AHR_HUMAN
ID AHR_HUMAN Reviewed; 848 AA.
AC P35869; A4D130; Q13728; Q13803; Q13804;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Aryl hydrocarbon receptor {ECO:0000303|PubMed:8393992};
DE Short=Ah receptor {ECO:0000303|PubMed:8393992};
DE Short=AhR {ECO:0000303|PubMed:8393992};
DE AltName: Full=Class E basic helix-loop-helix protein 76;
DE Short=bHLHe76;
DE Flags: Precursor;
GN Name=AHR {ECO:0000303|PubMed:8393992, ECO:0000312|HGNC:HGNC:348};
GN Synonyms=BHLHE76 {ECO:0000312|HGNC:HGNC:348};
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].
RC TISSUE=Liver;
RX PubMed=8393992; DOI=10.1093/nar/21.15.3578;
RA Itoh S., Kamataki T.;
RT "Human Ah receptor cDNA: analysis for highly conserved sequences.";
RL Nucleic Acids Res. 21:3578-3578(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=8246913;
RA Dolwick K.M., Schmidt J.V., Carver L.A., Swanson H.I., Bradfield C.A.;
RT "Cloning and expression of a human Ah receptor cDNA.";
RL Mol. Pharmacol. 44:911-917(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7883760; DOI=10.1093/oxfordjournals.jbchem.a124605;
RA Ema M., Matsushita N., Sogawa K., Ariyama T., Inazawa J., Nemoto T.,
RA Ota M., Oshimura M., Fujii-Kuriyama Y.;
RT "Human arylhydrocarbon receptor: functional expression and chromosomal
RT assignment to 7p21.";
RL J. Biochem. 116:845-851(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-235; 388-461 AND 764-848.
RX PubMed=16696038; DOI=10.1136/mp.49.1.m12;
RA Bennett P., Ramsden D.B., Williams A.C.;
RT "Complete structural characterisation of the human aryl hydrocarbon
RT receptor gene.";
RL Clin. Mol. Pathol. 49:M12-M16(1996).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-341, AND TISSUE SPECIFICITY.
RX PubMed=7515333; DOI=10.1093/carcin/15.5.801;
RA Hayashi S., Watanabe J., Nakachi K., Eguchi H., Gotoh O., Kawajiri K.;
RT "Interindividual difference in expression of human Ah receptor and related
RT P450 genes.";
RL Carcinogenesis 15:801-806(1994).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF VAL-381.
RX PubMed=7961644; DOI=10.1016/s0021-9258(18)46990-6;
RA Ema M., Ohe N., Suzuki M., Mimura J., Sogawa K., Ikawa S.,
RA Fujii-Kuriyama Y.;
RT "Dioxin binding activities of polymorphic forms of mouse and human
RT arylhydrocarbon receptors.";
RL J. Biol. Chem. 269:27337-27343(1994).
RN [11]
RP FUNCTION, AND SUBUNIT.
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 [12]
RP INDUCTION.
RX PubMed=11259615; DOI=10.1124/mol.59.4.716;
RA Wolff S., Harper P.A., Wong J.M.Y., Mostert V., Wang Y., Abel J.;
RT "Cell-specific regulation of human aryl hydrocarbon receptor expression by
RT transforming growth factor-beta(1).";
RL Mol. Pharmacol. 59:716-724(2001).
RN [13]
RP REVIEW ON ROLE IN CELL CYCLE.
RX PubMed=12213388; DOI=10.1016/s0009-2797(02)00069-8;
RA Puga A., Xia Y., Elferink C.;
RT "Role of the aryl hydrocarbon receptor in cell cycle regulation.";
RL Chem. Biol. Interact. 141:117-130(2002).
RN [14]
RP INTERACTION WITH NEDD8.
