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Protein

Aryl hydrocarbon receptor

Gene

AHR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ligand-activated transcriptional activator. Binds to the XRE promoter region of genes it activates. Activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons. Involved in cell-cycle regulation. Likely to play an important role in the development and maturation of many tissues. Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1. Inhibits PER1 by repressing the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of PER1.2 Publications

GO - Molecular functioni

  • DNA binding Source: DFLAT
  • E-box binding Source: UniProtKB
  • enhancer binding Source: MGI
  • Hsp90 protein binding Source: BHF-UCL
  • ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
  • protein dimerization activity Source: DFLAT
  • protein heterodimerization activity Source: DFLAT
  • RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: Ensembl
  • sequence-specific DNA binding Source: Ensembl
  • sequence-specific DNA binding transcription factor activity Source: MGI
  • signal transducer activity Source: InterPro
  • transcription factor binding Source: BHF-UCL
  • transcription regulatory region DNA binding Source: DFLAT

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • blood vessel development Source: DFLAT
  • cell cycle Source: UniProtKB-KW
  • circadian regulation of gene expression Source: UniProtKB
  • intracellular receptor signaling pathway Source: GOC
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: GO_Central
  • prostate gland development Source: Ensembl
  • regulation of B cell proliferation Source: DFLAT
  • regulation of gene expression Source: DFLAT
  • regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: DFLAT
  • response to toxic substance Source: UniProtKB
  • response to xenobiotic stimulus Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: UniProtKB
  • xenobiotic metabolic process Source: DFLAT
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor, Repressor

Keywords - Biological processi

Biological rhythms, Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SignaLinkiP35869.

Names & Taxonomyi

Protein namesi
Recommended name:
Aryl hydrocarbon receptor
Short name:
Ah receptor
Short name:
AhR
Alternative name(s):
Class E basic helix-loop-helix protein 76
Short name:
bHLHe76
Gene namesi
Name:AHR
Synonyms:BHLHE76
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:348. AHR.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Initially cytoplasmic; upon binding with ligand and interaction with a HSP90, it translocates to the nucleus.

GO - Cellular componenti

  • cytoplasm Source: DFLAT
  • cytosolic aryl hydrocarbon receptor complex Source: DFLAT
  • nuclear aryl hydrocarbon receptor complex Source: GO_Central
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • transcription factor complex Source: DFLAT
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi381 – 3811V → A: Increases specific ligand binding. 1 Publication
Mutagenesisi381 – 3811V → D: Abolishes specific ligand binding. 1 Publication
Mutagenesisi381 – 3811V → L or G: No effect on specific ligand binding. 1 Publication

Organism-specific databases

PharmGKBiPA24641.

Chemistry

DrugBankiDB01076. Atorvastatin.
DB00499. Flutamide.
DB01404. Ginseng.
DB01097. Leflunomide.
DB00379. Mexiletine.
DB00393. Nimodipine.

Polymorphism and mutation databases

BioMutaiAHR.
DMDMi3041653.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1010By similarityPRO_0000013450
Chaini11 – 848838Aryl hydrocarbon receptorPRO_0000013451Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP35869.
PaxDbiP35869.
PRIDEiP35869.

PTM databases

PhosphoSiteiP35869.

Expressioni

Tissue specificityi

Expressed in all tissues tested including blood, brain, heart, kidney, liver, lung, pancreas and skeletal muscle.2 Publications

Inductioni

Induced or repressed by TGFB1 and dioxin in a cell-type specific fashion. Repressed by cAMP, retinoic acid, and 12-O-tetradecanoyl phorbol-13 acetate (TPA).1 Publication

Gene expression databases

BgeeiP35869.
CleanExiHS_AHR.
ExpressionAtlasiP35869. baseline and differential.
GenevisibleiP35869. HS.

Organism-specific databases

HPAiCAB005072.
HPA029722.
HPA029723.

Interactioni

Subunit structurei

Binds MYBBP1A (By similarity). Efficient DNA binding requires dimerization with another bHLH protein. In the nucleus, heterodimer of AHR and ARNT. Interacts with coactivators including SRC-1, RIP140 and NOCA7, and with the corepressor SMRT. Interacts with NEDD8 and IVNS1ABP. Interacts with ARNTL/BMAL1.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARNTP275405EBI-80780,EBI-80809
EBNA3P129775EBI-80780,EBI-993115From a different organism.
NCOA7Q8NI082EBI-80780,EBI-80799
NCOR2Q9Y6182EBI-80780,EBI-80830

Protein-protein interaction databases

BioGridi106699. 39 interactions.
DIPiDIP-946N.
IntActiP35869. 11 interactions.
MINTiMINT-6597538.
STRINGi9606.ENSP00000242057.

