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ADH5 ADH5 SFA1 SFA1 FAA2 FAA2 ALD5 ALD5 POX1 POX1 ADH4 ADH4 FAA3 FAA3 POT1 POT1 ECI1 ECI1 ADH3 ADH3 HFD1 HFD1 ALD3 ALD3 ALD2 ALD2 FAA4 FAA4 ADH2 ADH2 ADH1 ADH1 FAA1 FAA1 ALD4 ALD4 ERG10 ERG10 ALD6 ALD6
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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ADH5Alcohol dehydrogenase isoenzyme V; involved in ethanol production; ADH5 has a paralog, ADH1, that arose from the whole genome duplication; Belongs to the zinc-containing alcohol dehydrogenase family. (351 aa)
SFA1Bifunctional alcohol dehydrogenase and formaldehyde dehydrogenase; formaldehyde dehydrogenase activity is glutathione-dependent; functions in formaldehyde detoxification and formation of long chain and complex alcohols, regulated by Hog1p-Sko1p; protein abundance increases in response to DNA replication stress. (386 aa)
FAA2Long-chain-fatty-acid--CoA ligase 2; Medium chain fatty acyl-CoA synthetase; activates imported fatty acids; accepts a wide range of fatty acid chain lengths with a preference for medium chains, C9:0-C13:0; localized to the peroxisome; comparative analysis suggests that a mitochondrially targeted form may result from translation starting at a non-canonical codon upstream of the annotated start codon. (744 aa)
ALD5Mitochondrial aldehyde dehydrogenase; involved in regulation or biosynthesis of electron transport chain components and acetate formation; activated by K+; utilizes NADP+ as the preferred coenzyme; constitutively expressed. (520 aa)
POX1Fatty-acyl coenzyme A oxidase; involved in the fatty acid beta-oxidation pathway; localized to the peroxisomal matrix. (748 aa)
ADH4Alcohol 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. (382 aa)
FAA3Long-chain-fatty-acid--CoA ligase 3; Long chain fatty acyl-CoA synthetase; activates imported fatty acids with a preference for C16:0-C18:0 chain lengths; green fluorescent protein (GFP)-fusion protein localizes to the cell periphery; Belongs to the ATP-dependent AMP-binding enzyme family. (694 aa)
POT13-ketoacyl-CoA thiolase, peroxisomal; 3-ketoacyl-CoA thiolase with broad chain length specificity; cleaves 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA during beta-oxidation of fatty acids. (417 aa)
ECI1Peroxisomal delta3,delta2-enoyl-CoA isomerase; hexameric protein that converts 3-hexenoyl-CoA to trans-2-hexenoyl-CoA, essential for the beta-oxidation of unsaturated fatty acids, oleate-induced; ECI1 has a paralog, DCI1, that arose from the whole genome duplication. (280 aa)
ADH3Mitochondrial alcohol dehydrogenase isozyme III; involved in the shuttling of mitochondrial NADH to the cytosol under anaerobic conditions and ethanol production. (375 aa)
HFD1Fatty aldehyde dehydrogenase HFD1; Dehydrogenase involved in ubiquinone and sphingolipid metabolism; oxidizes 4-hydroxybenzaldehyde into 4-hydroxybenzoic acid in ubiquinone biosynthesis; converts hexadecenal to hexadecenoic acid in sphingosine 1-phosphate breakdown pathway; located in the mitochondrial outer membrane and also in lipid particles; human homolog ALDH3A2, a fatty aldehyde dehydrogenase (FALDH) mutated in neurocutaneous disorder Sjogren-Larsson syndrome, can complement yeast hfd1 mutant. (532 aa)
ALD3Cytoplasmic aldehyde dehydrogenase; involved in beta-alanine synthesis; uses NAD+ as the preferred coenzyme; very similar to Ald2p; expression is induced by stress and repressed by glucose. (506 aa)
ALD2Cytoplasmic 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. (506 aa)
FAA4Long-chain-fatty-acid--CoA ligase 4; Long chain fatty acyl-CoA synthetase; activates fatty acids with a preference for C12:0-C16:0 chain lengths; role in the competitive import of long-chain fatty acids and sphingoid long-chain bases; role in stationary phase survival; localizes to lipid particles and the plasma membrane; role in sphingolipid-to-glycerolipid metabolism; forms cytoplasmic foci upon replication stress; faa1 faa4 double null complemented by any of human ACSBG1, ACSL1, 3, 4, 5, 6, SLC27A2, or 4; Belongs to the ATP-dependent AMP-binding enzyme family. (694 aa)
ADH2Glucose-repressible alcohol dehydrogenase II; catalyzes the conversion of ethanol to acetaldehyde; involved in the production of certain carboxylate esters; regulated by ADR1. (348 aa)
ADH1Alcohol dehydrogenase; fermentative isozyme active as homo- or heterotetramers; required for the reduction of acetaldehyde to ethanol, the last step in the glycolytic pathway; ADH1 has a paralog, ADH5, that arose from the whole genome duplication. (348 aa)
FAA1Long-chain-fatty-acid--CoA ligase 1; Long chain fatty acyl-CoA synthetase; activates fatty acids with a preference for C12:0-C16:0 chain lengths; role in the competitive import of long-chain fatty acids and sphingoid long-chain bases; accounts for most acyl-CoA synthetase activity; localizes to lipid particles and the plasma membrane; role in sphingolipid-to-glycerolipid metabolism; forms ER foci upon replication stress; faa1 faa4 double null complemented by any of human ACSBG1, ACSL1, 3, 4, 5, 6, SLC27A2, or 4. (700 aa)
ALD4Mitochondrial aldehyde dehydrogenase; required for growth on ethanol and conversion of acetaldehyde to acetate; phosphorylated; activity is K+ dependent; utilizes NADP+ or NAD+ equally as coenzymes; expression is glucose repressed; can substitute for cytosolic NADP-dependent aldehyde dehydrogenase when directed to the cytosol; human homolog ALDH2 can complement yeast ald4 mutant. (519 aa)
ERG10Acetyl-CoA C-acetyltransferase (acetoacetyl-CoA thiolase); cytosolic enzyme that transfers an acetyl group from one acetyl-CoA molecule to another, forming acetoacetyl-CoA; involved in the first step in mevalonate biosynthesis; human ACAT1 functionally complements the growth defect caused by repression of ERG10 expression; Belongs to the thiolase-like superfamily. Thiolase family. (398 aa)
ALD6Cytosolic aldehyde dehydrogenase; activated by Mg2+ and utilizes NADP+ as the preferred coenzyme; required for conversion of acetaldehyde to acetate; constitutively expressed; locates to the mitochondrial outer surface upon oxidative stress. (500 aa)
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
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