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P30561

- AHR_MOUSE

UniProt

P30561 - AHR_MOUSE

Protein

Aryl hydrocarbon receptor

Gene

Ahr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (25 Mar 2003)
      Previous versions | rss
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    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 PER1.8 Publications

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. E-box binding Source: UniProtKB
    3. enhancer binding Source: MGI
    4. Hsp90 protein binding Source: DFLAT
    5. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. protein heterodimerization activity Source: UniProtKB
    8. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: MGI
    9. sequence-specific DNA binding Source: MGI
    10. sequence-specific DNA binding transcription factor activity Source: MGI
    11. signal transducer activity Source: InterPro

    GO - Biological processi

    1. B-1 B cell homeostasis Source: DFLAT
    2. B cell differentiation Source: DFLAT
    3. B cell homeostasis Source: DFLAT
    4. blood circulation Source: DFLAT
    5. blood vessel development Source: DFLAT
    6. blood vessel morphogenesis Source: DFLAT
    7. blood vessel remodeling Source: DFLAT
    8. camera-type eye development Source: DFLAT
    9. cardiac left ventricle morphogenesis Source: DFLAT
    10. cell cycle Source: UniProtKB-KW
    11. cell morphogenesis Source: DFLAT
    12. cellular response to cAMP Source: UniProtKB
    13. circadian regulation of gene expression Source: UniProtKB
    14. circumferential growth involved in left ventricle morphogenesis Source: DFLAT
    15. common bile duct development Source: DFLAT
    16. embryonic hemopoiesis Source: DFLAT
    17. gland development Source: MGI
    18. glomerulus morphogenesis Source: DFLAT
    19. immune system process Source: DFLAT
    20. intracellular receptor signaling pathway Source: GOC
    21. kidney morphogenesis Source: DFLAT
    22. liver development Source: DFLAT
    23. lymphocyte homeostasis Source: DFLAT
    24. negative regulation of necrotic cell death Source: DFLAT
    25. negative regulation of systemic arterial blood pressure Source: DFLAT
    26. negative regulation of transcription, DNA-templated Source: UniProtKB
    27. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    28. negative regulation of vasoconstriction Source: DFLAT
    29. patterning of blood vessels Source: DFLAT
    30. positive regulation of cell size Source: DFLAT
    31. positive regulation of growth rate Source: DFLAT
    32. positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: MGI
    33. positive regulation of transcription, DNA-templated Source: UniProtKB
    34. post-embryonic hemopoiesis Source: DFLAT
    35. prostate gland development Source: MGI
    36. regulation of blood pressure Source: DFLAT
    37. regulation of blood vessel size Source: DFLAT
    38. regulation of heart growth Source: DFLAT
    39. regulation of transcription, DNA-templated Source: UniProtKB
    40. reproductive structure development Source: MGI
    41. response to stress Source: UniProtKB
    42. response to toxic substance Source: UniProtKB
    43. response to xenobiotic stimulus Source: UniProtKB
    44. smooth muscle tissue development Source: DFLAT
    45. spleen development Source: DFLAT
    46. T cell homeostasis Source: DFLAT
    47. transcription from RNA polymerase II promoter Source: UniProtKB
    48. venous blood vessel development Source: DFLAT
    49. xenobiotic metabolic process Source: MGI

    Keywords - Molecular functioni

    Activator, Receptor, Repressor

    Keywords - Biological processi

    Biological rhythms, Cell cycle, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aryl hydrocarbon receptor
    Short name:
    Ah receptor
    Short name:
    AhR
    Gene namesi
    Name:Ahr
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:105043. 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

    1. aryl hydrocarbon receptor complex Source: DFLAT
    2. cytoplasm Source: MGI
    3. cytosol Source: UniProtKB
    4. cytosolic aryl hydrocarbon receptor complex Source: DFLAT
    5. nuclear aryl hydrocarbon receptor complex Source: DFLAT
    6. nucleus Source: UniProtKB
    7. transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 992 PublicationsPRO_0000013452
    Chaini10 – 848839Aryl hydrocarbon receptorPRO_0000013453Add
    BLAST

    Proteomic databases

    PRIDEiP30561.

