NCE103 protein (Saccharomyces cerevisiae) - STRING interaction network
"NCE103" - Carbonic anhydrase in Saccharomyces cerevisiae
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Predicted Interactions
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Gene Fusion
NCE103Carbonic anhydrase; metalloenzyme that catalyzes CO2 hydration to bicarbonate and protons; poorly transcribed under aerobic conditions and at an undetectable level under anaerobic conditions; involved in non-classical protein export pathway; Catalyzes the reversible hydration of CO(2) to H(2)CO(3). The main role may be to provide inorganic carbon for the bicarbonate-dependent carboxylation reactions catalyzed by pyruvate carboxylase, acetyl-CoA carboxylase and carbamoyl- phosphate synthetase. Involved in protection against oxidative damage. Encodes a substrate for the non-classical pro [...] (221 aa)    
Predicted Functional Partners:
Pyruvate carboxylase isoform, cytoplasmic enzyme that converts pyruvate to oxaloacetate; highly similar to isoform Pyc2p but differentially regulated; mutations in the human homolog are associated with lactic acidosis; Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second (1178 aa)
Protein of unknown function; interacts with both the Reg1p/Glc7p phosphatase and the Snf1p kinase; May negatively regulate the SNF1 kinase by promoting the interaction of the REG1/GLC7 phosphatase complex with the kinase. Deletion of SIP5 promotes resistance to artimisin, which is probably an indirect effect of an action on the electron transport chain (489 aa)
Plasma membrane protein involved in maintaining membrane organization in stress conditions; induced by heat shock, oxidative stress, osmostress, stationary phase, glucose depletion, oleate and alcohol; regulated by HOG and Ras-Pka pathways; May play a role in a switch from carbohydrate utilizing metabolism to fatty acid utilizing metabolism (109 aa)
Acetyl-CoA carboxylase, biotin containing enzyme that catalyzes the carboxylation of acetyl-CoA to form malonyl-CoA; required for de novo biosynthesis of long-chain fatty acids; Carries out three functions- biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Involved in the synthesis of very-long-chain fatty acid synthesis which is required to maintain a functional nuclear envelope. Required for acylation and vacuolar membrane association of VAC8 which is necessary to maintain a normal morphology of the vacuole (2233 aa)
Enolase I, a phosphopyruvate hydratase that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression is repressed in response to glucose (437 aa)
Actin, structural protein involved in cell polarization, endocytosis, and other cytoskeletal functions; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells (375 aa)
Phosphoribosyl-5-amino-1-phosphoribosyl-4-imidazolecarboxiamide isomerase, catalyzes the fourth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; Catalyzes the isomerization of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (261 aa)
Subunit of a complex, with Slx4p, that hydrolyzes 5’ branches from duplex DNA in response to stalled or converging replication forks; function overlaps with that of Sgs1p-Top3p; Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for simple Y, 5’-flap and replication fork-like structures. It cleaves the strand bearing the 5’-non-homolog [...] (304 aa)
Triose phosphate isomerase, abundant glycolytic enzyme; mRNA half-life is regulated by iron availability; transcription is controlled by activators Reb1p, Gcr1p, and Rap1p through binding sites in the 5’ non-coding region; inhibition of Tpi1p activi /.../PEP (phosphoenolpyruvate) stimulates redox metabolism in respiring cells; E104D mutation in human TPI causes a rare autosomal disease (248 aa)
Hydroperoxide and superoxide-radical responsive glutathione-dependent oxidoreductase; monothiol glutaredoxin subfamily member along with Grx4p and Grx5p; protects cells from oxidative damage; Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (By similarity). Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit (Probable) (285 aa)
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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