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P35869 (AHR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:AHR
Synonyms:BHLHE76
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length848 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.11

Subunit structure

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. Ref.11 Ref.14 Ref.15

Subcellular location

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

Tissue specificity

Expressed in all tissues tested including blood, brain, heart, kidney, liver, lung, pancreas and skeletal muscle. Ref.2 Ref.9

Induction

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). Ref.12

Sequence similarities

Contains 1 bHLH (basic helix-loop-helix) domain.

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 2 PAS (PER-ARNT-SIM) domains.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
Receptor
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement Ref.13. Source: UniProtKB

blood vessel development

Non-traceable author statement PubMed 19538249. Source: DFLAT

cell cycle

Traceable author statement Ref.13. Source: UniProtKB

intracellular receptor signaling pathway

Inferred from direct assay Ref.11. Source: GOC

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of RNA polymerase II transcriptional preinitiation complex assembly

Inferred from electronic annotation. Source: Ensembl

prostate gland development

Inferred from electronic annotation. Source: Ensembl

regulation of B cell proliferation

Inferred from direct assay PubMed 15681594. Source: DFLAT

regulation of gene expression

Inferred from direct assay PubMed 15681594. Source: DFLAT

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15681594. Source: DFLAT

regulation of transcription, DNA-templated

Inferred from direct assay Ref.11. Source: UniProtKB

response to stress

Inferred from direct assay Ref.10. Source: UniProtKB

response to xenobiotic stimulus

Inferred from direct assay Ref.10. Source: UniProtKB

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.11. Source: UniProtKB

xenobiotic metabolic process

Traceable author statement PubMed 19538249. Source: DFLAT

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15681594. Source: DFLAT

cytosolic aryl hydrocarbon receptor complex

Traceable author statement PubMed 19538249. Source: DFLAT

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

transcription factor complex

Traceable author statement PubMed 19538249. Source: DFLAT

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15681594. Source: DFLAT

Hsp90 protein binding

Inferred from direct assay PubMed 9079689. Source: BHF-UCL

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

enhancer binding

Inferred from direct assay PubMed 23275542. Source: MGI

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay Ref.11. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11PubMed 16257957PubMed 9704006. Source: IntAct

protein dimerization activity

Traceable author statement PubMed 19538249. Source: DFLAT

protein heterodimerization activity

Traceable author statement PubMed 19538249. Source: DFLAT

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 11782478. Source: MGI

signal transducer activity

Inferred from electronic annotation. Source: InterPro

transcription factor binding

Inferred from physical interaction PubMed 9079689. Source: BHF-UCL

transcription regulatory region DNA binding

Inferred from direct assay PubMed 15681594. Source: DFLAT

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1010 By similarity
PRO_0000013450
Chain11 – 848838Aryl hydrocarbon receptor
PRO_0000013451

Regions

Domain27 – 8054bHLH
Domain111 – 18171PAS 1
Domain275 – 34268PAS 2
Domain348 – 38639PAC
Compositional bias600 – 64041Gln-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.17

Natural variations

Natural variant5171P → S. Ref.21
Corresponds to variant rs72552768 [ dbSNP | Ensembl ].
VAR_015516
Natural variant5541R → K. Ref.18 Ref.19 Ref.20
Corresponds to variant rs2066853 [ dbSNP | Ensembl ].
VAR_009281
Natural variant5701V → I. Ref.19 Ref.21
Corresponds to variant rs4986826 [ dbSNP | Ensembl ].
VAR_009282
Natural variant7861M → V. Ref.20
Corresponds to variant rs72552769 [ dbSNP | Ensembl ].
VAR_015517

Experimental info

Mutagenesis3811V → A: Increases specific ligand binding. Ref.10
Mutagenesis3811V → D: Abolishes specific ligand binding. Ref.10
Mutagenesis3811V → L or G: No effect on specific ligand binding. Ref.10
Sequence conflict1911E → EG in AAA92082. Ref.8
Sequence conflict340 – 3412MI → SD Ref.9
Sequence conflict807 – 84842LNETY…SSGFL → FK in BAA03857. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P35869 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 1BFE022871B7B028

FASTA84896,147
        10         20         30         40         50         60 
MNSSSANITY ASRKRRKPVQ KTVKPIPAEG IKSNPSKRHR DRLNTELDRL ASLLPFPQDV 

        70         80         90        100        110        120 
INKLDKLSVL RLSVSYLRAK SFFDVALKSS PTERNGGQDN CRAANFREGL NLQEGEFLLQ 

