• Version:
  • 11.0 [archived version]
STRINGSTRING
MDM1 MDM1 TRAP1 TRAP1 CLPB CLPB AHSA2 AHSA2 AHSA1 AHSA1 TTC12 TTC12 HSP90AB1 HSP90AB1 HSP90AA1 HSP90AA1 NCAM1 NCAM1 ANKK1 ANKK1 DRD2 DRD2
"TTC12" - Tetratricopeptide repeat domain containing in Homo sapiens
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.
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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
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Cooccurence
Coexpression
Experiments
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[Homology]
Score
TTC12Tetratricopeptide repeat domain containing (705 aa)    
Predicted Functional Partners:
ANKK1
Ankyrin repeat and kinase domain containing 1; Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family (765 aa)
     
 
  0.926
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)
   
 
  0.704
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)
   
 
  0.704
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)
   
 
  0.704
NCAM1
Neural cell adhesion molecule 1; This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc; CD molecules (884 aa)
           
  0.700
DRD2
D(2) dopamine receptor; Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase; Belongs to the G-protein coupled receptor 1 family (443 aa)
           
  0.671
MDM1
Nuclear protein MDM1; Microtubule-binding protein that negatively regulates centriole duplication. Binds to and stabilizes microtubules (714 aa)
           
  0.658
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
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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