ID2

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Template:Short description Template:For multi Template:Cs1 config An Error has occurred retrieving Wikidata item for infobox DNA-binding protein inhibitor ID-2 is a protein that in humans is encoded by the ID2 gene.[1]

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.[2] The ID2 protein may play a role in the development and resistance to therapies of glioblastoma, the most aggressive of brain cancers.[3]

Interactions

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

See also

References

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  1. ^ Page Module:Citation/CS1/styles.css has no content.Hara E, Yamaguchi T, Nojima H, Ide T, Campisi J, Okayama H, et al. (January 1994). "Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts". The Journal of Biological Chemistry. 269 (3): 2139–2145. doi:10.1016/S0021-9258(17)42146-6. PMID 8294468.
  2. ^ Page Module:Citation/CS1/styles.css has no content."Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein".
  3. ^ Page Module:Citation/CS1/styles.css has no content.Lee SB, Frattini V, Bansal M, Castano AM, Sherman D, Hutchinson K, et al. (January 2016). "An ID2-dependent mechanism for VHL inactivation in cancer". Nature. 529 (7585): 172–177. Bibcode:2016Natur.529..172L. doi:10.1038/nature16475. PMC 5384647. PMID 26735018.
  4. ^ Page Module:Citation/CS1/styles.css has no content.Langlands K, Yin X, Anand G, Prochownik EV (August 1997). "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". The Journal of Biological Chemistry. 272 (32): 19785–19793. doi:10.1074/jbc.272.32.19785. PMID 9242638.
  5. ^ Page Module:Citation/CS1/styles.css has no content.Law SF, Zhang YZ, Fashena SJ, Toby G, Estojak J, Golemis EA (October 1999). "Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain". Experimental Cell Research. 252 (1): 224–235. doi:10.1006/excr.1999.4609. PMID 10502414.

Further reading

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

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