    PTM databases

    PhosphoSiteiP30561.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested including brain, heart, kidney, liver, lung, muscle, ovary, skin, spleen and thymus.1 Publication

    Developmental stagei

    Between E10 and E12, abundantly expressed in neuroepithelium, branchial arches, cranial nerves, liver, heart and spinal ganglia.1 Publication

    Inductioni

    Induced or repressed by TGF-beta and dioxin in a cell-type specific fashion. Repressed by cAMP, retinoic acid, and TPA.1 Publication

    Gene expression databases

    GenevestigatoriP30561.

    Interactioni

    Subunit structurei

    Interacts with IVNS1ABP 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 MYBBP1A and NEDD8. Interacts with ARNTL/BMAL1.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    arntP798322EBI-78863,EBI-958635From a different organism.

    Protein-protein interaction databases

    BioGridi198037. 3 interactions.
    DIPiDIP-222N.
    IntActiP30561. 4 interactions.

    Structurei

    Secondary structure

    1
    848
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi110 – 1134
    Helixi114 – 1196
    Beta strandi120 – 1289
    Beta strandi131 – 1366
    Helixi140 – 1434
    Helixi148 – 1514
    Helixi156 – 1583
    Turni162 – 1643
    Helixi165 – 1728
    Beta strandi211 – 2199
    Beta strandi225 – 24016
    Beta strandi256 – 26510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4M4XX-ray2.55A/B110-267[»]
    ProteinModelPortaliP30561.
    SMRiP30561. Positions 30-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 7954bHLHPROSITE-ProRule annotationAdd
    BLAST
    Domaini116 – 17964PAS 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini269 – 33668PAS 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini342 – 38039PACAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi594 – 64855Gln-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.
    HOGENOMiHOG000252935.
    HOVERGENiHBG007313.
    KOiK09093.
    PhylomeDBiP30561.

    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.

    P30561-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSGANITYA SRKRRKPVQK TVKPIPAEGI KSNPSKRHRD RLNTELDRLA    50
    SLLPFPQDVI NKLDKLSVLR LSVSYLRAKS FFDVALKSTP ADRNGGQDQC 100
    RAQIRDWQDL QEGEFLLQAL NGFVLVVTAD ALVFYASSTI QDYLGFQQSD 150
    VIHQSVYELI HTEDRAEFQR QLHWALNPDS AQGVDEAHGP PQAAVYYTPD 200
    QLPPENASFM ERCFRCRLRC LLDNSSGFLA MNFQGRLKYL HGQNKKGKDG 250
    ALLPPQLALF AIATPLQPPS ILEIRTKNFI FRTKHKLDFT PIGCDAKGQL 300
    ILGYTEVELC TRGSGYQFIH AADMLHCAES HIRMIKTGES GMTVFRLFAK 350
    HSRWRWVQSN ARLIYRNGRP DYIIATQRPL TDEEGREHLQ KRSTSLPFMF 400
    ATGEAVLYEI SSPFSPIMDP LPIRTKSNTS RKDWAPQSTP SKDSFHPSSL 450
    MSALIQQDES IYLCPPSSPA PLDSHFLMGS VSKCGSWQDS FAAAGSEAAL 500
    KHEQIGHAQD VNLALSGGPS ELFPDNKNND LYNIMRNLGI DFEDIRSMQN 550
    EEFFRTDSTA AGEVDFKDID ITDEILTYVQ DSLNNSTLMN SACQQQPVTQ 600
    HLSCMLQERL QLEQQQQLQQ PPPQALEPQQ QLCQMVCPQQ DLGPKHTQIN 650
    GTFASWNPTP PVSFNCPQQE LKHYQLFSSL QGTAQEFPYK PEVDSVPYTQ 700
    NFAPCNQPLL PEHSKSVQLD FPGRDFEPSL HPTTSNLDFV SCLQVPENQS 750
    HGINSQSTMV SPQAYYAGAM SMYQCQPGPQ RTPVDQTQYS SEIPGSQAFL 800
    SKVQSRGIFN ETYSSDLSSI GHAAQTTGHL HHLAEARPLP DITPGGFL 848
    Length:848
    Mass (Da):95,017
    Last modified:March 25, 2003 - v3
    Checksum:iAA1560FA83DDD03C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti74 – 741S → T(PubMed:1325649)Curated
    Sequence conflicti74 – 741S → T(PubMed:8148872)Curated
    Sequence conflicti132 – 1332LV → FL(PubMed:1314586)Curated
    Sequence conflicti132 – 1332LV → FL(PubMed:8408082)Curated
    Sequence conflicti171 – 1722QL → HV(PubMed:1314586)Curated
    Sequence conflicti171 – 1722QL → HV(PubMed:8408082)Curated
    Sequence conflicti351 – 3511H → N in D38416. (PubMed:7961644)Curated

