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DPH6 protein (Saccharomyces cerevisiae) - STRING interaction network
"DPH6" - Putative protein of unknown function in Saccharomyces cerevisiae
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Predicted Interactions
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textmining
co-expression
protein homology
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DPH6Putative protein of unknown function; green fluorescent protein (GFP)-tagged protein localizes to the cytoplasm; YLR143W is not an essential gene; Amidase that catalyzes the last step of diphthamide biosynthesis using ammonium and ATP. Diphthamide biosynthesis consists in the conversion of an L-histidine residue in the translation elongation factor eEF-2 (EFT1 or EFT2) to diphthamide (685 aa)    
Predicted Functional Partners:
RRT2
WD40 domain-containing protein involved in endosomal recycling; forms a complex with Rtt10p that functions in the retromer-mediated pathway for recycling internalized cell-surface proteins; non-essential gene identified in a screen for mutants with /.../sed levels of rDNA transcription; null mutants display a weak carboxypeptidase Y missorting/secretion phenotype; human ortholog is WDR85; Catalyzes the demethylation of diphthine methyl ester to form diphthine, an intermediate in diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elonga [...] (387 aa)
     
 
  0.992
DPH5
Methyltransferase required for synthesis of diphthamide, which is a modified histidine residue of translation elongation factor 2 (Eft1p or Eft2p); not essential for viability; GFP-Dph5p fusion protein localizes to the cytoplasm; S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis (300 aa)
           
  0.899
EFT2
Elongation factor 2 (EF-2), also encoded by EFT1; catalyzes ribosomal translocation during protein synthesis; contains diphthamide, the unique posttranslationally modified histidine residue specifically ADP-ribosylated by diphtheria toxin; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated m [...] (842 aa)
     
 
  0.865
DPH2
Protein required, along with Dph1p, Kti11p, Jjj3p, and Dph5p, for synthesis of diphthamide, which is a modified histidine residue of translation elongation factor 2 (Eft1p or Eft2p); may act in a complex with Dph1p and Kti11p; Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L- methionine to a histidine residue. Diphthamide is a post- translational modification of histidine which occurs in elongation factor 2 (534 aa)
           
  0.840
DPH1
Protein required, along with Dph2p, Kti11p, Jjj3p, and Dph5p, for synthesis of diphthamide, which is a modified histidine residue of translation elongation factor 2 (Eft1p or Eft2p); may act in a complex with Dph2p and Kti11p; Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L- methionine to a histidine residue. Diphthamide is a post- translational modification of histidine which occurs in elongation factor 2 (425 aa)
           
  0.828
KTI11
Zn-ribbon protein that co-purifies with Dph1 and Dph2 in a complex required for synthesis of diphthamide on translation factor eEF2 and with Elongator subunits Iki3p, Elp2p, and Elp3p involved in modification of wobble nucleosides in tRNAs; Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L- methionine to a histidine residue. Diphthamide is a post- translational modification of histidine which occurs in elongation factor 2. Required for conferring sensitivity to K.lactis zymocin (82 aa)
     
   
  0.797
RRP46
Exosome non-catalytic core component; involved in 3’-5’ RNA processing and degradation in both the nucleus and the cytoplasm; has similarity to E. coli RNase PH and to human hRrp46p (EXOSC5); Non-catalytic component of the RNA exosome complex which has 3’->5’ exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding ’pervasive’ transcripts, such as [...] (223 aa)
   
 
    0.786
SKI6
Exosome non-catalytic core component; involved in 3’-5’ RNA processing and degradation in both the nucleus and the cytoplasm; has similarity to E. coli RNase PH and to human hRrp41p (EXOSC4); Non-catalytic component of the RNA exosome complex which has 3’->5’ exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding ’pervasive’ transcripts, such as [...] (246 aa)
       
    0.785
MTR3
Exosome non-catalytic core component; involved in 3’-5’ RNA processing and degradation in both the nucleus and the cytoplasm; has similarity to E. coli RNase PH and to human hMtr3p (EXOSC6); Non-catalytic component of the RNA exosome complex which has 3’->5’ exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding ’pervasive’ transcripts, such as a [...] (250 aa)
       
    0.785
PXL1
LIM domain-containing protein that localizes to sites of polarized growth, required for selection and/or maintenance of polarized growth sites, may modulate signaling by the GTPases Cdc42p and Rho1p; has similarity to metazoan paxillin (706 aa)
       
      0.782
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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