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    EFM3 protein-lysine N-methyltransferase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 853593, updated on 2-Nov-2024

    Summary

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    Official Symbol
    EFM3
    Official Full Name
    protein-lysine N-methyltransferase
    Primary source
    SGD:S000003890
    Locus tag
    YJR129C
    See related
    AllianceGenome:SGD:S000003890; FungiDB:YJR129C; VEuPathDB:YJR129C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables protein-lysine N-methyltransferase activity. Involved in peptidyl-lysine trimethylation. Located in cytoplasm. Orthologous to several human genes including EEF2KMT (eukaryotic elongation factor 2 lysine methyltransferase). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See EFM3 in Genome Data Viewer
    Location:
    chromosome: X
    Exon count:
    1
    Sequence:
    Chromosome: X; NC_001142.9 (664000..665019, complement)

    Chromosome X - NC_001142.9Genomic Context describing neighboring genes Neighboring gene Rsf2p Neighboring gene uncharacterized protein Neighboring gene ncRNA Neighboring gene cystathionine gamma-synthase Neighboring gene mannosyl-oligosaccharide 1,2-alpha-mannosidase

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001142.9

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Elongation factor methyltransferase 3--a novel eukaryotic lysine methyltransferase. Zhang L, et al. Biochem Biophys Res Commun, 2014 Aug 22. PMID 25086354
    2. The YJL185C, YLR376C and YJR129C genes of Saccharomyces cerevisiae are probably involved in regulation of the glyoxylate cycle. Boniewska-Bernacka E, et al. Acta Biochim Pol, 2006. PMID 17146497
    3. Translational roles of elongation factor 2 protein lysine methylation. Dzialo MC, et al. J Biol Chem, 2014 Oct 31. PMID 25231983, Free PMC Article
    4. Trans-acting antisense RNAs mediate transcriptional gene cosuppression in S. cerevisiae. Camblong J, et al. Genes Dev, 2009 Jul 1. PMID 19571181, Free PMC Article
    5. Identification and characterization of a novel evolutionarily conserved lysine-specific methyltransferase targeting eukaryotic translation elongation factor 2 (eEF2). Davydova E, et al. J Biol Chem, 2014 Oct 31. PMID 25231979, Free PMC Article

    See all (18) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Deletion of EFM2 or EFM3 increased sensitivity to translation inhibitors, indicating changes in the ability for EF2 to interact and communicate with ribosomal components.
      Title: Translational roles of elongation factor 2 protein lysine methylation.
    2. Previously uncharacterized lysine-specific methyltransferase FAM86A and Yjr129c introduce a functionally important lysine methylation in eEF2.
      Title: Identification and characterization of a novel evolutionarily conserved lysine-specific methyltransferase targeting eukaryotic translation elongation factor 2 (eEF2).
    3. Propose that YJR129C be named elongation factor methyltransferase 3 (Efm3). An immunoblotting screen of 21 putative methyltransferases showed a loss in the methylation of elongation factor 2 (EF2) on knockout of YJR129C.
      Title: Elongation factor methyltransferase 3--a novel eukaryotic lysine methyltransferase.
    4. the contribution of the ER24 gene product Ylr376Cp and of the two suppressor gene products Yjl185Cp and Yjr129Cp to a complex regulation of the glyoxylate cycle in yeast
      Title: The YJL185C, YLR376C and YJR129C genes of Saccharomyces cerevisiae are probably involved in regulation of the glyoxylate cycle.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables S-adenosylmethionine-dependent methyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables methyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein-lysine N-methyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables protein-lysine N-methyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in methylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in peptidyl-lysine trimethylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in peptidyl-lysine trimethylation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in regulation of translation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    protein-lysine N-methyltransferase
    NP_012663.2
    • S-adenosylmethionine-dependent methyltransferase; seven-beta-strand lysine methyltransferase which trimethylates translation elongation factor EF2 (Eft1p and Eft2p) at lysine 509; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm; ortholog of human gene FAM86A

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_001142.9 Reference assembly

      Range
      664000..665019 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001181787.2 → NP_012663.2  TPA: protein-lysine N-methyltransferase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012663.2

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VWU7, P47163
      UniProtKB/TrEMBL
      A6ZQ84, B3LQL1, N1P0A5
      Conserved Domains (1) summary
      cl17173
      Location:137 → 286
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P47163.2

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