Biology:ID2
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
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] 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]
Interactions
ID2 has been shown to interact with MyoD[4] and NEDD9.[5]
See also
References
- ↑ "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. Feb 1994. doi:10.1016/S0021-9258(17)42146-6. PMID 8294468.
- ↑ "Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3398.
- ↑ Lee, Sang Bae; Frattini, Veronique; Bansal, Mukesh; Castano, Angelica M.; Sherman, Dan; Hutchinson, Keino; Bruce, Jeffrey N.; Califano, Andrea et al. (2016). "An ID2-dependent mechanism for VHL inactivation in cancer". Nature 529 (7585): 172–177. doi:10.1038/nature16475. PMID 26735018. Bibcode: 2016Natur.529..172L.
- ↑ "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. 272 (32): 19785–93. Aug 1997. doi:10.1074/jbc.272.32.19785. PMID 9242638.
- ↑ "Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain". Exp. Cell Res. 252 (1): 224–35. Oct 1999. doi:10.1006/excr.1999.4609. PMID 10502414.
Further reading
- "A human Id-like helix-loop-helix protein expressed during early development". Proc. Natl. Acad. Sci. U.S.A. 89 (4): 1512–6. 1992. doi:10.1073/pnas.89.4.1512. PMID 1741406. Bibcode: 1992PNAS...89.1512B.
- "The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein". Genes Dev. 8 (11): 1270–84. 1994. doi:10.1101/gad.8.11.1270. PMID 7926730.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Two distinct cDNA sequences encoding the human helix-loop-helix protein Id2". Gene 133 (2): 305–6. 1993. doi:10.1016/0378-1119(93)90658-P. PMID 8224921.
- "Chromosomal assignment of human ID1 and ID2 genes". Genomics 30 (2): 385–7. 1996. doi:10.1006/geno.1995.0037. PMID 8586447.
- "Id2 specifically alters regulation of the cell cycle by tumor suppressor proteins". Mol. Cell. Biol. 16 (6): 2570–8. 1996. doi:10.1128/MCB.16.6.2570. PMID 8649364.
- "Cdk2-dependent phosphorylation of Id2 modulates activity of E2A-related transcription factors". EMBO J. 16 (2): 332–42. 1997. doi:10.1093/emboj/16.2.332. PMID 9029153.
- "Differential interactions of Id proteins with basic-helix-loop-helix transcription factors". J. Biol. Chem. 272 (32): 19785–93. 1997. doi:10.1074/jbc.272.32.19785. PMID 9242638.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors". EMBO J. 18 (4): 968–76. 1999. doi:10.1093/emboj/18.4.968. PMID 10022839.
- "Development of peripheral lymphoid organs and natural killer cells depends on the helix-loop-helix inhibitor Id2". Nature 397 (6721): 702–6. 1999. doi:10.1038/17812. PMID 10067894. Bibcode: 1999Natur.397..702Y.
- "Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain". Exp. Cell Res. 252 (1): 224–35. 1999. doi:10.1006/excr.1999.4609. PMID 10502414.
- "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 (3): 873–80. 2000. doi:10.1042/0264-6021:3440873. PMID 10585876.
- "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. 2000. doi:10.1006/bbrc.2000.3055. PMID 10891368.
- "Id2 is a retinoblastoma protein target and mediates signalling by Myc oncoproteins". Nature 407 (6804): 592–8. 2000. doi:10.1038/35036504. PMID 11034201. Bibcode: 2000Natur.407..592L.
- "Id Helix-Loop-Helix Proteins Antagonize Pax Transcription Factor Activity by Inhibiting DNA Binding". Mol. Cell. Biol. 21 (2): 524–33. 2001. doi:10.1128/MCB.21.2.524-533.2001. PMID 11134340.
- "A role for the helix-loop-helix protein Id2 in the control of oligodendrocyte development". Neuron 29 (3): 603–14. 2001. doi:10.1016/S0896-6273(01)00237-9. PMID 11301021.
- "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. 2001. doi:10.1089/104454901316976091. PMID 11560778.
- "Protein–Protein Interaction Panel Using Mouse Full-Length cDNAs". Genome Res. 11 (10): 1758–65. 2001. doi:10.1101/gr.180101. PMID 11591653.
External links
- ID2+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
- Overview of all the structural information available in the PDB for UniProt: Q02363 (DNA-binding protein inhibitor ID-2) at the PDBe-KB.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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