RX PubMed=12215427; DOI=10.1074/jbc.m202413200;
RA Antenos M., Casper R.F., Brown T.J.;
RT "Interaction with Nedd8, a ubiquitin-like protein, enhances the
RT transcriptional activity of the aryl hydrocarbon receptor.";
RL J. Biol. Chem. 277:44028-44034(2002).
RN [15]
RP INTERACTION WITH IVNS1ABP.
RX PubMed=16582008; DOI=10.1124/mol.106.024380;
RA Dunham E.E., Stevens E.A., Glover E., Bradfield C.A.;
RT "The aryl hydrocarbon receptor signaling pathway is modified through
RT interactions with a Kelch protein.";
RL Mol. Pharmacol. 70:8-15(2006).
RN [16]
RP REVIEW ON VARIANTS.
RX PubMed=12213390; DOI=10.1016/s0009-2797(02)00071-6;
RA Harper P.A., Wong J.M.Y., Lam M.S.M., Okey A.B.;
RT "Polymorphisms in the human AH receptor.";
RL Chem. Biol. Interact. 141:161-187(2002).
RN [17]
RP REVIEW ON LIGANDS.
RX PubMed=18076143; DOI=10.1021/tx7001965;
RA Nguyen L.P., Bradfield C.A.;
RT "The search for endogenous activators of the aryl hydrocarbon receptor.";
RL Chem. Res. Toxicol. 21:102-116(2008).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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., 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 [19]
RP FUNCTION, AND INTERACTION WITH TIPARP.
RX PubMed=23275542; DOI=10.1093/nar/gks1337;
RA MacPherson L., Tamblyn L., Rajendra S., Bralha F., McPherson J.P.,
RA Matthews J.;
RT "2,3,7,8-Tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase (TiPARP,
RT ARTD14) is a mono-ADP-ribosyltransferase and repressor of aryl hydrocarbon
RT receptor transactivation.";
RL Nucleic Acids Res. 41:1604-1621(2013).
RN [20]
RP FUNCTION, AND ADP-RIBOSYLATION.
RX PubMed=30373764; DOI=10.1042/bcj20180347;
RA Gomez A., Bindesboell C., Somisetty V.S., Grimaldi G., Hutin D.,
RA MacPherson L., Ahmed S., Tamblyn L., Cho T., Nebb H.I., Moen A.,
RA Anonsen J.H., Grant D.M., Matthews J.;
RT "Characterization of TCDD-Inducible Poly-ADP-Ribose Polymerase
RT (TIPARP/ARTD14) Catalytic Activity.";
RL Biochem. J. 475:3827-3846(2018).
RN [21]
RP TISSUE SPECIFICITY, AND INVOLVEMENT IN RP85.
RX PubMed=29726989; DOI=10.1093/hmg/ddy165;
RA Zhou Y., Li S., Huang L., Yang Y., Zhang L., Yang M., Liu W., Ramasamy K.,
RA Jiang Z., Sundaresan P., Zhu X., Yang Z.;
RT "A splicing mutation in aryl hydrocarbon receptor associated with retinitis
RT pigmentosa.";
RL Hum. Mol. Genet. 27:2563-2572(2018).
RN [22]
RP FUNCTION.
RX PubMed=32818467; DOI=10.1016/j.cell.2020.07.038;
RA Sadik A., Somarribas Patterson L.F., Oeztuerk S., Mohapatra S.R.,
RA Panitz V., Secker P.F., Pfaender P., Loth S., Salem H., Prentzell M.T.,
RA Berdel B., Iskar M., Faessler E., Reuter F., Kirst I., Kalter V.,
RA Foerster K.I., Jaeger E., Guevara C.R., Sobeh M., Hielscher T., Poschet G.,
RA Reinhardt A., Hassel J.C., Zapatka M., Hahn U., von Deimling A., Hopf C.,
RA Schlichting R., Escher B.I., Burhenne J., Haefeli W.E., Ishaque N.,
RA Boehme A., Schaeuble S., Thedieck K., Trump S., Seiffert M., Opitz C.A.;
RT "IL4I1 is a metabolic immune checkpoint that activates the AHR and promotes
RT tumor progression.";
RL Cell 182:1252-1270(2020).
