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ILV5 protein (Saccharomyces cerevisiae) - STRING interaction network
"ILV5" - Acetohydroxyacid reductoisomerase and mtDNA binding protein in Saccharomyces cerevisiae
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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ILV5Acetohydroxyacid reductoisomerase and mtDNA binding protein; involved in branched-chain amino acid biosynthesis and maintenance of wild-type mitochondrial DNA; found in mitochondrial nucleoids (395 aa)    
Predicted Functional Partners:
ILV3
Dihydroxyacid dehydratase, catalyzes third step in the common pathway leading to biosynthesis of branched-chain amino acids (585 aa)
 
  0.999
ILV2
Acetolactate synthase, catalyses the first common step in isoleucine and valine biosynthesis and is the target of several classes of inhibitors, localizes to the mitochondria; expression of the gene is under general amino acid control (687 aa)
 
 
  0.998
ILV6
Regulatory subunit of acetolactate synthase, which catalyzes the first step of branched-chain amino acid biosynthesis; enhances activity of the Ilv2p catalytic subunit, localizes to mitochondria; Stimulates activity of the acetolactate synthase catalytic subunit ILV2 seven- to tenfold and confers sensitivity to inhibition by valine and activation by ATP (309 aa)
   
  0.997
LEU1
Isopropylmalate isomerase, catalyzes the second step in the leucine biosynthesis pathway; Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate (779 aa)
   
   
  0.965
BAT2
Cytosolic branched-chain amino acid (BCAA) aminotransferase, preferentially involved in BCAA catabolism; homolog of murine ECA39; highly expressed during stationary phase and repressed during logarithmic phase; Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. Catalyzes the formation of methionine from 2-keto-4- methylthiobutyrate (KMTB) in the methionine salvage pathway primarily using branched chain amino acids (leucine, isoleucine, and valine) as well as lysine and proline as the amino donors. Involved in cell [...] (376 aa)
     
 
  0.942
ILV1
Threonine deaminase, catalyzes first step in isoleucine biosynthesis; expression is under general amino acid control; ILV1 locus exhibits highly positioned nucleosomes whose organization is independent of known ILV1 regulation (576 aa)
   
  0.897
LEU2
Beta-isopropylmalate dehydrogenase (IMDH), catalyzes the third step in the leucine biosynthesis pathway; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate (364 aa)
   
   
  0.891
LEU4
Alpha-isopropylmalate synthase (2-isopropylmalate synthase); the main isozyme responsible for the first step in the leucine biosynthesis pathway; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate) (619 aa)
   
   
  0.873
ARO1
Pentafunctional arom protein, catalyzes steps 2 through 6 in the biosynthesis of chorismate, which is a precursor to aromatic amino acids; The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis (1588 aa)
   
   
  0.854
RPP0
Conserved ribosomal protein P0 of the ribosomal stalk, which is involved in interaction between translational elongation factors and the ribosome; similar to rat P0, human P0, and E. coli L10e; phosphorylated on serine 302; Ribosomal protein P0 is the functional equivalent of E.coli protein L10 (312 aa)
     
   
  0.833
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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