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UniProtKB - P30561 (AHR_MOUSE)

Entry version 190 (16 Oct 2019)
Sequence version 3 (25 Mar 2003)
Previous versions | rss
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Protein

Aryl hydrocarbon receptor

Gene

Ahr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:28396409).9 Publications

Miscellaneous

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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding, Receptor, Repressor
Biological processBiological rhythms, Cell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-211945 Phase I - Functionalization of compounds
R-MMU-211976 Endogenous sterols
R-MMU-211981 Xenobiotics
R-MMU-8937144 Aryl hydrocarbon receptor signalling

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Aryl hydrocarbon receptor
Short name:
Ah receptor
Short name:
AhR
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Ahr
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:105043 Ahr

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

AHR knockdown in the retina results in reduced electroretinogram responses, thinning of the outer segment, and degeneration of photoreceptors.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi39R → D: Drastically reduces the binding affinity of AHR?ARNT to dioxin response element (DRE). Impairs ligand-induced nuclear translocation of AHR. 1 Publication1
Mutagenesisi42L → E: Significantly reduces binding affinities of the AHR?ARNT heterodimer to DRE. 1 Publication1
Mutagenesisi43N → A: Reduces the binding affinity of AHR?ARNT to the DRE by more than 10-fold. 1 Publication1
Mutagenesisi49L → E: Reduces the AHR induction transcription activity by 50%. Increases ligand-induced nuclear translocation of AHR. 1 Publication1
Mutagenesisi65K → E: Reduces the binding affinity of AHR?ARNT to the DRE by more than 10-fold. 1 Publication1
Mutagenesisi70R → D: Drastically reduces the AHR transcription activity inductiona. Increases constitutive AHR nuclear translocation in the absence of ligands. Reduces binding affinity for the DRE by more than 30-fold in vitro. 1 Publication1
Mutagenesisi112E → A: Reduces transcription activity. Decreases interaction with ARNT. 1 Publication1
Mutagenesisi115F → A: Highly disrupts the dimerization ability of AHR. 1 Publication1
Mutagenesisi115F → D: Highly disrupts the dimerization ability of AHR. Reduces the AHR transcription factor activity induction by 50%. 2 Publications1
Mutagenesisi116L → E: Highly disrupts the dimerization ability of AHR. Reduces transcription activity. Decreases interaction with ARNT. 1 Publication1
Mutagenesisi119A → D: Highly disrupts the dimerization ability of AHR. Reduces transcription activity. Impairs interaction with ARNT. 1 Publication1
Mutagenesisi120L → D: Significantly reduces binding affinities of the AHR?ARNT heterodimer to DRE. 1 Publication1
Mutagenesisi120L → E: Highly disrupts the dimerization ability of AHR. Reduces transcription activity. Impairs interaction with ARNT. 1 Publication1
Mutagenesisi124V → D: Highly disrupts the dimerization ability of AHR. Reduces transcription activity. Impairs interaction with ARNT. 1 Publication1
Mutagenesisi134F → D: Reduces the AHR induction activity by ?50%. Translocate to thee nucleus at a high level. 1 Publication1
Mutagenesisi152I → D: Completely abolished the AHR induction activity, the ligand-induced nuclear translocation of AHR, and drastically reduced DRE-binding in vitro. 1 Publication1
Mutagenesisi238K → D: Significantly reduces binding affinities of the AHR?ARNT heterodimer to DRE. 1 Publication1
Mutagenesisi240L → D: Significantly reduces binding affinities of the AHR?ARNT heterodimer to DRE. 1 Publication1
Mutagenesisi260F → D: Reduces transcription activity. Impairs interaction with ARNT. 1 Publication1
Mutagenesisi262I → D: Reduces transcription activity. Decreases interaction with ARNT. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL6099

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2951

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00000134521 – 92 Publications9
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001345310 – 848Aryl hydrocarbon receptorAdd BLAST839

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Mono-ADP-ribosylated, leading to inhibit transcription activator activity of AHR.By similarity

Keywords - PTMi

ADP-ribosylation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P30561

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P30561

PRoteomics IDEntifications database

More...PRIDEi		P30561

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P30561

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P30561

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Between 10 dpc and 12 dpc, abundantly expressed in neuroepithelium, branchial arches, cranial nerves, liver, heart and spinal ganglia.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:24001774).

Interacts with IVNS1ABP (By similarity). Efficient DNA binding requires dimerization with another bHLH protein.

Interacts with coactivators including SRC-1, RIP140 and NOCA7, and with the corepressor SMRT.

Interacts with MYBBP1A and NEDD8 (PubMed:11956195, PubMed:12215427).

Interacts with ARNTL/BMAL1 (PubMed:20106950).

Interacts with HSP90AB1 (PubMed:15581363).

Interacts with ARNT; the heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:24001774, PubMed:28396409).

Interacts with TIPARP; leading to mono-ADP-ribosylation of AHR and subsequent inhibition of AHR (By similarity).

