ID ARNT_HUMAN Reviewed; 789 AA. AC P27540; B2R9H1; C4AMA1; F8WAP6; Q59ED4; Q5QP39; Q8NDC7; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 11-NOV-2015, entry version 174. DE RecName: Full=Aryl hydrocarbon receptor nuclear translocator; DE Short=ARNT protein; DE AltName: Full=Class E basic helix-loop-helix protein 2; DE Short=bHLHe2; DE AltName: Full=Dioxin receptor, nuclear translocator; DE AltName: Full=Hypoxia-inducible factor 1-beta; DE Short=HIF-1-beta; DE Short=HIF1-beta; GN Name=ARNT; Synonyms=BHLHE2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RX PubMed=1852076; DOI=10.1126/science.1852076; RA Hoffman E.C., Reyes H., Chu F.-F., Sander F., Conley L.H., RA Brooks B.A., Hankinson O.; RT "Cloning of a factor required for activity of the Ah (dioxin) RT receptor."; RL Science 252:954-958(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Scheel J.; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis, Thalamus, and Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Aortic endothelium; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RT "Homo sapiens protein coding cDNA."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=11230166; DOI=10.1101/gr.GR1547R; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., RA Wambutt R., Korn B., Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and RT analysis of 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-517. RG NIEHS SNPs program; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP PROTEIN SEQUENCE OF 186-203 AND 662-694. RX PubMed=7539918; DOI=10.1073/pnas.92.12.5510; RA Wang G.L., Jiang B.-H., Rue E.A., Semenza G.L.; RT "Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS RT heterodimer regulated by cellular O2 tension."; RL Proc. Natl. Acad. Sci. U.S.A. 92:5510-5514(1995). RN [10] RP CHARACTERIZATION. RX PubMed=1317062; DOI=10.1126/science.256.5060.1193; RA Reyes H., Reisz-Porszasz S., Hankinson O.; RT "Identification of the Ah receptor nuclear translocator protein (Arnt) RT as a component of the DNA binding form of the Ah receptor."; RL Science 256:1193-1195(1992). RN [11] RP DNA-BINDING, AND MUTAGENESIS OF ARG-91; ASN-93; HIS-94; GLU-98; RP ARG-99; ARG-101 AND ARG-102. RX PubMed=8621524; DOI=10.1074/jbc.271.15.8843; RA Bacsi S.G., Hankinson O.; RT "Functional characterization of DNA-binding domains of the subunits of RT the heterodimeric aryl hydrocarbon receptor complex imputing novel and RT canonical basic helix-loop-helix protein-DNA interactions."; RL J. Biol. Chem. 271:8843-8850(1996). RN [12] RP INTERACTION WITH NOCA7. RX PubMed=10395741; DOI=10.1006/abbi.1999.1282; RA Nguyen T.A., Hoivik D., Lee J.-E., Safe S.; RT "Interactions of nuclear receptor coactivator/corepressor proteins RT with the aryl hydrocarbon receptor complex."; RL Arch. Biochem. Biophys. 367:250-257(1999). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP INTERACTION WITH HIF1A. RX PubMed=20699359; DOI=10.1242/jcs.068122; RA Kalousi A., Mylonis I., Politou A.S., Chachami G., Paraskeva E., RA Simos G.; RT "Casein kinase 1 regulates human hypoxia-inducible factor HIF-1."; RL J. Cell Sci. 123:2976-2986(2010). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Required for activity of the Ah (dioxin) receptor. This CC protein is required for the ligand-binding subunit to translocate CC from the cytosol to the nucleus after ligand binding. The complex CC then initiates transcription of genes involved in the activation CC of PAH procarcinogens. The heterodimer with HIF1A or EPAS1/HIF2A CC functions as a transcriptional regulator of the adaptive response CC to hypoxia. CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another CC bHLH protein. Forms a heterodimer with AHR, AHRR, HIF1A and CC EPAS1/HIF2A as well as with other bHLH proteins. Interacts with CC TACC3 (By similarity). Interacts with NOCA7. Heterodimer with CC HIF1A. {ECO:0000250, ECO:0000269|PubMed:10395741, CC ECO:0000269|PubMed:20699359}. CC -!- INTERACTION: CC P35869:AHR; NbExp=5; IntAct=EBI-80809, EBI-80780; CC Q16665:HIF1A; NbExp=9; IntAct=EBI-80809, EBI-447269; CC Q8NI08:NCOA7; NbExp=2; IntAct=EBI-80809, EBI-80799; CC Q9Y618:NCOR2; NbExp=2; IntAct=EBI-80809, EBI-80830; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Long; CC IsoId=P27540-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=P27540-2; Sequence=VSP_002092; CC Name=3; CC IsoId=P27540-3; Sequence=VSP_036532, VSP_036533; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=P27540-4; Sequence=VSP_055030; CC -!- SIMILARITY: Contains 1 bHLH (basic helix-loop-helix) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00981}. CC -!- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 PAS (PER-ARNT-SIM) domains. CC {ECO:0000255|PROSITE-ProRule:PRU00140}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD93114.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC Sequence=CAD38953.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/ARNTID223ch1q21.html"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/arnt/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M69238; AAA51777.1; -; mRNA. DR EMBL; Y18859; CAC21446.1; -; Genomic_DNA. DR EMBL; AJ251863; CAC21446.1; JOINED; Genomic_DNA. DR EMBL; AJ404851; CAC21446.1; JOINED; Genomic_DNA. DR EMBL; AJ404852; CAC21446.1; JOINED; Genomic_DNA. DR EMBL; AJ404853; CAC21446.1; JOINED; Genomic_DNA. DR EMBL; AJ404854; CAC21446.1; JOINED; Genomic_DNA. DR EMBL; AK290177; BAF82866.1; -; mRNA. DR EMBL; AK293027; BAF85716.1; -; mRNA. DR EMBL; AK313780; BAG36518.1; -; mRNA. DR EMBL; AB209877; BAD93114.1; ALT_INIT; mRNA. DR EMBL; AL834279; CAD38953.1; ALT_INIT; mRNA. DR EMBL; AY430083; AAQ96598.1; -; Genomic_DNA. DR EMBL; AL355860; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW53510.