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
cct-5T-complex protein 1 subunit epsilon; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. (542 aa)    
Predicted Functional Partners:
cct-6
T-complex protein 1 subunit zeta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
   
0.999
cct-3
T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis (By similarity). Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). Plays a role in microtubule polymerization.
   
0.999
cct-4
T-complex protein 1 subunit delta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
  
0.999
cct-1
T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
  
0.999
cct-7
T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
   
0.999
cct-2
T-complex protein 1 subunit beta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin; Belongs to the TCP-1 chaperonin family.
  
0.999
cct-8
T-complex protein 1 subunit theta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). Required for correct subcellular localization of pgl-1; Belongs to the TCP-1 chaperonin family.
   
0.999
T11G6.5
Uncharacterized protein.
   
 0.990
hsp-70
Heat Shock Protein; Belongs to the heat shock protein 70 family.
  
 0.975
pfd-4
Probable prefoldin subunit 4; Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity); Belongs to the prefoldin subunit beta family.
    
 
 0.877
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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