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P30561 (AHR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Gene names
Name:Ahr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.1 Ref.5 Ref.6 Ref.11 Ref.12 Ref.13 Ref.14

Subunit structure

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. Binds MYBBP1A. Interacts with NEDD8. Ref.15 Ref.17

Subcellular location

Cytoplasm. Nucleus. Note: Initially cytoplasmic; upon binding with ligand and interaction with a HSP90, it translocates to the nucleus. Ref.17

Tissue specificity

Expressed in all tissues tested including brain, heart, kidney, liver, lung, muscle, ovary, skin, spleen and thymus. Ref.14

Developmental stage

Between E10 and E12, abundantly expressed in neuroepithelium, branchial arches, cranial nerves, liver, heart and spinal ganglia. Ref.17

Induction

Induced or repressed by TGF-beta and dioxin in a cell-type specific fashion. Repressed by cAMP, retinoic acid, and TPA. Ref.10

Polymorphism

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

Miscellaneous

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

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
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Traceable author statement PubMed 15681594. Source: DFLAT

B cell homeostasis

Inferred from mutant phenotype PubMed 7732381. Source: DFLAT

B-1 B cell homeostasis

Traceable author statement PubMed 15681594. Source: DFLAT

T cell homeostasis

Inferred from mutant phenotype PubMed 7732381. Source: DFLAT

blood circulation

Inferred from mutant phenotype Ref.13. Source: DFLAT

blood vessel development

Inferred from mutant phenotype Ref.13. Source: DFLAT

blood vessel morphogenesis

Inferred from mutant phenotype Ref.13. Source: DFLAT

blood vessel remodeling

Inferred from mutant phenotype Ref.13. Source: DFLAT

camera-type eye development

Inferred from mutant phenotype Ref.13. Source: DFLAT

cardiac left ventricle morphogenesis

Inferred from mutant phenotype PubMed 14644620. Source: DFLAT

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell morphogenesis

Inferred from mutant phenotype Ref.13PubMed 16443691. Source: DFLAT

cellular response to cAMP

Inferred from direct assay PubMed 17329248. Source: UniProtKB

circumferential growth involved in left ventricle morphogenesis

Inferred from mutant phenotype PubMed 14644620. Source: DFLAT

common bile duct development

Inferred from mutant phenotype PubMed 16443691. Source: DFLAT

embryonic hemopoiesis

Inferred from mutant phenotype PubMed 16443691. Source: DFLAT

gland development

Inferred from mutant phenotype PubMed 12151645. Source: MGI

glomerulus morphogenesis

Inferred from mutant phenotype PubMed 14644620. Source: DFLAT

immune system process

Inferred from mutant phenotype PubMed 7732381. Source: DFLAT

intracellular receptor signaling pathway

Inferred from direct assay Ref.1. Source: GOC

kidney morphogenesis

Inferred from mutant phenotype PubMed 14644620. Source: DFLAT

liver development

Inferred from mutant phenotype Ref.13PubMed 16443691PubMed 7732381PubMed 8692887. Source: DFLAT

lymphocyte homeostasis

Inferred from mutant phenotype PubMed 7732381. Source: DFLAT

negative regulation of necrotic cell death

Inferred from mutant phenotype PubMed 16443691. Source: DFLAT

negative regulation of systemic arterial blood pressure

Inferred from mutant phenotype PubMed 14644620. Source: DFLAT

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18223155. Source: MGI

negative regulation of vasoconstriction

Inferred from mutant phenotype PubMed 14644620. Source: DFLAT

patterning of blood vessels

Inferred from mutant phenotype Ref.13. Source: DFLAT

positive regulation of RNA polymerase II transcriptional preinitiation complex assembly

