Biology:ID3 (gene)
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
DNA-binding protein inhibitor ID-3 is a protein that in humans is encoded by the ID3 gene.[1][2]
Function
Members of the ID family of helix-loop-helix (HLH) proteins lack a basic DNA-binding domain and inhibit transcription through formation of nonfunctional dimers that are incapable of binding to DNA.[supplied by OMIM][2]
Interactions
ID3 (gene) has been shown to interact with TCF3.[3][4]
Repressors of ID3
BTG2 binds to the promoter of Id3 and represses its activity. By this mechanism, the upregulation of Id3 in the hippocampus caused by BTG2 ablation prevents terminal differentiation of hippocampal neurons.[5]
See also
References
- ↑ "Mutually exclusive expression of a helix-loop-helix gene and N-myc in human neuroblastomas and in normal development". EMBO J. 11 (7): 2563–71. Aug 1992. doi:10.1002/j.1460-2075.1992.tb05321.x. PMID 1628620.
- ↑ 2.0 2.1 "Entrez Gene: ID3 inhibitor of DNA binding 3, dominant negative helix-loop-helix protein". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3399.
- ↑ "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. 273 (14): 8278–86. Apr 1998. doi:10.1074/jbc.273.14.8278. PMID 9525934.
- ↑ "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. 272 (32): 19785–93. Aug 1997. doi:10.1074/jbc.272.32.19785. PMID 9242638.
- ↑ Okazawa, Hitoshi, ed (2009). "Impaired terminal differentiation of hippocampal granule neurons and defective contextual memory in PC3/Tis21 knockout mice". PLOS ONE 4 (12): e8339. doi:10.1371/journal.pone.0008339. PMID 20020054. Bibcode: 2009PLoSO...4.8339F.
Further reading
- "A region of consistent deletion in neuroblastoma maps within human chromosome 1p36.2-36.3". Proc. Natl. Acad. Sci. U.S.A. 92 (12): 5520–4. 1995. doi:10.1073/pnas.92.12.5520. PMID 7777541. Bibcode: 1995PNAS...92.5520W.
- "Construction of a human full-length cDNA bank". Gene 150 (2): 243–50. 1994. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
- "Structural organisation and chromosomal mapping of the human Id-3 gene". Gene 151 (1–2): 309–14. 1994. doi:10.1016/0378-1119(94)90676-9. PMID 7828896.
- "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 8 (3): 599–607. 1993. PMID 8437843.
- "Expression of Id2 and Id3 mRNA in human lymphocytes". Leuk. Res. 19 (12): 989–96. 1995. doi:10.1016/0145-2126(95)00084-4. PMID 8632670.
- "A homology model of the Id-3 helix-loop-helix domain as a basis for structure-function predictions". Biochim. Biophys. Acta 1294 (2): 138–46. 1996. doi:10.1016/0167-4838(96)00008-8. PMID 8645731.
- "E2A basic-helix-loop-helix transcription factors are negatively regulated by serum growth factors and by the Id3 protein". Nucleic Acids Res. 24 (14): 2813–20. 1996. doi:10.1093/nar/24.14.2813. PMID 8759016.
- "Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism". J. Biol. Chem. 271 (39): 23603–6. 1996. doi:10.1074/jbc.271.39.23603. PMID 8798572.
- "Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism". FEBS Lett. 393 (1): 113–6. 1996. doi:10.1016/0014-5793(96)00868-X. PMID 8804437.
- "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. 272 (4): 2459–63. 1997. doi:10.1074/jbc.272.4.2459. PMID 8999959.
- "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. 272 (32): 19785–93. 1997. doi:10.1074/jbc.272.32.19785. PMID 9242638.
- "Regulation of Id3 cell cycle function by Cdk-2-dependent phosphorylation". Mol. Cell. Biol. 17 (12): 6815–21. 1997. doi:10.1128/MCB.17.12.6815. PMID 9372912.
- "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. 273 (14): 8278–86. 1998. doi:10.1074/jbc.273.14.8278. PMID 9525934.
- "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. 438 (1–2): 85–90. 1998. doi:10.1016/S0014-5793(98)01268-X. PMID 9821964.
- "Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors". EMBO J. 18 (4): 968–76. 1999. doi:10.1093/emboj/18.4.968. PMID 10022839.
- "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.. 344 344 Pt 3 (3): 873–80. 1999. doi:10.1042/0264-6021:3440873. PMID 10585876.
- "Degradation of Id proteins by the ubiquitin-proteasome pathway". FASEB J. 13 (15): 2257–64. 1999. doi:10.1096/fasebj.13.15.2257. PMID 10593873.
- "Protein-protein interaction panel using mouse full-length cDNAs". Genome Res. 11 (10): 1758–65. 2001. doi:10.1101/gr.180101. PMID 11591653.
- "Modulation of basic helix-loop-helix transcription complex formation by Id proteins during neuronal differentiation". J. Biol. Chem. 277 (11): 9118–26. 2002. doi:10.1074/jbc.M107713200. PMID 11756408.
External links
- ID3+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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