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For the ISO/IEC 7810 identification card standard, see ID-2 format.
Inhibitor of DNA binding 2, dominant negative helix-loop-helix protein
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols ID2 ; GIG8; ID2A; ID2H; bHLHb26
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 P41136
RefSeq (mRNA) NM_002166 NM_010496
RefSeq (protein) NP_002157 NP_034626
Location (UCSC) Chr 2:
8.68 – 8.68 Mb
Chr 12:
25.09 – 25.1 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] A research published by "Nature" in 01/2016, authored by italian researchers Antonio Iavarone and Anna Lasorella, from Columbia University, states that ID2 protein has a relevant role in the development and resistance to therapies of glioblastoma, the most aggressive of brain cancers.[3]


ID2 has been shown to interact with MyoD[4] and NEDD9.[5]

See also[edit]


  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. ^ "An ID2-dependent mechanism for VHL inactivation in cancer". 
  4. ^ Langlands K, Yin X, Anand G, Prochownik EV (Aug 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. 
  5. ^ Law SF, Zhang YZ, Fashena SJ, Toby G, Estojak J, Golemis EA (Oct 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. 

Further reading[edit]

External links[edit]

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