| Standard Name | BMH2 1 |
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| Systematic Name | YDR099W |
| Alias | SCD3 |
| Feature Type | ORF, Verified |
| Description | 14-3-3 protein, minor isoform; controls proteome at post-transcriptional level, binds proteins and DNA, involved in regulation of many processes including exocytosis, vesicle transport, Ras/MAPK signaling, and rapamycin-sensitive signaling; protein increases in abundance and relative distribution to the nucleus increases upon DNA replication stress; BMH2 has a paralog, BMH1, that arose from the whole genome duplication (2, 3, 4, 5 and see Summary Paragraph) |
| Name Description | Brain Modulosignalin Homologue 6 |
| Chromosomal Location | |
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| Genetic position: 63 cM |
| View Computational GO annotations for BMH2 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated |
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| Cellular Component | |
| Manually curated | |
| High-throughput |
| 256 total interaction(s) for 172 unique genes/features. | |
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| Genetic Interactions |
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| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
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| Genetic position: 63 cM | ||||||||||||||||||
| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | |||||||||||||||||
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| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000002506 |
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BMH2 is one of two genes in yeast that show strong similarity to the ubiquitous and highly conserved 14-3-3 gene family (7, 1). The function of 14-3-3 proteins is not well understood, but they may play a role in signal transduction (8). Although cells lacking BMH2 are viable, a double deletion of both BMH2 and its paralog BMH1 is lethal (7, 1). Cells lacking BMH1 and BMH2 can be rescued by expression of 14-3-3 proteins from Arabidopsis thaliana or Dictyostelium discoideum (9, 10). Bmh1p and Bmh2p are required for Ras/MAPK cascade signaling during pseudohyphal growth, and associate with Ste20p in vivo (11). There is also evidence that Bmh2p may interact with clathrin (Chc1p), suppress mutations in CDC25, interact with Tpk1p, and suppress growth inhibition by rapamycin (12, 7).
| 1) | 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 |
| 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) | 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 |
| 6) | 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 |
| 7) | 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 |
| 8) | Burbelo PD and Hall A (1995) 14-3-3 proteins. Hot numbers in signal transduction. Curr Biol 5(2):95-6 |
| 9) | 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 |
| 10) | Knetsch ML, et al. (1997) Isolation of a Dictyostelium discoideum 14-3-3 homologue. Biochim Biophys Acta 1357(2):243-8 |
| 11) | 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 |
| 12) | Bertram PG, et al. (1998) The 14-3-3 proteins positively regulate rapamycin-sensitive signaling. Curr Biol 8(23):1259-67 |