RN [23]
RP FUNCTION.
RX PubMed=32866000; DOI=10.1021/acs.jafc.0c03735;
RA Zhang X., Gan M., Li J., Li H., Su M., Tan D., Wang S., Jia M., Zhang L.,
RA Chen G.;
RT "An endogenous indole pyruvate pathway for tryptophan metabolism mediated
RT by IL4I1.";
RL J. Agric. Food Chem. 68:10678-10684(2020).
RN [24] {ECO:0007744|PDB:5NJ8}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 23-273 IN COMPLEXES WITH ARNT AND
RP DNA, REGION, MUTAGENESIS OF ARG-40; LEU-50; VAL-74; ALA-79; PHE-82;
RP LEU-118; LEU-122; PHE-136 AND ILE-154, FUNCTION, AND INTERACTION WITH ARNT.
RX PubMed=28602820; DOI=10.1016/j.str.2017.05.008;
RA Schulte K.W., Green E., Wilz A., Platten M., Daumke O.;
RT "Structural Basis for Aryl Hydrocarbon Receptor-Mediated Gene Activation.";
RL Structure 25:1025-1033(2017).
RN [25]
RP VARIANT LYS-554.
RX PubMed=7550366; DOI=10.1097/00008571-199506000-00003;
RA Kawajiri K., Watanabe J., Eguchi H., Nakachi K., Kiyohara C., Hayashi S.;
RT "Polymorphisms of human Ah receptor gene are not involved in lung cancer.";
RL Pharmacogenetics 5:151-158(1995).
RN [26]
RP VARIANTS LYS-554 AND ILE-570.
RX PubMed=10739168; DOI=10.1097/00008571-200002000-00003;
RA Smart J., Daly A.K.;
RT "Variation in induced CYP1A1 levels: relationship to CYP1A1, Ah receptor
RT and GSTM1 polymorphisms.";
RL Pharmacogenetics 10:11-24(2000).
RN [27]
RP VARIANTS LYS-554 AND VAL-786.
RX PubMed=11698344; DOI=10.1093/carcin/22.11.1819;
RA Cauchi S., Stucker I., Solas C., Laurent-Puig P., Cenee S., Hemon D.,
RA Jacquet M., Kremers P., Beaune P., Massaad-Massade L.;
RT "Polymorphisms of human aryl hydrocarbon receptor (AhR) gene in a French
RT population: relationship with CYP1A1 inducibility and lung cancer.";
RL Carcinogenesis 22:1819-1824(2001).
RN [28]
RP VARIANTS SER-517 AND ILE-570.
RX PubMed=11689007; DOI=10.1006/bbrc.2001.5861;
RA Wong J.M.Y., Okey A.B., Harper P.A.;
RT "Human aryl hydrocarbon receptor polymorphisms that result in loss of
RT CYP1A1 induction.";
RL Biochem. Biophys. Res. Commun. 288:990-996(2001).
