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Database: UniProt
Entry: P27540
LinkDB: P27540
Original site: P27540 
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   07-OCT-2020, entry version 219.
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:0000244|PDB:1X0O, ECO:0000244|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:0000244|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:0000244|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=7; 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/";
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; 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   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   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   PDBsum; 4XT2; -.
DR   PDBsum; 5TBM; -.
DR   PDBsum; 5UFP; -.
DR   PDBsum; 5V0L; -.
DR   PDBsum; 6CZW; -.
DR   PDBsum; 6D09; -.
DR   PDBsum; 6D0B; -.
DR   PDBsum; 6D0C; -.
DR   BMRB; P27540; -.
DR   SMR; P27540; -.
DR   BioGRID; 106898; 195.
DR   CORUM; P27540; -.
DR   DIP; DIP-30886N; -.
DR   ELM; P27540; -.
DR   IntAct; P27540; 36.
DR   MINT; P27540; -.
DR   STRING; 9606.ENSP00000351407; -.
DR   ChEMBL; CHEMBL5618; -.
DR   MoonDB; P27540; Predicted.
DR   GlyGen; P27540; 1 site, 1 O-linked glycan (1 site).
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; 648 antibodies.
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   CTD; 405; -.
DR   DisGeNET; 405; -.
DR   EuPathDB; HostDB:ENSG00000143437.20; -.
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   eggNOG; KOG3561; Eukaryota.
DR   GeneTree; ENSGT00940000157585; -.
DR   HOGENOM; CLU_011864_1_1_1; -.
DR   InParanoid; P27540; -.
DR   KO; K09097; -.
DR   OMA; AWPPADD; -.
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; 27 hits in 898 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 endocervix and 233 other tissues.
DR   ExpressionAtlas; P27540; baseline and differential.
DR   Genevisible; P27540; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
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; IEA:Ensembl.
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:0008134; F:transcription factor binding; IPI:BHF-UCL.
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: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:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR   CDD; cd00083; HLH; 1.
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; Polymorphism; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|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          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   COMPBIAS        99..102
FT                   /note="Poly-Arg"
FT   COMPBIAS        503..507
FT                   /note="Poly-Gln"
FT   COMPBIAS        710..769
FT                   /note="Gln-rich"
FT   COMPBIAS        738..741
FT                   /note="Poly-Ser"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000244|PubMed:22814378"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163"
FT   CROSSLNK        58
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|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:0000244|PDB:2K7S"
FT   STRAND          362..367
FT                   /evidence="ECO:0000244|PDB:3F1P"
FT   STRAND          371..376
FT                   /evidence="ECO:0000244|PDB:3F1P"
FT   HELIX           380..384
FT                   /evidence="ECO:0000244|PDB:3F1P"
FT   HELIX           388..390
FT                   /evidence="ECO:0000244|PDB:3F1P"
FT   TURN            391..393
FT                   /evidence="ECO:0000244|PDB:3F1P"
FT   HELIX           396..399
FT                   /evidence="ECO:0000244|PDB:3F1P"
FT   TURN            402..404
FT                   /evidence="ECO:0000244|PDB:3F1P"
FT   HELIX           405..415
FT                   /evidence="ECO:0000244|PDB:3F1P"
FT   TURN            416..420
FT                   /evidence="ECO:0000244|PDB:3F1N"
FT   STRAND          423..430
FT                   /evidence="ECO:0000244|PDB:3F1P"
FT   STRAND          436..446
FT                   /evidence="ECO:0000244|PDB:3F1P"
FT   TURN            449..451
FT                   /evidence="ECO:0000244|PDB:2B02"
FT   STRAND          456..463
FT                   /evidence="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
//
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