    Polymorphismi

    There are four common alleles; AHRB1; AHRB2; AHRB3 and AHRD. The sequence of AHRB2 is shown here.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti324 – 3241M → I in allele AHRB1; no increase in specific ligand binding. 6 Publications
    Natural varianti348 – 3481F → L in allele AHRB1 and allele AHRD; no reduction in specific ligand binding. 7 Publications
    Natural varianti375 – 3751A → V in allele AHRD; reduced specific ligand binding. 5 Publications
    Natural varianti471 – 4711P → L in allele AHRB1; no increase in specific ligand binding. 6 Publications
    Natural varianti533 – 5331N → S in allele AHRB1; no increase in specific ligand binding. 6 Publications
    Natural varianti589 – 5891M → I in allele AHRD. 2 Publications
    Natural varianti589 – 5891M → L in allele AHRB1; no increase in specific ligand binding. 5 Publications
    Natural varianti758 – 7581T → A in allele AHRB1 and allele AHRD. 7 Publications
    Natural varianti806 – 84843Missing in allele AHRB1.
    Add
    BLAST
    Natural varianti808 – 8081I → V in allele AHRB3. 1 Publication
    Natural varianti821 – 8211G → D in allele AHRB3. 1 Publication
    Natural varianti824 – 8241A → V in allele AHRB3. 1 Publication
    Natural varianti843 – 8486TPGGFL → SHLVGSCSSHARMKFIQEQD TGTVRVGHQYYFSKTFDSCI in allele AHRB3.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38417 mRNA. Translation: BAA07469.1.
    M94623 Unassigned DNA. Translation: AAA02896.1.
    L19749 Unassigned DNA. No translation available.
    L19750 Unassigned DNA. No translation available.
    L19751 Unassigned DNA. No translation available.
    L19752 Unassigned DNA. No translation available.
    L19753 Unassigned DNA. No translation available.
    L19754 Unassigned DNA. No translation available.
    L19755 Unassigned DNA. No translation available.
    L19756 Unassigned DNA. No translation available.
    L19757 Unassigned DNA. No translation available.
    L19758 Unassigned DNA. No translation available.
    L19759 Unassigned DNA. No translation available.
    D38416 mRNA. No translation available.
    AF325111 Genomic DNA. Translation: AAK13443.1.
    AF405560 mRNA. Translation: AAL89725.1.
    AF405561 mRNA. Translation: AAL89726.1.
    AF405562 mRNA. Translation: AAL89727.1.
    AF405563 mRNA. Translation: AAL89728.1.
    AF405566 mRNA. Translation: AAL89731.1.
    AF405567 mRNA. Translation: AAL89732.1.
    AF405570 mRNA. Translation: AAL89735.1.
    PIRiA46266.
    RefSeqiNP_038492.1. NM_013464.4.
    UniGeneiMm.341377.

