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    MDM12 ERMES complex subunit MDM12 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854153, updated on 3-Nov-2024

    Summary

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    Official Symbol
    MDM12
    Official Full Name
    ERMES complex subunit MDM12
    Primary source
    SGD:S000005369
    Locus tag
    YOL009C
    See related
    AllianceGenome:SGD:S000005369; FungiDB:YOL009C; VEuPathDB:YOL009C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Contributes to lipid transfer activity. Involved in several processes, including aminophospholipid transport; mitochondrion organization; and mitochondrion-endoplasmic reticulum membrane tethering. Located in mitochondrial outer membrane. Part of ERMES complex. Is active in mitochondria-associated endoplasmic reticulum membrane contact site. [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See MDM12 in Genome Data Viewer
    Location:
    chromosome: XV
    Exon count:
    1
    Sequence:
    Chromosome: XV; NC_001147.6 (309324..310139, complement)

    Chromosome XV - NC_001147.6Genomic Context describing neighboring genes Neighboring gene lysophospholipase Neighboring gene rRNA-processing endoribonuclease Neighboring gene ubiquinone-binding protein COQ10 Neighboring gene Csi2p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001147.6

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Crystal structures of Mmm1 and Mdm12-Mmm1 reveal mechanistic insight into phospholipid trafficking at ER-mitochondria contact sites. Jeong H, et al. Proc Natl Acad Sci U S A, 2017 Nov 7. PMID 29078410, Free PMC Article
    2. Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex. Jeong H, et al. EMBO Rep, 2016 Dec. PMID 27821511, Free PMC Article
    3. Improved Split-GFP Systems for Visualizing Organelle Contact Sites in Yeast and Human Cells. Tashiro S, et al. Front Cell Dev Biol, 2020. PMID 33330450, Free PMC Article
    4. A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery. Boldogh IR, et al. Mol Biol Cell, 2003 Nov. PMID 13679517, Free PMC Article
    5. Ubiquitination of ERMES components by the E3 ligase Rsp5 is involved in mitophagy. Belgareh-Touzé N, et al. Autophagy, 2017 Jan 2. PMID 27846375, Free PMC Article

    See all (84) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Therefore, the Mmm1-Mdm12 complex functions as a minimal unit that mediates lipid transfer between membranes.
      Title: Structure-function insights into direct lipid transfer between membranes by Mmm1-Mdm12 of ERMES.
    2. Mdm34 and Mdm12, 2 components of the endoplasmic reticulum-mitochondrial encounter structure, are ubiquitinated by the E3 ligase Rsp5
      Title: Ubiquitination of ERMES components by the E3 ligase Rsp5 is involved in mitophagy.
    3. These studies provide a novel understanding of the overall organization of SMP domains in the endoplasmic reticulum-mitochondria encounter structure (ERMES) complex, indicating that Mdm12 interacts with Mdm34 through head-to-head contact, and with Mmm1 through tail-to-tail contact of SMP domains.
      Title: Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex.
    4. Assembly of mitochondrial beta-barrel proteins represents a major function of the morphology proteins Mdm12/Mmm1.
      Title: The morphology proteins Mdm12/Mmm1 function in the major beta-barrel assembly pathway of mitochondria.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    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 lipid binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to lipid transfer activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables lipid transfer activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in aminophospholipid transport IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in intermembrane lipid transfer IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in lipid transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in mitochondrial genome maintenance IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in mitochondrial outer membrane translocase complex assembly IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in mitochondrion inheritance IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in mitochondrion organization IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in mitochondrion-endoplasmic reticulum membrane tethering IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in mitochondrion-endoplasmic reticulum membrane tethering IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in peroxisome organization IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in phospholipid transport IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in phospholipid transport IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in protein insertion into mitochondrial outer membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    part_of ERMES complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of ERMES complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of ERMES complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    located_in cytoplasm HDA PubMed 
    located_in endoplasmic reticulum IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in endoplasmic reticulum membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in mitochondria-associated endoplasmic reticulum membrane contact site IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mitochondrial outer membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mitochondrial outer membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrion HDA PubMed 
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleus HDA PubMed 
    located_in plasma membrane HDA PubMed 

    General protein information

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    Preferred Names
    ERMES complex subunit MDM12
    NP_014634.1
    • Mitochondrial outer membrane protein, ERMES complex subunit; required for transmission of mitochondria to daughter cells; required for mitophagy; may influence import and assembly of outer membrane beta-barrel proteins; localizes to mitochondria-ER contact sites; ERMES complex is often co-localized with peroxisomes and with concentrated areas of pyruvate dehydrogenase

    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_001147.6 Reference assembly

      Range
      309324..310139 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183263.1 → NP_014634.1  TPA: ERMES complex subunit MDM12 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014634.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      A6ZNJ7, B3LJ47, B5VRP4, D6W258, Q08064, Q92328
      UniProtKB/TrEMBL
      C7GJW1, C8ZHV6
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q92328.2

    Gene LinkOut

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