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CPR4 protein (Saccharomyces cerevisiae) - STRING interaction network
"CPR4" - Peptidyl-prolyl cis-trans isomerase in Saccharomyces cerevisiae
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Known Interactions
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Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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CPR4Peptidyl-prolyl cis-trans isomerase (cyclophilin), catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (318 aa)    
Predicted Functional Partners:
MCD1
Essential subunit of the cohesin complex required for sister chromatid cohesion in mitosis and meiosis; apoptosis induces cleavage and translocation of a C-terminal fragment to mitochondria; expression peaks in S phase; Cleavable component of the cohesin complex involved in chromosome cohesion during cell cycle. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by ESP1 and diss [...] (566 aa)
       
 
  0.730
FPR1
Peptidyl-prolyl cis-trans isomerase (PPIase), binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (114 aa)
 
 
 
  0.724
FPR2
Membrane-bound peptidyl-prolyl cis-trans isomerase (PPIase), binds to the drugs FK506 and rapamycin; expression pattern suggests possible involvement in ER protein trafficking; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. FKBP-13 may play a role in protein trafficking in the ER (135 aa)
 
 
 
  0.713
PDI1
Protein disulfide isomerase; multifunctional protein resident in the endoplasmic reticulum lumen, essential for the formation of disulfide bonds in secretory and cell-surface proteins, unscrambles non-native disulfide bonds; forms a complex with Mnl /.../t has exomannosidase activity, processing unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2 which promotes degradation in the unfolded protein response; Protein disulfide isomerase of ER lumen required for formation of disulfide bonds in secretory and cell-surface proteins and which unscrambles non-native disulfide bon [...] (522 aa)
     
 
  0.643
EUG1
Protein disulfide isomerase of the endoplasmic reticulum lumen, function overlaps with that of Pdi1p; may interact with nascent polypeptides in the ER; Probably interacts with nascent polypeptides in the endoplasmic reticulum. It is an essential gene only in the absence of PDI. Its native disulfide isomerase activity is very low (517 aa)
     
 
  0.630
RRF1
Mitochondrial ribosome recycling factor, essential for mitochondrial protein synthesis and for the maintenance of the respiratory function of mitochondria; Necessary for protein synthesis in mitochondria. Function as a ribosome recycling factor in mitochondria (230 aa)
     
      0.605
CPR7
Peptidyl-prolyl cis-trans isomerase (cyclophilin), catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds to Hsp82p and contributes to chaperone activity; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Plays a major role in negative regulation of the heat shock transcription factor (HSF) (393 aa)
   
   
  0.593
TIM44
Essential component of the Translocase of the Inner Mitochondrial membrane (TIM23 complex); tethers the import motor and regulatory factors (PAM complex) to the translocation channel (Tim23p-Tim17p core complex); 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. Recruits mitochondrial HSP70 and its co- chaperone (MGE1) to drive protein translocation into the matrix using ATP as an energy source (431 aa)
       
 
  0.583
GRX4
Hydroperoxide and superoxide-radical responsive glutathione-dependent oxidoreductase; monothiol glutaredoxin subfamily member along with Grx3p and Grx5p; protects cells from oxidative damage; mutant has increased aneuploidy tolerance; Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (By similarity). Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit (Probable) (244 aa)
     
 
  0.537
GRX3
Hydroperoxide and superoxide-radical responsive glutathione-dependent oxidoreductase; monothiol glutaredoxin subfamily member along with Grx4p and Grx5p; protects cells from oxidative damage; Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (By similarity). Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit (Probable) (285 aa)
     
 
  0.537
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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