ARNT_HUMAN
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 03-AUG-2022, entry version 227.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Brooks B.A.,
RA Hankinson O.;
RT "Cloning of a factor required for activity of the Ah (dioxin) 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 heterodimer
RT 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) as a
RT 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; ARG-99;
RP 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 the
RT 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 with the
RT aryl hydrocarbon receptor complex.";
RL Arch. Biochem. Biophys. 367:250-257(1999).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP 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., 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 SPECTROMETRY
RP [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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP INTERACTION WITH AHRR.
RX PubMed=28904176; DOI=10.1074/jbc.m117.812974;
RA Sakurai S., Shimizu T., Ohto U.;
RT "The crystal structure of the AhRR-ARNT heterodimer reveals the structural
RT basis of the repression of AhR-mediated transcription.";
RL J. Biol. Chem. 292:17609-17616(2017).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-58, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20] {ECO:0007744|PDB:1X0O, ECO:0007744|PDB:2A24}
RP STRUCTURE BY NMR OF 356-470 IN COMPLEX WITH EPAS1, SUBUNIT, AND INTERACTION
RP WITH EPAS1.
RX PubMed=16181639; DOI=10.1016/j.jmb.2005.08.043;
RA Card P.B., Erbel P.J., Gardner K.H.;
RT "Structural basis of ARNT PAS-B dimerization: use of a common beta-sheet
RT interface for hetero- and homodimerization.";
RL J. Mol. Biol. 353:664-677(2005).
RN [21] {ECO:0007744|PDB:2K7S}
RP STRUCTURE BY NMR OF 356-470.
RX PubMed=19196990; DOI=10.1073/pnas.0808270106;
RA Evans M.R., Card P.B., Gardner K.H.;
RT "ARNT PAS-B has a fragile native state structure with an alternative beta-
RT sheet register nearby in sequence space.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:2617-2622(2009).
RN [22] {ECO:0007744|PDB:5V0L}
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 70-346 IN COMPLEXES WITH AHR AND
RP DNA, FUNCTION, INTERACTION WITH AHR, AND REGION.
RX PubMed=28396409; DOI=10.1073/pnas.1617035114;
RA Seok S.H., Lee W., Jiang L., Molugu K., Zheng A., Li Y., Park S.,
RA Bradfield C.A., Xing Y.;
RT "Structural hierarchy controlling dimerization and target DNA recognition
RT in the AHR transcriptional complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:5431-5436(2017).
CC -!- FUNCTION: Required for activity of the Ah (dioxin) receptor. This
CC protein is required for the ligand-binding subunit to translocate from
CC the cytosol to the nucleus after ligand binding. The complex then
CC initiates transcription of genes involved in the activation of PAH
CC procarcinogens. The heterodimer binds to core DNA sequence 5'-TACGTG-3'
CC within the hypoxia response element (HRE) of target gene promoters and
CC functions as a transcriptional regulator of the adaptive response to
CC hypoxia (By similarity). The heterodimer ARNT:AHR binds to core DNA
CC sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of
CC target gene promoters and activates their transcription
CC (PubMed:28396409). {ECO:0000250|UniProtKB:P53762,
CC ECO:0000269|PubMed:28396409}.
CC -!- SUBUNIT: Monomer. Homodimer only upon binding to a DNA (By similarity).
CC Efficient DNA binding requires dimerization with another bHLH protein.
CC Interacts with TACC3 (By similarity). Interacts with HIF1A, EPAS1,
CC NPAS1 and NPAS3; forms a heterodimer that binds core DNA sequence 5'-
CC TACGTG-3' within the hypoxia response element (HRE) of target gene
CC promoters (PubMed:20699359, PubMed:16181639) (By similarity). Forms a
CC heterodimer with AHRR, as well as with other bHLH proteins (Probable).
CC Interacts with NOCA7 (PubMed:10395741). Interacts with TACC3 (By
CC similarity). Interacts with AHR; the heterodimer ARNT:AHR binds to core
CC DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of
CC target gene promoters and activates their transcription
CC (PubMed:28396409). Interacts with SIM1 and NPAS4 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P53762,
CC ECO:0000269|PubMed:10395741, ECO:0000269|PubMed:16181639,
CC ECO:0000269|PubMed:20699359, ECO:0000269|PubMed:28396409,
CC ECO:0000305|PubMed:28904176}.
CC -!- INTERACTION:
CC P27540; P35869: AHR; NbExp=6; IntAct=EBI-80809, EBI-80780;
CC P27540; Q99814: EPAS1; NbExp=8; IntAct=EBI-80809, EBI-447470;
CC P27540; Q16665: HIF1A; NbExp=12; IntAct=EBI-80809, EBI-447269;
CC P27540; Q8NI08: NCOA7; NbExp=2; IntAct=EBI-80809, EBI-80799;
CC P27540; 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 Name=4;
CC IsoId=P27540-4; Sequence=VSP_055030;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93114.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD38953.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ARNTID223ch1q21.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/arnt/";
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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 RefSeq; XP_016856778.1; XM_017001289.1. [P27540-3]
DR PDB; 1X0O; NMR; -; A=356-470.