By similarity6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		198037, 8 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P30561

Database of interacting proteins

More...DIPi		DIP-222N

Protein interaction database and analysis system

More...IntActi		P30561, 7 interactors

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000112137

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P30561

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1848
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P30561

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini26 – 79bHLHPROSITE-ProRule annotationAdd BLAST54
Domaini116 – 179PAS 1PROSITE-ProRule annotationAdd BLAST64
Domaini269 – 336PAS 2PROSITE-ProRule annotationAdd BLAST68
Domaini342 – 380PACAdd BLAST39

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni37 – 65DNA-bindingBy similarityAdd BLAST29
Regioni116 – 124Required for maintaining the overall integrity of the AHR:ARNT heterodimer and its transcriptional activity1 Publication9
Regioni260 – 262Required for maintaining the overall integrity of the AHR:ARNT heterodimer and its transcriptional activity1 Publication3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi594 – 648Gln-richAdd BLAST55

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The PAS 1 domain is essential for dimerization and also required for AHR:ARNT heterodimerization.1 Publication

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3560 Eukaryota
ENOG410XRZH LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000252935

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P30561

KEGG Orthology (KO)

More...KOi		K09093

Database of Orthologous Groups

More...OrthoDBi		174264at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P30561

Family and domain databases

Conserved Domains Database

More...CDDi		cd00083 HLH, 1 hit
cd00130 PAS, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		4.10.280.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR033348 AHR
IPR039091 AHR/AHRR
IPR011598 bHLH_dom
IPR036638 HLH_DNA-bd_sf
IPR001610 PAC
IPR000014 PAS
IPR035965 PAS-like_dom_sf
IPR013767 PAS_fold
IPR013655 PAS_fold_3

The PANTHER Classification System

More...PANTHERi		PTHR10649 PTHR10649, 1 hit
PTHR10649:SF9 PTHR10649:SF9, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00010 HLH, 1 hit
PF00989 PAS, 1 hit
PF08447 PAS_3, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00353 HLH, 1 hit
SM00086 PAC, 1 hit
SM00091 PAS, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47459 SSF47459, 1 hit
SSF55785 SSF55785, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50888 BHLH, 1 hit
PS50112 PAS, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P30561-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSGANITYA SRKRRKPVQK TVKPIPAEGI KSNPSKRHRD RLNTELDRLA 
        60         70         80         90        100
SLLPFPQDVI NKLDKLSVLR LSVSYLRAKS FFDVALKSTP ADRNGGQDQC 
       110        120        130        140        150
RAQIRDWQDL QEGEFLLQAL NGFVLVVTAD ALVFYASSTI QDYLGFQQSD 
       160        170        180        190        200
VIHQSVYELI HTEDRAEFQR QLHWALNPDS AQGVDEAHGP PQAAVYYTPD 
       210        220        230        240        250
QLPPENASFM ERCFRCRLRC LLDNSSGFLA MNFQGRLKYL HGQNKKGKDG 
       260        270        280        290        300
ALLPPQLALF AIATPLQPPS ILEIRTKNFI FRTKHKLDFT PIGCDAKGQL 
       310        320        330        340        350
ILGYTEVELC TRGSGYQFIH AADMLHCAES HIRMIKTGES GMTVFRLFAK 
       360        370        380        390        400
HSRWRWVQSN ARLIYRNGRP DYIIATQRPL TDEEGREHLQ KRSTSLPFMF 
       410        420        430        440        450
ATGEAVLYEI SSPFSPIMDP LPIRTKSNTS RKDWAPQSTP SKDSFHPSSL 
       460        470        480        490        500
MSALIQQDES IYLCPPSSPA PLDSHFLMGS VSKCGSWQDS FAAAGSEAAL 
       510        520        530        540        550
KHEQIGHAQD VNLALSGGPS ELFPDNKNND LYNIMRNLGI DFEDIRSMQN 
       560        570        580        590        600
EEFFRTDSTA AGEVDFKDID ITDEILTYVQ DSLNNSTLMN SACQQQPVTQ 
       610        620        630        640        650
HLSCMLQERL QLEQQQQLQQ PPPQALEPQQ QLCQMVCPQQ DLGPKHTQIN 
       660        670        680        690        700
GTFASWNPTP PVSFNCPQQE LKHYQLFSSL QGTAQEFPYK PEVDSVPYTQ 
       710        720        730        740        750
NFAPCNQPLL PEHSKSVQLD FPGRDFEPSL HPTTSNLDFV SCLQVPENQS 
       760        770        780        790        800
HGINSQSTMV SPQAYYAGAM SMYQCQPGPQ RTPVDQTQYS SEIPGSQAFL 
       810        820        830        840 
SKVQSRGIFN ETYSSDLSSI GHAAQTTGHL HHLAEARPLP DITPGGFL
Length:848
Mass (Da):95,017
Last modified:March 25, 2003 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iAA1560FA83DDD03C
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q3U5D9Q3U5D9_MOUSE
Aryl hydrocarbon receptor
Ahr
805Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0B4J1L1A0A0B4J1L1_MOUSE
Aryl hydrocarbon receptor
Ahr
114Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti74S → T (PubMed:1325649).Curated1
Sequence conflicti74S → T (PubMed:8148872).Curated1
Sequence conflicti132 – 133LV → FL (PubMed:1314586).Curated2
Sequence conflicti132 – 133LV → FL (PubMed:8408082).Curated2
Sequence conflicti171 – 172QL → HV (PubMed:1314586).Curated2
Sequence conflicti171 – 172QL → HV (PubMed:8408082).Curated2
Sequence conflicti351H → N in D38416 (PubMed:7961644).Curated1

