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Title: Id2  
Author: World Heritage Encyclopedia
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Subject: NeuroD, EMX homeogene, Engrailed (gene), HOXC8, HOXD8
Collection: Transcription Factors
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Inhibitor of DNA binding 2, dominant negative helix-loop-helix protein
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols  ; GIG8; ID2A; ID2H; bHLHb26
External IDs GeneCards:
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

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 1
  • Interactions 2
  • References 3
  • Further reading 4
  • External links 5

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.  
  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.  
  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.  

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.  
  • 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.  
  • 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.  
  • Kurabayashi M, Jeyaseelan R, Kedes L (1993). "Two distinct cDNA sequences encoding the human helix-loop-helix protein Id2". Gene 133 (2): 305–6.  
  • Mathew S, Chen W, Murty VV, et al. (1996). "Chromosomal assignment of human ID1 and ID2 genes". Genomics 30 (2): 385–7.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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 (Pt 3): 873–80.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • Suzuki H, Fukunishi Y, Kagawa I, et al. (2001). "Protein–Protein Interaction Panel Using Mouse Full-Length cDNAs". Genome Res. 11 (10): 1758–65.  

External links

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