ID2

For the ISO/IEC 7810 identification card standard, see ID-2 format. For the electric concept car, see Volkswagen ID.2all.

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, inhibitor of DNA binding 2
External IDs	OMIM: 600386; MGI: 96397; HomoloGene: 1632; GeneCards: ID2; OMA:ID2 - orthologs
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2p25.1 Start 8,678,845 bp[1] End 8,684,461 bp[1]
Gene location (Mouse) Chr. Chromosome 12 (mouse)[2] Band 12 A1.3|12 8.57 cM Start 25,143,798 bp[2] End 25,147,139 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in popliteal artery tibial arteries saphenous vein pericardium right lobe of liver granulocyte trachea lower lobe of lung renal medulla seminal vesicula Top expressed in vas deferens seminal vesicula lobe of cerebellum migratory enteric neural crest cell cerebellar vermis abdominal wall dermis left lung lobe hand parotid gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein dimerization activity transmembrane transporter binding protein binding DNA-binding transcription factor activity, RNA polymerase II-specific DNA-binding transcription factor activity transcription factor binding Cellular component nucleus cytosol cytoplasm protein-containing complex Biological process regulation of G1/S transition of mitotic cell cycle rhythmic process negative regulation of DNA-binding transcription factor activity regulation of transcription, DNA-templated positive regulation of transcription involved in G1/S transition of mitotic cell cycle multicellular organism development negative regulation of transcription, DNA-templated transcription, DNA-templated negative regulation of transcription by RNA polymerase II metanephros development natural killer cell differentiation thigmotaxis leukocyte differentiation membranous septum morphogenesis bundle of His development heart development circadian rhythm adult locomotory behavior entrainment of circadian clock positive regulation of gene expression negative regulation of gene expression oligodendrocyte development regulation of lipid metabolic process olfactory bulb development circadian regulation of gene expression mammary gland epithelial cell proliferation regulation of circadian rhythm entrainment of circadian clock by photoperiod enucleate erythrocyte differentiation negative regulation of DNA binding locomotor rhythm negative regulation of B cell differentiation positive regulation of fat cell differentiation positive regulation of erythrocyte differentiation positive regulation of macrophage differentiation negative regulation of neuron differentiation negative regulation of osteoblast differentiation positive regulation of blood pressure positive regulation of transcription, DNA-templated cell development cell maturation Peyer's patch development embryonic digestive tract morphogenesis positive regulation of smooth muscle cell proliferation neuron fate commitment cell morphogenesis involved in neuron differentiation positive regulation of astrocyte differentiation negative regulation of oligodendrocyte differentiation adipose tissue development mammary gland alveolus development epithelial cell differentiation involved in mammary gland alveolus development endodermal digestive tract morphogenesis cellular response to lithium ion cellular senescence negative regulation of neural precursor cell proliferation neuron differentiation regulation of cell cycle Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3398 15902 Ensembl ENSG00000115738 ENSMUSG00000020644 UniProt Q02363 P41136 RefSeq (mRNA) NM_002166 NM_010496 RefSeq (protein) NP_002157 NP_034626 Location (UCSC) Chr 2: 8.68 – 8.68 Mb Chr 12: 25.14 – 25.15 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

DNA-binding protein inhibitor ID-2 is a protein that in humans is encoded by the ID2 gene.^[5]

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.^[6] The ID2 protein may play a role in the development and resistance to therapies of glioblastoma, the most aggressive of brain cancers.^[7]

Interactions

ID2 has been shown to interact with MyoD^[8] and NEDD9.^[9]

See also

• Inhibitor of DNA-binding protein

References

1. GRCh38: Ensembl release 89: ENSG00000115738 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020644 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein".
7. 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.
8. 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.
9. 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