Structurei

3D structure databases

DisProtiDP00381.
ProteinModelPortaliP35869.
SMRiP35869. Positions 33-383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 8054bHLHPROSITE-ProRule annotationAdd
BLAST
Domaini111 – 18171PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini275 – 34268PAS 2PROSITE-ProRule annotationAdd
BLAST
Domaini348 – 38639PACAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi600 – 64041Gln-richAdd
BLAST

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation
Contains 2 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG253623.
GeneTreeiENSGT00760000118788.
HOGENOMiHOG000252935.
HOVERGENiHBG007313.
InParanoidiP35869.
KOiK09093.
OMAiQQLCQKM.
OrthoDBiEOG793BBM.
PhylomeDBiP35869.
TreeFamiTF352074.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR013655. PAS_fold_3.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
PF00989. PAS. 1 hit.
PF08447. PAS_3. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
PROSITEiPS50888. BHLH. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35869-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSSSANITY ASRKRRKPVQ KTVKPIPAEG IKSNPSKRHR DRLNTELDRL
60 70 80 90 100
ASLLPFPQDV INKLDKLSVL RLSVSYLRAK SFFDVALKSS PTERNGGQDN
110 120 130 140 150
CRAANFREGL NLQEGEFLLQ ALNGFVLVVT TDALVFYASS TIQDYLGFQQ
160 170 180 190 200
SDVIHQSVYE LIHTEDRAEF QRQLHWALNP SQCTESGQGI EEATGLPQTV
210 220 230 240 250
VCYNPDQIPP ENSPLMERCF ICRLRCLLDN SSGFLAMNFQ GKLKYLHGQK
260 270 280 290 300
KKGKDGSILP PQLALFAIAT PLQPPSILEI RTKNFIFRTK HKLDFTPIGC
310 320 330 340 350
DAKGRIVLGY TEAELCTRGS GYQFIHAADM LYCAESHIRM IKTGESGMIV
360 370 380 390 400
FRLLTKNNRW TWVQSNARLL YKNGRPDYII VTQRPLTDEE GTEHLRKRNT
410 420 430 440 450
KLPFMFTTGE AVLYEATNPF PAIMDPLPLR TKNGTSGKDS ATTSTLSKDS
460 470 480 490 500
LNPSSLLAAM MQQDESIYLY PASSTSSTAP FENNFFNESM NECRNWQDNT
510 520 530 540 550
APMGNDTILK HEQIDQPQDV NSFAGGHPGL FQDSKNSDLY SIMKNLGIDF
560 570 580 590 600
EDIRHMQNEK FFRNDFSGEV DFRDIDLTDE ILTYVQDSLS KSPFIPSDYQ
610 620 630 640 650
QQQSLALNSS CMVQEHLHLE QQQQHHQKQV VVEPQQQLCQ KMKHMQVNGM
660 670 680 690 700
FENWNSNQFV PFNCPQQDPQ QYNVFTDLHG ISQEFPYKSE MDSMPYTQNF
710 720 730 740 750
ISCNQPVLPQ HSKCTELDYP MGSFEPSPYP TTSSLEDFVT CLQLPENQKH
760 770 780 790 800
GLNPQSAIIT PQTCYAGAVS MYQCQPEPQH THVGQMQYNP VLPGQQAFLN
810 820 830 840
KFQNGVLNET YPAELNNINN TQTTTHLQPL HHPSEARPFP DLTSSGFL
Length:848
Mass (Da):96,147
Last modified:July 15, 1998 - v2
Checksum:i1BFE022871B7B028
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911E → EG in AAA92082 (PubMed:16696038).Curated
Sequence conflicti340 – 3412MI → SD (PubMed:7515333).Curated
Sequence conflicti807 – 84842LNETY…SSGFL → FK in BAA03857 (PubMed:8393992).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti517 – 5171P → S.1 Publication
Corresponds to variant rs72552768 [ dbSNP | Ensembl ].
VAR_015516
Natural varianti554 – 5541R → K.3 Publications
Corresponds to variant rs2066853 [ dbSNP | Ensembl ].
VAR_009281
Natural varianti570 – 5701V → I.2 Publications
Corresponds to variant rs4986826 [ dbSNP | Ensembl ].
VAR_009282
Natural varianti786 – 7861M → V.1 Publication
Corresponds to variant rs72552769 [ dbSNP | Ensembl ].
VAR_015517