CC -!- FUNCTION: Ligand-activated transcription factor that enables cells to
CC adapt to changing conditions by sensing compounds from the environment,
CC diet, microbiome and cellular metabolism, and which plays important
CC roles in development, immunity and cancer (PubMed:30373764,
CC PubMed:23275542, PubMed:7961644, PubMed:32818467). Upon ligand binding,
CC translocates into the nucleus, where it heterodimerizes with ARNT and
CC induces transcription by binding to xenobiotic response elements (XRE)
CC (PubMed:30373764, PubMed:23275542, PubMed:7961644). Regulates a variety
CC of biological processes, including angiogenesis, hematopoiesis, drug
CC and lipid metabolism, cell motility and immune modulation
CC (PubMed:12213388). Xenobiotics can act as ligands: upon xenobiotic-
CC binding, activates the expression of multiple phase I and II xenobiotic
CC chemical metabolizing enzyme genes (such as the CYP1A1 gene)
CC (PubMed:7961644). Mediates biochemical and toxic effects of halogenated
CC aromatic hydrocarbons (PubMed:7961644). Next to xenobiotics, natural
CC ligands derived from plants, microbiota, and endogenous metabolism are
CC potent AHR agonists (PubMed:18076143). Tryptophan (Trp) derivatives
CC constitute an important class of endogenous AHR ligands
CC (PubMed:32866000, PubMed:32818467). Acts as a negative regulator of
CC anti-tumor immunity: indoles and kynurenic acid generated by Trp
CC catabolism act as ligand and activate AHR, thereby promoting AHR-driven
CC cancer cell motility and suppressing adaptive immunity
CC (PubMed:32818467). Regulates the circadian clock by inhibiting the
CC basal and circadian expression of the core circadian component PER1
CC (PubMed:28602820). Inhibits PER1 by repressing the CLOCK-ARNTL/BMAL1
CC heterodimer mediated transcriptional activation of PER1
CC (PubMed:28602820). The heterodimer ARNT:AHR binds to core DNA sequence
CC 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene
CC promoters and activates their transcription (PubMed:28602820).
CC {ECO:0000269|PubMed:23275542, ECO:0000269|PubMed:28602820,
CC ECO:0000269|PubMed:30373764, ECO:0000269|PubMed:32818467,
CC ECO:0000269|PubMed:32866000, ECO:0000269|PubMed:7961644,
CC ECO:0000303|PubMed:12213388, ECO:0000303|PubMed:18076143}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterodimer; efficient DNA binding
CC requires dimerization with another bHLH protein (PubMed:10395741,
CC PubMed:28602820). Interacts with ARNT; the heterodimer ARNT:AHR binds
CC to core DNA sequence 5'-TGCGTG-3' within the dioxin response element
CC (DRE) of target gene promoters and activates their transcription
CC (PubMed:28602820). Binds MYBBP1A (By similarity). Interacts with
CC coactivators including SRC-1, RIP140 and NOCA7, and with the
CC corepressor SMRT (PubMed:10395741). Interacts with NEDD8 and IVNS1ABP
CC (PubMed:12215427, PubMed:16582008). Interacts with ARNTL/BMAL1 (By
CC similarity). Interacts with HSP90AB1 (By similarity). Interacts with
CC TIPARP; leading to mono-ADP-ribosylation of AHR and subsequent
CC inhibition of AHR (PubMed:23275542, PubMed:30373764).
CC {ECO:0000250|UniProtKB:P30561, ECO:0000269|PubMed:10395741,
CC ECO:0000269|PubMed:12215427, ECO:0000269|PubMed:16582008,
CC ECO:0000269|PubMed:23275542, ECO:0000269|PubMed:28602820,
CC ECO:0000269|PubMed:30373764}.
CC -!- INTERACTION:
CC P35869; P27540: ARNT; NbExp=6; IntAct=EBI-80780, EBI-80809;
CC P35869; Q8NI08: NCOA7; NbExp=2; IntAct=EBI-80780, EBI-80799;
CC P35869; Q9Y618: NCOR2; NbExp=2; IntAct=EBI-80780, EBI-80830;
CC P35869; P12977: EBNA3; Xeno; NbExp=5; IntAct=EBI-80780, EBI-993115;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30561}. Nucleus
CC {ECO:0000250|UniProtKB:P30561}. Note=Initially cytoplasmic; upon
CC binding with ligand and interaction with a HSP90, it translocates to
CC the nucleus. {ECO:0000250|UniProtKB:P30561}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested including blood,
CC brain, heart, kidney, liver, lung, pancreas and skeletal muscle.
CC Expressed in retinal photoreceptors (PubMed:29726989).