       130        140        150        160        170        180 
ALNGFVLVVT TDALVFYASS TIQDYLGFQQ SDVIHQSVYE LIHTEDRAEF QRQLHWALNP 

       190        200        210        220        230        240 
SQCTESGQGI EEATGLPQTV VCYNPDQIPP ENSPLMERCF ICRLRCLLDN SSGFLAMNFQ 

       250        260        270        280        290        300 
GKLKYLHGQK KKGKDGSILP PQLALFAIAT PLQPPSILEI RTKNFIFRTK HKLDFTPIGC 

       310        320        330        340        350        360 
DAKGRIVLGY TEAELCTRGS GYQFIHAADM LYCAESHIRM IKTGESGMIV FRLLTKNNRW 

       370        380        390        400        410        420 
TWVQSNARLL YKNGRPDYII VTQRPLTDEE GTEHLRKRNT KLPFMFTTGE AVLYEATNPF 

       430        440        450        460        470        480 
PAIMDPLPLR TKNGTSGKDS ATTSTLSKDS LNPSSLLAAM MQQDESIYLY PASSTSSTAP 

       490        500        510        520        530        540 
FENNFFNESM NECRNWQDNT APMGNDTILK HEQIDQPQDV NSFAGGHPGL FQDSKNSDLY 

       550        560        570        580        590        600 
SIMKNLGIDF EDIRHMQNEK FFRNDFSGEV DFRDIDLTDE ILTYVQDSLS KSPFIPSDYQ 

       610        620        630        640        650        660 
QQQSLALNSS CMVQEHLHLE QQQQHHQKQV VVEPQQQLCQ KMKHMQVNGM FENWNSNQFV 

       670        680        690        700        710        720 
PFNCPQQDPQ QYNVFTDLHG ISQEFPYKSE MDSMPYTQNF ISCNQPVLPQ HSKCTELDYP 

       730        740        750        760        770        780 
MGSFEPSPYP TTSSLEDFVT CLQLPENQKH GLNPQSAIIT PQTCYAGAVS MYQCQPEPQH 

       790        800        810        820        830        840 
THVGQMQYNP VLPGQQAFLN KFQNGVLNET YPAELNNINN TQTTTHLQPL HHPSEARPFP 


DLTSSGFL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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]"Polymorphisms in the human AH receptor."
Harper P.A., Wong J.M.Y., Lam M.S.M., Okey A.B.
Chem. Biol. Interact. 141:161-187(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , 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.
CCDSCCDS5366.1.
PIRS59514.
RefSeqNP_001612.1. NM_001621.4.
UniGeneHs.171189.

3D structure databases

DisProtDP00381.
ProteinModelPortalP35869.
SMRP35869. Positions 31-383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106699. 37 interactions.
DIPDIP-946N.
IntActP35869. 11 interactions.
MINTMINT-6597538.
STRING9606.ENSP00000242057.

Chemistry

BindingDBP35869.
ChEMBLCHEMBL3201.

PTM databases

PhosphoSiteP35869.

Polymorphism databases

DMDM3041653.

Proteomic databases

MaxQBP35869.
PaxDbP35869.
PRIDEP35869.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242057; ENSP00000242057; ENSG00000106546.
ENST00000463496; ENSP00000436466; ENSG00000106546.
GeneID196.
KEGGhsa:196.
UCSCuc011jxz.1. human.

Organism-specific databases

CTD196.
GeneCardsGC07P017304.
HGNCHGNC:348. AHR.
HPACAB005072.
HPA029722.
HPA029723.
MIM600253. gene.
neXtProtNX_P35869.
PharmGKBPA24641.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253623.
HOGENOMHOG000252935.
HOVERGENHBG007313.
InParanoidP35869.
KOK09093.
OMAQQLCQKM.
OrthoDBEOG793BBM.
PhylomeDBP35869.
TreeFamTF352074.

Enzyme and pathway databases

SignaLinkP35869.

Gene expression databases

BgeeP35869.
CleanExHS_AHR.
GenevestigatorP35869.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR013655. PAS_fold_3.
[Graphical view]
PfamPF00010. HLH. 1 hit.
PF00989. PAS. 1 hit.
PF08447. PAS_3. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
PROSITEPS50888. BHLH. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAHR. human.
GeneWikiAryl_hydrocarbon_receptor.
GenomeRNAi196.
NextBio786.
PROP35869.
SOURCESearch...

Entry information

Entry nameAHR_HUMAN
AccessionPrimary (citable) accession number: P35869
Secondary accession number(s): A4D130 expand/collapse secondary AC list , Q13728, Q13803, Q13804
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 15, 1998
Last modified: July 9, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM