THC Science

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
Gene location (Human)
Chr.	Chromosome 2 (human)
End	8,684,461 bp
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)
End	25,147,139 bp
RNA expression pattern
	Top expressed in
	Top expressed in
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
	Sources:Amigo / QuickGO
Orthologs
	3398
	15902
	ENSG00000115738
	ENSMUSG00000020644
	Q02363
	P41136
	NM_002166
	NM_010496
	NP_002157
	NP_034626
	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[edit]

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[edit]

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

References[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000115738 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020644 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. doi:10.1016/S0021-9258(17)42146-6. PMID 8294468.
^ "Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein".
^ Lee, Sang Bae; Frattini, Veronique; Bansal, Mukesh; Castano, Angelica M.; Sherman, Dan; Hutchinson, Keino; Bruce, Jeffrey N.; Califano, Andrea; Liu, Guangchao; Cardozo, Timothy; Iavarone, Antonio; Lasorella, Anna (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.
^ 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.
^ 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[edit]

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. 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 (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. doi:10.1128/MCB.16.6.2570. 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. Bibcode:1999Natur.397..702Y. doi:10.1038/17812. PMID 10067894. S2CID 4428856.
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 (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. Bibcode:2000Natur.407..592L. doi:10.1038/35036504. PMID 11034201. S2CID 4335368.
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. S2CID 7978661.
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[edit]

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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000115738 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid8294468-5] 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. doi:10.1016/S0021-9258(17)42146-6. PMID 8294468.

[entrez-6] "Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein".

[nature-7] Lee, Sang Bae; Frattini, Veronique; Bansal, Mukesh; Castano, Angelica M.; Sherman, Dan; Hutchinson, Keino; Bruce, Jeffrey N.; Califano, Andrea; Liu, Guangchao; Cardozo, Timothy; Iavarone, Antonio; Lasorella, Anna (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.

[pmid9242638-8] 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.

[pmid10502414-9] 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.

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