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GNT1 protein (Saccharomyces cerevisiae) - STRING interaction network
"GNT1" - N-acetylglucosaminyltransferase capable of modification of N-linked glycans in the Golgi apparatus in Saccharomyces cerevisiae
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Known Interactions
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experimentally determined
Predicted Interactions
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textmining
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GNT1N-acetylglucosaminyltransferase capable of modification of N-linked glycans in the Golgi apparatus; N-acetylglucosaminyltransferase involved in the Golgi- specific modification of N-linked glycans (491 aa)    
Predicted Functional Partners:
SPT14
UDP-GlcNAc-binding and catalytic subunit of the enzyme that mediates the first step in glycosylphosphatidylinositol (GPI) biosynthesis, mutations cause defects in transcription and in biogenesis of cell wall proteins; Catalytic subunit in the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis (452 aa)
       
 
  0.691
ALG1
Mannosyltransferase; involved in asparagine-linked glycosylation in the endoplasmic reticulum (ER); essential for viability; human homolog ALG1 complements yeast null mutant; Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER (449 aa)
       
 
  0.669
GPI19
Subunit of GPI-GlcNAc transferase involved in synthesis of N-acetylglucosaminyl phosphatidylinositol (GlcNAc-PI), which is the first intermediate in glycosylphosphatidylinositol (GPI) anchor synthesis, shares similarity with mammalian PIG-P; Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis. Involved in cell wall biosynthesis (140 aa)
           
  0.636
ALG11
Alpha-1,2-mannosyltransferase, catalyzes sequential addition of the two terminal alpha 1,2-mannose residues to the Man5GlcNAc2-PP-dolichol intermediate during asparagine-linked glycosylation in the ER; Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man(5)GlcNAc(2)-PP- dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum (548 aa)
       
 
  0.635
CNE1
Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast; Interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (502 aa)
           
  0.579
ALG2
Mannosyltransferase that catalyzes two consecutive steps in the N-linked glycosylation pathway; alg2 mutants exhibit temperature-sensitive growth and abnormal accumulation of the lipid-linked oligosaccharide Man2GlcNAc2-PP-Dol; Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)- dolichol diphosphate (503 aa)
       
 
  0.572
ALG6
Alpha 1,3 glucosyltransferase, involved in transfer of oligosaccharides from dolichyl pyrophosphate to asparagine residues of proteins during N-linked protein glycosylation; mutations in human ortholog are associated with disease; Adds the first glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Man(9)GlcNAc(2)-PP-Dol (544 aa)
           
  0.558
OCH1
Mannosyltransferase of the cis-Golgi apparatus, initiates the polymannose outer chain elongation of N-linked oligosaccharides of glycoproteins; Mannosyltransferase involved in outer chain elongation of asparagine-linked oligosaccharides of the type Man(9)GlcNAc(2). Adds the first alpha-1,6-mannose to the Man(8)GlNAc(2) and Man(9)GlcNAc(2), but not Man(5)GlcNAc(2), endoplasmic reticulum intermediates. Represents the first enzymatic event required for synthesis of outer chain mannose linkages on yeast secretory proteins. Has also the potential to transfer a second alpha-1,6- mannose to t [...] (480 aa)
     
   
  0.542
GSY2
Glycogen synthase, similar to Gsy1p; expression induced by glucose limitation, nitrogen starvation, heat shock, and stationary phase; activity regulated by cAMP-dependent, Snf1p and Pho85p kinases as well as by the Gac1p-Glc7p phosphatase; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis of glycogen (705 aa)
       
 
  0.536
GSY1
Glycogen synthase with similarity to Gsy2p, the more highly expressed yeast homolog; expression induced by glucose limitation, nitrogen starvation, environmental stress, and entry into stationary phase; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis of glycogen (708 aa)
       
 
  0.536
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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