
Health Dictionary
Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
BCLAF1
Introduction
Bcl-2-associated transcription factor 1 is a Bcl-2 family protein in humans that is encoded by the BCLAF1 gene.[1][2][3]
This gene encodes a transcriptional repressor that interacts with several members of the BCL-2 family of proteins. Overexpression of this protein induces apoptosis, which can be suppressed by co-expression of BCL2 proteins. The protein localizes to dot-like structures throughout the nucleus and redistributes to a zone near the nuclear envelope in cells undergoing apoptosis. Multiple transcript variants encoding different protein isoforms have been found for this gene.[3]
References
References
- ↑ Nagase T, Seki N, Ishikawa K, Tanaka A, Nomura N (Nov 1996). “Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1”. DNA Res. 3 (1): 17–24. doi:10.1093/dnares/3.1.17. PMID 8724849.
- ↑ Kasof GM, Goyal L, White E (Jun 1999). “Btf, a Novel Death-Promoting Transcriptional Repressor That Interacts with Bcl-2-Related Proteins”. Mol Cell Biol. 19 (6): 4390–404. doi:10.1128/mcb.19.6.4390. PMC 104398. PMID 10330179.
- ↑ 3.0 3.1 “Entrez Gene: BCLAF1 BCL2-associated transcription factor 1”.
Further reading
Further reading
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Mungall AJ, Palmer SA, Sims SK, et al. (2003). “The DNA sequence and analysis of human chromosome 6”. Nature. 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
- Haraguchi T, Holaska JM, Yamane M, et al. (2004). “Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery–Dreifuss muscular dystrophy”. Eur. J. Biochem. 271 (5): 1035–45. doi:10.1111/j.1432-1033.2004.04007.x. PMID 15009215.
- Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). “Large-scale characterization of HeLa cell nuclear phosphoproteins”. Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
- Jin J, Smith FD, Stark C, et al. (2004). “Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization”. Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). “The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Zheng H, Hu P, Quinn DF, Wang YK (2005). “Phosphotyrosine proteomic study of interferon alpha signaling pathway using a combination of immunoprecipitation and immobilized metal affinity chromatography”. Mol. Cell. Proteomics. 4 (6): 721–30. doi:10.1074/mcp.M400077-MCP200. PMID 15659558.
- Mansharamani M, Wilson KL (2005). “Direct binding of nuclear membrane protein MAN1 to emerin in vitro and two modes of binding to barrier-to-autointegration factor”. J. Biol. Chem. 280 (14): 13863–70. doi:10.1074/jbc.M413020200. PMID 15681850.
- Kim JE, Tannenbaum SR, White FM (2005). “Global phosphoproteome of HT-29 human colon adenocarcinoma cells”. J. Proteome Res. 4 (4): 1339–46. doi:10.1021/pr050048h. PMID 16083285.
- Nousiainen M, Silljé HH, Sauer G, et al. (2006). “Phosphoproteome analysis of the human mitotic spindle”. Proc. Natl. Acad. Sci. U.S.A. 103 (14): 5391–6. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
- Beausoleil SA, Villén J, Gerber SA, et al. (2006). “A probability-based approach for high-throughput protein phosphorylation analysis and site localization”. Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
- Olsen JV, Blagoev B, Gnad F, et al. (2006). “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks”. Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- Liu H, Lu ZG, Miki Y, Yoshida K (2007). “Protein Kinase C δ Induces Transcription of the TP53 Tumor Suppressor Gene by Controlling Death-Promoting Factor Btf in the Apoptotic Response to DNA Damage”. Mol. Cell. Biol. 27 (24): 8480–91. doi:10.1128/MCB.01126-07. PMC 2169390. PMID 17938203.
External links
External links
- FactorBook BCLAF1
- Human BCLAF1 genome location and BCLAF1 gene details page in the UCSC Genome Browser.
