AHR
entrez
196
canonical
uniprot
P35869
canonical
ensembl
ENSG00000106546
resolver
ensp
ENSP00000242057
resolver
ensp
ENSP00000436466
resolver
enst
ENST00000242057
resolver
enst
ENST00000463496
resolver
genesymbol
AHR
resolver
genesymbol_syn
BHLHE76
resolver
hgnc
HGNC:348
resolver
uniprot
A4D130
resolver
uniprot
Q13728
resolver
uniprot
Q13803
resolver
uniprot
Q13804
resolver
uniprot_entry
AHR_HUMAN
resolver
uniprot_sec
A4D130
resolver
uniprot_sec
Q13728
resolver
uniprot_sec
Q13803
resolver
uniprot_sec
Q13804
resolver
amino_acid_sequence
MNSSSANITYASRKRRKPVQKTVKPIPAEGIKSNPSKRHRDRLNTELDRLASLLPFPQDVINKLDKLSVLRLSVSYLRAKSFFDVALKSSPTERNGGQDNCRAANFREGLNLQEGEFLLQALNGFVLVVTTDALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALNPSQCTESGQGIEEATGLPQTVVCYNPDQIPPENSPLMERCFICRLRCLLDNSSGFLAMNFQGKLKYLHGQKKKGKDGSILPPQLALFAIATPLQPPSILEIRTKNFIFRTKHKLDFTPIGCDAKGRIVLGYTEAELCTRGSGYQFIHAADMLYCAESHIRMIKTGESGMIVFRLLTKNNRWTWVQSNARLLYKNGRPDYIIVTQRPLTDEEGTEHLRKRNTKLPFMFTTGEAVLYEATNPFPAIMDPLPLRTKNGTSGKDSATTSTLSKDSLNPSSLLAAMMQQDESIYLYPASSTSSTAPFENNFFNESMNECRNWQDNTAPMGNDTILKHEQIDQPQDVNSFAGGHPGLFQDSKNSDLYSIMKNLGIDFEDIRHMQNEKFFRNDFSGEVDFRDIDLTDEILTYVQDSLSKSPFIPSDYQQQQSLALNSSCMVQEHLHLEQQQQHHQKQVVVEPQQQLCQKMKHMQVNGMFENWNSNQFVPFNCPQQDPQQYNVFTDLHGISQEFPYKSEMDSMPYTQNFISCNQPVLPQHSKCTELDYPMGSFEPSPYPTTSSLEDFVTCLQLPENQKHGLNPQSAIITPQTCYAGAVSMYQCQPEPQHTHVGQMQYNPVLPGQQAFLNKFQNGVLNETYPAELNNINNTQTTTHLQPLHHPSEARPFPDLTSSGFL
uniprot
proteins
disease_involvement
DISEASE: Retinitis pigmentosa 85 (RP85) [MIM:618345]: A form of retinitis pigmentosa, a retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP85 is an autosomal recessive form manifesting as early-onset progressive difficulty to adapt in dim light and gradually decreasing visual acuity in both eyes. {ECO:0000269|PubMed:29726989}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Foveal hypoplasia 3 (FVH3) [MIM:620958]: An autosomal recessive form of foveal hypoplasia, a developmental defect of the eye defined as the lack of foveal depression with continuity of all neurosensory retinal layers in the presumed foveal area. Clinical features include absence of foveal pit on optical coherence tomography, absence of foveal hyperpigmentation, absence of foveal avascularity, absence of foveal and macular reflexes, decreased visual acuity, and nystagmus. {ECO:0000269|PubMed:31009037, ECO:0000269|PubMed:33193710, ECO:0000269|PubMed:35188035}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Ligand-activated transcription factor that enables cells to adapt to changing conditions by sensing compounds from the environment, diet, microbiome and cellular metabolism, and which plays important roles in development, immunity and cancer (PubMed:23275542, PubMed:30373764, PubMed:32818467, PubMed:7961644). Upon ligand binding, translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE) (PubMed:23275542, PubMed:30373764, PubMed:7961644). Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation (PubMed:12213388). Xenobiotics can act as ligands: upon xenobiotic-binding, activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene) (PubMed:7961644, PubMed:33193710). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons (PubMed:34521881, PubMed:7961644). Next to xenobiotics, natural ligands derived from plants, microbiota, and endogenous metabolism are potent AHR agonists (PubMed:18076143). Tryptophan (Trp) derivatives constitute an important class of endogenous AHR ligands (PubMed:32818467, PubMed:32866000). Acts as a negative regulator of anti-tumor immunity: indoles and kynurenic acid generated by Trp catabolism act as ligand and activate AHR, thereby promoting AHR-driven cancer cell motility and suppressing adaptive immunity (PubMed:32818467). Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1 (PubMed:28602820). Inhibits PER1 by repressing the CLOCK-BMAL1 heterodimer mediated transcriptional activation of PER1 (PubMed:28602820). The heterodimer ARNT:AHR binds to the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:28602820). {ECO:0000269|PubMed:23275542, ECO:0000269|PubMed:28602820, ECO:0000269|PubMed:30373764, ECO:0000269|PubMed:32818467, ECO:0000269|PubMed:32866000, ECO:0000269|PubMed:33193710, ECO:0000269|PubMed:34521881, ECO:0000269|PubMed:7961644, ECO:0000303|PubMed:12213388, ECO:0000303|PubMed:18076143}.
uniprot
proteins
mass_dalton
96147
uniprot
proteins
mutagenesis
MUTAGEN 36; /note="S->G: Strongly reduces transcription factor activity."; /evidence="ECO:0000269|PubMed:34521881"; MUTAGEN 39; /note="H->G: Almost abolishes transcription factor activity. No effect on nuclear translocation upon ligand binding."; /evidence="ECO:0000269|PubMed:34521881"; MUTAGEN 40; /note="R->D: Abolishes transcription factor activity. Alters on nuclear translocation upon ligand binding."; /evidence="ECO:0000269|PubMed:28602820, ECO:0000269|PubMed:34521881"; MUTAGEN 50; /note="L->D: Abolishes transcription factor activity; when associated with D-79 and D-82."; /evidence="ECO:0000269|PubMed:28602820, ECO:0000269|PubMed:34521881"; MUTAGEN 74; /note="V->D: Interferes with transcription factor activity."; /evidence="ECO:0000269|PubMed:28602820"; MUTAGEN 79; /note="A->D: Abolishes transcription factor activity; when associated with D-50 and D-82."; /evidence="ECO:0000269|PubMed:28602820, ECO:0000269|PubMed:34521881"; MUTAGEN 82; /note="F->D: Abolishes transcription factor activity; when associated with D-50 and D-79."; /evidence="ECO:0000269|PubMed:28602820, ECO:0000269|PubMed:34521881"; MUTAGEN 118..122; /note="LLQAL->ELQDE: Strongly reduces transcription factor activity."; /evidence="ECO:0000269|PubMed:34521881"; MUTAGEN 118; /note="L->D: Interferes with transcription factor activity."; /evidence="ECO:0000269|PubMed:28602820"; MUTAGEN 122; /note="L->D: Interferes with transcription factor activity."; /evidence="ECO:0000269|PubMed:28602820"; MUTAGEN 136; /note="F->D: Interferes with transcription factor activity."; /evidence="ECO:0000269|PubMed:28602820"; MUTAGEN 154; /note="I->D: Interferes with transcription factor activity."; /evidence="ECO:0000269|PubMed:28602820"; MUTAGEN 381; /note="V->A: Increases specific ligand binding."; /evidence="ECO:0000269|PubMed:7961644"; MUTAGEN 381; /note="V->D: Abolishes specific ligand binding."; /evidence="ECO:0000269|PubMed:7961644"; MUTAGEN 381; /note="V->L,G: No effect on specific ligand binding."; /evidence="ECO:0000269|PubMed:7961644
uniprot
proteins
post_translational_modification
PTM: Mono-ADP-ribosylated, leading to inhibit transcription activator activity of AHR. {ECO:0000269|PubMed:30373764}.
uniprot
proteins
pubmed
10395741
uniprot
proteins
pubmed
10739168
uniprot
proteins
pubmed
11259615
uniprot
proteins
pubmed
11689007
uniprot
proteins
pubmed
11698344
uniprot
proteins
pubmed
12213388
uniprot
proteins
pubmed
12213390
uniprot
proteins
pubmed
12215427
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16582008
uniprot
proteins
pubmed
16696038
uniprot
proteins
pubmed
18076143
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23275542
uniprot
proteins
pubmed
28602820
uniprot
proteins
pubmed
29726989
uniprot
proteins
pubmed
30373764
uniprot
proteins
pubmed
31009037
uniprot
proteins
pubmed
32818467
uniprot
proteins
pubmed
32866000
uniprot
proteins
pubmed
33193710
uniprot
proteins
pubmed
34521881
uniprot
proteins
pubmed
35188035
uniprot
proteins
pubmed
7515333
uniprot
proteins
pubmed
7550366
uniprot
proteins
pubmed
7883760
uniprot
proteins
pubmed
7961644
uniprot
proteins
pubmed
8246913
uniprot
proteins
pubmed
8393992
uniprot
proteins
sequence_length
848
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:34521881}. Nucleus {ECO:0000269|PubMed:34521881}. Note=Initially cytoplasmic; upon binding with ligand and interaction with a HSP90, it translocates to the nucleus. {ECO:0000269|PubMed:34521881}.
uniprot
proteins