CC {ECO:0000269|PubMed:29726989, ECO:0000269|PubMed:7515333,
CC ECO:0000269|PubMed:8246913}.
CC -!- INDUCTION: Induced or repressed by TGFB1 and dioxin in a cell-type
CC specific fashion. Repressed by cAMP, retinoic acid, and 12-O-
CC tetradecanoyl phorbol-13 acetate (TPA). {ECO:0000269|PubMed:11259615}.
CC -!- DOMAIN: The PAS 1 domain is essential for dimerization and also
CC required for AHR:ARNT heterodimerization.
CC {ECO:0000250|UniProtKB:P30561}.
CC -!- PTM: Mono-ADP-ribosylated, leading to inhibit transcription activator
CC activity of AHR. {ECO:0000269|PubMed:30373764}.
CC -!- DISEASE: Retinitis pigmentosa 85 (RP85) [MIM:618345]: A form of
CC retinitis pigmentosa, a retinal dystrophy belonging to the group of
CC pigmentary retinopathies. Retinitis pigmentosa is characterized by
CC retinal pigment deposits visible on fundus examination and primary loss
CC of rod photoreceptor cells followed by secondary loss of cone
CC photoreceptors. Patients typically have night vision blindness and loss
CC of midperipheral visual field. As their condition progresses, they lose
CC their far peripheral visual field and eventually central vision as
CC well. RP85 is an autosomal recessive form manifesting as early-onset
CC progressive difficulty to adapt in dim light and gradually decreasing
CC visual acuity in both eyes. {ECO:0000269|PubMed:29726989}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; D16354; BAA03857.1; -; mRNA.
DR EMBL; L19872; AAA16210.1; -; mRNA.
DR EMBL; AC003075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236948; EAL24281.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93686.1; -; Genomic_DNA.
DR EMBL; BC069390; AAH69390.1; -; mRNA.
DR EMBL; BC070080; AAH70080.1; -; mRNA.
DR EMBL; U28063; AAA92082.1; -; Genomic_DNA.
DR EMBL; U27656; AAA92082.1; JOINED; Genomic_DNA.
DR EMBL; U27657; AAA92082.1; JOINED; Genomic_DNA.
DR EMBL; U28060; AAA92082.1; JOINED; Genomic_DNA.
DR EMBL; U28061; AAA92082.1; JOINED; Genomic_DNA.
DR EMBL; U28062; AAA92082.1; JOINED; Genomic_DNA.
DR EMBL; U28064; AAA92083.1; -; Genomic_DNA.
DR EMBL; U28066; AAA92084.1; -; Genomic_DNA.
DR EMBL; U28065; AAA92084.1; JOINED; Genomic_DNA.
DR EMBL; D38044; BAA07235.1; -; Genomic_DNA.
DR CCDS; CCDS5366.1; -.
DR PIR; S59514; S59514.
DR RefSeq; NP_001612.1; NM_001621.4.
DR PDB; 5NJ8; X-ray; 3.30 A; A/C=23-273.
DR PDBsum; 5NJ8; -.
DR AlphaFoldDB; P35869; -.
DR SMR; P35869; -.
DR BioGRID; 106699; 177.
DR CORUM; P35869; -.
DR DIP; DIP-946N; -.
DR ELM; P35869; -.
DR IntAct; P35869; 20.
DR STRING; 9606.ENSP00000242057; -.
DR BindingDB; P35869; -.
DR ChEMBL; CHEMBL3201; -.
DR DrugBank; DB08624; 1-[(4S)-4-amino-5-(1,3-benzothiazol-2-yl)-5-oxopentyl]guanidine.
DR DrugBank; DB01076; Atorvastatin.
DR DrugBank; DB06732; beta-Naphthoflavone.
DR DrugBank; DB12328; Cantharidin.
DR DrugBank; DB08995; Diosmin.
DR DrugBank; DB07715; Emodin.
DR DrugBank; DB12116; Epigallocatechin gallate.
