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CIR2 protein (Saccharomyces cerevisiae) - STRING interaction network
"CIR2" - Putative ortholog of human electron transfer flavoprotein dehydrogenase in Saccharomyces cerevisiae
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Predicted Interactions
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CIR2Putative ortholog of human electron transfer flavoprotein dehydrogenase (ETF-dH); found in a large supramolecular complex with other mitochondrial dehydrogenases; may have a role in oxidative stress response; Accepts electrons from ETF and reduces ubiquinone (631 aa)    
Predicted Functional Partners:
AIM45
Putative ortholog of mammalian electron transfer flavoprotein complex subunit ETF-alpha; interacts with frataxin, Yfh1p; null mutant displays elevated frequency of mitochondrial genome loss; may have a role in oxidative stress response; The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl- CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity) (344 aa)
 
 
  0.996
CIR1
Mitochondrial protein that interacts with frataxin (Yfh1p); putative ortholog of mammalian electron transfer flavoprotein complex subunit ETF-beta; may have a role in oxidative stress response; The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl- CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity) (261 aa)
 
 
  0.993
COQ2
Para hydroxybenzoate- polyprenyl transferase, catalyzes the second step in ubiquinone (coenzyme Q) biosynthesis; Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate (372 aa)
   
 
  0.755
FUM1
Fumarase, converts fumaric acid to L-malic acid in the TCA cycle; cytosolic and mitochondrial distribution determined by the N-terminal targeting sequence, protein conformation, and status of glyoxylate shunt; phosphorylated in mitochondria (488 aa)
     
 
  0.671
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)
       
 
  0.668
TRX1
Cytoplasmic thioredoxin isoenzyme of the thioredoxin system which protects cells against oxidative and reductive stress, forms LMA1 complex with Pbi2p, acts as a cofactor for Tsa1p, required for ER-Golgi transport and vacuole inheritance; Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and r [...] (103 aa)
       
 
  0.588
TRX2
Cytoplasmic thioredoxin isoenzyme of the thioredoxin system which protects cells against oxidative and reductive stress, forms LMA1 complex with Pbi2p, acts as a cofactor for Tsa1p, required for ER-Golgi transport and vacuole inheritance; Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and r [...] (104 aa)
       
 
  0.588
MPD1
Member of the protein disulfide isomerase (PDI) family; interacts with and inhibits the chaperone activity of Cne1p; MPD1 overexpression in a pdi1 null mutant suppresses defects in Pdi1p functions such as carboxypeptidase Y maturation; Participates in the folding of proteins containing disulfide bonds (318 aa)
       
 
  0.577
MPD2
Member of the protein disulfide isomerase (PDI) family, exhibits chaperone activity; overexpression suppresses the lethality of a pdi1 deletion but does not complement all Pdi1p functions; undergoes oxidation by Ero1p; Non essential disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. Able to fold proteins by being directly oxidized by ERO1 (277 aa)
       
 
  0.577
EPS1
ER protein with chaperone and co-chaperone activity, involved in retention of resident ER proteins; has a role in recognizing proteins targeted for ER-associated degradation (ERAD), member of the protein disulfide isomerase family; Acts as a membrane-bound chaperone in endoplasmic reticulum quality control. Probably facilitates presentation of substrate to membrane-bound components of the degradation machinery (701 aa)
       
 
  0.577
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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