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YJL055W protein (Saccharomyces cerevisiae) - STRING interaction network
"YJL055W" - Putative protein of unknown function, proposed to be involved in the metabolism of purine and pyrimidine base analogues in Saccharomyces cerevisiae
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Predicted Interactions
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textmining
co-expression
protein homology
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YJL055WPutative protein of unknown function, proposed to be involved in the metabolism of purine and pyrimidine base analogues; deletion mutants are sensitive to HAP and AHA; overexpression confers resistance to 5-FOA and 5-FU (245 aa)    
Predicted Functional Partners:
HAM1
Conserved protein with deoxyribonucleoside triphosphate pyrophosphohydrolase activity, mediates exclusion of noncanonical purines from deoxyribonucleoside triphosphate pools; mutant is sensitive to the base analog 6-N-hydroxylaminopurine; Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2’-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and 5-bromodeoxyuridine 5’-triphosphate (BrdUTP) to their respective monophosphate derivatives. Xanthosine 5’-triphosphate (XTP) is also a potential substrate [...] (197 aa)
   
 
  0.877
CPA2
Large subunit of carbamoyl phosphate synthetase, which catalyzes a step in the synthesis of citrulline, an arginine precursor (1118 aa)
       
 
  0.741
CPA1
Small subunit of carbamoyl phosphate synthetase, which catalyzes a step in the synthesis of citrulline, an arginine precursor; translationally regulated by an attenuator peptide encoded by YOR302W within the CPA1 mRNA 5’-leader (411 aa)
       
 
  0.730
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)
       
    0.690
ADH4
Alcohol dehydrogenase isoenzyme type IV, dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency; Reduces acetaldehyde to ethanol during glucose fermentation. Specific for ethanol. Shows drastically reduced activity towards primary alcohols from 4 carbon atoms upward. Isomers of aliphatic alcohol, as well as secondary alcohols and glycerol are not used at all (382 aa)
       
  0.680
CAF16
Part of evolutionarily-conserved CCR4-NOT regulatory complex; contains single ABC-type ATPase domain but no transmembrane domain; interacts with several subunits of Mediator (289 aa)
 
            0.644
GLR1
Cytosolic and mitochondrial glutathione oxidoreductase, converts oxidized glutathione to reduced glutathione; mitochondrial but not cytosolic form has a role in resistance to hyperoxia; Maintains high levels of reduced glutathione in the cytosol (483 aa)
       
  0.635
IRC15
Microtubule associated protein; regulates microtubule dynamics; required for accurate meiotic chromosome segregation; null mutant displays large budded cells due to delayed mitotic progression, increased levels of spontaneous Rad52 foci (499 aa)
       
  0.635
LPD1
Dihydrolipoamide dehydrogenase, the lipoamide dehydrogenase component (E3) of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase multi-enzyme complexes; Lipoamide dehydrogenase is a component of the alpha- ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine (499 aa)
       
  0.635
KGD1
Subunit of the mitochondrial alpha-ketoglutarate dehydrogenase complex; catalyzes a key step in the tricarboxylic acid (TCA) cycle, the oxidative decarboxylation of alpha-ketoglutarate to form succinyl-CoA; The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components- 2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (1014 aa)
     
 
    0.634
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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