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P30561

- AHR_MOUSE

UniProt

P30561 - AHR_MOUSE

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Protein
Aryl hydrocarbon receptor
Gene
Ahr
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 PER1.7 Publications

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. Hsp90 protein binding Source: DFLAT
  3. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: MGI
  4. enhancer binding Source: MGI
  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. sequence-specific DNA binding Source: MGI
  9. sequence-specific DNA binding transcription factor activity Source: MGI
  10. signal transducer activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. B cell differentiation Source: DFLAT
  2. B cell homeostasis Source: DFLAT
  3. B-1 B cell homeostasis Source: DFLAT
  4. T cell homeostasis Source: DFLAT
  5. blood circulation Source: DFLAT
  6. blood vessel development Source: DFLAT
  7. blood vessel morphogenesis Source: DFLAT
  8. blood vessel remodeling Source: DFLAT
  9. camera-type eye development Source: DFLAT
  10. cardiac left ventricle morphogenesis Source: DFLAT
  11. cell cycle Source: UniProtKB-KW
  12. cell morphogenesis Source: DFLAT
  13. cellular response to cAMP 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 from RNA polymerase II promoter Source: MGI
  27. negative regulation of vasoconstriction Source: DFLAT
  28. patterning of blood vessels Source: DFLAT
  29. positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: MGI
  30. positive regulation of cell size Source: DFLAT
  31. positive regulation of growth rate Source: DFLAT
  32. positive regulation of transcription, DNA-templated Source: MGI
  33. post-embryonic hemopoiesis Source: DFLAT
  34. prostate gland development Source: MGI
  35. regulation of blood pressure Source: DFLAT
  36. regulation of blood vessel size Source: DFLAT
  37. regulation of heart growth Source: DFLAT
  38. regulation of transcription, DNA-templated Source: UniProtKB
  39. reproductive structure development Source: MGI
  40. response to stress Source: UniProtKB
  41. response to toxic substance Source: UniProtKB
  42. response to xenobiotic stimulus Source: UniProtKB
  43. smooth muscle tissue development Source: DFLAT
  44. spleen development Source: DFLAT
  45. transcription from RNA polymerase II promoter Source: UniProtKB
  46. venous blood vessel development Source: DFLAT
  47. xenobiotic metabolic process Source: MGI
Complete GO annotation...

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.1 Publication

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 99
PRO_0000013452
Chaini10 – 848839Aryl hydrocarbon receptor
PRO_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/BMAL1.2 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

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 7954bHLH
Add
BLAST
Domaini116 – 17964PAS 1
Add
BLAST
Domaini269 – 33668PAS 2
Add
BLAST
Domaini342 – 38039PAC
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi594 – 64855Gln-rich
Add
BLAST

Sequence similaritiesi

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741S → T1 Publication
Sequence conflicti74 – 741S → T1 Publication
Sequence conflicti132 – 1332LV → FL1 Publication
Sequence conflicti132 – 1332LV → FL1 Publication
Sequence conflicti171 – 1722QL → HV1 Publication
Sequence conflicti171 – 1722QL → HV1 Publication
Sequence conflicti351 – 3511H → N in D38416. 1 Publication

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...

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: September 3, 2014
This is version 148 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

Similar proteinsi