Misplaced Pages

Aryl hydrocarbon receptor nuclear translocator

Article snapshot taken from Wikipedia with creative commons attribution-sharealike license. Give it a read and then ask your questions in the chat. We can research this topic together.
Protein-coding gene in the species Homo sapiens

ARNT
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4PKY, 1X0O, 2A24, 2B02, 2HV1, 2K7S, 3F1N, 3F1O, 3F1P, 3H7W, 3H82, 4EQ1, 4GHI, 4GS9, 4H6J, 4LPZ, 4XT2

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
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)
Chromosome 1 (human)Genomic location for ARNTGenomic location for ARNT
Band1q21.3Start150,809,713 bp
End150,876,708 bp
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)
Chromosome 3 (mouse)Genomic location for ARNTGenomic location for ARNT
Band3 F2.1|3 40.74 cMStart95,341,699 bp
End95,404,551 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • epithelium of colon

  • Achilles tendon

  • sural nerve

  • canal of the cervix

  • left ovary

  • right ovary

  • gastric mucosa

  • stromal cell of endometrium

  • ectocervix

  • body of uterus
Top expressed in
  • ascending aorta

  • aortic valve

  • parotid gland

  • muscle of thigh

  • tongue

  • cumulus cell

  • molar

  • atrium

  • pineal gland

  • external carotid artery
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

405

11863

Ensembl

ENSG00000143437

ENSMUSG00000015522

UniProt

P27540

P53762

RefSeq (mRNA)
NM_001197325
NM_001286035
NM_001286036
NM_001668
NM_178426

NM_178427
NM_001350224
NM_001350225
NM_001350226

NM_001037737
NM_009709

RefSeq (protein)
NP_001184254
NP_001272964
NP_001272965
NP_001659
NP_848514

NP_001337153
NP_001337154
NP_001337155

NP_001032826
NP_033839

Location (UCSC)Chr 1: 150.81 – 150.88 MbChr 3: 95.34 – 95.4 Mb
PubMed search
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 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. ^ GRCh38: Ensembl release 89: ENSG00000143437Ensembl, May 2017
  2. ^ 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. ^ 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. ^ 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. ^ 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

External links

PDB gallery
  • 1x0o: human ARNT C-terminal PAS domain 1x0o: human ARNT C-terminal PAS domain
  • 2a24: HADDOCK Structure of HIF-2a/ARNT PAS-B Heterodimer 2a24: HADDOCK Structure of HIF-2a/ARNT PAS-B Heterodimer
  • 2b02: Crystal Structure of ARNT PAS-B Domain 2b02: Crystal Structure of ARNT PAS-B Domain
Transcription factors and intracellular receptors
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies

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

Categories: