MTQ2 protein (Saccharomyces cerevisiae) - STRING interaction network
"MTQ2" - S-adenosylmethionine-dependent methyltransferase of the seven beta-strand family in Saccharomyces cerevisiae
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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Gene Fusion
MTQ2S-adenosylmethionine-dependent methyltransferase of the seven beta-strand family; subunit of complex with Trm112p that methylates translation release factor Sup45p (eRF1) in the ternary complex eRF1-eRF3-GTP; similar to E.coli PrmC; Methylates eRF1 on ’Gln-182’ using S-adenosyl L- methionine as methyl donor. eRF1 needs to be complexed to eRF3 in its GTP-bound form to be efficiently methylated (221 aa)    
Predicted Functional Partners:
Subunit of tRNA methyltransferase (MTase) complexes in combination with Trm9p and Trm11p; subunit of complex with Mtq2p that methylates Sup45p (eRF1) in the ternary complex eRF1-eRF3-GTP; deletion confers resistance to zymocin; Acts as an activator of both rRNA/tRNA and protein methyltransferases. Together with methyltransferase MTQ2, required for the methylation of eRF1 on ’Gln-182’. Together with methyltransferase TRM11, required for the formation of 2- methylguanosine at position 10 (m2G10) in tRNA. Together with methyltransferase BUD23, required for the formation of 7- methylguanin [...] (135 aa)
Polypeptide release factor (eRF1) in translation termination; mutant form acts as a recessive omnipotent suppressor; methylated by Mtq2p-Trm112p in ternary complex eRF1-eRF3-GTP; mutation of methylation site confers resistance to zymocin; Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA (437 aa)
Mitochondrial translation release factor, involved in stop codon recognition and hydrolysis of the peptidyl-tRNA bond during mitochondrial translation; lack of MRF1 causes mitochondrial genome instability; Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain termination codons UAA and UAG (413 aa)
Translation termination factor eRF3, has a role in mRNA deadenylation and decay; altered protein conformation creates the [PSI(+)] prion that alters translational fidelity and results in a nonsense suppressor phenotype; Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides. Recruited by polyadenylate-binding protein PAB1 to poly(A)-tails of mRNAs. Interaction with PAB1 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening (685 aa)
tRNA methyltransferase, catalyzes esterification of modified uridine nucleotides in tRNA(Arg3) and tRNA(Glu), likely as part of a complex with Trm112p; deletion confers resistance to zymocin; Required for the methylation of the wobble bases at position 34 in tRNA. Appears to have a role in stress-response (279 aa)
Protein of unknown function; mtc6 is synthetically sick with cdc13-1; May be involved in telomere capping (526 aa)
Catalytic subunit of an adoMet-dependent tRNA methyltransferase complex (Trm11p-Trm112p), required for the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs; contains a THUMP domain and a methyltransferase domain; Catalytic subunit of an S-adenosyl-L-methionine- dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs (433 aa)
Protein involved in inserting tail-anchored proteins into ER membranes; forms a complex with Mdy2p; highly conserved across species and homologous to human gene C7orf20; May play a role in insertion of tail-anchored proteins into the endoplasmic reticulum membrane (312 aa)
Pho85p cyclin of the Pho80p subfamily, forms a functional kinase complex with Pho85p which phosphorylates Mmr1p and is regulated by Pho81p; involved in glycogen metabolism, expression is cell-cycle regulated; Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Together with cyclin PCL6, controls glycogen phosphorylase and glycogen synthase activities in response to nutrient availablility. The PCL7-PHO85 cyclin-CDK holoenzyme has GLC8 kinase activity and phosphorylates and inactivates the phosphatase PP1-2 inhibitor GLC8, causing activation of PP1-2, which then dephosphorylates a [...] (285 aa)
tRNA methyltransferase required for synthesis of wybutosine, a modified guanosine found at the 3’-position adjacent to the anticodon of phenylalanine tRNA which supports reading frame maintenance by stabilizing codon-anticodon interactions; S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3’-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Probably methylates N-4 position of wybutosine-86 to produce wybutosine-72 (273 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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