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
Tcp1T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity) (556 aa)    
Predicted Functional Partners:
Cct8
Chaperonin subunit 8 (Theta) (Predicted), isoform CRA_a; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis
   
0.999
Cct4
T-complex protein 1 subunit delta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity); Belongs to the TCP-1 chaperonin family
   
0.999
Cct5
T-complex protein 1 subunit epsilon; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity)
   
0.999
Cct7
Chaperonin-containing TCP1 subunit 7; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis
   
0.999
Cct2
T-complex protein 1 subunit beta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin
   
0.998
Cct3
T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. Plays a role in the assembly of the von Hippel-Lindau ubiquitination complex (By similarity). Interacts with DNAAF4 (By similarity)
  
0.994
Cct6b
Chaperonin containing Tcp1, subunit 6B (Zeta 2); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis
   
0.990
Cct6a
Chaperonin containing Tcp1, subunit 6A (Zeta 1); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis
   
0.987
Bbs10
Putative uncharacterized protein RGD1560748_predicted; Bardet-Biedl syndrome 10
   
 
 0.951
ENSRNOG00000000656
Uncharacterized protein
  
 
0.946
Your Current Organism:
Rattus norvegicus
NCBI taxonomy Id: 10116
Other names: Buffalo rat, Gunn rats, Norway rat, R. norvegicus, Rattus PC12 clone IS, Rattus norvegicus, Rattus rattiscus, Rattus sp. strain Wistar, Sprague-Dawley rat, Wistar rats, brown rat, laboratory rat, rat, rats, zitter rats
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