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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
cct-1T-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 (549 aa)    
Predicted Functional Partners:
cct-5
T-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
  
0.999
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-7
Chaperonin Containing TCP-1; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis
  
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
eef-1G
Probable elongation factor 1-gamma; Probably plays a role in anchoring the complex to other cellular components
   
 
 0.990
Y73B3A.10
Protein Y73B3A.10 (Y73B3A.10) mRNA, complete cds
   
 
 0.988
ran-1
GTP-binding nuclear protein ran-1; Ran GTPase system comprises ran-1, ran-2 and ran-3 and is essential in nucleocytoplasmic transport. Ran-1 is a GTP- binding protein that mediates the interaction between mitotic chromosomes and kinetochore microtubules. Plays a crucial role in nuclear envelope assembly at the end of each cell division. Required for the import of protein into the nucleus and also for RNA export. RCC1 (ran-3)/Ran (ran-1) complex (together with other proteins) acts as a component of a signal transmission pathway that detects unreplicated DNA
   
  
 0.965
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Caenorhabditis elegans, Rhabditis elegans, roundworm
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