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    MARCH family ubiquitin-protein ligase E3 [ Schizosaccharomyces pombe (fission yeast) ]

    Gene ID: 2540242, updated on 18-Sep-2024

    Summary

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    Official Full Name
    MARCH family ubiquitin-protein ligase E3
    Primary source
    PomBase:SPBC32F12.07c
    Locus tag
    SPOM_SPBC32F12.07C
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Schizosaccharomyces pombe (strain: 972h-)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces
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    Genomic context

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    Location:
    chromosome: II
    Exon count:
    1
    Sequence:
    Chromosome: II; NC_003423.3 (2795240..2797713, complement)

    Chromosome II - NC_003423.3Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene gamma-tubulin Gtb1 Neighboring gene protein Cwf12 Neighboring gene P-TEFB-associated cyclin T Pch1 Neighboring gene ncRNA Neighboring gene ncRNA Neighboring gene DASH complex subunit Duo1

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_003423.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Abo1 is required for the H3K9me2 to H3K9me3 transition in heterochromatin. Dong W, et al. Sci Rep, 2020 Apr 8. PMID 32269268, Free PMC Article
    2. Phosphorylation of the RNA-binding protein Zfs1 modulates sexual differentiation in fission yeast. Navarro FJ, et al. J Cell Sci, 2017 Dec 15. PMID 29084823, Free PMC Article
    3. Hierarchical modularity and the evolution of genetic interactomes across species. Ryan CJ, et al. Mol Cell, 2012 Jun 8. PMID 22681890, Free PMC Article
    4. Transcription and RNA-processing in fission yeast mitochondria. Schäfer B, et al. RNA, 2005 May. PMID 15811919, Free PMC Article
    5. The genome sequence of Schizosaccharomyces pombe. Wood V, et al. Nature, 2002 Feb 21. PMID 11859360

    See all (9) 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 PomBase

    Function Evidence Code Pubs
    enables ubiquitin protein ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables zinc ion binding ISM
    Inferred from Sequence Model
    more info
    		  
    Process Evidence Code Pubs
    involved_in positive regulation of mitochondrial fission ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in protein polyubiquitination IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in regulation of mitochondrial fission IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Component Evidence Code Pubs
    is_active_in mitochondrial outer membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    MARCH family ubiquitin-protein ligase E3

    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_003423.3 Reference assembly

      Range
      2795240..2797713 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001022069.3 → NP_596150.1  MARCH family ubiquitin-protein ligase E3 [Schizosaccharomyces pombe]

      See identical proteins and their annotated locations for NP_596150.1

      Status: PROVISIONAL

      UniProtKB/Swiss-Prot
      O74371
      Conserved Domains (1) summary
      cl17238
      Location:14 → 63
      RING; RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc; defined by the 'cross-brace' motif C-X2-C-X(9-39)-C-X(1-3)- H-X(2-3)-(N/C/H)-X2-C-X(4-48)C-X2-C; probably involved in ...
    Nucleotide Protein
    Heading Accession and Version

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