YNL134C protein (Saccharomyces cerevisiae) - STRING interaction network
"YNL134C" - Putative protein of unknown function with similarity to dehydrogenases from other model organisms in Saccharomyces cerevisiae
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
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Gene Fusion
YNL134CPutative protein of unknown function with similarity to dehydrogenases from other model organisms; green fluorescent protein (GFP)-fusion protein localizes to both the cytoplasm and nucleus and is induced by the DNA-damaging agent MMS (376 aa)    
Predicted Functional Partners:
Possible chaperone and cysteine protease with similarity to E. coli Hsp31; member of the DJ-1/ThiJ/PfpI superfamily, which includes human DJ-1 involved in Parkinson’s disease; exists as a dimer and contains a putative metal-binding site; Catalyzes the conversion of methylglyoxal (MG) to D- lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals (PubMed-24302734). Involved in protection against reactive oxygen species (ROS) (PubMed-17395014). Important for viability in stationary phase. May negatively regulate TORC1 in respon [...] (237 aa)
Major isoform of the large subunit of ribonucleotide-diphosphate reductase; the RNR complex catalyzes rate-limiting step in dNTP synthesis, regulated by DNA replication and DNA damage checkpoint pathways via localization of small subunits; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (888 aa)
3-methylbutanal reductase and NADPH-dependent methylglyoxal reductase (D-lactaldehyde dehydrogenase); stress induced (osmotic, ionic, oxidative, heat shock and heavy metals); regulated by the HOG pathway; Catalyzes the irreversible reduction of the cytotoxic compound methylglyoxal (MG) to (S)-lactaldehyde as an alternative to detoxification of MG by glyoxalase I GLO1. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation. Also catalyzes the reduction of 3-methylbutanal to 3- methylbutan [...] (342 aa)
Succinate semialdehyde dehydrogenase involved in the utilization of gamma-aminobutyrate (GABA) as a nitrogen source; part of the 4-aminobutyrate and glutamate degradation pathways; localized to the cytoplasm (497 aa)
Putative protein of unknown function with similarity to medium chain dehydrogenase/reductases; expression induced by stresses including osmotic shock, DNA damaging agents, and other chemicals; GFP-fusion protein localizes to the cytoplasm (365 aa)
NADPH-dependent medium chain alcohol dehydrogenase with broad substrate specificity; member of the cinnamyl family of alcohol dehydrogenases; may be involved in fusel alcohol synthesis or in aldehyde tolerance; NADP-dependent alcohol dehydrogenase with a broad substrate specificity (360 aa)
Beta subunit of fatty acid synthetase, which catalyzes the synthesis of long-chain saturated fatty acids; contains acetyltransacylase, dehydratase, enoyl reductase, malonyl transacylase, and palmitoyl transacylase activities; Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for- [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase (2051 aa)
Putative fatty aldehyde dehydrogenase, located in the mitochondrial outer membrane and also in lipid particles; has similarity to human fatty aldehyde dehydrogenase (FALDH) which is implicated in Sjogren-Larsson syndrome; Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid (532 aa)
NADPH-dependent alpha-keto amide reductase; reduces aromatic alpha-keto amides, aliphatic alpha-keto esters, and aromatic alpha-keto esters; member of the aldo-keto reductase (AKR) family; Reduces aromatic alpha-keto amides, aliphatic and aromatic alpha-keto esters, but not beta-keto esters (312 aa)
Cytoplasmic aldehyde dehydrogenase, involved in ethanol oxidation and beta-alanine biosynthesis; uses NAD+ as the preferred coenzyme; expression is stress induced and glucose repressed; very similar to Ald3p; Cytoplasmic aldehyde dehydrogenase involved in ethanol oxidation. Required for pantothenic acid production through the conversion of 3-aminopropanal to beta-alanine, an intermediate in pantothenic acid (vitamin B5) and coenzyme A (CoA) biosynthesis (506 aa)
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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