DUS4 protein (Saccharomyces cerevisiae) - STRING interaction network
"DUS4" - Dihydrouridine synthase, member of a widespread family of conserved proteins including Smm1p, Dus1p, and Dus3p in Saccharomyces cerevisiae
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 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 each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
DUS4Dihydrouridine synthase, member of a widespread family of conserved proteins including Smm1p, Dus1p, and Dus3p; Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U20a and U20b in cytoplasmic tRNAs (367 aa)    
Predicted Functional Partners:
Bifunctional enzyme containing both alcohol dehydrogenase and glutathione-dependent formaldehyde dehydrogenase activities, functions in formaldehyde detoxification and formation of long chain and complex alcohols, regulated by Hog1p-Sko1p; Oxidizes long-chain alcohols and, in the presence of glutathione, is able to oxidize formaldehyde. Is responsible for yeast resistance to formaldehyde (386 aa)
Pseudouridine synthase, catalyzes only the formation of pseudouridine-55 (Psi55), a highly conserved tRNA modification, in mitochondrial and cytoplasmic tRNAs; PUS4 overexpression leads to translational derepression of GCN4 (Gcd- phenotype); Responsible for synthesis of pseudouridine from uracil- 55 in the psi GC loop of transfer RNAs (403 aa)
Cytoplasmic protein of unknown function; non-essential gene that is induced in a GDH1 deleted strain with altered redox metabolism; GFP-fusion protein is induced in response to the DNA-damaging agent MMS (168 aa)
Iron-sulfer protein required for synthesis of Wybutosine modified tRNA; Wybutosine is a modified guanosine found at the 3’-position adjacent to the anticodon of phenylalanine tRNA which supports reading frame maintenance by stabilizing codon-anticod /.../eractions; induction by Yap5p in response to iron provides protection from high iron toxicity; overexpression results in increased cellular iron; Component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3’-position adjacent to the anticodon of eukaryotic phenylalanine [...] (810 aa)
Noncatalytic subunit of a tRNA methyltransferase complex; Trm8p and Trm82p comprise an enzyme that catalyzes a methyl-transfer from S-adenosyl-l-methionine to the N(7) atom of guanine at position 46 in tRNA; Trm8 lacks catalytic activity if not boun /.../rm82p; Methyltransferase that catalyzes the formation of N(7)- methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity (286 aa)
tRNA(m(1)G37)methyltransferase, methylates a tRNA base adjacent to the anticodon that has a role in prevention of frameshifting; highly conserved across Archaea, Bacteria, and Eukarya; Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5’ of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding. Postspliced cytoplasmic tRNAs are imported into the nucleus, wh [...] (499 aa)
Multifunctional enzyme of the folic acid biosynthesis pathway, has dihydropteroate synthetase, dihydro-6-hydroxymethylpterin pyrophosphokinase, and dihydroneopterin aldolase activities; Catalyzes three sequential steps of tetrahydrofolate biosynthesis (824 aa)
Sulfite reductase beta subunit, involved in amino acid biosynthesis, transcription repressed by methionine; Catalyzes the reduction of sulfite to sulfide, one of several activities required for the biosynthesis of L-cysteine from sulfate (1442 aa)
Urea amidolyase, contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation; Hydrolysis of urea to ammonia and CO(2) (1835 aa)
GMP synthase; highly conserved enzyme that catalyzes the second step in the biosynthesis of GMP from inosine 5’-phosphate (IMP); transcription is not subject to regulation by guanine but is negatively regulated by nutrient starvation; reduction-of-f /.../n mutation gua1-G388D causes changes in cellular guanine nucleotide pools, defects in general protein synthesis, and impaired translation of GCN4 mRNA (525 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
Server load: low (3%) [HD]