ID3 (gene)

From Wikipedia, the free encyclopedia

Inhibitor of DNA binding 3, dominant negative helix-loop-helix protein

Identifiers

ID3; HEIR-1

External IDs

OMIM: 600277 MGI: 96398 HomoloGene: 1633

Gene ontology
Molecular Function:	• transcription corepressor activity • protein domain specific binding
Cellular Component:	• nucleus
Biological Process:	• negative regulation of transcription from RNA polymerase II promoter • multicellular organismal development • heart development • negative regulation of transcription • epithelial cell differentiation • negative regulation of transcription factor activity

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002167 (mRNA)
NP_002158 (protein)

NM_008321 (mRNA)
NP_032347 (protein)

Location

Chr 1: 23.76 - 23.76 Mb

Chr 4: 135.42 - 135.42 Mb

Pubmed search

[1]

[2]

Inhibitor of DNA binding 3, dominant negative helix-loop-helix protein, also known as ID3, is a human gene.^[1]

Members of the ID family of helix-loop-helix (HLH) proteins lack a basic DNA-binding domain and inhibit transcription through formation of nonfunctional dimers that are incapable of binding to DNA.[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: ID3 inhibitor of DNA binding 3, dominant negative helix-loop-helix protein.

[edit] Further reading

Ellmeier W, Aguzzi A, Kleiner E, et al. (1992). "Mutually exclusive expression of a helix-loop-helix gene and N-myc in human neuroblastomas and in normal development.". EMBO J. 11 (7): 2563-71. PMID 1628620.
White PS, Maris JM, Beltinger C, et al. (1995). "A region of consistent deletion in neuroblastoma maps within human chromosome 1p36.2-36.3.". Proc. Natl. Acad. Sci. U.S.A. 92 (12): 5520-4. PMID 7777541.
Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank.". Gene 150 (2): 243-50. PMID 7821789.
Deed RW, Hirose T, Mitchell EL, et al. (1995). "Structural organisation and chromosomal mapping of the human Id-3 gene.". Gene 151 (1-2): 309-14. PMID 7828896.
Deed RW, Bianchi SM, Atherton GT, et al. (1993). "An immediate early human gene encodes an Id-like helix-loop-helix protein and is regulated by protein kinase C activation in diverse cell types.". Oncogene 8 (3): 599-607. PMID 8437843.
Ishiguro A, Spirin K, Shiohara M, et al. (1996). "Expression of Id2 and Id3 mRNA in human lymphocytes.". Leuk. Res. 19 (12): 989-96. PMID 8632670.
Wibley J, Deed R, Jasiok M, et al. (1996). "A homology model of the Id-3 helix-loop-helix domain as a basis for structure-function predictions.". Biochim. Biophys. Acta 1294 (2): 138-46. PMID 8645731.
Loveys DA, Streiff MB, Kato GJ (1996). "E2A basic-helix-loop-helix transcription factors are negatively regulated by serum growth factors and by the Id3 protein.". Nucleic Acids Res. 24 (14): 2813-20. PMID 8759016.
Deed RW, Armitage S, Norton JD (1996). "Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism.". J. Biol. Chem. 271 (39): 23603-6. PMID 8798572.
Deed RW, Jasiok M, Norton JD (1996). "Attenuated function of a variant form of the helix-loop-helix protein, Id-3, generated by an alternative splicing mechanism.". FEBS Lett. 393 (1): 113-6. PMID 8804437.
Chen B, Lim RW (1997). "Physical and functional interactions between the transcriptional inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism regulating muscle-specific gene expression.". J. Biol. Chem. 272 (4): 2459-63. PMID 8999959.
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.
Deed RW, Hara E, Atherton GT, et al. (1997). "Regulation of Id3 cell cycle function by Cdk-2-dependent phosphorylation.". Mol. Cell. Biol. 17 (12): 6815-21. PMID 9372912.
Deed RW, Jasiok M, Norton JD (1998). "Lymphoid-specific expression of the Id3 gene in hematopoietic cells. Selective antagonism of E2A basic helix-loop-helix protein associated with Id3-induced differentiation of erythroleukemia cells.". J. Biol. Chem. 273 (14): 8278-86. PMID 9525934.
Asp J, Thornemo M, Inerot S, Lindahl A (1998). "The helix-loop-helix transcription factors Id1 and Id3 have a functional role in control of cell division in human normal and neoplastic chondrocytes.". FEBS Lett. 438 (1-2): 85-90. PMID 9821964.
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.
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.
Bounpheng MA, Dimas JJ, Dodds SG, Christy BA (2000). "Degradation of Id proteins by the ubiquitin-proteasome pathway.". FASEB J. 13 (15): 2257-64. PMID 10593873.
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.
Jögi A, Persson P, Grynfeld A, et al. (2002). "Modulation of basic helix-loop-helix transcription complex formation by Id proteins during neuronal differentiation.". J. Biol. Chem. 277 (11): 9118-26. doi:10.1074/jbc.M107713200. PMID 11756408.

[edit] External links

MeSH ID3+protein,+human

This article on a gene on chromosome 1 is a stub. You can help Wikipedia by expanding it.

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)	AP-2

(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	HIVEP1

(2.5) Alternating composition	AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B

(3) Helix-turn-helix
domains

(3.1) Homeo domain	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)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)

(3.4) Heat Shock Factors	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	p53

(4.4) MADS box	Mef2 (A, B, C, D) • SRF

(4.7) High mobility group	HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other
transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) • HBP1

(0.3) Pocket domain	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