DR PDB; 2A24; NMR; -; B=358-465.
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 PDB; 4XT2; X-ray; 1.70 A; B/D=356-470.
DR PDB; 5TBM; X-ray; 1.85 A; B=356-467.
DR PDB; 5UFP; X-ray; 1.90 A; B=356-467.
DR PDB; 5V0L; X-ray; 4.00 A; A=70-346.
DR PDB; 6CZW; X-ray; 1.60 A; B=356-470.
DR PDB; 6D09; X-ray; 1.85 A; B=356-470.
DR PDB; 6D0B; X-ray; 1.60 A; B=356-470.
DR PDB; 6D0C; X-ray; 1.50 A; B=356-470.
DR PDB; 6X21; X-ray; 1.54 A; B=356-467.
DR PDB; 6X28; X-ray; 1.92 A; B=356-467.
DR PDB; 6X2H; X-ray; 2.00 A; B=356-467.
DR PDB; 6X37; X-ray; 1.94 A; B=356-467.
DR PDB; 6X3D; X-ray; 2.00 A; B=356-467.
DR PDBsum; 1X0O; -.
DR PDBsum; 2A24; -.
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 PDBsum; 4XT2; -.
DR PDBsum; 5TBM; -.
DR PDBsum; 5UFP; -.
DR PDBsum; 5V0L; -.
DR PDBsum; 6CZW; -.
DR PDBsum; 6D09; -.
DR PDBsum; 6D0B; -.
DR PDBsum; 6D0C; -.
DR PDBsum; 6X21; -.
DR PDBsum; 6X28; -.
DR PDBsum; 6X2H; -.
DR PDBsum; 6X37; -.
DR PDBsum; 6X3D; -.
DR AlphaFoldDB; P27540; -.
DR BMRB; P27540; -.
DR SMR; P27540; -.
DR BioGRID; 106898; 228.
DR CORUM; P27540; -.
DR DIP; DIP-30886N; -.
DR ELM; P27540; -.
DR IntAct; P27540; 43.
DR MINT; P27540; -.
DR STRING; 9606.ENSP00000351407; -.
DR ChEMBL; CHEMBL5618; -.
DR MoonDB; P27540; Predicted.
DR GlyGen; P27540; 4 sites, 2 O-linked glycans (4 sites).
DR iPTMnet; P27540; -.
DR PhosphoSitePlus; P27540; -.
DR BioMuta; ARNT; -.
DR DMDM; 114163; -.
DR EPD; P27540; -.
DR jPOST; P27540; -.
DR MassIVE; P27540; -.
DR MaxQB; P27540; -.
DR PaxDb; P27540; -.
DR PeptideAtlas; P27540; -.
DR PRIDE; P27540; -.
DR ProteomicsDB; 30540; -.
DR ProteomicsDB; 54398; -. [P27540-1]
DR ProteomicsDB; 54399; -. [P27540-2]
DR ProteomicsDB; 54400; -. [P27540-3]
DR Antibodypedia; 916; 703 antibodies from 43 providers.
DR DNASU; 405; -.
DR Ensembl; ENST00000354396.6; ENSP00000346372.2; ENSG00000143437.21. [P27540-4]
DR Ensembl; ENST00000358595.10; ENSP00000351407.5; ENSG00000143437.21. [P27540-1]
DR Ensembl; ENST00000505755.5; ENSP00000427571.1; ENSG00000143437.21. [P27540-2]
DR Ensembl; ENST00000515192.5; ENSP00000423851.1; ENSG00000143437.21. [P27540-3]
DR GeneID; 405; -.
DR KEGG; hsa:405; -.
DR MANE-Select; ENST00000358595.10; ENSP00000351407.5; NM_001668.4; NP_001659.1.
DR UCSC; uc001evr.2; human. [P27540-1]
DR CTD; 405; -.
DR DisGeNET; 405; -.
DR GeneCards; ARNT; -.
DR HGNC; HGNC:700; ARNT.
DR HPA; ENSG00000143437; Low tissue specificity.
DR MIM; 126110; gene.
DR neXtProt; NX_P27540; -.
DR OpenTargets; ENSG00000143437; -.
DR PharmGKB; PA24994; -.
DR VEuPathDB; HostDB:ENSG00000143437; -.
DR eggNOG; KOG3561; Eukaryota.
DR GeneTree; ENSGT00940000157585; -.
