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    NEM1 Nem1-Spo7 phosphatase catalytic subunit NEM1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856393, updated on 2-Nov-2024

    Summary

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    Official Symbol
    NEM1
    Official Full Name
    Nem1-Spo7 phosphatase catalytic subunit NEM1
    Primary source
    SGD:S000001046
    Locus tag
    YHR004C
    See related
    AllianceGenome:SGD:S000001046; FungiDB:YHR004C; VEuPathDB:YHR004C
    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 phosphoprotein phosphatase activity. Involved in lipid droplet formation; nuclear envelope organization; and regulation of lipid biosynthetic process. Located in endoplasmic reticulum; lipid droplet; and membrane. Part of Nem1-Spo7 phosphatase complex. Orthologous to human CTDNEP1 (CTD nuclear envelope phosphatase 1). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See NEM1 in Genome Data Viewer
    Location:
    chromosome: VIII
    Exon count:
    1
    Sequence:
    Chromosome: VIII; NC_001140.6 (111754..113094, complement)

    Chromosome VIII - NC_001140.6Genomic Context describing neighboring genes Neighboring gene coenzyme A transporter Neighboring gene tRNA threonylcarbamoyladenosine dehydratase Neighboring gene guanine nucleotide-binding protein subunit alpha Neighboring gene protein transporter TIM10

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001140.6

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. A putative NEM1 homologue regulates lipid droplet biogenesis via PAH1 in Tetrahymena thermophila. Shukla S, et al. J Biosci, 2018 Sep. PMID 30207315
    2. Catalytic core function of yeast Pah1 phosphatidate phosphatase reveals structural insight into its membrane localization and activity control. Han GS, et al. J Biol Chem, 2024 Jan. PMID 38097185, Free PMC Article
    3. NEM1 acts as a suppressor of apoptotic phenotypes in LSM4 yeast mutants. Palermo V, et al. FEMS Yeast Res, 2015 Nov. PMID 26316593
    4. Proteomics-Based Monitoring of Pathway Activity Reveals that Blocking Diacylglycerol Biosynthesis Rescues from Alpha-Synuclein Toxicity. Soste M, et al. Cell Syst, 2019 Sep 25. PMID 31521608, Free PMC Article
    5. Conserved regions of the regulatory subunit Spo7 are required for Nem1-Spo7/Pah1 phosphatase cascade function in yeast lipid synthesis. Jog R, et al. J Biol Chem, 2023 May. PMID 37030502, Free PMC Article

    See all (89) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Phosphorylation-mediated regulation of the Nem1-Spo7/Pah1 phosphatase cascade in yeast lipid synthesis.
      Title: Phosphorylation-mediated regulation of the Nem1-Spo7/Pah1 phosphatase cascade in yeast lipid synthesis.
    2. Seipin and Nem1 establish discrete ER subdomains to initiate yeast lipid droplet biogenesis.
      Title: Seipin and Nem1 establish discrete ER subdomains to initiate yeast lipid droplet biogenesis.
    3. The Spo7 sequence LLI is required for Nem1-Spo7/Pah1 phosphatase cascade function in yeast lipid metabolism.
      Title: The Spo7 sequence LLI is required for Nem1-Spo7/Pah1 phosphatase cascade function in yeast lipid metabolism.
    4. the TORC1-Nem1/Spo7-Pah1 axis is a master regulator of not only macroautophagy but also microautophagy in budding yeast
      Title: The TORC1-Nem1/Spo7-Pah1/lipin axis regulates microautophagy induction in budding yeast.
    5. Together, our data suggest that Nem1-Sop7-mediated regulation of membrane biogenesis is needed to promote mitophagy in yeast.
      Title: The Nem1-Spo7 protein phosphatase complex is required for efficient mitophagy in yeast.
    6. Nem1p regulates nuclear growth by controlling phospholipid biosynthesis and it is required for normal nuclear envelope morphology and sporulation.
      Title: NEM1 acts as a suppressor of apoptotic phenotypes in LSM4 yeast mutants.
    7. Acidic tail-dependent binding and dephosphorylation of Pah1p by the Nem1p-Spo7p complex is an important determinant of its function in lipid and membrane biogenesis.
      Title: Regulation of lipid droplet and membrane biogenesis by the acidic tail of the phosphatidate phosphatase Pah1p.
    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 myosin phosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables phosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to phosphoprotein phosphatase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables phosphoprotein phosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein serine/threonine phosphatase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables protein serine/threonine phosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in lipid droplet formation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in negative regulation of phospholipid biosynthetic process IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in nuclear envelope organization IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in positive regulation of lipid biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in regulation of phospholipid biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of Nem1-Spo7 phosphatase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    located_in endoplasmic reticulum IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in endoplasmic reticulum IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in endoplasmic reticulum membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in lipid droplet IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrion HDA PubMed 
    located_in nuclear membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    Nem1-Spo7 phosphatase catalytic subunit NEM1
    NP_011867.1
    • Probable catalytic subunit of Nem1p-Spo7p phosphatase holoenzyme; regulates nuclear/ER membrane association and activation of Pah1p, a phosphatidate phosphatase involved in the production of diacylglycerol DAG for lipid droplet biogenesis; regulates nuclear growth by controlling phospholipid biosynthesis; required for normal nuclear envelope morphology and sporulation; phosphatase activity of the Nem1p-Spo7p complex is inhibited by Ice2p; homolog of the human protein Dullard

    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_001140.6 Reference assembly

      Range
      111754..113094 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179134.1 → NP_011867.1  TPA: Nem1-Spo7 phosphatase catalytic subunit NEM1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_011867.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D3DKU7, P38757
      UniProtKB/TrEMBL
      B3LSC2, B5VJT0, C8ZA70
      Conserved Domains (1) summary
      COG5190
      Location:9 → 446
      FCP1; TFIIF-interacting CTD phosphatase, includes NLI-interacting factor [Transcription]
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P38757.1

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