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SNO2 protein (Saccharomyces cerevisiae) - STRING interaction network
"SNO2" - Protein of unknown function, nearly identical to Sno3p in Saccharomyces cerevisiae
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Predicted Interactions
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SNO2Protein of unknown function, nearly identical to Sno3p; expression is induced before the diauxic shift and also in the absence of thiamin; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5’-phosphate. The resulting ammonia molecule is channeled to the active site of a SNZ isoform (222 aa)    
Predicted Functional Partners:
SNZ2
Member of a stationary phase-induced gene family; transcription of SNZ2 is induced prior to diauxic shift, and also in the absence of thiamin in a Thi2p-dependent manner; forms a coregulated gene pair with SNO2; interacts with Thi11p; Catalyzes the formation of pyridoxal 5’-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by a SNO isoform. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively (298 aa)
 
  0.999
SNZ3
Member of a stationary phase-induced gene family; transcription of SNZ2 is induced prior to diauxic shift, and also in the absence of thiamin in a Thi2p-dependent manner; forms a coregulated gene pair with SNO3; Catalyzes the formation of pyridoxal 5’-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by a SNO isoform. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively (298 aa)
 
  0.999
SNZ1
Protein involved in vitamin B6 biosynthesis; member of a stationary phase-induced gene family; coregulated with SNO1; interacts with Sno1p and with Yhr198p, perhaps as a multiprotein complex containing other Snz and Sno proteins; Catalyzes the formation of pyridoxal 5’-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by a SNO isoform. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively (297 aa)
 
  0.999
SNO3
Protein of unknown function, nearly identical to Sno2p; expression is induced before the diauxic shift and also in the absence of thiamin; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5’-phosphate. The resulting ammonia molecule is channeled to the active site of a SNZ isoform (222 aa)
   
0.964
BUD16
Putative pyridoxal kinase, a key enzyme involved in pyridoxal 5’-phosphate synthesis, the active form of vitamin B6; required for genome integrity; involved in bud-site selection; similarity to yeast BUD17 and human pyridoxal kinase (PDXK); Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). Important for bud site selection (312 aa)
     
  0.945
PDX3
Pyridoxine (pyridoxamine) phosphate oxidase, has homologs in E. coli and Myxococcus xanthus; transcription is under the general control of nitrogen metabolism; Catalyzes the oxidation of either pyridoxine 5’- phosphate (PNP) or pyridoxamine 5’-phosphate (PMP) into pyridoxal 5’-phosphate (PLP) (228 aa)
       
  0.940
BUD17
Putative pyridoxal kinase, a key enzyme in vitamin B6 metabolism; involved in bud-site selection; diploid mutants display a random rather than a bipolar budding pattern; similarity to yeast BUD16 and human pyridoxal kinase (PDXK); Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). Important for bud site selection (317 aa)
     
  0.940
SNO1
Protein of unconfirmed function, involved in pyridoxine metabolism; expression is induced during stationary phase; forms a putative glutamine amidotransferase complex with Snz1p, with Sno1p serving as the glutaminase; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5’-phosphate. The resulting ammonia molecule is channeled to the active site of a SNZ isoform (224 aa)
   
 
0.857
IMD2
Inosine monophosphate dehydrogenase, catalyzes the rate-limiting step in GTP biosynthesis, expression is induced by mycophenolic acid resulting in resistance to the drug, expression is repressed by nutrient limitatio; Catalyzes the conversion of inosine 5’-phosphate (IMP) to xanthosine 5’-phosphate (XMP), the first committed and rate- limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. In contrast to the other IMPDH alleles IMD3 and IMD4, the enzymatic activity of IMD2 seems to be intrinsically drug resistant (523 aa)
   
 
  0.712
IMD1
Nonfunctional protein with homology to IMP dehydrogenase; probable pseudogene, located close to the telomere; is not expressed at detectable levels; YAR073W and YAR075W comprise a continuous reading frame in some strains of S. cerevisiae (403 aa)
   
 
  0.712
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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