STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
pdi-1Protein disulfide-isomerase 1; Belongs to the protein disulfide isomerase family. (485 aa)    
Predicted Functional Partners:
ero-1
Endoplasmic reticulum oxidoreductin-1; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes pdi-1, the enzyme catalyzing protein disulfide formation, in order to allow pdi-1 to sustain additional rounds of disulfide formation. Following pdi reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell (By similarity).
   
 0.960
hsp-3
Heat shock 70 kDa protein C; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.
  
 
 0.796
hsp-4
Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family.
  
 
 0.745
crt-1
Calreticulin; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegen [...]
   
 
 0.728
prdx-6
Thioredoxin domain-containing protein.
  
 
 0.705
enpl-1
Endoplasmin homolog; Molecular chaperone that functions in the processing and transport of secreted proteins; Belongs to the heat shock protein 90 family.
   
 
 0.695
prdx-2
Thioredoxin domain-containing protein.
  
 
 0.669
sec-61
Plug_translocon domain-containing protein.
   
 
 0.651
pdi-6
Protein disulfide-isomerase A6 homolog; May function as a chaperone that inhibits aggregation of misfolded proteins (By similarity). May negatively regulate the unfolded protein response (UPR) through binding to UPR sensors ; Belongs to the protein disulfide isomerase family.
  
 
0.640
dld-1
Dihydrolipoyl dehydrogenase, mitochondrial.
  
 
 0.617
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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