    Genome annotation databases

    GeneIDi11622.
    KEGGimmu:11622.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38417 mRNA. Translation: BAA07469.1 .
    M94623 Unassigned DNA. Translation: AAA02896.1 .
    L19749 Unassigned DNA. No translation available.
    L19750 Unassigned DNA. No translation available.
    L19751 Unassigned DNA. No translation available.
    L19752 Unassigned DNA. No translation available.
    L19753 Unassigned DNA. No translation available.
    L19754 Unassigned DNA. No translation available.
    L19755 Unassigned DNA. No translation available.
    L19756 Unassigned DNA. No translation available.
    L19757 Unassigned DNA. No translation available.
    L19758 Unassigned DNA. No translation available.
    L19759 Unassigned DNA. No translation available.
    D38416 mRNA. No translation available.
    AF325111 Genomic DNA. Translation: AAK13443.1 .
    AF405560 mRNA. Translation: AAL89725.1 .
    AF405561 mRNA. Translation: AAL89726.1 .
    AF405562 mRNA. Translation: AAL89727.1 .
    AF405563 mRNA. Translation: AAL89728.1 .
    AF405566 mRNA. Translation: AAL89731.1 .
    AF405567 mRNA. Translation: AAL89732.1 .
    AF405570 mRNA. Translation: AAL89735.1 .
    PIRi A46266.
    RefSeqi NP_038492.1. NM_013464.4.
    UniGenei Mm.341377.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4M4X X-ray 2.55 A/B 110-267 [» ]
    ProteinModelPortali P30561.
    SMRi P30561. Positions 30-386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198037. 3 interactions.
    DIPi DIP-222N.
    IntActi P30561. 4 interactions.

    Chemistry

    BindingDBi P30561.
    ChEMBLi CHEMBL6099.

    PTM databases

    PhosphoSitei P30561.

    Proteomic databases

    PRIDEi P30561.

    Protocols and materials databases

    DNASUi 11622.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 11622.
    KEGGi mmu:11622.

    Organism-specific databases

    CTDi 196.
    MGIi MGI:105043. Ahr.

    Phylogenomic databases

    eggNOGi NOG253623.
    HOGENOMi HOG000252935.
    HOVERGENi HBG007313.
    KOi K09093.
    PhylomeDBi P30561.

    Miscellaneous databases

    ChiTaRSi AHR. mouse.
    NextBioi 279171.
    PROi P30561.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori P30561.

