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DUG2 protein (Saccharomyces cerevisiae) - STRING interaction network
"DUG2" - Probable di- and tri-peptidase 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
Others
textmining
co-expression
protein homology
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[Homology]
Score
DUG2Probable di- and tri-peptidase; forms a complex with Dug1p and Dug3p to degrade glutathione (GSH) and other peptides containing a gamma-glu-X bond in an alternative pathway to GSH degradation by gamma-glutamyl transpeptidase (Ecm38p); Component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond (878 aa)    
Predicted Functional Partners:
DUG3
Probable glutamine amidotransferase, forms a complex with Dug1p and Dug2p to degrade glutathione (GSH) and other peptides containing a gamma-glu-X bond in an alternative pathway to GSH degradation by gamma-glutamyl transpeptidase (Ecm38p); Component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond (357 aa)
 
   
  0.999
DUG1
Cys-Gly metallo-di-peptidase; forms a complex with Dug2p and Dug3p to degrade glutathione (GSH) and other peptides containing a gamma-glu-X bond in an alternative pathway to GSH degradation by gamma-glutamyl transpeptidase (Ecm38p); Catalytic component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Functions also in a DUG2- DUG3-independent manner as a dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides (481 aa)
   
 
0.947
URA2
Bifunctional carbamoylphosphate synthetase/aspartate transcarbamylase; catalyzes the first two enzymatic steps in the de novo biosynthesis of pyrimidines; both activities are subject to feedback inhibition by UTP; This protein is a "fusion" protein encoding three enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase) (2214 aa)
       
  0.901
NCS2
Protein required for thiolation of the uridine at the wobble position of Lys(UUU) and Glu(UUC) tRNAs; has a role in urmylation and in invasive and pseudohyphal growth; inhibits replication of Brome mosaic virus in S. cerevisiae; Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in p [...] (493 aa)
       
      0.868
ARG1
Arginosuccinate synthetase, catalyzes the formation of L-argininosuccinate from citrulline and L-aspartate in the arginine biosynthesis pathway; potential Cdc28p substrate; Catalyzes the eighth step in arginine biosynthesis. Also has a catabolic function as the first enzyme of citrulline utilization as nitrogen source via arginine and the reactions involved in the arginase pathway (420 aa)
   
  0.819
ARG3
Ornithine carbamoyltransferase; also known as carbamoylphosphate-L-ornithine carbamoyltransferase; catalyzes the biosynthesis of the arginine precursor citrulline (338 aa)
   
 
  0.808
ARG5,6
Protein that is processed in the mitochondrion to yield acetylglutamate kinase and N-acetyl-gamma-glutamyl-phosphate reductase, which catalyze the 2nd and 3rd steps in arginine biosynthesis; enzymes form a complex with Arg2p (863 aa)
   
 
  0.806
ARG8
Acetylornithine aminotransferase, catalyzes the fourth step in the biosynthesis of the arginine precursor ornithine (423 aa)
       
  0.797
CAR2
L-ornithine transaminase (OTAse), catalyzes the second step of arginine degradation, expression is dually-regulated by allophanate induction and a specific arginine induction process; not nitrogen catabolite repression sensitive (424 aa)
       
  0.797
THI22
Protein with similarity to hydroxymethylpyrimidine phosphate kinases; member of a gene family with THI20 and THI21; not required for thiamine biosynthesis; Is not required for thiamine biosynthesis (572 aa)
       
  0.784
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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