ID3 (gene)
| Inhibitor of DNA binding 3, dominant negative helix-loop-helix protein | |||||||||||
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| Identifiers | |||||||||||
| Symbols | ID3 ; HEIR-1 | ||||||||||
| External IDs | Template:OMIM5 Template:MGI HomoloGene: 1633 | ||||||||||
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| RNA expression pattern | |||||||||||
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| Orthologs | |||||||||||
| Template:GNF Ortholog box | |||||||||||
| Species | Human | Mouse | |||||||||
| Entrez | n/a | n/a | |||||||||
| Ensembl | n/a | n/a | |||||||||
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| RefSeq (mRNA) | n/a | n/a | |||||||||
| RefSeq (protein) | n/a | n/a | |||||||||
| Location (UCSC) | n/a | n/a | |||||||||
| PubMed search | n/a | n/a | |||||||||
Inhibitor of DNA binding 3, dominant negative helix-loop-helix protein, also known as ID3, is a human gene.[1]
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][1]
References
Further reading
- Ellmeier W, Aguzzi A, Kleiner E; et al. (1992). "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. PMID 1628620.
- White PS, Maris JM, Beltinger C; et al. (1995). "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. PMID 7777541.
- Kato S, Sekine S, Oh SW; et al. (1995). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. PMID 7821789.
- Deed RW, Hirose T, Mitchell EL; et al. (1995). "Structural organisation and chromosomal mapping of the human Id-3 gene". Gene. 151 (1–2): 309–14. PMID 7828896.
- Deed RW, Bianchi SM, Atherton GT; et al. (1993). "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. PMID 8437843.
- Ishiguro A, Spirin K, Shiohara M; et al. (1996). "Expression of Id2 and Id3 mRNA in human lymphocytes". Leuk. Res. 19 (12): 989–96. PMID 8632670.
- Wibley J, Deed R, Jasiok M; et al. (1996). "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. PMID 8645731.
- Loveys DA, Streiff MB, Kato GJ (1996). "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. PMID 8759016.
- Deed RW, Armitage S, Norton JD (1996). "Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism". J. Biol. Chem. 271 (39): 23603–6. PMID 8798572.
- Deed RW, Jasiok M, Norton JD (1996). "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. PMID 8804437.
- Chen B, Lim RW (1997). "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. PMID 8999959.
- Langlands K, Yin X, Anand G, Prochownik EV (1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. 272 (32): 19785–93. PMID 9242638.
- Deed RW, Hara E, Atherton GT; et al. (1997). "Regulation of Id3 cell cycle function by Cdk-2-dependent phosphorylation". Mol. Cell. Biol. 17 (12): 6815–21. PMID 9372912.
- Deed RW, Jasiok M, Norton JD (1998). "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. PMID 9525934.
- Asp J, Thornemo M, Inerot S, Lindahl A (1998). "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. PMID 9821964.
- Yates PR, Atherton GT, Deed RW; et al. (1999). "Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors". EMBO J. 18 (4): 968–76. doi:10.1093/emboj/18.4.968. PMID 10022839.
- Moldes M, Boizard M, Liepvre XL; et al. (2000). "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 Pt 3: 873–80. PMID 10585876.
- Bounpheng MA, Dimas JJ, Dodds SG, Christy BA (2000). "Degradation of Id proteins by the ubiquitin-proteasome pathway". FASEB J. 13 (15): 2257–64. PMID 10593873.
- Suzuki H, Fukunishi Y, Kagawa I; et al. (2001). "Protein-protein interaction panel using mouse full-length cDNAs". Genome Res. 11 (10): 1758–65. doi:10.1101/gr.180101. PMID 11591653.
- Jögi A, Persson P, Grynfeld A; et al. (2002). "Modulation of basic helix-loop-helix transcription complex formation by Id proteins during neuronal differentiation". J. Biol. Chem. 277 (11): 9118–26. doi:10.1074/jbc.M107713200. PMID 11756408.
External links
- ID3+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.