Inferred from direct assay PubMed 8215422. Source: MGI

positive regulation of cell size

Inferred from mutant phenotype Ref.13. Source: DFLAT

positive regulation of growth rate

Inferred from mutant phenotype PubMed 7732381PubMed 8692887. Source: DFLAT

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 1313028. Source: MGI

post-embryonic hemopoiesis

Inferred from mutant phenotype PubMed 8692887. Source: DFLAT

prostate gland development

Inferred from mutant phenotype PubMed 12151645. Source: MGI

regulation of blood pressure

Traceable author statement PubMed 16443691. Source: DFLAT

regulation of blood vessel size

Inferred from mutant phenotype PubMed 16443691. Source: DFLAT

regulation of heart growth

Traceable author statement PubMed 14644620PubMed 16443691. Source: DFLAT

regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

reproductive structure development

Inferred from mutant phenotype PubMed 12151645. Source: MGI

response to stress

Inferred from direct assay Ref.1. Source: UniProtKB

response to toxic substance

Inferred from direct assay PubMed 17329248. Source: UniProtKB

response to xenobiotic stimulus

Inferred from direct assay Ref.5. Source: UniProtKB

smooth muscle tissue development

Inferred from mutant phenotype PubMed 16443691. Source: DFLAT

spleen development

Inferred from mutant phenotype PubMed 7732381PubMed 8692887. Source: DFLAT

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: UniProtKB

venous blood vessel development

Inferred from mutant phenotype PubMed 16443691. Source: DFLAT

xenobiotic metabolic process

Traceable author statement PubMed 405846. Source: MGI

   Cellular_componentaryl hydrocarbon receptor complex

Traceable author statement PubMed 17569696. Source: DFLAT

cytoplasm

Inferred from direct assay Ref.17. Source: MGI

cytosol

Inferred from direct assay PubMed 17329248. Source: UniProtKB

cytosolic aryl hydrocarbon receptor complex

Traceable author statement PubMed 17569696. Source: DFLAT

nuclear aryl hydrocarbon receptor complex

Traceable author statement PubMed 17569696. Source: DFLAT

nucleus

Inferred from direct assay Ref.1PubMed 17329248. Source: UniProtKB

transcription factor complex

Traceable author statement PubMed 11025203. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 1313028. Source: MGI

Hsp90 protein binding

Traceable author statement PubMed 17569696. Source: DFLAT

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

Inferred from direct assay PubMed 18223155. Source: MGI

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

Inferred from direct assay Ref.1. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction PubMed 11230806. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 1605850. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 1313028PubMed 8215422. Source: MGI

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

arntP798322EBI-78863,EBI-958635From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 99
PRO_0000013452
Chain10 – 848839Aryl hydrocarbon receptor
PRO_0000013453

Regions

Domain26 – 7954bHLH
Domain116 – 17964PAS 1
Domain269 – 33668PAS 2
Domain342 – 38039PAC
Compositional bias594 – 64855Gln-rich

Natural variations

Natural variant3241M → I in allele AHRB1; no increase in specific ligand binding. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.8
Natural variant3481F → L in allele AHRB1 and allele AHRD; no reduction in specific ligand binding. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.7 Ref.8
Natural variant3751A → V in allele AHRD; reduced specific ligand binding. Ref.3 Ref.5 Ref.6 Ref.7 Ref.8
Natural variant4711P → L in allele AHRB1; no increase in specific ligand binding. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.8
Natural variant5331N → S in allele AHRB1; no increase in specific ligand binding. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.8
Natural variant5891M → I in allele AHRD. Ref.7 Ref.8
Natural variant5891M → L in allele AHRB1; no increase in specific ligand binding. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
Natural variant7581T → A in allele AHRB1 and allele AHRD. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.7 Ref.8
Natural variant806 – 84843Missing in allele AHRB1.
Natural variant8081I → V in allele AHRB3. Ref.6
Natural variant8211G → D in allele AHRB3. Ref.6
Natural variant8241A → V in allele AHRB3. Ref.6
Natural variant843 – 8486TPGGFL → SHLVGSCSSHARMKFIQEQD TGTVRVGHQYYFSKTFDSCI in allele AHRB3.

Experimental info

Sequence conflict741S → T Ref.2
Sequence conflict741S → T Ref.3
Sequence conflict132 – 1332LV → FL Ref.1
Sequence conflict132 – 1332LV → FL Ref.4
Sequence conflict171 – 1722QL → HV Ref.1
Sequence conflict171 – 1722QL → HV Ref.4
Sequence conflict3511H → N in D38416. Ref.5

Secondary structure

...................... 848
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30561 [UniParc].

