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    BEM3 GTPase-activating protein BEM3 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855988, updated on 9-Dec-2024

    Summary

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    Official Symbol
    BEM3
    Official Full Name
    GTPase-activating protein BEM3
    Primary source
    SGD:S000006036
    Locus tag
    YPL115C
    See related
    AllianceGenome:SGD:S000006036; FungiDB:YPL115C; VEuPathDB:YPL115C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables GTPase activator activity and phosphatidylinositol-3-phosphate binding activity. Involved in establishment of cell polarity; negative regulation of Rho protein signal transduction; and septin ring organization. Located in several cellular components, including cellular bud tip; incipient cellular bud site; and mating projection tip. [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See BEM3 in Genome Data Viewer
    Location:
    chromosome: XVI
    Exon count:
    1
    Sequence:
    Chromosome: XVI; NC_001148.4 (332100..335486, complement)

    Chromosome XVI - NC_001148.4Genomic Context describing neighboring genes Neighboring gene isopentenyl-diphosphate delta-isomerase IDI1 Neighboring gene histone deacetylase Neighboring gene glyoxylate reductase Neighboring gene Pex25p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001148.4

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Bem3, a Cdc42 GTPase-activating protein, traffics to an intracellular compartment and recruits the secretory Rab GTPase Sec4 to endomembranes. Mukherjee D, et al. J Cell Sci, 2013 Oct 15. PMID 23943876, Free PMC Article
    2. Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae. Ali I, et al. Acta Crystallogr F Struct Biol Commun, 2018 May 1. PMID 29718000, Free PMC Article
    3. Biochemical comparisons of the Saccharomyces cerevisiae Bem2 and Bem3 proteins. Delineation of a limit Cdc42 GTPase-activating protein domain. Zheng Y, et al. J Biol Chem, 1993 Nov 25. PMID 8227021
    4. Crystal Structure of the Epo1-Bem3 Complex for Bud Growth. Wang J, et al. Int J Mol Sci, 2021 Apr 7. PMID 33917059, Free PMC Article
    5. The mitotic exit network regulates the spatiotemporal activity of Cdc42 to maintain cell size. Gihana GM, et al. J Cell Biol, 2021 Jan 4. PMID 33284320, Free PMC Article

    See all (86) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. We find that Kss1 also localizes to the sites of polarized growth and Bem3 interacts with Kss1 at the septin-ring assembly site. TD2 localization is largely mediated by its interaction with the polarisome component Epo1 via heterotypic coiled-coil interaction. This finding reveals a novel role for the polarisome in linking Bem3 to its functional target,Cdc42.
      Title: Roles of an N-terminal coiled-coil-containing domain in the localization and function of Bem3, a Rho GTPase-activating protein in budding yeast.
    2. Bem2p and Bem3p may function as global inhibitors of Cdc42p activation during G1, and their inactivation by the Cdc28p/Cln kinase contributes to site-specific activation of Cdc42p at bud emergence
      Title: Phosphorylation of Bem2p and Bem3p may contribute to local activation of Cdc42p at bud emergence.
    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 GTPase activator activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables GTPase activator activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables GTPase activator activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables GTPase activator activity IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    enables phosphatidylinositol binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables phosphatidylinositol-3-phosphate binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in cytoskeleton organization IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in establishment of cell polarity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in negative regulation of Rho protein signal transduction IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in negative regulation of Rho protein signal transduction IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in negative regulation of Rho protein signal transduction IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    involved_in septin ring organization IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in signal transduction IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in small GTPase-mediated signal transduction IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cell cortex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cell cortex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cell cortex IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in cell tip IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cellular bud IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cellular bud tip IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in incipient cellular bud site IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mating projection tip HDA PubMed 
    located_in mating projection tip IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in plasma membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    is_active_in site of polarized growth IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    GTPase-activating protein BEM3
    NP_015210.1
    • Rho GTPase activating protein (RhoGAP); involved in control of the cytoskeleton organization; targets the essential Rho-GTPase Cdc42p, which controls establishment and maintenance of cell polarity, including bud-site assembly

    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_001148.4 Reference assembly

      Range
      332100..335486 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183929.1 → NP_015210.1  TPA: GTPase-activating protein BEM3 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_015210.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W3Q3, P32873
      UniProtKB/TrEMBL
      B5VT51, N1NVW1
      Conserved Domains (3) summary
      smart00312
      Location:520 → 622
      PX; PhoX homologous domain, present in p47phox and p40phox
      cd13277
      Location:633 → 741
      PH_Bem3; Bud emergence protein 3 (Bem3) Pleckstrin homology (PH) domain
      cl02570
      Location:904 → 1110
      RhoGAP; GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P32873.3

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