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Inhibitor of DNA binding 3, dominant negative helix-loop-helix protein
Symbols ID3; HEIR-1
External IDs OMIM600277 MGI96398 HomoloGene1633 GeneCards: ID3 Gene
RNA expression pattern
PBB GE ID3 207826 s at tn.png
More reference expression data
Species Human Mouse
Entrez 3399 15903
Ensembl ENSG00000117318 ENSMUSG00000007872
UniProt Q02535 Q545W1
RefSeq (mRNA) NM_002167 NM_008321
RefSeq (protein) NP_002158 NP_032347
Location (UCSC) Chr 1:
23.76 - 23.76 Mb
Chr 4:
135.42 - 135.42 Mb
PubMed search [1] [2]

DNA-binding protein inhibitor ID-3 is a protein that in humans is encoded by the ID3 gene.[1][2]

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]



ID3 (gene) has been shown to interact with TCF3.[3][4]

See also


  1. ^ Ellmeier W, Aguzzi A, Kleiner E, Kurzbauer R, Weith A (Aug 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.  
  2. ^ a b "Entrez Gene: ID3 inhibitor of DNA binding 3, dominant negative helix-loop-helix protein".  
  3. ^ Deed, R W; Jasiok M, Norton J D (Apr. 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. (UNITED STATES) 273 (14): 8278–86. ISSN 0021-9258. PMID 9525934.  
  4. ^ Langlands, K; Yin X, Anand G, Prochownik E V (Aug. 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. (UNITED STATES) 272 (32): 19785–93. ISSN 0021-9258. PMID 9242638.  

Further reading

  • 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. doi:10.1073/pnas.92.12.5520. PMID 7777541.  
  • Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank.". Gene 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. 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. doi:10.1016/0378-1119(94)90676-9. 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. doi:10.1016/0145-2126(95)00084-4. 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. doi:10.1093/nar/24.14.2813. 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. doi:10.1074/jbc.271.39.23603. 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. doi:10.1016/0014-5793(96)00868-X. 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. doi:10.1074/jbc.272.4.2459. 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. doi:10.1074/jbc.272.32.19785. 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. doi:10.1074/jbc.273.14.8278. 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. doi:10.1016/S0014-5793(98)01268-X. 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

This article incorporates text from the United States National Library of Medicine, which is in the public domain.



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