ID2

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Inhibitor of DNA binding 2, dominant negative helix-loop-helix protein
Identifiers
Symbol(s) ID2; GIG8; ID2A; ID2H; MGC26389
External IDs OMIM: 600386 MGI: 96397 HomoloGene: 1632
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 3398 15902
Ensembl ENSG00000115738 ENSMUSG00000020644
Uniprot Q02363 Q545T4
Refseq NM_002166 (mRNA)
NP_002157 (protein)		 NM_010496 (mRNA)
NP_034626 (protein)
Location Chr 2: 8.74 - 8.74 Mb Chr 12: 25.68 - 25.69 Mb
Pubmed search [1] [2]

Inhibitor of DNA binding 2, dominant negative helix-loop-helix protein, also known as ID2, is a human 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.[1]

[edit] References

  1. ^ Entrez Gene: ID2 inhibitor of DNA binding 2, dominant negative helix-loop-helix protein.


[edit] 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. PMID 1741406. 
  • 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. 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. 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. PMID 8224921. 
  • Hara E, Yamaguchi T, Nojima H, et al. (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. 
  • 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. 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. 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. 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. 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. PMID 10022839. 
  • 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: 873–80. 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, 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. PMID 11134340. 
  • 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. 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. PMID 11591653. 

[edit] External links


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

v • d • e
Transcription factors and intracellular receptors
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • BATF • BLZF1 • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3, L1) • CREM • DBP • DDIT3 • GABPA • HLF • MAF (B, F, G, K) • NFE (2, L1, L2) • NRL • NRF1 • XBP1
(1.2) Basic helix-loop-helix (bHLH)
ATOH1 • AhR • AHRR • ARNT • ASCL1 • BHLHB2 • BMAL (ARNTL, ARNTL2) • CLOCK • EPAS1 • HAND (1, 2) • HES (5, 6) • HEY (1, 2, L) • HES1 • HIF (1A, 3A) • ID (1, 2, 3, 4) • LYL1 • MXD4 • MYCL1 • MYCN • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • Neurogenins • NeuroD (1, 2) • NPAS (1, 2, 3) • OLIG (1, 2) • Scleraxis • TAL1 • Twist • USF1
(1.3) bHLH-ZIP
MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger
DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP)
(2.2) Other Cys4
GATA (1, 2, 3, 4, 5, 6) • MTA (1, 2, 3)
(2.3) Cys2His2
ATBF1 • BCL(6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF: 1, 2, TFIIH: 1, 2, 4, 2I, 3A, 3C1, 3C2) • GFI1 • GLI-Krüppel family (1, 2, 3, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 4, 5, 6, 9, 10, 11, 12, 13) • MTF1 • MYT1 • OSR1 • Sp1 • zinc finger ((3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 318, 330, 346, 350, 365, 366, 384, 451, 452, 471, 593, 638, 649, 655) • Zbtb7 (7A) • ZBT (16, 17, 33)
(2.4) Cys6
(2.5) Alternating composition
AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B
(3) Helix-turn-helix
domains
ARX • CDX (1, 2) • CRX • CUTL1 • DLX (3, 4, 5) • EMX2 • EN (1, 2) • FHL (1, 2, 3) • HESX1 • HHEX • HLX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) • HOPX • MEIS (1, 2) • MEOX2 • MNX1 • MSX (1, 2) • NANOG • NKX (2-1, 2-5, 3-1) • PHF (3, 6, 10, 17) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) • OTX (1, 2) • PDX1
(3.2) Paired box
PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)
E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)
HSF (1, 2, 4)
(3.5) Tryptophan clusters
ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2) • ETV (1, 4, 5, 6) • FLI1 • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB • MYBL2
(3.6) TEA domain
transcriptional enhancer factor 1, 2
(4) β-Scaffold factors with
minor groove contacts
(4.1) Rel homology region
NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (C1, C2, C3, C4, 5)
(4.2) STAT
STAT (1, 2, 3, 4, 5, 6)
(4.3) p53
(4.4) MADS box
Mef2 (A, B, C, D) • SRF
HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1
(4.10) Cold-shock domain
(4.11) Runt
(0) Other
transcription factors
(0.2) HMGI(Y)
HMGA (1, 2) • HBP1
Rb • RBL1 • RBL2
(0.5) AP-2/EREBP-related factors
Apetala 2 • EREBP • B3
(0.6) Miscellaneous
ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • IFI (16, 35) • MLL (2, 3, T1) • MNDA • NFI (A, B, C, X) • NFY (A, B, C) • Rho/Sigma • R-SMAD