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YNL200C protein (Saccharomyces cerevisiae) - STRING interaction network
"YNL200C" - NADHX epimerase in Saccharomyces cerevisiae
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experimentally determined
Predicted Interactions
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textmining
co-expression
protein homology
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YNL200CNADHX epimerase; catalyzes isomerization of (R)- and (S)-NADHX; homologous to AIBP in mammals and the N- terminal domain of YjeF in E.coli; enzyme is widespread in eukaryotes, prokaryotes and archaea; the authentic, non-tagged protein is detected in /.../y purified mitochondria in high-throughput studies; Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S- specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX (246 aa)    
Predicted Functional Partners:
YKL151C
NADHX dehydratase; converts (S)-NADHX to NADH in an ATP-dependent manner; homologous to Carkd in mammals, and the C-terminal domain of YjeF in E.coli; enzyme is widespread in eukaryotes, prokaryotes and archaea; YKL151C promoter contains STREs (stre /.../ponse elements) and expression is induced by heat shock or methyl methanesulfonate; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm; Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S [...] (337 aa)
 
 
  0.984
TFS1
Protein that interacts with and inhibits carboxypeptidase Y and Ira2p; phosphatidylethanolamine-binding protein (PEBP) family member; targets to vacuolar membranes during stationary phase; acetylated by NatB N-terminal acetyltransferase; Specific and potent inhibitor of carboxypeptidase Y (219 aa)
     
        0.980
DCS2
Non-essential, stress induced regulatory protein; modulates m7G-oligoribonucleotide metabolism; inhibits Dcs1p; regulated by Msn2p, Msn4p, and the Ras-cAMP-cAPK signaling pathway; mutant has increased aneuploidy tolerance; Plays a role in the cleavage of a residual cap structure following the degradation of mRNAs by the 3’->5’ exosome-mediated mRNA decay pathway. Stress-induced regulatory protein that modulates the m7GpppX diphosphatase activity of DCS1 (353 aa)
     
   
  0.963
DHH1
Cytoplasmic DExD/H-box helicase, stimulates mRNA decapping; coordinates distinct steps in mRNA function and decay, interacts with both the decapping and deadenylase complexes, may have a role in mRNA export and translation; C-terminus of Dhh1p inter /.../ith Ngr1p and promotes POR1, but not EDC1 mRNA decay; ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping by activating the decapping enzyme DCP1 (PubMed-11780629, PubMed-12032091, PubMed-11696541, PubMed-12730603, PubMed-15703442. PubMed-15706350). Is involved in G1/S DNA-damage checkpoint rec [...] (506 aa)
     
 
  0.954
SOL4
6-phosphogluconolactonase with similarity to Sol3p; Hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate (255 aa)
   
   
  0.954
DCP2
Catalytic subunit of the Dcp1p-Dcp2p decapping enzyme complex, which removes the 5’ cap structure from mRNAs prior to their degradation; member of the Nudix hydrolase family; Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (PubMed-10508173, PubMed-11139489, PubMed-11741542). Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5’-phosphorylated mRNA fragment and 7m- GDP (PubMed-12554866). Decapping is the major pathway of mRNA degradation in yeast and occurs throu [...] (970 aa)
     
 
  0.952
MSC1
Protein of unknown function; mutant is defective in directing meiotic recombination events to homologous chromatids; the authentic, non-tagged protein is detected in highly purified mitochondria and is phosphorylated (513 aa)
     
   
  0.949
GAD1
Glutamate decarboxylase, converts glutamate into gamma-aminobutyric acid (GABA) during glutamate catabolism; involved in response to oxidative stress (585 aa)
   
        0.946
PGM2
Phosphoglucomutase, catalyzes the conversion from glucose-1-phosphate to glucose-6-phosphate, which is a key step in hexose metabolism; functions as the acceptor for a Glc-phosphotransferase; Major phosphoglucomutase isozyme that catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6- phosphate (PubMed-5784209). Constitutes about 80-90% of the phosphoglucomutase activity in the cell (PubMed-14264884, PubMed-5231755). Key enzyme in hexose metabolism. The forward reaction is an essential step in the energy metabolism of galactose since the product of the galactose [...] (569 aa)
     
        0.932
GLK1
Glucokinase, catalyzes the phosphorylation of glucose at C6 in the first irreversible step of glucose metabolism; one of three glucose phosphorylating enzymes; expression regulated by non-fermentable carbon sources; Two isoenzymes, hexokinase-1 and hexokinase-2, can phosphorylate keto- and aldohexoses in yeast, whereas a third isoenzyme, GLK, is specific for aldohexoses. All glucose phosphorylating enzymes are involved in glucose uptake (500 aa)
     
   
  0.931
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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