Aryl hydrocarbon receptor nuclear translocator

Aryl hydrocarbon receptor nuclear translocator
Aryl hydrocarbon receptor nuclear translocator

PDB rendering based on 1x0o.
Symbols ARNT; HIF-1-beta; HIF-1beta; HIF1-beta; HIF1B; HIF1BETA; TANGO; bHLHe2
External IDs OMIM126110 MGI88071 HomoloGene1261 GeneCards: ARNT Gene
RNA expression pattern
PBB GE ARNT 218221 at tn.png
PBB GE ARNT 210828 s at tn.png
PBB GE ARNT 218222 x at tn.png
More reference expression data
Species Human Mouse
Entrez 405 11863
Ensembl ENSG00000143437 ENSMUSG00000015522
UniProt P27540 Q3U7X2
RefSeq (mRNA) NM_001197325.1 NM_001037737
RefSeq (protein) NP_001184254.1 NP_001032826
Location (UCSC) Chr 1:
150.78 – 150.85 Mb
Chr 3:
95.24 – 95.3 Mb
PubMed search [1] [2]

The ARNT gene encodes the aryl hydrocarbon receptor nuclear translocator protein that forms a complex with ligand-bound aryl hydrocarbon receptor (AhR), and is required for receptor function. The encoded protein has also been identified as the beta subunit of a heterodimeric transcription factor, hypoxia-inducible factor 1 (HIF1). A t(1;12)(q21;p13) translocation, which results in a TEL-ARNT fusion protein, is associated with acute myeloblastic leukemia. Three alternatively spliced variants encoding different isoforms have been described for this gene.

The aryl hydrocarbon receptor (AhR) is involved in the induction of several enzymes that participate in xenobiotic metabolism. The ligand-free, cytosolic form of the aryl hydrocarbon receptor is complexed to heat shock protein 90. Binding of ligand, which includes dioxin and polycyclic aromatic hydrocarbons, results in translocation of the ligand-binding subunit only to the nucleus. Induction of enzymes involved in xenobiotic metabolism occurs through binding of the ligand-bound AhR to xenobiotic responsive elements in the promoters of genes for these enzymes.



Aryl hydrocarbon receptor nuclear translocator has been shown to interact with HIF1A,[1][2] SRC-1,[3] AIP,[4][5] SIM1,[6][1] Aryl hydrocarbon receptor,[7][8][9][10] EPAS1,[2] SIM2[6][11][1][12] and Nuclear receptor coactivator 2.[3]


  1. ^ a b c Woods, Susan L; Whitelaw Murray L (Mar. 2002). "Differential activities of murine single minded 1 (SIM1) and SIM2 on a hypoxic response element. Cross-talk between basic helix-loop-helix/per-Arnt-Sim homology transcription factors". J. Biol. Chem. (United States) 277 (12): 10236–43. doi:10.1074/jbc.M110752200. ISSN 0021-9258. PMID 11782478. 
  2. ^ a b Hogenesch, J B; Chan W K, Jackiw V H, Brown R C, Gu Y Z, Pray-Grant M, Perdew G H, Bradfield C A (Mar. 1997). "Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway". J. Biol. Chem. (UNITED STATES) 272 (13): 8581–93. doi:10.1074/jbc.272.13.8581. ISSN 0021-9258. PMID 9079689. 
  3. ^ a b Beischlag, Timothy V; Wang Song, Rose David W, Torchia Joseph, Reisz-Porszasz Suzanne, Muhammad Khurshid, Nelson Walter E, Probst Markus R, Rosenfeld Michael G, Hankinson Oliver (Jun. 2002). "Recruitment of the NCoA/SRC-1/p160 family of transcriptional coactivators by the aryl hydrocarbon receptor/aryl hydrocarbon receptor nuclear translocator complex". Mol. Cell. Biol. (United States) 22 (12): 4319–33. doi:10.1128/MCB.22.12.4319-4333.2002. ISSN 0270-7306. PMC 133867. PMID 12024042. 
  4. ^ Carver, L A; Bradfield C A (Apr. 1997). "Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo". J. Biol. Chem. (UNITED STATES) 272 (17): 11452–6. doi:10.1074/jbc.272.17.11452. ISSN 0021-9258. PMID 9111057. 
  5. ^ Kazlauskas, A; Sundström S, Poellinger L, Pongratz I (Apr. 2001). "The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor". Mol. Cell. Biol. (United States) 21 (7): 2594–607. doi:10.1128/MCB.21.7.2594-2607.2001. ISSN 0270-7306. PMC 86890. PMID 11259606. 
  6. ^ a b Probst, M R; Fan C M, Tessier-Lavigne M, Hankinson O (Feb. 1997). "Two murine homologs of the Drosophila single-minded protein that interact with the mouse aryl hydrocarbon receptor nuclear translocator protein". J. Biol. Chem. (UNITED STATES) 272 (7): 4451–7. doi:10.1074/jbc.272.7.4451. ISSN 0021-9258. PMID 9020169. 
  7. ^ Lindebro, M C; Poellinger L, Whitelaw M L (Jul. 1995). "Protein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complex". EMBO J. (ENGLAND) 14 (14): 3528–39. ISSN 0261-4189. PMC 394421. PMID 7628454. 
  8. ^ Whitelaw, M; Pongratz I, Wilhelmsson A, Gustafsson J A, Poellinger L (Apr. 1993). "Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor". Mol. Cell. Biol. (UNITED STATES) 13 (4): 2504–14. ISSN 0270-7306. PMC 359572. PMID 8384309. 
  9. ^ Yamaguchi, Y; Kuo M T (Oct. 1995). "Functional analysis of aryl hydrocarbon receptor nuclear translocator interactions with aryl hydrocarbon receptor in the yeast two-hybrid system". Biochem. Pharmacol. (ENGLAND) 50 (8): 1295–302. doi:10.1016/0006-2952(95)02016-6. ISSN 0006-2952. PMID 7488247. 
  10. ^ Mimura, J; Ema M, Sogawa K, Fujii-Kuriyama Y (Jan. 1999). "Identification of a novel mechanism of regulation of Ah (dioxin) receptor function". Genes Dev. (UNITED STATES) 13 (1): 20–5. doi:10.1101/gad.13.1.20. ISSN 0890-9369. PMC 316371. PMID 9887096. 
  11. ^ Ooe, Norihisa; Saito Koichi, Mikami Nobuyoshi, Nakatuka Iwao, Kaneko Hideo (Jan. 2004). "Identification of a novel basic helix-loop-helix-PAS factor, NXF, reveals a Sim2 competitive, positive regulatory role in dendritic-cytoskeleton modulator drebrin gene expression". Mol. Cell. Biol. (United States) 24 (2): 608–16. doi:10.1128/MCB.24.2.608-616.2004. ISSN 0270-7306. PMC 343817. PMID 14701734. 
  12. ^ Moffett, P; Reece M, Pelletier J (Sep. 1997). "The murine Sim-2 gene product inhibits transcription by active repression and functional interference". Mol. Cell. Biol. (UNITED STATES) 17 (9): 4933–47. ISSN 0270-7306. PMC 232345. PMID 9271372. 

Further reading

External links

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

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