerase A4; Protein disulfide isomerase family A member 4; Belongs to the protein disulfide isomerase family (645 aa)
     
 
  0.991
ATF6
Cyclic AMP-dependent transcription factor ATF-6 alpha; Transmembrane glycoprotein of the endoplasmic reticulum that functions as a transcription activator and initiates the unfolded protein response (UPR) during endoplasmic reticulum stress. Cleaved upon ER stress, the N-terminal processed cyclic AMP-dependent transcription factor ATF-6 alpha translocates to the nucleus where it activates transcription of genes involved in the UPR. Binds DNA on the 5’-CCAC[GA]-3’half of the ER stress response element (ERSE) (5’-CCAAT-N(9)-CCAC[GA]-3’) and of ERSE II (5’- ATTGG-N-CCACG-3’). Binding to E [...] (670 aa)
     
 
  0.985
RCN1
Reticulocalbin-1; May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment; EF-hand domain containing (331 aa)
     
    0.983
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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