DR DrugBank; DB00499; Flutamide.
DR DrugBank; DB01404; Ginseng.
DR DrugBank; DB11577; Indigotindisulfonic acid.
DR DrugBank; DB12379; Indirubin.
DR DrugBank; DB02052; Indirubin-3'-monoxime.
DR DrugBank; DB11937; Kynurenic Acid.
DR DrugBank; DB01097; Leflunomide.
DR DrugBank; DB00379; Mexiletine.
DR DrugBank; DB00393; Nimodipine.
DR DrugBank; DB00338; Omeprazole.
DR DrugBank; DB04216; Quercetin.
DR DrugBank; DB02709; Resveratrol.
DR DrugCentral; P35869; -.
DR GuidetoPHARMACOLOGY; 2951; -.
DR iPTMnet; P35869; -.
DR PhosphoSitePlus; P35869; -.
DR BioMuta; AHR; -.
DR DMDM; 3041653; -.
DR EPD; P35869; -.
DR jPOST; P35869; -.
DR MassIVE; P35869; -.
DR MaxQB; P35869; -.
DR PaxDb; P35869; -.
DR PeptideAtlas; P35869; -.
DR PRIDE; P35869; -.
DR ProteomicsDB; 55159; -.
DR Antibodypedia; 3909; 1039 antibodies from 46 providers.
DR DNASU; 196; -.
DR Ensembl; ENST00000242057.9; ENSP00000242057.4; ENSG00000106546.14.
DR Ensembl; ENST00000463496.1; ENSP00000436466.1; ENSG00000106546.14.
DR GeneID; 196; -.
DR KEGG; hsa:196; -.
DR MANE-Select; ENST00000242057.9; ENSP00000242057.4; NM_001621.5; NP_001612.1.
DR UCSC; uc011jxz.2; human.
DR CTD; 196; -.
DR DisGeNET; 196; -.
DR GeneCards; AHR; -.
DR HGNC; HGNC:348; AHR.
DR HPA; ENSG00000106546; Low tissue specificity.
DR MalaCards; AHR; -.
DR MIM; 600253; gene.
DR MIM; 618345; phenotype.
DR neXtProt; NX_P35869; -.
DR OpenTargets; ENSG00000106546; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA24641; -.
DR VEuPathDB; HostDB:ENSG00000106546; -.
DR eggNOG; KOG3560; Eukaryota.
DR GeneTree; ENSGT00940000154486; -.
DR HOGENOM; CLU_010044_1_1_1; -.
DR InParanoid; P35869; -.
DR OMA; GCDAKGQ; -.
DR OrthoDB; 174264at2759; -.
DR PhylomeDB; P35869; -.
DR TreeFam; TF352074; -.
DR PathwayCommons; P35869; -.
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; P35869; -.
DR SIGNOR; P35869; -.
DR BioGRID-ORCS; 196; 79 hits in 1111 CRISPR screens.
DR ChiTaRS; AHR; human.
DR GeneWiki; Aryl_hydrocarbon_receptor; -.
DR GenomeRNAi; 196; -.
DR Pharos; P35869; Tchem.
DR PRO; PR:P35869; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P35869; protein.
DR Bgee; ENSG00000106546; Expressed in visceral pleura and 194 other tissues.
DR ExpressionAtlas; P35869; baseline and differential.
DR Genevisible; P35869; 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; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0034752; C:cytosolic aryl hydrocarbon receptor complex; TAS:DFLAT.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0005667; C:transcription regulator complex; TAS:DFLAT.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:DFLAT.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:BHF-UCL.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; IPI:CAFA.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IPI:CAFA.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:DFLAT.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:CAFA.
DR GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR GO; GO:0001568; P:blood vessel development; NAS:DFLAT.
