STRINGSTRING
Cct8 protein (mouse) - STRING interaction network
"Cct8" - Chaperonin containing Tcp1, subunit 8 in Mus musculus
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
Cct8Chaperonin containing Tcp1, subunit 8 (theta); 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) (548 aa)    
Predicted Functional Partners:
Cct3
Chaperonin containing Tcp1, subunit 3 (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 DYX1C1 (545 aa)
   
0.999
Cct4
Chaperonin containing Tcp1, subunit 4 (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) (539 aa)
   
0.999
Cct6a
Chaperonin containing Tcp1, subunit 6a (zeta) (532 aa)
   
0.999
Cct2
Chaperonin containing Tcp1, subunit 2 (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 (By similarity) (535 aa)
     
0.999
Cct5
Chaperonin containing Tcp1, subunit 5 (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) (541 aa)
     
0.999
Cct6b
Chaperonin containing Tcp1, subunit 6b (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). May have specific functions in the folding of testicular proteins and for interactions with testicular molecular chaperones (531 aa)
   
0.999
Tcp1
T-complex protein 1; 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)
   
0.999
Cct7
Chaperonin containing Tcp1, subunit 7 (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 (544 aa)
   
0.998
Bbs10
Bardet-Biedl syndrome 10 (human); Probable 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. Involved in adipogenic differentiation (By similarity) (713 aa)
     
 
  0.980
Mkks
McKusick-Kaufman syndrome; Probable 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 (By similarity). May play a role in protein processing in limb, cardiac and reproductive system development. May play a role in cytokinesis (By similarity) (570 aa)
     
 
  0.972
Your Current Organism:
Mus musculus
NCBI taxonomy Id: 10090
Other names: LK3 transgenic mice, M. musculus, Mus, Mus muscaris, Mus musculus, Mus sp. 129SV, house mouse, mice, mouse, nude mice, transgenic mice
Server load: low (6%) [HD]