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53513.1; -; Genomic_DNA. DR CCDS; CCDS65641.1; -. [P27540-3] DR CCDS; CCDS65642.1; -. [P27540-4] DR CCDS; CCDS970.1; -. [P27540-1] DR CCDS; CCDS971.1; -. [P27540-2] DR PIR; I59550; I59550. DR RefSeq; NP_001184254.1; NM_001197325.1. DR RefSeq; NP_001272964.1; NM_001286035.1. [P27540-3] DR RefSeq; NP_001272965.1; NM_001286036.1. [P27540-4] DR RefSeq; NP_001659.1; NM_001668.3. [P27540-1] DR RefSeq; NP_848514.1; NM_178427.2. [P27540-2] DR UniGene; Hs.632446; -. DR PDB; 1D7G; Model; -; C=87-145. DR PDB; 1X0O; NMR; -; A=356-470. DR PDB; 2A24; NMR; -; B=358-465. DR PDB; 2ARN; Model; -; A=335-462. DR PDB; 2B02; X-ray; 1.50 A; A=354-470. DR PDB; 2HV1; NMR; -; A/B=356-470. DR PDB; 2K7S; NMR; -; A=356-470. DR PDB; 3F1N; X-ray; 1.48 A; B=356-470. DR PDB; 3F1O; X-ray; 1.60 A; B=356-470. DR PDB; 3F1P; X-ray; 1.17 A; B=356-470. DR PDB; 3H7W; X-ray; 1.65 A; B=356-470. DR PDB; 3H82; X-ray; 1.50 A; B=356-470. DR PDB; 4EQ1; X-ray; 1.60 A; A/B=357-464. DR PDB; 4GHI; X-ray; 1.50 A; B=356-470. DR PDB; 4GS9; X-ray; 1.72 A; B=356-470. DR PDB; 4H6J; X-ray; 1.52 A; B=357-470. DR PDB; 4LPZ; X-ray; 3.15 A; A/B=356-470. DR PDB; 4PKY; X-ray; 3.20 A; A/D=356-470. DR PDBsum; 1D7G; -. DR PDBsum; 1X0O; -. DR PDBsum; 2A24; -. DR PDBsum; 2ARN; -. DR PDBsum; 2B02; -. DR PDBsum; 2HV1; -. DR PDBsum; 2K7S; -. DR PDBsum; 3F1N; -. DR PDBsum; 3F1O; -. DR PDBsum; 3F1P; -. DR PDBsum; 3H7W; -. DR PDBsum; 3H82; -. DR PDBsum; 4EQ1; -. DR PDBsum; 4GHI; -. DR PDBsum; 4GS9; -. DR PDBsum; 4H6J; -. DR PDBsum; 4LPZ; -. DR PDBsum; 4PKY; -. DR ProteinModelPortal; P27540; -. DR SMR; P27540; 90-464. DR BioGrid; 106898; 47. DR DIP; DIP-30886N; -. DR IntAct; P27540; 18. DR MINT; MINT-1196758; -. DR STRING; 9606.ENSP00000351407; -. DR ChEMBL; CHEMBL5618; -. DR PhosphoSite; P27540; -. DR BioMuta; ARNT; -. DR DMDM; 114163; -. DR MaxQB; P27540; -. DR PaxDb; P27540; -. DR PRIDE; P27540; -. DR DNASU; 405; -. DR Ensembl; ENST00000354396; ENSP00000346372; ENSG00000143437. [P27540-4] DR Ensembl; ENST00000358595; ENSP00000351407; ENSG00000143437. [P27540-1] DR Ensembl; ENST00000505755; ENSP00000427571; ENSG00000143437. [P27540-2] DR Ensembl; ENST00000515192; ENSP00000423851; ENSG00000143437. [P27540-3] DR GeneID; 405; -. DR KEGG; hsa:405; -. DR UCSC; uc001evr.2; human. [P27540-1] DR UCSC; uc001evs.2; human. [P27540-2] DR UCSC; uc009wmb.2; human. [P27540-3] DR CTD; 405; -. DR GeneCards; ARNT; -. DR HGNC; HGNC:700; ARNT. DR HPA; CAB004318; -. DR HPA; HPA001759; -. DR MIM; 126110; gene. DR neXtProt; NX_P27540; -. DR PharmGKB; PA24994; -. DR eggNOG; ENOG410IQ5T; Eukaryota. DR eggNOG; ENOG410XVHF; LUCA. DR GeneTree; ENSGT00760000118788; -. DR HOGENOM; HOG000234380; -. DR HOVERGEN; HBG000164; -. DR InParanoid; P27540; -. DR KO; K09097; -. DR OMA; IVEFCHP; -. DR OrthoDB; EOG7V1FQ8; -. DR PhylomeDB; P27540; -. DR TreeFam; TF319983; -. DR Reactome; R-HSA-1234158; Regulation of gene expression by Hypoxia-inducible Factor. DR SignaLink; P27540; -. DR ChiTaRS; ARNT; human. DR EvolutionaryTrace; P27540; -. DR GeneWiki; Aryl_hydrocarbon_receptor_nuclear_translocator; -. DR GenomeRNAi; 405; -. DR NextBio; 1693; -. DR PRO; PR:P27540; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; P27540; -. DR CleanEx; HS_ARNT; -. DR ExpressionAtlas; P27540; baseline and differential. DR Genevisible; P27540; HS. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:BHF-UCL. DR GO; GO:0004874; F:aryl hydrocarbon receptor activity; IEA:Ensembl. DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:BHF-UCL. DR GO; GO:0035326; F:enhancer binding; IDA:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL. DR GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc. DR GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL. DR GO; GO:0030154; P:cell differentiation; IEA:Ensembl. DR GO; GO:0071456; P:cellular response to hypoxia; TAS:Reactome. DR GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl. DR GO; GO:0042789; P:mRNA transcription from RNA polymerase II promoter; IC:BHF-UCL. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IC:BHF-UCL. DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IC:BHF-UCL. DR GO; GO:0045821; P:positive regulation of glycolytic process; IC:BHF-UCL. DR GO; GO:0046886; P:positive regulation of hormone biosynthetic process; IDA:BHF-UCL. DR GO; GO:0033235; P:positive regulation of protein sumoylation; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL. DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IDA:BHF-UCL. DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IC:BHF-UCL. DR GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome. DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IDA:BHF-UCL. DR GO; GO:0001666; P:response to hypoxia; IDA:BHF-UCL. DR GO; GO:0006351; P:transcription, DNA-templated; TAS:ProtInc. DR Gene3D; 4.10.280.10; -; 1. DR InterPro; IPR011598; bHLH_dom. DR InterPro; IPR001067; Nuc_translocat. DR InterPro; IPR001610; PAC. DR InterPro; IPR000014; PAS. DR InterPro; IPR013767; PAS_fold. DR Pfam; PF00010; HLH; 1. DR Pfam; PF00989; PAS; 1. DR PRINTS; PR00785; NCTRNSLOCATR. DR SMART; SM00353; HLH; 1. DR SMART; SM00086; PAC; 1. DR SMART; SM00091; PAS; 2. DR SUPFAM; SSF47459; SSF47459; 1. DR SUPFAM; SSF55785; SSF55785; 4. DR TIGRFAMs; TIGR00229; sensory_box; 1. DR PROSITE; PS50888; BHLH; 1. DR PROSITE; PS50112; PAS; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; KW Complete proteome; Direct protein sequencing; DNA-binding; Nucleus; KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; KW Transcription; Transcription regulation. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}. FT CHAIN 2 789 Aryl hydrocarbon receptor nuclear FT translocator. FT /FTId=PRO_0000127118. FT DOMAIN 89 142 bHLH. {ECO:0000255|PROSITE- FT ProRule:PRU00981}. FT DOMAIN 161 235 PAS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00140}. FT DOMAIN 349 419 PAS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00140}. FT DOMAIN 424 467 PAC. FT COMPBIAS 99 102 Poly-Arg. FT COMPBIAS 503 507 Poly-Gln. FT COMPBIAS 710 769 Gln-rich. FT COMPBIAS 738 741 Poly-Ser. