STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
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
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
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; Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily (386 aa)    
Predicted Functional Partners:
YJL068C
Esterase that can function as an S-formylglutathione hydrolase; non-essential intracellular esterase; may be involved in the detoxification of formaldehyde, which can be metabolized to S-formylglutathione; similar to human esterase D
 0.999
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
  
 
 0.998
ARO10
Transaminated amino acid decarboxylase; Phenylpyruvate decarboxylase; catalyzes decarboxylation of phenylpyruvate to phenylacetaldehyde, which is the first specific step in the Ehrlich pathway; involved in protein N-terminal Met and Ala catabolism
   
 
 0.982
SAH1
Adenosylhomocysteinase; S-adenosyl-L-homocysteine hydrolase; catabolizes S-adenosyl-L-homocysteine which is formed after donation of the activated methyl group of S-adenosyl-L-methionine (AdoMet) to an acceptor; regulates cellular lipid homoeostasis by regulating phosphatidylcholine(PC)synthesis and triacylglycerol (TG) levels
   
 
 0.978
PDC6
Minor isoform of pyruvate decarboxylase; decarboxylates pyruvate to acetaldehyde, involved in amino acid catabolism; transcription is glucose- and ethanol-dependent, and is strongly induced during sulfur limitation; Belongs to the TPP enzyme family
   
 
 0.976
PDC5
Pyruvate decarboxylase isozyme 2; Minor isoform of pyruvate decarboxylase; key enzyme in alcoholic fermentation, decarboxylates pyruvate to acetaldehyde, regulation is glucose- and ethanol-dependent, repressed by thiamine, involved in amino acid catabolism
   
 
 0.976
THI3
Thiamine metabolism regulatory protein THI3; Regulatory protein that binds Pdc2p and Thi2p transcription factors; activates thiamine biosynthesis transcription factors Pdc2p and Thi2p by binding to them, but releases and de-activates them upon binding to thiamine pyrophosphate (TPP), the end product of the pathway; has similarity to decarboxylases but enzymatic activity is not detected
   
 
 0.973
PDC1
Major of three pyruvate decarboxylase isozymes; key enzyme in alcoholic fermentation; decarboxylates pyruvate to acetaldehyde; involved in amino acid catabolism; subject to glucose-, ethanol-, and autoregulation; activated by phosphorylation in response to glucose levels; N-terminally propionylated in vivo; Belongs to the TPP enzyme family
   
 
 0.973
ADO1
Adenosine kinase; required for the utilization of S-adenosylmethionine (AdoMet); may be involved in recycling adenosine produced through the methyl cycle
   
   0.962
ALD3
Cytoplasmic 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
  
 0.886
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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