DR GO; GO:0019933; P:cAMP-mediated signaling; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1904613; P:cellular response to 2,3,7,8-tetrachlorodibenzodioxine; IDA:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
DR GO; GO:1904322; P:cellular response to forskolin; IDA:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0002841; P:negative regulation of T cell mediated immune response to tumor cell; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0002819; P:regulation of adaptive immune response; IDA:UniProtKB.
DR GO; GO:0030888; P:regulation of B cell proliferation; IDA:DFLAT.
DR GO; GO:0010468; P:regulation of gene expression; IDA:DFLAT.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:DFLAT.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:DFLAT.
DR CDD; cd00130; PAS; 2.
DR DisProt; DP00381; -.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR033348; AHR.
DR InterPro; IPR039091; AHR/AHRR.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR PANTHER; PTHR10649; PTHR10649; 1.
DR PANTHER; PTHR10649:SF9; PTHR10649:SF9; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
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 PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; ADP-ribosylation; Biological rhythms;
KW Cell cycle; Cytoplasm; DNA-binding; Nucleus; Receptor; Reference proteome;
KW Repeat; Repressor; Retinitis pigmentosa; Transcription;
KW Transcription regulation.
FT PROPEP 1..10
FT /evidence="ECO:0000250|UniProtKB:P30561"
FT /id="PRO_0000013450"
FT CHAIN 11..848
FT /note="Aryl hydrocarbon receptor"
FT /id="PRO_0000013451"
FT DOMAIN 27..80
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 111..181
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 275..342
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 348..386
FT /note="PAC"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..66
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:28602820"
FT REGION 118..126
FT /note="Required for maintaining the overall integrity of
FT the AHR:ARNT heterodimer and its transcriptional activity"
FT /evidence="ECO:0000250|UniProtKB:P30561"
FT REGION 266..268
FT /note="Required for maintaining the overall integrity of
FT the AHR:ARNT heterodimer and its transcriptional activity"
FT /evidence="ECO:0000250|UniProtKB:P30561"
FT REGION 824..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VARIANT 517
FT /note="P -> S (in dbSNP:rs72552768)"
FT /evidence="ECO:0000269|PubMed:11689007"
FT /id="VAR_015516"
FT VARIANT 554
FT /note="R -> K (in dbSNP:rs2066853)"
FT /evidence="ECO:0000269|PubMed:10739168,
FT ECO:0000269|PubMed:11698344, ECO:0000269|PubMed:7550366"
FT /id="VAR_009281"
FT VARIANT 570
FT /note="V -> I (in dbSNP:rs4986826)"
FT /evidence="ECO:0000269|PubMed:10739168,
FT ECO:0000269|PubMed:11689007"
FT /id="VAR_009282"
FT VARIANT 786
FT /note="M -> V (in dbSNP:rs72552769)"
FT /evidence="ECO:0000269|PubMed:11698344"
FT /id="VAR_015517"
FT MUTAGEN 40
FT /note="R->D: Decreases transcription factor activity."
FT /evidence="ECO:0000269|PubMed:28602820"
FT MUTAGEN 50
FT /note="L->D: Interfers with transcription factor activity."
FT /evidence="ECO:0000269|PubMed:28602820"
FT MUTAGEN 74
FT /note="V->D: Interfers with transcription factor activity."
FT /evidence="ECO:0000269|PubMed:28602820"
FT MUTAGEN 79
FT /note="A->D: Interfers with transcription factor activity."
FT /evidence="ECO:0000269|PubMed:28602820"
FT MUTAGEN 82
FT /note="F->D: Interfers with transcription factor activity."
FT /evidence="ECO:0000269|PubMed:28602820"
FT MUTAGEN 118
FT /note="L->D: Interfers with transcription factor activity."
FT /evidence="ECO:0000269|PubMed:28602820"
FT MUTAGEN 122
FT /note="L->D: Interfers with transcription factor activity."
FT /evidence="ECO:0000269|PubMed:28602820"
FT MUTAGEN 136
FT /note="F->D: Interfers with transcription factor activity."