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000244|PubMed:22814378}. FT MOD_RES 77 77 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT VAR_SEQ 1 9 Missing (in isoform 3). FT {ECO:0000303|PubMed:11230166}. FT /FTId=VSP_036532. FT VAR_SEQ 77 91 Missing (in isoform 2). FT {ECO:0000303|PubMed:1852076}. FT /FTId=VSP_002092. FT VAR_SEQ 319 323 Missing (in isoform 3). FT {ECO:0000303|PubMed:11230166}. FT /FTId=VSP_036533. FT VAR_SEQ 601 602 Missing (in isoform 4). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_055030. FT VARIANT 430 430 R -> Q (in dbSNP:rs2229175). FT /FTId=VAR_024280. FT VARIANT 435 435 E -> K (in dbSNP:rs2229176). FT /FTId=VAR_049537. FT VARIANT 511 511 D -> N (in dbSNP:rs1805133). FT /FTId=VAR_014819. FT VARIANT 517 517 D -> E (in dbSNP:rs10305741). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_018906. FT VARIANT 706 706 P -> L (in dbSNP:rs2275237). FT /FTId=VAR_020189. FT MUTAGEN 91 91 R->A: Diminishes DNA interaction. FT {ECO:0000269|PubMed:8621524}. FT MUTAGEN 93 93 N->A: Diminishes DNA interaction. FT {ECO:0000269|PubMed:8621524}. FT MUTAGEN 94 94 H->A: Severely diminishes DNA FT interaction. FT {ECO:0000269|PubMed:8621524}. FT MUTAGEN 98 98 E->A: Severely diminishes DNA FT interaction. FT {ECO:0000269|PubMed:8621524}. FT MUTAGEN 99 99 R->A: Diminishes DNA interaction. FT {ECO:0000269|PubMed:8621524}. FT MUTAGEN 101 101 R->A: Severely diminishes DNA FT interaction. FT {ECO:0000269|PubMed:8621524}. FT MUTAGEN 102 102 R->A: Severely diminishes DNA FT interaction. FT {ECO:0000269|PubMed:8621524}. FT CONFLICT 627 627 R -> H (in Ref. 3; BAG36518). FT {ECO:0000305}. FT STRAND 356 358 {ECO:0000244|PDB:2K7S}. FT STRAND 362 367 {ECO:0000244|PDB:3F1P}. FT STRAND 371 376 {ECO:0000244|PDB:3F1P}. FT HELIX 380 384 {ECO:0000244|PDB:3F1P}. FT HELIX 388 390 {ECO:0000244|PDB:3F1P}. FT TURN 391 393 {ECO:0000244|PDB:3F1P}. FT HELIX 396 399 {ECO:0000244|PDB:3F1P}. FT TURN 402 404 {ECO:0000244|PDB:3F1P}. FT HELIX 405 415 {ECO:0000244|PDB:3F1P}. FT TURN 416 420 {ECO:0000244|PDB:3F1N}. FT STRAND 423 430 {ECO:0000244|PDB:3F1P}. FT STRAND 436 446 {ECO:0000244|PDB:3F1P}. FT TURN 449 451 {ECO:0000244|PDB:2B02}. FT STRAND 456 463 {ECO:0000244|PDB:3F1P}. SQ SEQUENCE 789 AA; 86636 MW; 2E278F8E62BFBF6D CRC64; MAATTANPEM TSDVPSLGPA IASGNSGPGI QGGGAIVQRA IKRRPGLDFD DDGEGNSKFL RCDDDQMSND KERFARSDDE QSSADKERLA RENHSEIERR RRNKMTAYIT ELSDMVPTCS ALARKPDKLT ILRMAVSHMK SLRGTGNTST DGSYKPSFLT DQELKHLILE AADGFLFIVS CETGRVVYVS DSVTPVLNQP QSEWFGSTLY DQVHPDDVDK LREQLSTSEN ALTGRILDLK TGTVKKEGQQ SSMRMCMGSR RSFICRMRCG SSSVDPVSVN RLSFVRNRCR NGLGSVKDGE PHFVVVHCTG YIKAWPPAGV SLPDDDPEAG QGSKFCLVAI GRLQVTSSPN CTDMSNVCQP TEFISRHNIE GIFTFVDHRC VATVGYQPQE LLGKNIVEFC HPEDQQLLRD SFQQVVKLKG QVLSVMFRFR SKNQEWLWMR TSSFTFQNPY SDEIEYIICT NTNVKNSSQE PRPTLSNTIQ RPQLGPTANL PLEMGSGQLA PRQQQQQTEL DMVPGRDGLA SYNHSQVVQP VTTTGPEHSK PLEKSDGLFA QDRDPRFSEI YHNINADQSK GISSSTVPAT QQLFSQGNTF PPTPRPAENF RNSGLAPPVT IVQPSASAGQ MLAQISRHSN PTQGATPTWT PTTRSGFSAQ QVATQATAKT RTSQFGVGSF QTPSSFSSMS LPGAPTASPG AAAYPSLTNR GSNFAPETGQ TAGQFQTRTA EGVGVWPQWQ GQQPHHRSSS SEQHVQQPPA QQPGQPEVFQ EMLSMLGDQS NSYNNEEFPD LTMFPPFSE //