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  • 11.0 [archived version]
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IKZF2 IKZF2 THSD1 THSD1 INSC INSC TTC28 TTC28 AHSA2 AHSA2 HSP90AB1 HSP90AB1 CLPB CLPB TRAP1 TRAP1 HSP90AA1 HSP90AA1 HSPD1 HSPD1 AHSA1 AHSA1
"TTC28" - Tetratricopeptide repeat protein 28 in Homo sapiens
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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TTC28Tetratricopeptide repeat protein 28; During mitosis, may be involved in the condensation of spindle midzone microtubules, leading to the formation of midbody; Tetratricopeptide repeat domain containing (2481 aa)    
Predicted Functional Partners:
INSC
Protein inscuteable homolog; May function as an adapter linking the Par3 complex to the GPSM1/GPSM2 complex. Involved in spindle orientation during mitosis. May regulate cell proliferation and differentiation in the developing nervous system. May play a role in the asymmetric division of fibroblasts and participate in the process of stratification of the squamous epithelium (By similarity); Armadillo-like helical domain containing (579 aa)
       
 
  0.755
HSP90AB1
Heat shock protein HSP 90-beta; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interacti [...] (724 aa)
   
 
  0.705
HSP90AA1
Heat shock protein HSP 90-alpha; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a ra [...] (854 aa)
   
 
  0.705
TRAP1
Heat shock protein 75 kDa, mitochondrial; Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA; Belongs to the heat shock protein 90 family (704 aa)
   
 
  0.705
THSD1
Thrombospondin type-1 domain-containing protein 1; Thrombospondin type 1 domain containing 1 (852 aa)
     
   
  0.659
AHSA2
Activator of 90 kDa heat shock protein ATPase homolog 2; Co-chaperone that stimulates HSP90 ATPase activity (137 aa)
     
 
  0.651
AHSA1
Activator of 90 kDa heat shock protein ATPase homolog 1; Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (338 aa)
     
 
  0.651
CLPB
Caseinolytic peptidase B protein homolog; May function as a regulatory ATPase and be related to secretion/protein trafficking process; AAA ATPases (707 aa)
     
 
  0.638
IKZF2
Zinc finger protein Helios; Associates with Ikaros at centromeric heterochromatin; Zinc fingers C2H2-type (526 aa)
       
 
  0.618
HSPD1
60 kDa heat shock protein, mitochondrial; Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per rin [...] (573 aa)
     
   
  0.615
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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