ID3 (gene)

Inhibitor of DNA binding 3, dominant negative helix-loop-helix protein
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2LFH​
Identifiers
Symbols	ID3 ; HEIR-1; bHLHb25
External IDs	OMIM: 600277 MGI: 96398 HomoloGene: 1633 GeneCards: ID3 Gene
Gene ontology Molecular function • transcription factor activity, sequence-specific DNA binding • transcription corepressor activity • protein binding • transcription factor binding • protein domain specific binding • protein dimerization activity Cellular component • nucleus • nucleoplasm • cytoplasm • microtubule cytoskeleton Biological process • negative regulation of transcription from RNA polymerase II promoter • metanephros development • regulation of DNA replication • transcription, DNA-templated • multicellular organismal development • central nervous system development • heart development • muscle organ development • circadian rhythm • response to wounding • neuron differentiation • epithelial cell differentiation • notochord development • odontogenesis • positive regulation of apoptotic process • negative regulation of sequence-specific DNA binding transcription factor activity • negative regulation of myoblast differentiation • negative regulation of osteoblast differentiation • negative regulation of transcription, DNA-templated • regulation of cell cycle Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3399	15903
Ensembl	ENSG00000117318	ENSMUSG00000007872
UniProt	Q02535	P41133
RefSeq (mRNA)	NM_002167	NM_008321
RefSeq (protein)	NP_002158	NP_032347
Location (UCSC)	Chr 1: 23.56 – 23.56 Mb	Chr 4: 136.14 – 136.15 Mb
PubMed search

DNA-binding protein inhibitor ID-3 is a protein that in humans is encoded by the ID3 gene.^[1][2]

Function

Members of the ID family of helix-loop-helix (HLH) proteins lack a basic DNA-binding domain and inhibit transcription through formation of nonfunctional dimers that are incapable of binding to DNA.[supplied by OMIM]^[2]

Interactions

ID3 (gene) has been shown to interact with TCF3.^[3][4]

Repressors of ID3

BTG2 binds to the promoter of Id3 and represses its activity. By this mechanism, the upregulation of Id3 in the hippocampus caused by BTG2 ablation prevents terminal differentiation of hippocampal neurons.^[5]

See also

• Inhibitor of DNA-binding protein

References

1. Ellmeier W, Aguzzi A, Kleiner E, Kurzbauer R, Weith A (Aug 1992). "Mutually exclusive expression of a helix-loop-helix gene and N-myc in human neuroblastomas and in normal development". EMBO J. 11 (7): 2563–71. PMC 556731. PMID 1628620.
2. "Entrez Gene: ID3 inhibitor of DNA binding 3, dominant negative helix-loop-helix protein".
3. Deed RW, Jasiok M, Norton JD (Apr 1998). "Lymphoid-specific expression of the Id3 gene in hematopoietic cells. Selective antagonism of E2A basic helix-loop-helix protein associated with Id3-induced differentiation of erythroleukemia cells". J. Biol. Chem. 273 (14): 8278–86. doi:10.1074/jbc.273.14.8278. PMID 9525934.
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. Farioli-Vecchioli S, Saraulli D, Costanzi M, Leonardi L, Cinà I, Micheli L, Nutini M, Longone P, Oh SP, Cestari V, Tirone F (2009). Okazawa H, ed. "Impaired terminal differentiation of hippocampal granule neurons and defective contextual memory in PC3/Tis21 knockout mice". PLoS ONE 4 (12): e8339. doi:10.1371/journal.pone.0008339. PMC 2791842. PMID 20020054.

