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    FYV10 glucose-induced degradation complex subunit FYV10 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854710, updated on 11-Apr-2024

    Summary

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    Gene symbol
    FYV10
    Gene description
    glucose-induced degradation complex subunit FYV10
    Primary source
    SGD:S000001359
    Locus tag
    YIL097W
    See related
    AllianceGenome:SGD:S000001359
    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
    GID9
    Summary
    Contributes to ubiquitin protein ligase activity. Involved in negative regulation of apoptotic process; negative regulation of gluconeogenesis; and proteasome-mediated ubiquitin-dependent protein catabolic process. Located in cytoplasm and nucleus. Part of GID complex. Orthologous to human MAEA (macrophage erythroblast attacher, E3 ubiquitin ligase). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    Location:
    chromosome: IX
    Exon count:
    1
    Sequence:
    Chromosome: IX; NC_001141.2 (180427..181977)

    Chromosome IX - NC_001141.2Genomic Context describing neighboring genes Neighboring gene glucan 1,4-alpha-glucosidase Neighboring gene Fmc1p Neighboring gene 25S rRNA (uracil2634-N3)-methyltransferase Neighboring gene tRNA-Ile

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001141.2

    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. Timer-based proteomic profiling of the ubiquitin-proteasome system reveals a substrate receptor of the GID ubiquitin ligase. Kong KE, et al. Mol Cell, 2021 Jun 3. PMID 33974913, Free PMC Article
    3. Regulation of the Gid ubiquitin ligase recognition subunit Gid4. Menssen R, et al. FEBS Lett, 2018 Oct. PMID 30136317
    4. Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite-induced degradation of gluconeogenic enzymes. Menssen R, et al. J Biol Chem, 2012 Jul 20. PMID 22645139, Free PMC Article
    5. Cryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation. Qiao S, et al. Nat Commun, 2022 Jun 1. PMID 35650207, Free PMC Article

    See all (45) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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 IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to ubiquitin-protein transferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Process Evidence Code Pubs
    involved_in negative regulation of apoptotic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    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
    		  
    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 
    located_in cytoplasm HDA 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 nucleus HDA PubMed 
    is_active_in nucleus IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    glucose-induced degradation complex subunit FYV10
    NP_012169.1
    • Subunit of GID complex; involved in proteasome-dependent catabolite inactivation of gluconeogenic enzymes FBPase, PEPCK, and c-MDH; forms dimer with Rmd5p that is then recruited to GID Complex by Gid8p; contains a degenerate RING finger motif needed for GID complex ubiquitin ligase activity in vivo, as well as CTLH and CRA domains; plays role in anti-apoptosis; required for survival upon exposure to K1 killer toxin

    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_001141.2 Reference assembly

      Range
      180427..181977
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179445.1 → NP_012169.1  TPA: glucose-induced degradation complex subunit FYV10 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012169.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VVJ0, P40492
      UniProtKB/TrEMBL
      A0A6A5PZU1, A6ZVI0, B3LTU4, C8ZAF3, N1P4F3
      Conserved Domains (1) summary
      pfam10607
      Location:187 → 392
      CLTH; CTLH/CRA C-terminal to LisH motif domain
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P40492.1

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