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16354 mRNA. Translation: BAA03857.1.
L19872 mRNA. Translation: AAA16210.1.
AC003075 Genomic DNA. No translation available.
CH236948 Genomic DNA. Translation: EAL24281.1.
CH471073 Genomic DNA. Translation: EAW93686.1.
BC069390 mRNA. Translation: AAH69390.1.
BC070080 mRNA. Translation: AAH70080.1.
U28063
, U27656, U27657, U28060, U28061, U28062 Genomic DNA. Translation: AAA92082.1.
U28064 Genomic DNA. Translation: AAA92083.1.
U28066, U28065 Genomic DNA. Translation: AAA92084.1.
D38044 Genomic DNA. Translation: BAA07235.1.
CCDSiCCDS5366.1.
PIRiS59514.
RefSeqiNP_001612.1. NM_001621.4.
UniGeneiHs.171189.

Genome annotation databases

EnsembliENST00000242057; ENSP00000242057; ENSG00000106546.
ENST00000463496; ENSP00000436466; ENSG00000106546.
GeneIDi196.
KEGGihsa:196.
UCSCiuc011jxz.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16354 mRNA. Translation: BAA03857.1.
L19872 mRNA. Translation: AAA16210.1.
AC003075 Genomic DNA. No translation available.
CH236948 Genomic DNA. Translation: EAL24281.1.
CH471073 Genomic DNA. Translation: EAW93686.1.
BC069390 mRNA. Translation: AAH69390.1.
BC070080 mRNA. Translation: AAH70080.1.
U28063
, U27656, U27657, U28060, U28061, U28062 Genomic DNA. Translation: AAA92082.1.
U28064 Genomic DNA. Translation: AAA92083.1.
U28066, U28065 Genomic DNA. Translation: AAA92084.1.
D38044 Genomic DNA. Translation: BAA07235.1.
CCDSiCCDS5366.1.
PIRiS59514.
RefSeqiNP_001612.1. NM_001621.4.
UniGeneiHs.171189.

3D structure databases

DisProtiDP00381.
ProteinModelPortaliP35869.
SMRiP35869. Positions 33-383.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106699. 39 interactions.
DIPiDIP-946N.
IntActiP35869. 11 interactions.
MINTiMINT-6597538.
STRINGi9606.ENSP00000242057.

Chemistry

BindingDBiP35869.
ChEMBLiCHEMBL3201.
DrugBankiDB01076. Atorvastatin.
DB00499. Flutamide.
DB01404. Ginseng.
DB01097. Leflunomide.
DB00379. Mexiletine.
DB00393. Nimodipine.

PTM databases

PhosphoSiteiP35869.

Polymorphism and mutation databases

BioMutaiAHR.
DMDMi3041653.

Proteomic databases

MaxQBiP35869.
PaxDbiP35869.
PRIDEiP35869.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000242057; ENSP00000242057; ENSG00000106546.
ENST00000463496; ENSP00000436466; ENSG00000106546.
GeneIDi196.
KEGGihsa:196.
UCSCiuc011jxz.1. human.

Organism-specific databases

CTDi196.
GeneCardsiGC07P017304.
HGNCiHGNC:348. AHR.
HPAiCAB005072.
HPA029722.
HPA029723.
MIMi600253. gene.
neXtProtiNX_P35869.
PharmGKBiPA24641.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG253623.
GeneTreeiENSGT00760000118788.
HOGENOMiHOG000252935.
HOVERGENiHBG007313.
InParanoidiP35869.
KOiK09093.
OMAiQQLCQKM.
OrthoDBiEOG793BBM.
PhylomeDBiP35869.
TreeFamiTF352074.

Enzyme and pathway databases

SignaLinkiP35869.

Miscellaneous databases

ChiTaRSiAHR. human.
GeneWikiiAryl_hydrocarbon_receptor.
GenomeRNAii196.
NextBioi786.
PROiP35869.
SOURCEiSearch...

