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PIN4 protein (Latimeria chalumnae) - STRING interaction network
"PIN4" - Protein (peptidylprolyl cis/trans isomerase) NIMA-interacting, 4 in Latimeria chalumnae
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query proteins and first shell of interactors
white nodes:
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
Others
textmining
co-expression
protein homology
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Gene Fusion
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[Homology]
Score
PIN4Protein (peptidylprolyl cis/trans isomerase) NIMA-interacting, 4 (parvulin) (148 aa)    
Predicted Functional Partners:
SUPT5H
Suppressor of Ty 5 homolog (S. cerevisiae) (1081 aa)
     
 
  0.704
PPIE
Peptidylprolyl isomerase E (cyclophilin E); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (302 aa)
     
 
  0.679
GPHN
Gephyrin (777 aa)
     
 
  0.649
IMPDH1
IMP (inosine 5’-monophosphate) dehydrogenase 1 (515 aa)
     
 
  0.615
SAMM50
Sorting and assembly machinery component 50 homolog (S. cerevisiae) (302 aa)
   
 
  0.605
FKBP1B
FK506 binding protein 1B, 12.6 kDa (79 aa)
     
 
  0.601
FKBP1A
FK506 binding protein 1A, 12kDa (142 aa)
     
 
  0.601
TIMM44
Translocase of inner mitochondrial membrane 44 homolog (yeast); Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner (434 aa)
       
      0.590
RRBP1
Ribosome binding protein 1 homolog 180kDa (dog) (1345 aa)
       
      0.590
SCO2
SCO2 cytochrome c oxidase assembly protein (269 aa)
       
      0.590
Your Current Organism:
Latimeria chalumnae
NCBI taxonomy Id: 7897
Other names: Actinistia, Choanichthyes, Coelacanthidae, Coelacanthiformes, Coelacanthimorpha, Crossopterygii, L. chalumnae, Latimeria, Latimeria chalumnae, Latimeriidae, coelacanth, coelacanths, lobe-finned fishes
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