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BNR1 formin BNR1 [ Saccharomyces cerevisiae S288C ]

Gene ID: 854647, updated on 24-Jan-2026
Official Symbol
BNR1
Official Full Name
formin BNR1
Primary source
SGD:S000001421
Locus tag
YIL159W
See related
AllianceGenome:SGD:S000001421; FungiDB:YIL159W; VEuPathDB:YIL159W
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 profilin binding activity. Involved in actin cytoskeleton organization; barbed-end actin filament capping; and cellular hyperosmotic response. Located in cell division site and cellular bud neck. Is active in cytosol. Human ortholog(s) of this gene implicated in autosomal dominant nonsyndromic deafness 1 and sensorineural hearing loss. Orthologous to human DIAPH1 (diaphanous related formin 1). [provided by Alliance of Genome Resources, Jul 2025]
Orthologs
all
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See BNR1 in Genome Data Viewer
Location:
chromosome: IX
Exon count:
1
Sequence:
Chromosome: IX; NC_001141.2 (41825..45952)

Chromosome IX - NC_001141.2Genomic Context describing neighboring genes Neighboring gene Smu2p Neighboring gene acetyl-CoA C-acyltransferase Neighboring gene Aim20p Neighboring gene Coa1p

Genomic Sequence:
NC_001141.2

Go to nucleotide: Graphics FASTA GenBank

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Smy1 regulation of Bnr1 activity is required for efficient secretory vesicle traffic.
    Title: Common formin-regulating sequences in Smy1 and Bud14 are required for the control of actin cable assembly in vivo.
  2. F-actin stabilization is regulated by yeast formins Bni1p and Bnr1p
    Title: Importance of a Lys113-Glu195 intermonomer ionic bond in F-actin stabilization and regulation by yeast formins Bni1p and Bnr1p.
  3. Yor304c-a/Bil1 colocalizes with Bud6 and functions in the Bnr1 pathway for actin assembly
    Title: Ligand-induced activation of a formin-NPF pair leads to collaborative actin nucleation.
  4. During polarization, cells change from fast to slow cable dynamics through spatio-temporal regulation of Bni1, Bnr1 and Myo2.
    Title: Cortical actin dynamics driven by formins and myosin V.
  5. Bnr1p has two separable regions that each contribute to its bud neck localization
    Title: The yeast formin Bnr1p has two localization regions that show spatially and temporally distinct association with septin structures.
  6. Yeast expressing the nonlocalized actin nucleating/assembly formin homology (FH) 1-FH2 domains of Bnr1p or Bni1p as the sole formin grow well.
    Title: Polarized growth in budding yeast in the absence of a localized formin.
  7. BNI1 and BNR1 contribute to Bud6p-dependent microtubule-cortex interactions by controlling Bud6p localisation.
    Title: Dissecting the involvement of formins in Bud6p-mediated cortical capture of microtubules in S. cerevisiae.
  8. Bni1 and Bnr1 are regulated by Bud6
    Title: Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6.
  9. different formin isoforms have roles in maintaining stable and dynamic axes in the same yeast cell
    Title: Stable and dynamic axes of polarity use distinct formin isoforms in budding yeast.
  10. Bnr1 was confined to the bud neck and did not exchange with a cytoplasmic pool.
    Title: Yeast formins Bni1 and Bnr1 utilize different modes of cortical interaction during the assembly of actin cables.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables actin binding IEA
Inferred from Electronic Annotation
more info
  
enables actin filament binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables profilin binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables profilin binding IEA
Inferred from Electronic Annotation
more info
  
enables profilin binding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables small GTPase binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in actin cytoskeleton organization IEA
Inferred from Electronic Annotation
more info
  
involved_in actin filament bundle assembly IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in actin filament bundle assembly IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in actin filament bundle assembly IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in actin filament bundle assembly IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in actin nucleation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in actin nucleation IEA
Inferred from Electronic Annotation
more info
  
involved_in barbed-end actin filament capping IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in barbed-end actin filament capping IEA
Inferred from Electronic Annotation
more info
  
involved_in cellular hyperosmotic response IEA
Inferred from Electronic Annotation
more info
  
involved_in cellular hyperosmotic response IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in formin-nucleated actin cable assembly IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in formin-nucleated actin cable assembly IEA
Inferred from Electronic Annotation
more info
  
involved_in formin-nucleated actin cable assembly IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in formin-nucleated actin cable assembly IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in mitotic actomyosin contractile ring assembly IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in mitotic actomyosin contractile ring assembly IEA
Inferred from Electronic Annotation
more info
  
involved_in mitotic actomyosin contractile ring assembly IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in regulation of actin cytoskeleton organization IGI
Inferred from Genetic Interaction
more info
 PubMed 
Component Evidence Code Pubs
located_in cell division site IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cell division site IEA
Inferred from Electronic Annotation
more info
  
is_active_in cellular bud neck IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cellular bud neck IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cellular bud neck IEA
Inferred from Electronic Annotation
more info
  
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
is_active_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in mating projection tip IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in mitotic actomyosin contractile ring IBA
Inferred from Biological aspect of Ancestor
more info
  
Preferred Names
formin BNR1
NP_012107.1
  • Formin; nucleates the formation of linear actin filaments; involved in processes such as budding and mitotic spindle orientation which require the formation of polarized actin cables; activity is regulated by Hof1p and by the Bud14p-Kel1p-Kel2p complex; dephosphorylated and delocalized from the division site in a Glc7p/Ref2p-dependent manner; functionally redundant with BNI1

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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_001141.2 Reference assembly

    Range
    41825..45952
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001179507.1 → NP_012107.1  formin BNR1

    See identical proteins and their annotated locations for NP_012107.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VVC7, P40450
    UniProtKB/TrEMBL
    G2WFZ2, N1P0Y3
    Conserved Domains (1) summary
    pfam02181
    Location:868 → 1265
    FH2; Formin Homology 2 Domain
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P40450.1

Gene LinkOut

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