Transcription factor IIIA is a protein that in humans is encoded by the GTF3A gene.[5][6]
It was first purified and identified as the first mammalian gene-specific activator by Robert G. Roeder in 1980,[7] and later characterized by Wolffe and Brown in 1988.
The TFIIIA in Xenopus was the first zinc finger protein discovered.[8]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000122034 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000016503 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Arakawa H, Nagase H, Hayashi N, Ogawa M, Nagata M, Fujiwara T, et al. (Jul 1995). "Molecular cloning, characterization, and chromosomal mapping of a novel human gene (GTF3A) that is highly homologous to Xenopus transcription factor IIIA". Cytogenetics and Cell Genetics. 70 (3–4): 235–8. doi:10.1159/000134041. PMID 7789179.
- ^ "Entrez Gene: GTF3A general transcription factor IIIA".
- ^ Engelke DR, Ng SY, Shastry BS, Roeder RG (Mar 1980). "Specific interaction of a purified transcription factor with an internal control region of 5S RNA genes". Cell. 19 (3): 717–28. doi:10.1016/S0092-8674(80)80048-1. PMID 6153931. S2CID 23955175.
- ^ Bruno M, Mahgoub M, Macfarlan TS (December 2019). "The Arms Race Between KRAB-Zinc Finger Proteins and Endogenous Retroelements and Its Impact on Mammals". Annual Review of Genetics. 53 (1). Annual Reviews: 393–416. doi:10.1146/annurev-genet-112618-043717. PMID 31518518. S2CID 202572327.
Further reading
- Engelke DR, Ng SY, Shastry BS, Roeder RG (Mar 1980). "Specific interaction of a purified transcription factor with an internal control region of 5S RNA genes". Cell. 19 (3): 717–28. doi:10.1016/S0092-8674(80)80048-1. PMID 6153931. S2CID 23955175.
- Murphy JE, Keen JH (May 1992). "Recognition sites for clathrin-associated proteins AP-2 and AP-3 on clathrin triskelia". The Journal of Biological Chemistry. 267 (15): 10850–5. doi:10.1016/S0021-9258(19)50096-5. PMID 1587861.
- Seifart KH, Wang L, Waldschmidt R, Jahn D, Wingender E (January 1989). "Purification of human transcription factor IIIA and its interaction with a chemically synthesized gene encoding human 5 S rRNA". The Journal of Biological Chemistry. 264 (3): 1702–9. doi:10.1016/S0021-9258(18)94243-2. PMID 2912980.
- Drew PD, Nagle JW, Canning RD, Ozato K, Biddison WE, Becker KG (July 1995). "Cloning and expression analysis of a human cDNA homologous to Xenopus TFIIIA". Gene. 159 (2): 215–8. doi:10.1016/0378-1119(95)00145-V. PMID 7622052.
- Moorefield B, Roeder RG (August 1994). "Purification and characterization of human transcription factor IIIA". The Journal of Biological Chemistry. 269 (33): 20857–65. doi:10.1016/S0021-9258(17)31901-4. PMID 8063702.
- Fridell RA, Fischer U, Lührmann R, Meyer BE, Meinkoth JL, Malim MH, Cullen BR (April 1996). "Amphibian transcription factor IIIA proteins contain a sequence element functionally equivalent to the nuclear export signal of human immunodeficiency virus type 1 Rev". Proceedings of the National Academy of Sciences of the United States of America. 93 (7): 2936–40. Bibcode:1996PNAS...93.2936F. doi:10.1073/pnas.93.7.2936. PMC 39738. PMID 8610146.
- Oettel S, Härtel F, Kober I, Iben S, Seifart KH (June 1997). "Human transcription factors IIIC2, IIIC1 and a novel component IIIC0 fulfil different aspects of DNA binding to various pol III genes". Nucleic Acids Research. 25 (12): 2440–7. doi:10.1093/nar/25.12.2440. PMC 146769. PMID 9171097.
