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  • 11.0 [archived version]
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ATP5J ATP5J DUT DUT PPID PPID FKBP7 FKBP7 PCYOX1 PCYOX1 PPIA PPIA PIN4 PIN4 ERP27 ERP27 PIN1 PIN1 FOXRED2 FOXRED2 PPIB PPIB
"FKBP7" - Peptidylprolyl isomerase 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
Others
textmining
co-expression
protein homology
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Score
FKBP7Peptidylprolyl isomerase; EF-hand domain containing (222 aa)    
Predicted Functional Partners:
ATP5J
ATP synthase-coupling factor 6, mitochondrial; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of t [...] (116 aa)
     
      0.864
DUT
Deoxyuridine 5’-triphosphate nucleotidohydrolase, mitochondrial; This enzyme is involved in nucleotide metabolism- it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA; Belongs to the dUTPase family (252 aa)
     
      0.834
PIN4
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4; Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA; Belongs to the PpiC/parvulin rotamase family. PIN4 subfamily (156 aa)
     
 
  0.768
PIN1
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr- Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. Can transactivate multiple [...] (163 aa)
     
 
  0.765
PPIA
Peptidyl-prolyl cis-trans isomerase A; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. PPIase A subfamily (165 aa)
     
 
  0.756
PPIB
Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Cyclophilin peptidylprolyl isomerases (216 aa)
     
 
  0.743
ERP27
Endoplasmic reticulum protein 27; Belongs to the protein disulfide isomerase family (273 aa)
       
 
  0.687
PPID
Peptidyl-prolyl cis-trans isomerase D; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexe [...] (370 aa)
       
 
  0.685
PCYOX1
Prenylcysteine oxidase 1; Involved in the degradation of prenylated proteins. Cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine (505 aa)
     
   
  0.671
FOXRED2
FAD-dependent oxidoreductase domain-containing protein 2; Probable flavoprotein which may function in endoplasmic reticulum associated degradation (ERAD). May bind non-native proteins in the endoplasmic reticulum and target them to the ubiquitination machinery for subsequent degradation (684 aa)
           
  0.667
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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