Further reading

• White PS, Maris JM, Beltinger C, Sulman E, Marshall HN, Fujimori M, Kaufman BA, Biegel JA, Allen C, Hilliard C, Valentine MB, Look AT, Enomoto H, Sakiyama S, Brodeur GM (1995). "A region of consistent deletion in neuroblastoma maps within human chromosome 1p36.2-36.3". Proc. Natl. Acad. Sci. U.S.A. 92 (12): 5520–4. doi:10.1073/pnas.92.12.5520. PMC 41727. PMID 7777541.
• Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, Yokoyama-Kobayashi M, Aoki T (1994). "Construction of a human full-length cDNA bank". Gene 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
• Deed RW, Hirose T, Mitchell EL, Santibanez-Koref MF, Norton JD (1994). "Structural organisation and chromosomal mapping of the human Id-3 gene". Gene 151 (1-2): 309–14. doi:10.1016/0378-1119(94)90676-9. PMID 7828896.
• Deed RW, Bianchi SM, Atherton GT, Johnston D, Santibanez-Koref M, Murphy JJ, Norton JD (1993). "An immediate early human gene encodes an Id-like helix-loop-helix protein and is regulated by protein kinase C activation in diverse cell types". Oncogene 8 (3): 599–607. PMID 8437843.
• Ishiguro A, Spirin K, Shiohara M, Tobler A, Norton JD, Rigolet M, Shimbo T, Koeffler HP (1995). "Expression of Id2 and Id3 mRNA in human lymphocytes". Leuk. Res. 19 (12): 989–96. doi:10.1016/0145-2126(95)00084-4. PMID 8632670.
• Wibley J, Deed R, Jasiok M, Douglas K, Norton J (1996). "A homology model of the Id-3 helix-loop-helix domain as a basis for structure-function predictions". Biochim. Biophys. Acta 1294 (2): 138–46. doi:10.1016/0167-4838(96)00008-8. PMID 8645731.
• Loveys DA, Streiff MB, Kato GJ (1996). "E2A basic-helix-loop-helix transcription factors are negatively regulated by serum growth factors and by the Id3 protein". Nucleic Acids Res. 24 (14): 2813–20. doi:10.1093/nar/24.14.2813. PMC 145994. PMID 8759016.
• Deed RW, Armitage S, Norton JD (1996). "Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism". J. Biol. Chem. 271 (39): 23603–6. doi:10.1074/jbc.271.39.23603. PMID 8798572.
• Deed RW, Jasiok M, Norton JD (1996). "Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism". FEBS Lett. 393 (1): 113–6. doi:10.1016/0014-5793(96)00868-X. PMID 8804437.
• Chen B, Lim RW (1997). "Physical and functional interactions between the transcriptional inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism regulating muscle-specific gene expression". J. Biol. Chem. 272 (4): 2459–63. doi:10.1074/jbc.272.4.2459. PMID 8999959.
• 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. doi:10.1074/jbc.272.32.19785. PMID 9242638.
• Deed RW, Hara E, Atherton GT, Peters G, Norton JD (1997). "Regulation of Id3 cell cycle function by Cdk-2-dependent phosphorylation". Mol. Cell. Biol. 17 (12): 6815–21. PMC 232537. PMID 9372912.
• Deed RW, Jasiok M, Norton JD (1998). "Lymphoid-specific expression of the Id3 gene in hematopoietic cells. Selective antagonism of E2A basic helix-loop-helix protein associated with Id3-induced differentiation of erythroleukemia cells". J. Biol. Chem. 273 (14): 8278–86. doi:10.1074/jbc.273.14.8278. PMID 9525934.
• Asp J, Thornemo M, Inerot S, Lindahl A (1998). "The helix-loop-helix transcription factors Id1 and Id3 have a functional role in control of cell division in human normal and neoplastic chondrocytes". FEBS Lett. 438 (1-2): 85–90. doi:10.1016/S0014-5793(98)01268-X. PMID 9821964.
• Yates PR, Atherton GT, Deed RW, Norton JD, Sharrocks AD (1999). "Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors". EMBO J. 18 (4): 968–76. doi:10.1093/emboj/18.4.968. PMC 1171189. PMID 10022839.
• Moldes M, Boizard M, Liepvre XL, Fève B, Dugail I, Pairault J (1999). "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. 344 Pt 3: 873–80. doi:10.1042/0264-6021:3440873. PMC 1220711. PMID 10585876.
• Bounpheng MA, Dimas JJ, Dodds SG, Christy BA (1999). "Degradation of Id proteins by the ubiquitin-proteasome pathway". FASEB J. 13 (15): 2257–64. PMID 10593873.
• Suzuki H, Fukunishi Y, Kagawa I, Saito R, Oda H, Endo T, Kondo S, Bono H, Okazaki Y, Hayashizaki Y (2001). "Protein-protein interaction panel using mouse full-length cDNAs". Genome Res. 11 (10): 1758–65. doi:10.1101/gr.180101. PMC 311163. PMID 11591653.
• Jögi A, Persson P, Grynfeld A, Påhlman S, Axelson H (2002). "Modulation of basic helix-loop-helix transcription complex formation by Id proteins during neuronal differentiation". J. Biol. Chem. 277 (11): 9118–26. doi:10.1074/jbc.M107713200. PMID 11756408.

External links

• ID3 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)

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