Aryl hydrocarbon receptor nuclear translocator

ARNT
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesARNT, HIF-1-beta, HIF-1beta, HIF1-beta, HIF1B, HIF1BETA, TANGO, bHLHe2, aryl hydrocarbon receptor nuclear translocator, Aryl hydrocarbon receptor nuclear translocator
External IDsOMIM: 126110; MGI: 88071; HomoloGene: 1261; GeneCards: ARNT; OMA:ARNT - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001037737
NM_009709

RefSeq (protein)

NP_001032826
NP_033839

Location (UCSC)Chr 1: 150.81 – 150.88 MbChr 3: 95.34 – 95.4 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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 into[verification needed] 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.

Interactions

Aryl hydrocarbon receptor nuclear translocator has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000143437Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000015522Ensembl, 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. ^ Carver LA, Bradfield CA (April 1997). "Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo". The Journal of Biological Chemistry. 272 (17): 11452–11456. doi:10.1074/jbc.272.17.11452. PMID 9111057.
  6. ^ Kazlauskas A, Sundström S, Poellinger L, Pongratz I (April 2001). "The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor". Molecular and Cellular Biology. 21 (7): 2594–2607. doi:10.1128/MCB.21.7.2594-2607.2001. PMC 86890. PMID 11259606.
  7. ^ Lindebro MC, Poellinger L, Whitelaw ML (July 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". The EMBO Journal. 14 (14): 3528–3539. doi:10.1002/j.1460-2075.1995.tb07359.x. PMC 394421. PMID 7628454.
  8. ^ Whitelaw M, Pongratz I, Wilhelmsson A, Gustafsson JA, Poellinger L (April 1993). "Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor". Molecular and Cellular Biology. 13 (4): 2504–2514. doi:10.1128/MCB.13.4.2504. PMC 359572. PMID 8384309.
  9. ^ Yamaguchi Y, Kuo MT (October 1995). "Functional analysis of aryl hydrocarbon receptor nuclear translocator interactions with aryl hydrocarbon receptor in the yeast two-hybrid system". Biochemical Pharmacology. 50 (8): 1295–1302. doi:10.1016/0006-2952(95)02016-6. PMID 7488247.
  10. ^ Mimura J, Ema M, Sogawa K, Fujii-Kuriyama Y (January 1999). "Identification of a novel mechanism of regulation of Ah (dioxin) receptor function". Genes & Development. 13 (1): 20–25. doi:10.1101/gad.13.1.20. PMC 316371. PMID 9887096.
  11. ^ a b Hogenesch JB, Chan WK, Jackiw VH, Brown RC, Gu YZ, Pray-Grant M, et al. (March 1997). "Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway". The Journal of Biological Chemistry. 272 (13): 8581–8593. doi:10.1074/jbc.272.13.8581. PMID 9079689.
  12. ^ a b c Woods SL, Whitelaw ML (March 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". The Journal of Biological Chemistry. 277 (12): 10236–10243. doi:10.1074/jbc.M110752200. PMID 11782478.
  13. ^ Beischlag TV, Wang S, Rose DW, Torchia J, Reisz-Porszasz S, Muhammad K, et al. (June 2002). "Recruitment of the NCoA/SRC-1/p160 family of transcriptional coactivators by the aryl hydrocarbon receptor/aryl hydrocarbon receptor nuclear translocator complex". Molecular and Cellular Biology. 22 (12): 4319–4333. doi:10.1128/mcb.22.12.4319-4333.2002. PMC 133867. PMID 12024042.
  14. ^ a b Probst MR, Fan CM, Tessier-Lavigne M, Hankinson O (February 1997). "Two murine homologs of the Drosophila single-minded protein that interact with the mouse aryl hydrocarbon receptor nuclear translocator protein". The Journal of Biological Chemistry. 272 (7): 4451–4457. doi:10.1074/jbc.272.7.4451. PMID 9020169.
  15. ^ Ooe N, Saito K, Mikami N, Nakatuka I, Kaneko H (January 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". Molecular and Cellular Biology. 24 (2): 608–616. doi:10.1128/mcb.24.2.608-616.2004. PMC 343817. PMID 14701734.
  16. ^ Moffett P, Reece M, Pelletier J (September 1997). "The murine Sim-2 gene product inhibits transcription by active repression and functional interference". Molecular and Cellular Biology. 17 (9): 4933–4947. doi:10.1128/mcb.17.9.4933. PMC 232345. PMID 9271372.

Further reading

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

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