ID2

Inhibitor of DNA binding 2, dominant negative helix-loop-helix protein
Identifiers
Symbols	ID2; GIG8; ID2A; ID2H; MGC26389; bHLHb26
External IDs	OMIM: 600386 MGI: 96397 HomoloGene: 1632 GeneCards: ID2 Gene
Gene Ontology Molecular function • protein binding Cellular component • chromatin • nucleus • nucleolus • cytoplasm • cytosol • protein complex Biological process • negative regulation of transcription from RNA polymerase II promoter • leukocyte differentiation • bundle of His development • multicellular organismal development • heart development • entrainment of circadian clock • positive regulation of gene expression • negative regulation of gene expression • mammary gland epithelial cell proliferation • enucleate erythrocyte differentiation • negative regulation of sequence-specific DNA binding transcription factor activity • positive regulation of macrophage differentiation • negative regulation of neuron differentiation • positive regulation of blood pressure • positive regulation of cell cycle • negative regulation of transcription, DNA-dependent • positive regulation of transcription, DNA-dependent • embryonic digestive tract morphogenesis • positive regulation of smooth muscle cell proliferation • neuron fate commitment • response to protein stimulus • mammary gland alveolus development • epithelial cell differentiation involved in mammary gland alveolus development • endodermal digestive tract morphogenesis • positive regulation of cell cycle arrest • cellular response to lithium ion • cellular senescence • negative regulation of neural precursor cell proliferation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3398	15902
Ensembl	ENSG00000115738	ENSMUSG00000020644
UniProt	Q02363	Q545T4
RefSeq (mRNA)	NM_002166.4	NM_010496.3
RefSeq (protein)	NP_002157.2	NP_034626.1
Location (UCSC)	Chr 2: 8.82 – 8.82 Mb	Chr 12: 25.78 – 25.78 Mb
PubMed search	[1]	[2]

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

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.

See also

• Inhibitor of DNA-binding protein

Interactions

ID2 has been shown to interact with MyoD and NEDD9.

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=48481. 
• Iavarone A, Garg P, Lasorella A, et al. (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, et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=231247. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1169639. 
• 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, et al. (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, et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171189. 
• Yokota Y, Mansouri A, Mori S, et al. (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, et al. (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, et al. (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. PMC 1220711. PMID 10585876. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1220711. 
• 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, et al. (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, et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=86614. 
• Wang S, Sdrulla A, Johnson JE, et al. (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, et al. (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, et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=311163. 

External links

• MeSH ID2+protein,+human

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