Last modified March 25, 2003. Version 3.
Checksum: AA1560FA83DDD03C

FASTA84895,017
        10         20         30         40         50         60 
MSSGANITYA SRKRRKPVQK TVKPIPAEGI KSNPSKRHRD RLNTELDRLA SLLPFPQDVI 

        70         80         90        100        110        120 
NKLDKLSVLR LSVSYLRAKS FFDVALKSTP ADRNGGQDQC RAQIRDWQDL QEGEFLLQAL 

       130        140        150        160        170        180 
NGFVLVVTAD ALVFYASSTI QDYLGFQQSD VIHQSVYELI HTEDRAEFQR QLHWALNPDS 

       190        200        210        220        230        240 
AQGVDEAHGP PQAAVYYTPD QLPPENASFM ERCFRCRLRC LLDNSSGFLA MNFQGRLKYL 

       250        260        270        280        290        300 
HGQNKKGKDG ALLPPQLALF AIATPLQPPS ILEIRTKNFI FRTKHKLDFT PIGCDAKGQL 

       310        320        330        340        350        360 
ILGYTEVELC TRGSGYQFIH AADMLHCAES HIRMIKTGES GMTVFRLFAK HSRWRWVQSN 

       370        380        390        400        410        420 
ARLIYRNGRP DYIIATQRPL TDEEGREHLQ KRSTSLPFMF ATGEAVLYEI SSPFSPIMDP 

       430        440        450        460        470        480 
LPIRTKSNTS RKDWAPQSTP SKDSFHPSSL MSALIQQDES IYLCPPSSPA PLDSHFLMGS 

       490        500        510        520        530        540 
VSKCGSWQDS FAAAGSEAAL KHEQIGHAQD VNLALSGGPS ELFPDNKNND LYNIMRNLGI 

       550        560        570        580        590        600 
DFEDIRSMQN EEFFRTDSTA AGEVDFKDID ITDEILTYVQ DSLNNSTLMN SACQQQPVTQ 

       610        620        630        640        650        660 
HLSCMLQERL QLEQQQQLQQ PPPQALEPQQ QLCQMVCPQQ DLGPKHTQIN GTFASWNPTP 

       670        680        690        700        710        720 
PVSFNCPQQE LKHYQLFSSL QGTAQEFPYK PEVDSVPYTQ NFAPCNQPLL PEHSKSVQLD 

       730        740        750        760        770        780 
FPGRDFEPSL HPTTSNLDFV SCLQVPENQS HGINSQSTMV SPQAYYAGAM SMYQCQPGPQ 

       790        800        810        820        830        840 
RTPVDQTQYS SEIPGSQAFL SKVQSRGIFN ETYSSDLSSI GHAAQTTGHL HHLAEARPLP 


DITPGGFL 

« Hide

References

[1]"cDNA cloning and structure of mouse putative Ah receptor."
Ema M., Sogawa K., Watanabe N., Chujoh Y., Matsushita N., Gotoh O., Funae Y., Fujii-Kuriyama Y.
Biochem. Biophys. Res. Commun. 184:246-253(1992) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA46266.
RefSeqNP_038492.1. NM_013464.4.
UniGeneMm.341377.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4M4XX-ray2.55A/B110-267[»]
ProteinModelPortalP30561.
SMRP30561. Positions 31-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198037. 3 interactions.
DIPDIP-222N.
IntActP30561. 4 interactions.

Chemistry

BindingDBP30561.
ChEMBLCHEMBL6099.

PTM databases

PhosphoSiteP30561.

Proteomic databases

PRIDEP30561.

Protocols and materials databases

DNASU11622.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID11622.
KEGGmmu:11622.

Organism-specific databases

CTD196.
MGIMGI:105043. Ahr.

Phylogenomic databases

eggNOGNOG253623.
HOGENOMHOG000252935.
HOVERGENHBG007313.
KOK09093.
PhylomeDBP30561.

Gene expression databases

GenevestigatorP30561.

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. mouse.
NextBio279171.
PROP30561.
SOURCESearch...

Entry information

Entry nameAHR_MOUSE
AccessionPrimary (citable) accession number: P30561
Secondary accession number(s): Q8QZX6 expand/collapse secondary AC list , Q8R4S3, Q99P79, Q9QVY1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: March 25, 2003
Last modified: April 16, 2014
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot