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BEM3 GTPase-activating protein BEM3 [ Saccharomyces cerevisiae S288C ]

Gene ID: 855988, updated on 18-Sep-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 several processes, including negative regulation of Rho protein signal transduction; positive regulation of GTPase activity; and septin ring organization. Located in cell cortex; cellular bud tip; and mating projection tip. Part of incipient cellular bud site. [provided by Alliance of Genome Resources, Apr 2022]
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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. 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
  2. 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
  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. Roles of an N-terminal coiled-coil-containing domain in the localization and function of Bem3, a Rho GTPase-activating protein in budding yeast. Nie WC, et al. Fungal Genet Biol, 2017 Feb. PMID 28064039

See all (82) 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 establishment of cell polarity IBA
Inferred from Biological aspect of Ancestor
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 IBA
Inferred from Biological aspect of Ancestor
more info
  
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 
is_active_in cell division site IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in cellular bud 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 
is_active_in mating projection tip IBA
Inferred from Biological aspect of Ancestor
more info
  
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
  

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

Gene LinkOut

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