BMH1/YER177W Summary Help

Standard Name BMH1 1
Systematic Name YER177W
Alias APR6
Feature Type ORF, Verified
Description 14-3-3 protein, major isoform; controls proteome at post-transcriptional level, binds proteins and DNA, involved in regulation of exocytosis, vesicle transport, Ras/MAPK and rapamycin-sensitive signaling, aggresome formation, spindle position checkpoint; protein increases in abundance and relative distribution to the nucleus increases upon DNA replication stress; antiapoptotic gene similar to human 14-3-3; BMH1 has a paralog, BMH2, that arose from whole genome duplication (2, 3, 4, 5, 6, 7, 8 and see Summary Paragraph)
Name Description Brain Modulosignalin Homologue 1
Chromosomal Location
ChrV:545611 to 546414 | ORF Map | GBrowse
Genetic position: 148 cM
Gene Ontology Annotations All BMH1 GO evidence and references
  View Computational GO annotations for BMH1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 16 genes
Classical genetics
Large-scale survey
482 total interaction(s) for 306 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 125
  • Affinity Capture-RNA: 4
  • Affinity Capture-Western: 32
  • Biochemical Activity: 1
  • Co-fractionation: 1
  • Co-purification: 2
  • Far Western: 1
  • PCA: 4
  • Protein-peptide: 4
  • Reconstituted Complex: 5
  • Two-hybrid: 11

Genetic Interactions
  • Dosage Growth Defect: 14
  • Dosage Lethality: 1
  • Dosage Rescue: 12
  • Negative Genetic: 137
  • Phenotypic Enhancement: 17
  • Phenotypic Suppression: 1
  • Positive Genetic: 48
  • Synthetic Growth Defect: 29
  • Synthetic Lethality: 17
  • Synthetic Rescue: 16

Expression Summary
Length (a.a.) 267
Molecular Weight (Da) 30,091
Isoelectric Point (pI) 4.65
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrV:545611 to 546414 | ORF Map | GBrowse
Genetic position: 148 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..804 545611..546414 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000979

BMH1 is one of two genes in yeast that show strong similarity to the ubiquitous and highly conserved 14-3-3 gene family (1). 14-3-3 proteins are acidic dimeric molecules that likely play a role in signal transduction (9). Although cells lacking BMH1 are viable, a double deletion of both BMH1 and its paralog BMH2 is lethal (10, 11). Cells lacking BMH1 and BMH2 can be rescued by expression of 14-3-3 proteins from Arabidopsis thaliana or Dictyostelium discoideum (12, 13). Bmh1p and Bmh2p are required for Ras/MAPK cascade signaling during pseudohyphal growth, and associate with Ste20p in vivo (14). There is also evidence that Bmh1p may enhance Raf function, interact with clathrin (Chc1p), suppress mutations in CDC25, interact with Tpk1p, and suppress growth inhibition by rapamycin (15, 16, 10).

Last updated: 1999-09-01 Contact SGD

References cited on this page View Complete Literature Guide for BMH1
1) van Heusden GP, et al.  (1992) Characterization of the yeast BMH1 gene encoding a putative protein homologous to mammalian protein kinase II activators and protein kinase C inhibitors. FEBS Lett 302(2):145-50
2) van Hemert MJ, et al.  (2001) Yeast 14-3-3 proteins. Yeast 18(10):889-95
3) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
4) Bruckmann A, et al.  (2007) Post-Transcriptional Control of the Saccharomyces cerevisiae Proteome by 14-3-3 Proteins. J Proteome Res 6(5):1689-1699
5) Clapp C, et al.  (2012) 14-3-3 Protects against stress-induced apoptosis. Cell Death Dis 3():e348
6) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
7) Xu Z, et al.  (2013) 14-3-3 protein targets misfolded chaperone-associated proteins to aggresomes. J Cell Sci 126(Pt 18):4173-86
8) Caydasi AK, et al.  (2014) The 14-3-3 protein Bmh1 functions in the spindle position checkpoint by breaking Bfa1 asymmetry at yeast centrosomes. Mol Biol Cell 25(14):2143-51
9) Burbelo PD and Hall A  (1995) 14-3-3 proteins. Hot numbers in signal transduction. Curr Biol 5(2):95-6
10) Gelperin D, et al.  (1995) 14-3-3 proteins: potential roles in vesicular transport and Ras signaling in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 92(25):11539-43
11) van Heusden GP, et al.  (1995) The 14-3-3 proteins encoded by the BMH1 and BMH2 genes are essential in the yeast Saccharomyces cerevisiae and can be replaced by a plant homologue. Eur J Biochem 229(1):45-53
12) van Heusden GP, et al.  (1996) Four Arabidopsis thaliana 14-3-3 protein isoforms can complement the lethal yeast bmh1 bmh2 double disruption. FEBS Lett 391(3):252-6
13) Knetsch ML, et al.  (1997) Isolation of a Dictyostelium discoideum 14-3-3 homologue. Biochim Biophys Acta 1357(2):243-8
14) Roberts RL, et al.  (1997) 14-3-3 proteins are essential for RAS/MAPK cascade signaling during pseudohyphal development in S. cerevisiae. Cell 89(7):1055-65
15) Bertram PG, et al.  (1998) The 14-3-3 proteins positively regulate rapamycin-sensitive signaling. Curr Biol 8(23):1259-67
16) Irie K, et al.  (1994) Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase. Science 265(5179):1716-9