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Inhibitor of DNA binding 2, dominant negative helix-loop-helix protein
Symbols ID2; GIG8; ID2A; ID2H; MGC26389
External IDs OMIM600386 MGI96397 HomoloGene1632 GeneCards: ID2 Gene
RNA expression pattern
PBB GE ID2 201565 s at tn.png
PBB GE ID2 201566 x at tn.png
More reference expression data
Species Human Mouse
Entrez 3398 15902
Ensembl ENSG00000115738 ENSMUSG00000020644
UniProt Q02363 Q545T4
RefSeq (mRNA) NM_002166 NM_010496
RefSeq (protein) NP_002157 NP_034626
Location (UCSC) Chr 2:
8.74 - 8.74 Mb
Chr 12:
25.68 - 25.69 Mb
PubMed search [1] [2]

DNA-binding protein inhibitor ID-2 is a protein that in humans is encoded by the ID2 gene.[1]

The protein encoded by this gene belongs to the inhibitor of DNA binding (ID) family, members of which are transcriptional regulators that contain a helix-loop-helix (HLH) domain but not a basic domain. Members of the ID family inhibit the functions of basic helix-loop-helix transcription factors in a dominant-negative manner by suppressing their heterodimerization partners through the HLH domains. This protein may play a role in negatively regulating cell differentiation. A pseudogene has been identified for this gene.[2]


See also


ID2 has been shown to interact with MyoD[3] and NEDD9.[4]


  1. ^ Hara E, Yamaguchi T, Nojima H, Ide T, Campisi J, Okayama H, Oda K (Feb 1994). "Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts". J Biol Chem 269 (3): 2139–45. PMID 8294468.  
  2. ^ "Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein".  
  3. ^ 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.  
  4. ^ Law, S F; Zhang Y Z, Fashena S J, Toby G, Estojak J, Golemis E A (Oct. 1999). "Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain". Exp. Cell Res. (UNITED STATES) 252 (1): 224–35. doi:10.1006/excr.1999.4609. ISSN 0014-4827. PMID 10502414.  

Further reading

  • Biggs J, Murphy EV, Israel MA (1992). "A human Id-like helix-loop-helix protein expressed during early development.". Proc. Natl. Acad. Sci. U.S.A. 89 (4): 1512–6. doi:10.1073/pnas.89.4.1512. PMID 1741406.  
  • Iavarone A, Garg P, Lasorella A, et al. (1994). "The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein.". Genes Dev. 8 (11): 1270–84. doi:10.1101/gad.8.11.1270. PMID 7926730.  
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.  
  • Kurabayashi M, Jeyaseelan R, Kedes L (1993). "Two distinct cDNA sequences encoding the human helix-loop-helix protein Id2.". Gene 133 (2): 305–6. doi:10.1016/0378-1119(93)90658-P. PMID 8224921.  
  • Mathew S, Chen W, Murty VV, et al. (1996). "Chromosomal assignment of human ID1 and ID2 genes.". Genomics 30 (2): 385–7. doi:10.1006/geno.1995.0037. PMID 8586447.  
  • Lasorella A, Iavarone A, Israel MA (1996). "Id2 specifically alters regulation of the cell cycle by tumor suppressor proteins.". Mol. Cell. Biol. 16 (6): 2570–8. PMID 8649364.  
  • Hara E, Hall M, Peters G (1997). "Cdk2-dependent phosphorylation of Id2 modulates activity of E2A-related transcription factors.". EMBO J. 16 (2): 332–42. doi:10.1093/emboj/16.2.332. PMID 9029153.  
  • 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.  
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.  
  • 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.  
  • Yokota Y, Mansouri A, Mori S, et al. (1999). "Development of peripheral lymphoid organs and natural killer cells depends on the helix-loop-helix inhibitor Id2.". Nature 397 (6721): 702–6. doi:10.1038/17812. PMID 10067894.  
  • Law SF, Zhang YZ, Fashena SJ, et al. (1999). "Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain.". Exp. Cell Res. 252 (1): 224–35. doi:10.1006/excr.1999.4609. PMID 10502414.  
  • 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.  
  • Liu J, Shi W, Warburton D (2000). "A cysteine residue in the helix-loop-helix domain of Id2 is critical for homodimerization and function.". Biochem. Biophys. Res. Commun. 273 (3): 1042–7. doi:10.1006/bbrc.2000.3055. PMID 10891368.  
  • Lasorella A, Noseda M, Beyna M, et al. (2000). "Id2 is a retinoblastoma protein target and mediates signalling by Myc oncoproteins.". Nature 407 (6804): 592–8. doi:10.1038/35036504. PMID 11034201.  
  • Roberts EC, Deed RW, Inoue T, et al. (2001). "Id helix-loop-helix proteins antagonize pax transcription factor activity by inhibiting DNA binding.". Mol. Cell. Biol. 21 (2): 524–33. doi:10.1128/MCB.21.2.524-533.2001. PMID 11134340.  
  • Wang S, Sdrulla A, Johnson JE, et al. (2001). "A role for the helix-loop-helix protein Id2 in the control of oligodendrocyte development.". Neuron 29 (3): 603–14. doi:10.1016/S0896-6273(01)00237-9. PMID 11301021.  
  • Wong J, Funes-Duran M, Ahlberg J, et al. (2001). "Characterization of a basic helix-loop-helix protein, ABF-1: nuclear localization, transcriptional properties, and interaction with Id-2.". DNA Cell Biol. 20 (8): 465–71. doi:10.1089/104454901316976091. PMID 11560778.  
  • 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.  

External links

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



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