DR HOGENOM; CLU_011864_1_1_1; -.
DR InParanoid; P27540; -.
DR OMA; VRRRFWG; -.
DR OrthoDB; 331262at2759; -.
DR PhylomeDB; P27540; -.
DR TreeFam; TF319983; -.
DR PathwayCommons; P27540; -.
DR Reactome; R-HSA-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR Reactome; R-HSA-211976; Endogenous sterols.
DR Reactome; R-HSA-211981; Xenobiotics.
DR Reactome; R-HSA-8937144; Aryl hydrocarbon receptor signalling.
DR SignaLink; P27540; -.
DR SIGNOR; P27540; -.
DR BioGRID-ORCS; 405; 58 hits in 1107 CRISPR screens.
DR ChiTaRS; ARNT; human.
DR EvolutionaryTrace; P27540; -.
DR GeneWiki; Aryl_hydrocarbon_receptor_nuclear_translocator; -.
DR GenomeRNAi; 405; -.
DR Pharos; P27540; Tbio.
DR PRO; PR:P27540; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P27540; protein.
DR Bgee; ENSG00000143437; Expressed in colonic epithelium and 200 other tissues.
DR ExpressionAtlas; P27540; baseline and differential.
DR Genevisible; P27540; HS.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IBA:GO_Central.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:BHF-UCL.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:Ensembl.
DR GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
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 by RNA polymerase II; 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 CDD; cd00130; PAS; 2.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR001067; Nuc_translocat.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
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; 2.
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 Direct protein sequencing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..789
FT /note="Aryl hydrocarbon receptor nuclear translocator"
FT /id="PRO_0000127118"
FT DOMAIN 89..142
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 161..235
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 349..419
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 424..467
FT /note="PAC"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..128
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:28396409"
FT REGION 112..264
FT /note="Required for heterodimer formation with EPAS1"
FT /evidence="ECO:0000250|UniProtKB:P53762"
FT REGION 112..168
FT /note="Required for heterodimer formation with HIF1A"
FT /evidence="ECO:0000250|UniProtKB:P53762"
FT REGION 167..171
FT /note="Mediates the transcription activity and dimerization
FT of the AHR:ARNT complex"
FT /evidence="ECO:0000250|UniProtKB:P53762"
FT REGION 465..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_036532"
FT VAR_SEQ 77..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1852076"
FT /id="VSP_002092"
FT VAR_SEQ 319..323
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_036533"
FT VAR_SEQ 601..602
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_055030"
FT VARIANT 430
FT /note="R -> Q (in dbSNP:rs2229175)"
FT /id="VAR_024280"
FT VARIANT 511
FT /note="D -> N (in dbSNP:rs1805133)"
FT /id="VAR_014819"
FT VARIANT 517
FT /note="D -> E (in dbSNP:rs10305741)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_018906"
FT VARIANT 706
FT /note="P -> L (in dbSNP:rs2275237)"
FT /id="VAR_020189"
FT MUTAGEN 91
FT /note="R->A: Diminishes DNA interaction."
FT /evidence="ECO:0000269|PubMed:8621524"
FT MUTAGEN 93
FT /note="N->A: Diminishes DNA interaction."
FT /evidence="ECO:0000269|PubMed:8621524"
FT MUTAGEN 94
FT /note="H->A: Severely diminishes DNA interaction."
FT /evidence="ECO:0000269|PubMed:8621524"
FT MUTAGEN 98
FT /note="E->A: Severely diminishes DNA interaction."
FT /evidence="ECO:0000269|PubMed:8621524"
FT MUTAGEN 99
FT /note="R->A: Diminishes DNA interaction."
FT /evidence="ECO:0000269|PubMed:8621524"
FT MUTAGEN 101
FT /note="R->A: Severely diminishes DNA interaction."
FT /evidence="ECO:0000269|PubMed:8621524"
FT MUTAGEN 102
FT /note="R->A: Severely diminishes DNA interaction."
FT /evidence="ECO:0000269|PubMed:8621524"
FT CONFLICT 627
FT /note="R -> H (in Ref. 3; BAG36518)"
FT /evidence="ECO:0000305"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:2K7S"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:3F1P"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:3F1P"
FT HELIX 380..384
FT /evidence="ECO:0007829|PDB:3F1P"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:3F1P"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:3F1P"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:3F1P"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:3F1P"
FT HELIX 405..415
FT /evidence="ECO:0007829|PDB:3F1P"
FT TURN 416..420
FT /evidence="ECO:0007829|PDB:3F1N"
FT STRAND 423..430
FT /evidence="ECO:0007829|PDB:3F1P"
FT STRAND 436..446
FT /evidence="ECO:0007829|PDB:3F1P"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:2B02"
FT STRAND 456..463
FT /evidence="ECO:0007829|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
