U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    EFM2 S-adenosylmethionine-dependent methyltransferase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852574, updated on 9-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    EFM2
    Official Full Name
    S-adenosylmethionine-dependent methyltransferase
    Primary source
    SGD:S000000475
    Locus tag
    YBR271W
    See related
    AllianceGenome:SGD:S000000475; FungiDB:YBR271W; VEuPathDB:YBR271W
    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 positive regulation of translational termination. Located in cytoplasm. [provided by Alliance of Genome Resources, Dec 2024]
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    See EFM2 in Genome Data Viewer
    Location:
    chromosome: II
    Exon count:
    1
    Sequence:
    Chromosome: II; NC_001134.8 (744852..746111)

    Chromosome II - NC_001134.8Genomic Context describing neighboring genes Neighboring gene Sdh8p Neighboring gene Bit2p Neighboring gene Hsm3p Neighboring gene Ubx7p

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_001134.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    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. Translational roles of elongation factor 2 protein lysine methylation. Dzialo MC, et al. J Biol Chem, 2014 Oct 31. PMID 25231983, Free PMC Article
    3. Methylation of translation-associated proteins in Saccharomyces cerevisiae: Identification of methylated lysines and their methyltransferases. Couttas TA, et al. Proteomics, 2012 Apr. PMID 22522802
    4. Comprehensive structural and substrate specificity classification of the Saccharomyces cerevisiae methyltransferome. Wlodarski T, et al. PLoS One, 2011. PMID 21858014, Free PMC Article
    5. Stoichiometry of Saccharomyces cerevisiae lysine methylation: insights into non-histone protein lysine methyltransferase activity. Hart-Smith G, et al. J Proteome Res, 2014 Mar 7. PMID 24517342

    See all (25) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables S-adenosylmethionine-dependent methyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    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 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 
    enables protein-lysine N-methyltransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in methylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in positive regulation of translational termination IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

    Go to the top of the page Help
    Preferred Names
    S-adenosylmethionine-dependent methyltransferase
    NP_009830.3
    • S-adenosylmethionine-dependent methyltransferase; seven-beta-strand lysine methyltransferase which dimethylates translation elongation factor EF2 (Eft1p and Eft2p) at lysine 613 and methylates EF3 (Yef3p) at lysine 187; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm; involved in regulation of translational termination; predicted involvement in ribosome biogenesis

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    Genome Annotation

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

    Reference assembly

    Genomic

    1. NC_001134.8 Reference assembly

      Range
      744852..746111
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001178619.3 → NP_009830.3  TPA: S-adenosylmethionine-dependent methyltransferase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_009830.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VQR7, P38347
      UniProtKB/TrEMBL
      A6ZLL0, B3LMP1, B5VEL6, C7GMW0, D3UF19, G2W9S5, N1P8V0
      Conserved Domains (1) summary
      cl17173
      Location:213 → 344
      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
    P38347.1

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Other Literature Sources
    Molecular Biology Databases
    Research Materials
    Tools