Gene expression databases

BgeeiP35869.
CleanExiHS_AHR.
ExpressionAtlasiP35869. baseline and differential.
GenevisibleiP35869. HS.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR013655. PAS_fold_3.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
PF00989. PAS. 1 hit.
PF08447. PAS_3. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
PROSITEiPS50888. BHLH. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human Ah receptor cDNA: analysis for highly conserved sequences."
    Itoh S., Kamataki T.
    Nucleic Acids Res. 21:3578-3578(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Cloning and expression of a human Ah receptor cDNA."
    Dolwick K.M., Schmidt J.V., Carver L.A., Swanson H.I., Bradfield C.A.
    Mol. Pharmacol. 44:911-917(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. "Human arylhydrocarbon receptor: functional expression and chromosomal assignment to 7p21."
    Ema M., Matsushita N., Sogawa K., Ariyama T., Inazawa J., Nemoto T., Ota M., Oshimura M., Fujii-Kuriyama Y.
    J. Biochem. 116:845-851(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  8. "Complete structural characterisation of the human aryl hydrocarbon receptor gene."
    Bennett P., Ramsden D.B., Williams A.C.
    Clin. Mol. Pathol. 49:M12-M16(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-235; 388-461 AND 764-848.
  9. "Interindividual difference in expression of human Ah receptor and related P450 genes."
    Hayashi S., Watanabe J., Nakachi K., Eguchi H., Gotoh O., Kawajiri K.
    Carcinogenesis 15:801-806(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-341, TISSUE SPECIFICITY.
  10. "Dioxin binding activities of polymorphic forms of mouse and human arylhydrocarbon receptors."
    Ema M., Ohe N., Suzuki M., Mimura J., Sogawa K., Ikawa S., Fujii-Kuriyama Y.
    J. Biol. Chem. 269:27337-27343(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF VAL-381.
  11. "Interactions of nuclear receptor coactivator/corepressor proteins with the aryl hydrocarbon receptor complex."
    Nguyen T.A., Hoivik D., Lee J.-E., Safe S.
    Arch. Biochem. Biophys. 367:250-257(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  12. "Cell-specific regulation of human aryl hydrocarbon receptor expression by transforming growth factor-beta(1)."
    Wolff S., Harper P.A., Wong J.M.Y., Mostert V., Wang Y., Abel J.
    Mol. Pharmacol. 59:716-724(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  13. "Role of the aryl hydrocarbon receptor in cell cycle regulation."
    Puga A., Xia Y., Elferink C.
    Chem. Biol. Interact. 141:117-130(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN CELL CYCLE.
  14. "Interaction with Nedd8, a ubiquitin-like protein, enhances the transcriptional activity of the aryl hydrocarbon receptor."
    Antenos M., Casper R.F., Brown T.J.
    J. Biol. Chem. 277:44028-44034(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEDD8.
  15. "The aryl hydrocarbon receptor signaling pathway is modified through interactions with a Kelch protein."
    Dunham E.E., Stevens E.A., Glover E., Bradfield C.A.
    Mol. Pharmacol. 70:8-15(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IVNS1ABP.
  16. Cited for: REVIEW ON VARIANTS.
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Polymorphisms of human Ah receptor gene are not involved in lung cancer."
    Kawajiri K., Watanabe J., Eguchi H., Nakachi K., Kiyohara C., Hayashi S.
    Pharmacogenetics 5:151-158(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LYS-554.
  19. "Variation in induced CYP1A1 levels: relationship to CYP1A1, Ah receptor and GSTM1 polymorphisms."
    Smart J., Daly A.K.
    Pharmacogenetics 10:11-24(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LYS-554 AND ILE-570.
  20. "Polymorphisms of human aryl hydrocarbon receptor (AhR) gene in a French population: relationship with CYP1A1 inducibility and lung cancer."
    Cauchi S., Stucker I., Solas C., Laurent-Puig P., Cenee S., Hemon D., Jacquet M., Kremers P., Beaune P., Massaad-Massade L.
    Carcinogenesis 22:1819-1824(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LYS-554 AND VAL-786.
  21. "Human aryl hydrocarbon receptor polymorphisms that result in loss of CYP1A1 induction."
    Wong J.M.Y., Okey A.B., Harper P.A.
    Biochem. Biophys. Res. Commun. 288:990-996(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SER-517 AND ILE-570.

Entry informationi

Entry nameiAHR_HUMAN
AccessioniPrimary (citable) accession number: P35869
Secondary accession number(s): A4D130
, Q13728, Q13803, Q13804
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 15, 1998
Last modified: June 24, 2015
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.