FT /evidence="ECO:0000269|PubMed:28602820"
FT MUTAGEN 154
FT /note="I->D: Interfers with transcription factor activity."
FT /evidence="ECO:0000269|PubMed:28602820"
FT MUTAGEN 381
FT /note="V->A: Increases specific ligand binding."
FT /evidence="ECO:0000269|PubMed:7961644"
FT MUTAGEN 381
FT /note="V->D: Abolishes specific ligand binding."
FT /evidence="ECO:0000269|PubMed:7961644"
FT MUTAGEN 381
FT /note="V->L,G: No effect on specific ligand binding."
FT /evidence="ECO:0000269|PubMed:7961644"
FT CONFLICT 191
FT /note="E -> EG (in Ref. 8; AAA92082)"
FT /evidence="ECO:0000305"
FT CONFLICT 340..341
FT /note="MI -> SD (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 807..848
FT /note="LNETYPAELNNINNTQTTTHLQPLHHPSEARPFPDLTSSGFL -> FK (in
FT Ref. 1; BAA03857)"
FT /evidence="ECO:0000305"
FT HELIX 35..52
FT /evidence="ECO:0007829|PDB:5NJ8"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5NJ8"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:5NJ8"
FT HELIX 66..86
FT /evidence="ECO:0007829|PDB:5NJ8"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:5NJ8"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:5NJ8"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:5NJ8"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5NJ8"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:5NJ8"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:5NJ8"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:5NJ8"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:5NJ8"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:5NJ8"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:5NJ8"
FT STRAND 235..246
FT /evidence="ECO:0007829|PDB:5NJ8"
FT STRAND 262..270
FT /evidence="ECO:0007829|PDB:5NJ8"
SQ SEQUENCE 848 AA; 96147 MW; 1BFE022871B7B028 CRC64;
MNSSSANITY ASRKRRKPVQ KTVKPIPAEG IKSNPSKRHR DRLNTELDRL ASLLPFPQDV
INKLDKLSVL RLSVSYLRAK SFFDVALKSS PTERNGGQDN CRAANFREGL NLQEGEFLLQ
ALNGFVLVVT TDALVFYASS TIQDYLGFQQ SDVIHQSVYE LIHTEDRAEF QRQLHWALNP
SQCTESGQGI EEATGLPQTV VCYNPDQIPP ENSPLMERCF ICRLRCLLDN SSGFLAMNFQ
GKLKYLHGQK KKGKDGSILP PQLALFAIAT PLQPPSILEI RTKNFIFRTK HKLDFTPIGC
DAKGRIVLGY TEAELCTRGS GYQFIHAADM LYCAESHIRM IKTGESGMIV FRLLTKNNRW
TWVQSNARLL YKNGRPDYII VTQRPLTDEE GTEHLRKRNT KLPFMFTTGE AVLYEATNPF
PAIMDPLPLR TKNGTSGKDS ATTSTLSKDS LNPSSLLAAM MQQDESIYLY PASSTSSTAP
FENNFFNESM NECRNWQDNT APMGNDTILK HEQIDQPQDV NSFAGGHPGL FQDSKNSDLY
SIMKNLGIDF EDIRHMQNEK FFRNDFSGEV DFRDIDLTDE ILTYVQDSLS KSPFIPSDYQ
QQQSLALNSS CMVQEHLHLE QQQQHHQKQV VVEPQQQLCQ KMKHMQVNGM FENWNSNQFV
PFNCPQQDPQ QYNVFTDLHG ISQEFPYKSE MDSMPYTQNF ISCNQPVLPQ HSKCTELDYP
MGSFEPSPYP TTSSLEDFVT CLQLPENQKH GLNPQSAIIT PQTCYAGAVS MYQCQPEPQH
THVGQMQYNP VLPGQQAFLN KFQNGVLNET YPAELNNINN TQTTTHLQPL HHPSEARPFP
DLTSSGFL