    Family and domain databases

    Gene3Di 4.10.280.10. 1 hit.
    InterProi IPR011598. bHLH_dom.
    IPR001610. PAC.
    IPR000014. PAS.
    IPR013767. PAS_fold.
    IPR013655. PAS_fold_3.
    [Graphical view ]
    Pfami PF00010. HLH. 1 hit.
    PF00989. PAS. 1 hit.
    PF08447. PAS_3. 1 hit.
    [Graphical view ]
    SMARTi SM00353. HLH. 1 hit.
    SM00086. PAC. 1 hit.
    SM00091. PAS. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47459. SSF47459. 1 hit.
    SSF55785. SSF55785. 2 hits.
    PROSITEi PS50888. BHLH. 1 hit.
    PS50112. PAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANTS ILE-324; LEU-348; LEU-471; SER-533; LEU-589 AND ALA-758.
      Strain: C57L.
      Tissue: Hepatoma.
    2. "Cloning of the Ah-receptor cDNA reveals a distinctive ligand-activated transcription factor."
      Burbach K.M., Poland A., Bradfield C.A.
      Proc. Natl. Acad. Sci. U.S.A. 89:8185-8189(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 10-36; 232-261; 335-350 AND 636-646, VARIANTS ILE-324; LEU-348; LEU-471; SER-533; LEU-589 AND ALA-758.
      Strain: C57BL/6J and C57L.
      Tissue: Liver.
    3. "Ten nucleotide differences, five of which cause amino acid changes, are associated with the Ah receptor locus polymorphism of C57BL/6 and DBA/2 mice."
      Chang C.-Y., Smith D.R., Prasad V.S., Sidman C.L., Nebert D.W., Puga A.
      Pharmacogenetics 3:312-321(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE, VARIANTS ILE-324; LEU-348; VAL-375; LEU-471; SER-533; LEU-589 AND ALA-758.
      Strain: C57BL/6J and DBA/2J.
    4. "Molecular characterization of the murine Ahr gene. Organization, promoter analysis, and chromosomal assignment."
      Schmidt J.V., Carver L.A., Bradfield C.A.
      J. Biol. Chem. 268:22203-22209(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    5. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANTS ILE-324; LEU-348; VAL-375; LEU-471; SER-533; LEU-589 AND ALA-758, CHARACTERIZATION OF VARIANTS ILE-324; VAL-375; LEU-471; SER-533 AND LEU-589.
      Strain: C57BL/6 and DBA/2J.
      Tissue: Liver.
    6. "Analysis of the four alleles of the murine aryl hydrocarbon receptor."
      Poland A., Palen D., Glover E.
      Mol. Pharmacol. 46:915-921(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE, FUNCTION, VARIANTS ILE-324; LEU-348; VAL-375; LEU-471; SER-533; LEU-589; ALA-758; VAL-808; ASP-821 AND VAL-824, CHARACTERIZATION OF VARIANTS LEU-348 AND VAL-375.
      Strain: C57BL/6.
    7. "Mouse aryl-hydrocarbon receptor (AhR) genomic region."
      Hadd A.G., Nguyen L.P., Garrigues C.S., Thomas R.S., Rank D.R., Penn S.G., LaPres J.J., Roach D., Blaga I., Schneider J., Shilova K., Bradfield C.A., Jovanovich S.B.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-348; VAL-375; ILE-589 AND ALA-758.
      Strain: 129/SvJ.
    8. "Sequence variation and phylogenetic history of the mouse Ahr gene."
      Thomas R.S., Penn S.G., Holden K., Bradfield C.A., Rank D.R.
      Pharmacogenetics 12:151-163(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ILE-324; LEU-348; VAL-375; LEU-471; SER-533; ILE-589 AND ALA-758.
      Strain: A/J, BALB/cBY, C3H/HeJ, C57BL/6J, CBA/J, DBA/2J and SJL/J.
    9. "Purification and N-terminal amino acid sequence of the Ah receptor from the C57BL/6J mouse."
      Bradfield C.A., Glover E., Poland A.
      Mol. Pharmacol. 39:13-19(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 10-36.
    10. "Differential regulation of mouse Ah receptor gene expression in cell lines of different tissue origins."
      FitzGerald C.T., Fernandez-Salguero P., Gonzalez F.J., Nebert D.W., Puga A.
      Arch. Biochem. Biophys. 333:170-178(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    11. "Aryl-hydrocarbon receptor-deficient mice are resistant to 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced toxicity."
      Fernandez-Salguero P.M., Hilbert D.M., Rudikoff S., Ward J.M., Gonzalez F.J.
      Toxicol. Appl. Pharmacol. 140:173-179(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Loss of teratogenic response to 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) in mice lacking the Ah (dioxin) receptor."
      Mimura J., Yamashita K., Nakamura K., Morita M., Takagi T.N., Nakao K., Ema M., Sogawa K., Yasuda M., Katsuki M., Fujii-Kuriyama Y.
      Genes Cells 2:645-654(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Portosystemic shunting and persistent fetal vascular structures in aryl hydrocarbon receptor-deficient mice."
      Lahvis G.P., Lindell S.L., Thomas R.S., McCuskey R.S., Murphy C., Glover E., Bentz M., Southard J., Bradfield C.A.
      Proc. Natl. Acad. Sci. U.S.A. 97:10442-10447(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Benzoapyrene carcinogenicity is lost in mice lacking the aryl hydrocarbon receptor."
      Shimizu Y., Nakatsuru Y., Ichinose M., Takahashi Y., Kume H., Mimura J., Fujii-Kuriyama Y., Ishikawa T.
      Proc. Natl. Acad. Sci. U.S.A. 97:779-782(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    15. "Myb-binding protein 1a augments AhR-dependent gene expression."
      Jones L.C., Okino S.T., Gonda T.J., Whitlock J.P. Jr.
      J. Biol. Chem. 277:22515-22519(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYBBP1A.
    16. "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.
    17. "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, LACK OF NEDDYLATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    18. "Disruption of CLOCK-BMAL1 transcriptional activity is responsible for aryl hydrocarbon receptor-mediated regulation of Period1 gene."
      Xu C.X., Krager S.L., Liao D.F., Tischkau S.A.
      Toxicol. Sci. 115:98-108(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARNTL.

    Entry informationi

    Entry nameiAHR_MOUSE
    AccessioniPrimary (citable) accession number: P30561
    Secondary accession number(s): Q8QZX6
    , Q8R4S3, Q99P79, Q9QVY1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: March 25, 2003
    Last modified: October 1, 2014
    This is version 149 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Although it interacts with NEDD8, it does not seem to be neddylated.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3