- Moreland RJ, Dresser ME, Rodgers JS, Roe BA, Conaway JW, Conaway RC, Hanas JS (May 2000). "Identification of a transcription factor IIIA-interacting protein". Nucleic Acids Research. 28 (9): 1986–93. doi:10.1093/nar/28.9.1986. PMC 103300. PMID 10756201.
- Rao DS, Chang JC, Kumar PD, Mizukami I, Smithson GM, Bradley SV, et al. (November 2001). "Huntingtin interacting protein 1 Is a clathrin coat binding protein required for differentiation of late spermatogenic progenitors". Molecular and Cellular Biology. 21 (22): 7796–806. doi:10.1128/MCB.21.22.7796-7806.2001. PMC 99949. PMID 11604514.
- Hanas JS, Hocker JR, Cheng YG, Lerner MR, Brackett DJ, Lightfoot SA, et al. (January 2002). "cDNA cloning, DNA binding, and evolution of mammalian transcription factor IIIA". Gene. 282 (1–2): 43–52. doi:10.1016/S0378-1119(01)00796-X. PMID 11814676.
- Weser S, Riemann J, Seifart KH, Meissner W (May 2003). "Assembly and isolation of intermediate steps of transcription complexes formed on the human 5S rRNA gene". Nucleic Acids Research. 31 (9): 2408–16. doi:10.1093/nar/gkg345. PMC 154231. PMID 12711686.
- Pellikainen JM, Ropponen KM, Kataja VV, Kellokoski JK, Eskelinen MJ, Kosma VM (November 2004). "Expression of matrix metalloproteinase (MMP)-2 and MMP-9 in breast cancer with a special reference to activator protein-2, HER2, and prognosis". Clinical Cancer Research. 10 (22): 7621–8. doi:10.1158/1078-0432.CCR-04-1061. PMID 15569994.
- Paing MM, Johnston CA, Siderovski DP, Trejo J (April 2006). "Clathrin adaptor AP2 regulates thrombin receptor constitutive internalization and endothelial cell resensitization". Molecular and Cellular Biology. 26 (8): 3231–42. doi:10.1128/MCB.26.8.3231-3242.2006. PMC 1446942. PMID 16581796.
- Yamashita A, Takada T, Nemoto K, Yamamoto G, Torii R (July 2006). "Transient suppression of PPARgamma directed ES cells into an osteoblastic lineage". FEBS Letters. 580 (17): 4121–5. Bibcode:2006FEBSL.580.4121Y. doi:10.1016/j.febslet.2006.06.057. PMID 16828750. S2CID 84554520.
- Schwartz B, Melnikova VO, Tellez C, Mourad-Zeidan A, Blehm K, Zhao YJ, et al. (June 2007). "Loss of AP-2alpha results in deregulation of E-cadherin and MMP-9 and an increase in tumorigenicity of colon cancer cells in vivo". Oncogene. 26 (28): 4049–58. doi:10.1038/sj.onc.1210193. PMID 17224907.
External links
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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(1) Basic domains |
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(1.1) Basic leucine zipper (bZIP) | |
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(1.2) Basic helix-loop-helix (bHLH) | Group A | |
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Group B | |
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Group C bHLH-PAS | |
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Group D | |
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Group E | |
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Group F bHLH-COE | |
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(1.3) bHLH-ZIP | |
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(1.4) NF-1 | |
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(1.5) RF-X | |
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(1.6) Basic helix-span-helix (bHSH) | |
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(2) Zinc finger DNA-binding domains |
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(2.1) Nuclear receptor (Cys4) | subfamily 1 | |
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subfamily 2 | |
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subfamily 3 | |
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subfamily 4 | |
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subfamily 5 | |
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subfamily 6 | |
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subfamily 0 | |
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(2.2) Other Cys4 | |
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(2.3) Cys2His2 | |
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(2.4) Cys6 | |
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(2.5) Alternating composition | |
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(2.6) WRKY | |
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(4) β-Scaffold factors with minor groove contacts |
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(0) Other transcription factors |
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see also transcription factor/coregulator deficiencies |