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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 [3] [4] Wikidata
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DNA-binding protein inhibitor ID-2 is a protein that in humans is encoded by the ID2 gene.[5]

Function

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.[6] 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.[7]

Interactions

ID2 has been shown to interact with MyoD[8] and NEDD9.[9]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000115738 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020644 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ 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. 
  6. ^ "Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein". 
  7. ^ "An ID2-dependent mechanism for VHL inactivation in cancer". 
  8. ^ 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. 
  9. ^ 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

External links

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