ID2

ID2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4AYA
Identifiers
Aliases	ID2, GIG8, ID2A, ID2H, bHLHb26, inhibitor of DNA binding 2, HLH protein
External IDs	MGI: 96397 HomoloGene: 1632 GeneCards: ID2
Gene ontology Molecular function • protein dimerization activity • ion channel binding • protein binding Cellular component • nucleus • nucleoplasm • protein complex • cytosol • centrosome • cytoplasm Biological process • negative regulation of gene expression • circadian rhythm • cellular response to lithium ion • regulation of lipid metabolic process • regulation of G1/S transition of mitotic cell cycle • positive regulation of fat cell differentiation • cellular senescence • circadian regulation of gene expression • cell development • rhythmic process • negative regulation of neuron differentiation • positive regulation of cell cycle arrest • positive regulation of blood pressure • endodermal digestive tract morphogenesis • natural killer cell differentiation • entrainment of circadian clock by photoperiod • negative regulation of sequence-specific DNA binding transcription factor activity • locomotor rhythm • negative regulation of oligodendrocyte differentiation • regulation of circadian rhythm • regulation of transcription, DNA-templated • positive regulation of macrophage differentiation • positive regulation of transcription involved in G1/S transition of mitotic cell cycle • positive regulation of transcription, DNA-templated • entrainment of circadian clock • negative regulation of DNA binding • adipose tissue development • cell maturation • enucleate erythrocyte differentiation • Peyer's patch development • negative regulation of B cell differentiation • epithelial cell differentiation involved in mammary gland alveolus development • mammary gland epithelial cell proliferation • heart development • embryonic digestive tract morphogenesis • positive regulation of gene expression • oligodendrocyte development • positive regulation of erythrocyte differentiation • metanephros development • multicellular organism development • positive regulation of astrocyte differentiation • positive regulation of smooth muscle cell proliferation • olfactory bulb development • mammary gland alveolus development • thigmotaxis • adult locomotory behavior • negative regulation of neural precursor cell proliferation • bundle of His development • negative regulation of osteoblast differentiation • negative regulation of transcription from RNA polymerase II promoter • membranous septum morphogenesis • negative regulation of transcription, DNA-templated • leukocyte differentiation • cell morphogenesis involved in neuron differentiation • transcription, DNA-templated • neuron fate commitment Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3398	15902
Ensembl	ENSG00000115738	ENSMUSG00000020644
UniProt	Q02363	P41136
RefSeq (mRNA)	NM_002166	NM_010496
RefSeq (protein)	NP_002157.2	NP_034626.1
Location (UCSC)	Chr 2: 8.68 – 8.68 Mb	Chr 12: 25.09 – 25.1 Mb
PubMed search	[1]	[2]
Wikidata

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

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.^[4] 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.^[5]

Interactions

ID2 has been shown to interact with MyoD^[6] and NEDD9.^[7]

See also

• Inhibitor of DNA-binding protein

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. "Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein".
5. "An ID2-dependent mechanism for VHL inactivation in cancer".
6. 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.
7. 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

• Biggs J, Murphy EV, Israel MA (1992). "A human Id-like helix-loop-helix protein expressed during early development". Proc. Natl. Acad. Sci. U.S.A. 89 (4): 1512–6. doi:10.1073/pnas.89.4.1512. PMC 48481. PMID 1741406.
• Iavarone A, Garg P, Lasorella A, Hsu J, Israel MA (1994). "The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein". Genes Dev. 8 (11): 1270–84. doi:10.1101/gad.8.11.1270. PMID 7926730.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Kurabayashi M, Jeyaseelan R, Kedes L (1993). "Two distinct cDNA sequences encoding the human helix-loop-helix protein Id2". Gene. 133 (2): 305–6. doi:10.1016/0378-1119(93)90658-P. PMID 8224921.
• Mathew S, Chen W, Murty VV, Benezra R, Chaganti RS (1996). "Chromosomal assignment of human ID1 and ID2 genes". Genomics. 30 (2): 385–7. doi:10.1006/geno.1995.0037. PMID 8586447.
• Lasorella A, Iavarone A, Israel MA (1996). "Id2 specifically alters regulation of the cell cycle by tumor suppressor proteins". Mol. Cell. Biol. 16 (6): 2570–8. PMC 231247. PMID 8649364.
• Hara E, Hall M, Peters G (1997). "Cdk2-dependent phosphorylation of Id2 modulates activity of E2A-related transcription factors". EMBO J. 16 (2): 332–42. doi:10.1093/emboj/16.2.332. PMC 1169639. PMID 9029153.
• 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.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• 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.
• Yokota Y, Mansouri A, Mori S, Sugawara S, Adachi S, Nishikawa S, Gruss P (1999). "Development of peripheral lymphoid organs and natural killer cells depends on the helix-loop-helix inhibitor Id2". Nature. 397 (6721): 702–6. doi:10.1038/17812. PMID 10067894.
• Law SF, Zhang YZ, Fashena SJ, Toby G, Estojak J, Golemis EA (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.
• Moldes M, Boizard M, Liepvre XL, Fève B, Dugail I, Pairault J (2000). "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 Pt 3 (Pt 3): 873–80. doi:10.1042/0264-6021:3440873. PMC 1220711. PMID 10585876.
• Liu J, Shi W, Warburton D (2000). "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. doi:10.1006/bbrc.2000.3055. PMID 10891368.
• Lasorella A, Noseda M, Beyna M, Yokota Y, Iavarone A (2000). "Id2 is a retinoblastoma protein target and mediates signalling by Myc oncoproteins". Nature. 407 (6804): 592–8. doi:10.1038/35036504. PMID 11034201.
• Roberts EC, Deed RW, Inoue T, Norton JD, Sharrocks AD (2001). "Id Helix-Loop-Helix Proteins Antagonize Pax Transcription Factor Activity by Inhibiting DNA Binding". Mol. Cell. Biol. 21 (2): 524–33. doi:10.1128/MCB.21.2.524-533.2001. PMC 86614. PMID 11134340.
• Wang S, Sdrulla A, Johnson JE, Yokota Y, Barres BA (2001). "A role for the helix-loop-helix protein Id2 in the control of oligodendrocyte development". Neuron. 29 (3): 603–14. doi:10.1016/S0896-6273(01)00237-9. PMID 11301021.
• Wong J, Funes-Duran M, Ahlberg J, Round J, O'Connell R, Miller R, Chen E, Richmond PA, Vierra CA (2001). "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. doi:10.1089/104454901316976091. PMID 11560778.
• 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.

External links

• ID2 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.