ID3(分化抑制因子3,Inhibitor of Differentiation 3),正式名稱爲「inhibitor of DNA binding 3, HLH protein」(DNA結合抑制因子3,HLH(螺旋-環-螺旋)蛋白)。人ID3蛋白由ID3基因編碼[5][6]。
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分化抑制因子(ID)家族螺旋-環-螺旋(HLH)蛋白質缺乏基因的DNA結合結構域。它通過與其他的HLH蛋白形成異二聚體,阻止其與DNA結合,進而抑制其功能[6]。
ID3能與TCF3(轉錄因子3)發生相互作用[7][8]。
BTG2能與ID3基因的啓動子結合,進而抑制其ID3基因的活性。如果敲除海馬的BTG2基因的話,海馬ID3表達就會上調,進而使其神經元無法發生末端分化[9]。
Deed RW, Jasiok M, Norton JD. Lymphoid-specific expression of the Id3 gene in hematopoietic cells. Selective antagonism of E2A basic helix-loop-helix protein associated with Id3-induced differentiation of erythroleukemia cells. J. Biol. Chem. Apr 1998, 273 (14): 8278–86. PMID 9525934. doi:10.1074/jbc.273.14.8278.
Langlands K, Yin X, Anand G, Prochownik EV. Differential interactions of Id proteins with basic-helix-loop-helix transcription factors. J. Biol. Chem. Aug 1997, 272 (32): 19785–93. PMID 9242638. doi:10.1074/jbc.272.32.19785.
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. PMID 7777541. doi:10.1073/pnas.92.12.5520.
- Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, Yokoyama-Kobayashi M, Aoki T. Construction of a human full-length cDNA bank. Gene. 1994, 150 (2): 243–50. PMID 7821789. doi:10.1016/0378-1119(94)90433-2.
- Deed RW, Hirose T, Mitchell EL, Santibanez-Koref MF, Norton JD. Structural organisation and chromosomal mapping of the human Id-3 gene. Gene. 1994, 151 (1-2): 309–14. PMID 7828896. doi:10.1016/0378-1119(94)90676-9.
- Deed RW, Bianchi SM, Atherton GT, Johnston D, Santibanez-Koref M, Murphy JJ, Norton JD. An immediate early human gene encodes an Id-like helix-loop-helix protein and is regulated by protein kinase C activation in diverse cell types. Oncogene. 1993, 8 (3): 599–607. PMID 8437843.
- Ishiguro A, Spirin K, Shiohara M, Tobler A, Norton JD, Rigolet M, Shimbo T, Koeffler HP. Expression of Id2 and Id3 mRNA in human lymphocytes. Leuk. Res. 1995, 19 (12): 989–96. PMID 8632670. doi:10.1016/0145-2126(95)00084-4.
- Wibley J, Deed R, Jasiok M, Douglas K, Norton J. A homology model of the Id-3 helix-loop-helix domain as a basis for structure-function predictions. Biochim. Biophys. Acta. 1996, 1294 (2): 138–46. PMID 8645731. doi:10.1016/0167-4838(96)00008-8.
- Loveys DA, Streiff MB, Kato GJ. E2A basic-helix-loop-helix transcription factors are negatively regulated by serum growth factors and by the Id3 protein. Nucleic Acids Res. 1996, 24 (14): 2813–20. PMC 145994
. PMID 8759016. doi:10.1093/nar/24.14.2813.
- Deed RW, Armitage S, Norton JD. Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism. J. Biol. Chem. 1996, 271 (39): 23603–6. PMID 8798572. doi:10.1074/jbc.271.39.23603.
- Deed RW, Jasiok M, Norton JD. Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism. FEBS Lett. 1996, 393 (1): 113–6. PMID 8804437. doi:10.1016/0014-5793(96)00868-X.
- Chen B, Lim RW. Physical and functional interactions between the transcriptional inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism regulating muscle-specific gene expression. J. Biol. Chem. 1997, 272 (4): 2459–63. PMID 8999959. doi:10.1074/jbc.272.4.2459.
- Langlands K, Yin X, Anand G, Prochownik EV. Differential interactions of Id proteins with basic-helix-loop-helix transcription factors. J. Biol. Chem. 1997, 272 (32): 19785–93. PMID 9242638. doi:10.1074/jbc.272.32.19785.
- Deed RW, Hara E, Atherton GT, Peters G, Norton JD. Regulation of Id3 cell cycle function by Cdk-2-dependent phosphorylation. Mol. Cell. Biol. 1997, 17 (12): 6815–21. PMC 232537
. PMID 9372912.
- Deed RW, Jasiok M, Norton JD. Lymphoid-specific expression of the Id3 gene in hematopoietic cells. Selective antagonism of E2A basic helix-loop-helix protein associated with Id3-induced differentiation of erythroleukemia cells. J. Biol. Chem. 1998, 273 (14): 8278–86. PMID 9525934. doi:10.1074/jbc.273.14.8278.
- Asp J, Thornemo M, Inerot S, Lindahl A. The helix-loop-helix transcription factors Id1 and Id3 have a functional role in control of cell division in human normal and neoplastic chondrocytes. FEBS Lett. 1998, 438 (1-2): 85–90. PMID 9821964. doi:10.1016/S0014-5793(98)01268-X.
- Yates PR, Atherton GT, Deed RW, Norton JD, Sharrocks AD. Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors. EMBO J. 1999, 18 (4): 968–76. PMC 1171189
. PMID 10022839. doi:10.1093/emboj/18.4.968.
- Moldes M, Boizard M, Liepvre XL, Fève B, Dugail I, Pairault J. Functional antagonism between inhibitor of DNA binding (Id) and adipocyte determination and differentiation factor 1/sterol regulatory element-binding protein-1c (ADD1/SREBP-1c) trans-factors for the regulation of fatty acid synthase promoter in adipocytes. Biochem. J. 344. 1999,. 344 Pt 3: 873–80. PMC 1220711
. PMID 10585876. doi:10.1042/0264-6021:3440873.
- Bounpheng MA, Dimas JJ, Dodds SG, Christy BA. Degradation of Id proteins by the ubiquitin-proteasome pathway. FASEB J. 1999, 13 (15): 2257–64. PMID 10593873.
- Suzuki H, Fukunishi Y, Kagawa I, Saito R, Oda H, Endo T, Kondo S, Bono H, Okazaki Y, Hayashizaki Y. Protein-protein interaction panel using mouse full-length cDNAs. Genome Res. 2001, 11 (10): 1758–65. PMC 311163
. PMID 11591653. doi:10.1101/gr.180101.
- Jögi A, Persson P, Grynfeld A, Påhlman S, Axelson H. Modulation of basic helix-loop-helix transcription complex formation by Id proteins during neuronal differentiation. J. Biol. Chem. 2002, 277 (11): 9118–26. PMID 11756408. doi:10.1074/jbc.M107713200.
ID3 (基因)引用了美國國家醫學圖書館提供的資料,這些資料屬於公共領域。