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-8T-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 (548 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-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
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
pas-5
Proteasome subunit alpha type-5; The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity)
  
 0.990
Y73B3A.10
Protein Y73B3A.10 (Y73B3A.10) mRNA, complete cds
   
 
 0.988
rpn-11
26S proteasome non-ATPase regulatory subunit 14; Metalloprotease component of the 26S proteasome that specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The function of the 'Lys-63'-specific deubiquitination of the proteasome is unclear (By similarity)
   
 0.987
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Caenorhabditis elegans, Rhabditis elegans, roundworm
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