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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
CCT2T-complex protein 1 subunit beta; Subunit beta of the cytosolic chaperonin Cct ring complex; related to Tcp1p, required for the assembly of actin and tubulins in vivo (527 aa)    
Predicted Functional Partners:
CCT4
T-complex protein 1 subunit delta; Subunit of the cytosolic chaperonin Cct ring complex; related to Tcp1p, required for the assembly of actin and tubulins in vivo
  
0.999
CCT6
T-complex protein 1 subunit zeta; Subunit of the cytosolic chaperonin Cct ring complex; related to Tcp1p, essential protein that is required for the assembly of actin and tubulins in vivo; contains an ATP-binding motif
  
0.999
TCP1
Alpha subunit of chaperonin-containing T-complex; complex mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein
  
0.999
CCT8
T-complex protein 1 subunit theta; Subunit of the cytosolic chaperonin Cct ring complex; related to Tcp1p, required for the assembly of actin and tubulins in vivo
  
0.999
CCT3
T-complex protein 1 subunit gamma; Subunit of the cytosolic chaperonin Cct ring complex; related to Tcp1p, required for the assembly of actin and tubulins in vivo; capable of binding Q/N rich proteins and mediating their folding
  
0.999
CCT7
T-complex protein 1 subunit eta; Subunit of the cytosolic chaperonin Cct ring complex; related to Tcp1p, required for the assembly of actin and tubulins in vivo; mutant has increased aneuploidy tolerance
  
0.999
CCT5
T-complex protein 1 subunit epsilon; Subunit of the cytosolic chaperonin Cct ring complex; related to Tcp1p, required for the assembly of actin and tubulins in vivo
  
0.999
CDC55
Regulatory subunit B of protein phosphatase 2A (PP2A); Zds1p/2p-dependent localization to cytoplasm promotes mitotic entry; localization to nucleus prevents mitotic exit; required for correct nuclear division, chromosome segregation during achiasmate meiosis; maintains nucleolar sequestration of Cdc14p during early meiosis; limits formation of PP2A-Rts1p holocomplexes to ensure timely dissolution of sister chromosome cohesion; homolog of mammalian B55
    
 
 0.971
FAR8
Protein involved in recovery from arrest in response to pheromone; acts in a cell cycle arrest recovery pathway independent from Far1p; interacts with Far3p, Far7p, Far9p, Far10p, and Far11p
   
   0.962
PPH21
Catalytic subunit of protein phosphatase 2A (PP2A); functionally redundant with Pph22p; methylated at C terminus; forms alternate complexes with several regulatory subunits; involved in signal transduction and regulation of mitosis; forms nuclear foci upon DNA replication stress; PPH21 has a paralog, PPH22, that arose from the whole genome duplication
   
   0.961
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.