BEM1 phosphatidylinositol-3-phosphate-binding protein BEM1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: BEM1
Official Full Name: phosphatidylinositol-3-phosphate-binding protein BEM1
Primary source: SGD:S000000404
Locus tag: YBR200W
See related: AllianceGenome:SGD:S000000404; FungiDB:YBR200W; VEuPathDB:YBR200W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: SRO1
Summary: Enables molecular adaptor activity and phosphatidylinositol-3-phosphate binding activity. Involved in cell morphogenesis involved in conjugation with cellular fusion; maintenance of protein location; and positive regulation of vacuole fusion, non-autophagic. Located in several cellular components, including cellular bud neck; cellular bud tip; and incipient cellular bud site. Human ortholog(s) of this gene implicated in Frank-Ter Haar syndrome; autosomal recessive chronic granulomatous disease 3; and rheumatoid arthritis. Orthologous to human SH3PXD2B (SH3 and PX domains 2B) and NCF4 (neutrophil cytosolic factor 4). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See BEM1 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 1

Sequence:: Chromosome: II; NC_001134.8 (620872..622527)

Chromosome II - NC_001134.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001134.8

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Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Generation and characterization of conditional yeast mutants affecting each of the 2 essential functions of the scaffolding proteins Boi1/2 and Bem1.
Title: Generation and characterization of conditional yeast mutants affecting each of the 2 essential functions of the scaffolding proteins Boi1/2 and Bem1.
Using optogenetics, the authors probe yeast polarization and find that local recruitment of Cdc24 or Bem1 is sufficient to induce polarization by triggering self-sustaining Cdc42 activity.
Title: Cell cycle entry triggers a switch between two modes of Cdc42 activation during yeast polarization.
Here, the authors find that Bem1 directly augments the guanine exchange factor (GEF) activity of Cdc24.
Title: Scaffold-mediated gating of Cdc42 signalling flux.
Biochemical analysis confirmed that this mutation disturbs the interaction with Bem1 but not the fold of the protein. The larger dataset obtained by NGS achieved a more complete representation of the bipartite interaction interface of Cdc24.
Title: A Split-Ubiquitin Based Strategy Selecting for Protein Complex-Interfering Mutations.
Exo70p directly and specifically binds to the polarity determinant scaffold protein Bem1p. The interaction involves multiple domains of both Exo70p and Bem1p.
Title: Bem1p contributes to secretory pathway polarization through a direct interaction with Exo70p.
The PB1 domains of yeast Bem1 and Cdc24 proteins form obligate heterodimers.
Title: Directed dimerization: an in vivo expression system for functional studies of type II phytochromes.
Nbp2p SH3 domain made contacts with the Ste20 peptide core RXXPXXP motif and the Bem1p SH3b domain made stronger contacts with residues flanking the core motif.
Title: Distinct peptide binding specificities of Src homology 3 (SH3) protein domains can be determined by modulation of local energetics across the binding interface.
A Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function.
Title: A Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function.
analysis of the solution structure of a novel Cdc42 binding module of Bem1 and its interaction with Ste20 and Cdc42
Title: Solution structure of a novel Cdc42 binding module of Bem1 and its interaction with Ste20 and Cdc42.
study presents the tertiary structure of the heterodimer of Bem1 and Cdc24 PB1 domains determined by NMR spectroscopy
Title: NMR structure of the heterodimer of Bem1 and Cdc24 PB1 domains from Saccharomyces cerevisiae.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables molecular adaptor activity	IPI Inferred from Physical 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
enables protein-macromolecule adaptor activity	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in cell morphogenesis involved in conjugation with cellular fusion	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in conjugation with cellular fusion	IBA Inferred from Biological aspect of Ancestor more info
involved_in maintenance of protein location	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of vacuole fusion, non-autophagic	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cell cortex	IDA Inferred from Direct Assay more info	PubMed
located_in cellular bud neck	IDA Inferred from Direct Assay more info	PubMed
located_in cellular bud tip	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytoskeleton	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 more info	PubMed
is_active_in mating projection tip	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	HDA more info	PubMed
located_in site of polarized growth	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: phosphatidylinositol-3-phosphate-binding protein BEM1

NP_009759.3

Protein containing SH3-domains; involved in establishing cell polarity and morphogenesis; functions as a scaffold protein for complexes that include Cdc24p, Ste5p, Ste20p, and Rsr1p

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

NC_001134.8 Reference assembly

Range

620872..622527

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178548.3 → NP_009759.3 TPA: phosphatidylinositol-3-phosphate-binding protein BEM1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_009759.3

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VQJ6, P29366

UniProtKB/TrEMBL

A6ZLE1, B3LMW0, B5VEF0, C7GKG1, D3UEU6, G2W9K3, N1P6Y9

Conserved Domains (4) summary

cd06890
Location:284 → 400

PX_Bem1p; The phosphoinositide binding Phox Homology domain of Bem1p

cd11878
Location:76 → 127

SH3_Bem1p_1; First Src Homology 3 domain of Bud emergence protein 1 and similar domains

cd11879
Location:159 → 214

SH3_Bem1p_2; Second Src Homology 3 domain of Bud emergence protein 1 and similar domains

smart00666
Location:478 → 549

PB1; PB1 domain