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti324M → I in allele AHRB1; no increase in specific ligand binding. 6 Publications1
Natural varianti348F → L in allele AHRB1 and allele AHRD; no reduction in specific ligand binding. 7 Publications1
Natural varianti375A → V in allele AHRD; reduced specific ligand binding. 5 Publications1
Natural varianti471P → L in allele AHRB1; no increase in specific ligand binding. 6 Publications1
Natural varianti533N → S in allele AHRB1; no increase in specific ligand binding. 6 Publications1
Natural varianti589M → I in allele AHRD. 2 Publications1
Natural varianti589M → L in allele AHRB1; no increase in specific ligand binding. 5 Publications1
Natural varianti758T → A in allele AHRB1 and allele AHRD. 7 Publications1
Natural varianti806 – 848Missing in allele AHRB1. Add BLAST43
Natural varianti808I → V in allele AHRB3. 1 Publication1
Natural varianti821G → D in allele AHRB3. 1 Publication1
Natural varianti824A → V in allele AHRB3. 1 Publication1
Natural varianti843 – 848TPGGFL → SHLVGSCSSHARMKFIQEQD TGTVRVGHQYYFSKTFDSCI in allele AHRB3. 6

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
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

Protein sequence database of the Protein Information Resource

More...PIRi		A46266

NCBI Reference Sequences

More...RefSeqi		NP_038492.1, NM_013464.4

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		11622

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:11622

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4M4XX-ray2.55A/B110-267[»]
5V0LX-ray4.00B29-267[»]
SMRiP30561
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi198037, 8 interactors
CORUMiP30561
DIPiDIP-222N
IntActiP30561, 7 interactors
STRINGi10090.ENSMUSP00000112137

Chemistry databases

BindingDBiP30561
ChEMBLiCHEMBL6099
GuidetoPHARMACOLOGYi2951

PTM databases

iPTMnetiP30561
PhosphoSitePlusiP30561

Proteomic databases

MaxQBiP30561
PaxDbiP30561
PRIDEiP30561

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		11622

Genome annotation databases

GeneIDi11622
KEGGimmu:11622

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		196
MGIiMGI:105043 Ahr

Phylogenomic databases

eggNOGiKOG3560 Eukaryota
ENOG410XRZH LUCA
HOGENOMiHOG000252935
InParanoidiP30561
KOiK09093
OrthoDBi174264at2759
PhylomeDBiP30561

Enzyme and pathway databases

ReactomeiR-MMU-211945 Phase I - Functionalization of compounds
R-MMU-211976 Endogenous sterols
R-MMU-211981 Xenobiotics
R-MMU-8937144 Aryl hydrocarbon receptor signalling

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Ahr mouse

Protein Ontology

More...PROi		PR:P30561

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Family and domain databases

CDDicd00083 HLH, 1 hit
cd00130 PAS, 2 hits
Gene3Di4.10.280.10, 1 hit
InterProiView protein in InterPro
IPR033348 AHR
IPR039091 AHR/AHRR
IPR011598 bHLH_dom
IPR036638 HLH_DNA-bd_sf
IPR001610 PAC
IPR000014 PAS
IPR035965 PAS-like_dom_sf
IPR013767 PAS_fold
IPR013655 PAS_fold_3
PANTHERiPTHR10649 PTHR10649, 1 hit
PTHR10649:SF9 PTHR10649:SF9, 1 hit
PfamiView protein in Pfam
PF00010 HLH, 1 hit
PF00989 PAS, 1 hit
PF08447 PAS_3, 1 hit
SMARTiView protein in SMART
SM00353 HLH, 1 hit
SM00086 PAC, 1 hit
SM00091 PAS, 2 hits
SUPFAMiSSF47459 SSF47459, 1 hit
SSF55785 SSF55785, 2 hits
PROSITEiView protein in PROSITE
PS50888 BHLH, 1 hit
PS50112 PAS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAHR_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P30561
Secondary accession number(s): Q8QZX6
, Q8R4S3, Q99P79, Q9QVY1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: March 25, 2003
Last modified: October 16, 2019
This is version 190 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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
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