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    RMD5 ubiquitin-protein ligase RMD5 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851842, updated on 9-Dec-2024

    Summary

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    Official Symbol
    RMD5
    Official Full Name
    ubiquitin-protein ligase RMD5
    Primary source
    SGD:S000002663
    Locus tag
    YDR255C
    See related
    AllianceGenome:SGD:S000002663; FungiDB:YDR255C; VEuPathDB:YDR255C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Also known as
    GID2
    Summary
    Enables ubiquitin protein ligase activity. Involved in negative regulation of gluconeogenesis and proteasome-mediated ubiquitin-dependent protein catabolic process. Located in cytosol and peroxisome. Part of GID complex. Orthologous to human RMND5A (required for meiotic nuclear division 5 homolog A) and RMND5B (required for meiotic nuclear division 5 homolog B). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See RMD5 in Genome Data Viewer
    Location:
    chromosome: IV
    Exon count:
    1
    Sequence:
    Chromosome: IV; NC_001136.10 (966557..967822, complement)

    Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene Met32p Neighboring gene Chl4p Neighboring gene catalase A Neighboring gene ribosomal lysine N-methyltransferase

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001136.10

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation. Braun B, et al. FEBS Lett, 2011 Dec 15. PMID 22044534
    2. Mutation in gene coding for glucose-induced degradation-deficient protein contributes to high malate production in yeast strain No. 28 and No. 77 used for industrial brewing of sake. Negoro H, et al. Biosci Biotechnol Biochem, 2021 Apr 24. PMID 33686405
    3. The Rewiring of Ubiquitination Targets in a Pathogenic Yeast Promotes Metabolic Flexibility, Host Colonization and Virulence. Childers DS, et al. PLoS Pathog, 2016 Apr. PMID 27073846, Free PMC Article
    4. Proteins of newly isolated mutants and the amino-terminal proline are essential for ubiquitin-proteasome-catalyzed catabolite degradation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae. Hämmerle M, et al. J Biol Chem, 1998 Sep 25. PMID 9737955
    5. Gid10 as an alternative N-recognin of the Pro/N-degron pathway. Melnykov A, et al. Proc Natl Acad Sci U S A, 2019 Aug 6. PMID 31337681, Free PMC Article

    See all (53) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Mutation in gene coding for glucose-induced degradation-deficient protein contributes to high malate production in yeast strain No. 28 and No. 77 used for industrial brewing of sake.
      Title: Mutation in gene coding for glucose-induced degradation-deficient protein contributes to high malate production in yeast strain No. 28 and No. 77 used for industrial brewing of sake.
    2. Three members of the VID and GID gene families, VID30/GID1, GID2, and VID28/GID5 are needed for the rapamycin or nitrogen starvation-induced degradation of the high-affinity hexose transporter Hxt7p is shown here.
      Title: Components of the Vid30c are needed for the rapamycin-induced degradation of the high-affinity hexose transporter Hxt7p in Saccharomyces cerevisiae.
    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 metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ubiquitin protein ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ubiquitin protein ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ubiquitin protein ligase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    contributes_to ubiquitin-protein transferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables zinc ion binding RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in negative regulation of gluconeogenesis IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in negative regulation of gluconeogenesis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proteasome-mediated ubiquitin-dependent protein catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in proteasome-mediated ubiquitin-dependent protein catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in proteasome-mediated ubiquitin-dependent protein catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein ubiquitination IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in ubiquitin-dependent protein catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of GID complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of GID complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleus HDA PubMed 
    is_active_in nucleus IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in peroxisome IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    ubiquitin-protein ligase RMD5
    NP_010541.3
    • Component of GID Complex that confers ubiquitin ligase (U3) activity; necessary for polyubiquitination and degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase; forms dimer with Fyv10p that is then recruited to GID Complex by Gid8p; also required for sporulation; conserved protein that has a degenerate RING finger domain

    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_001136.10 Reference assembly

      Range
      966557..967822 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001180563.3 → NP_010541.3  TPA: ubiquitin-protein ligase RMD5 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_010541.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VSN5, Q12508
      UniProtKB/TrEMBL
      A6ZYK7, B3LG35, B5VGD9, C7GTJ0, C8Z5G7, G2WAZ8, N1P6Z2
      Conserved Domains (1) summary
      COG5109
      Location:13 → 418
      COG5109; Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q12508.1

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