• Biggs J, Murphy EV, Israel MA (February 1992). "A human Id-like helix-loop-helix protein expressed during early development". Proceedings of the National Academy of Sciences of the United States of America. 89 (4): 1512–1516. Bibcode:1992PNAS...89.1512B. doi:10.1073/pnas.89.4.1512. PMC 48481. PMID 1741406.
• Iavarone A, Garg P, Lasorella A, Hsu J, Israel MA (June 1994). "The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein". Genes & Development. 8 (11): 1270–1284. doi:10.1101/gad.8.11.1270. PMID 7926730.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Kurabayashi M, Jeyaseelan R, Kedes L (November 1993). "Two distinct cDNA sequences encoding the human helix-loop-helix protein Id2". Gene. 133 (2): 305–306. doi:10.1016/0378-1119(93)90658-P. PMID 8224921.
• Mathew S, Chen W, Murty VV, Benezra R, Chaganti RS (November 1995). "Chromosomal assignment of human ID1 and ID2 genes". Genomics. 30 (2): 385–387. doi:10.1006/geno.1995.0037. PMID 8586447.
• Lasorella A, Iavarone A, Israel MA (June 1996). "Id2 specifically alters regulation of the cell cycle by tumor suppressor proteins". Molecular and Cellular Biology. 16 (6): 2570–2578. doi:10.1128/MCB.16.6.2570. PMC 231247. PMID 8649364.
• Hara E, Hall M, Peters G (January 1997). "Cdk2-dependent phosphorylation of Id2 modulates activity of E2A-related transcription factors". The EMBO Journal. 16 (2): 332–342. doi:10.1093/emboj/16.2.332. PMC 1169639. PMID 9029153.
• 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.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Yates PR, Atherton GT, Deed RW, Norton JD, Sharrocks AD (February 1999). "Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors". The EMBO Journal. 18 (4): 968–976. doi:10.1093/emboj/18.4.968. PMC 1171189. PMID 10022839.
• Yokota Y, Mansouri A, Mori S, Sugawara S, Adachi S, Nishikawa S, et al. (February 1999). "Development of peripheral lymphoid organs and natural killer cells depends on the helix-loop-helix inhibitor Id2". Nature. 397 (6721): 702–706. Bibcode:1999Natur.397..702Y. doi:10.1038/17812. PMID 10067894. S2CID 4428856.
• 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.
• Moldes M, Boizard M, Liepvre XL, Fève B, Dugail I, Pairault J (December 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". The Biochemical Journal. 344 (Pt 3): 873–880. doi:10.1042/0264-6021:3440873. PMC 1220711. PMID 10585876.
• Liu J, Shi W, Warburton D (July 2000). "A cysteine residue in the helix-loop-helix domain of Id2 is critical for homodimerization and function". Biochemical and Biophysical Research Communications. 273 (3): 1042–1047. doi:10.1006/bbrc.2000.3055. PMID 10891368.
• Lasorella A, Noseda M, Beyna M, Yokota Y, Iavarone A (October 2000). "Id2 is a retinoblastoma protein target and mediates signalling by Myc oncoproteins". Nature. 407 (6804): 592–598. Bibcode:2000Natur.407..592L. doi:10.1038/35036504. PMID 11034201. S2CID 4335368.
• Roberts EC, Deed RW, Inoue T, Norton JD, Sharrocks AD (January 2001). "Id helix-loop-helix proteins antagonize pax transcription factor activity by inhibiting DNA binding". Molecular and Cellular Biology. 21 (2): 524–533. doi:10.1128/MCB.21.2.524-533.2001. PMC 86614. PMID 11134340.
• Wang S, Sdrulla A, Johnson JE, Yokota Y, Barres BA (March 2001). "A role for the helix-loop-helix protein Id2 in the control of oligodendrocyte development". Neuron. 29 (3): 603–614. doi:10.1016/S0896-6273(01)00237-9. PMID 11301021. S2CID 7978661.
• Wong J, Funes-Duran M, Ahlberg J, Round J, O'Connell R, Miller R, et al. (August 2001). "Characterization of a basic helix-loop-helix protein, ABF-1: nuclear localization, transcriptional properties, and interaction with Id-2". DNA and Cell Biology. 20 (8): 465–471. doi:10.1089/104454901316976091. PMID 11560778.
• Suzuki H, Fukunishi Y, Kagawa I, Saito R, Oda H, Endo T, et al. (October 2001). "Protein-protein interaction panel using mouse full-length cDNAs". Genome Research. 11 (10): 1758–1765. doi:10.1101/gr.180101. PMC 311163. PMID 11591653.

External links

• ID2+protein,+human at the U.S. 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.