P53762 · ARNT_MOUSE
- ProteinAryl hydrocarbon receptor nuclear translocator
- GeneArnt
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids791 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens (By similarity).
The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia (PubMed:26245371, PubMed:27782878).
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:28602820).
The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia (PubMed:26245371, PubMed:27782878).
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:28602820).
Required for activity of the AHR. Upon ligand binding, AHR translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE). Not required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex initiates transcription of genes involved in the regulation of a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation (By similarity).
The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia (PubMed:26245371, PubMed:27782878).
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:26245371, PubMed:27782878, PubMed:28602820).
The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia (PubMed:26245371, PubMed:27782878).
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:26245371, PubMed:27782878, PubMed:28602820).
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAryl hydrocarbon receptor nuclear translocator
- Short namesARNT protein
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP53762
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 94 | Reduces DNA binding. | ||||
Sequence: H → A | ||||||
Mutagenesis | 98 | Reduces DNA binding. | ||||
Sequence: E → A | ||||||
Mutagenesis | 102 | Reduces DNA binding. Decreases transcription factor activity. | ||||
Sequence: R → E | ||||||
Mutagenesis | 112 | Interferes with transcription factor activity. | ||||
Sequence: L → D | ||||||
Mutagenesis | 112 | Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability. | ||||
Sequence: L → E | ||||||
Mutagenesis | 132 | Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability. | ||||
Sequence: L → E | ||||||
Mutagenesis | 136 | Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability. | ||||
Sequence: V → D | ||||||
Mutagenesis | 139 | Interferes with transcription factor activity. | ||||
Sequence: M → D | ||||||
Mutagenesis | 164 | Does not affect transcription factor activity. | ||||
Sequence: L → D | ||||||
Mutagenesis | 167 | Highly reduces transcription activity. Impairs interaction with AHR. Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability. | ||||
Sequence: L → E | ||||||
Mutagenesis | 168 | Highly reduces transcription activity. Impairs interaction with AHR. Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability. | ||||
Sequence: I → D | ||||||
Mutagenesis | 171 | Reduces transcription activity. Markedly reduces interaction with AHR. Impairs heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability. | ||||
Sequence: A → D | ||||||
Mutagenesis | 264 | Impairs heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability. | ||||
Sequence: I → D | ||||||
Mutagenesis | 266 | Markedly decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability. | ||||
Sequence: R → A | ||||||
Mutagenesis | 305 | Markedly decreases heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability. | ||||
Sequence: V → D | ||||||
Mutagenesis | 307 | Decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability. | ||||
Sequence: H → A | ||||||
Mutagenesis | 366 | Markedly decreases heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Impairs heterodimer formation with EPAS1; when associated with N-448. Impairs heterodimer formation with HIF1A; when associated with N-448. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability. | ||||
Sequence: R → A | ||||||
Mutagenesis | 448 | Decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Impairs heterodimer formation with EPAS1; when associated with A-366. Impairs heterodimer formation with HIF1A; when associated with A-366. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability. | ||||
Sequence: N → A | ||||||
Mutagenesis | 456 | Decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability. | ||||
Sequence: Y → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 23 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000127119 | 2-791 | Aryl hydrocarbon receptor nuclear translocator | |||
Sequence: AATTANPEMTSDVPSLGPTIASGNPGPGIQGGGAVVQRAIKRRSGLDFDDEVEVNTKFLRCDDDQMCNDKERFARSDDEQSSADKERLARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKPSFLTDQELKHLILEAADGFLFIVSCETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGRVLDLKTGTVKKEGQQSSMRMCMGSRRSFICRMRCGTSSVDPVSMNRLSFLRNRCRNGLGSVKEGEPHFVVVHCTGYIKAWPPAGVSLPDDDPEAGQGSKFCLVAIGRLQVTSSPNCTDMSNICQPTEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQVVKLKGQVLSVMFRFRSKTREWLWMRTSSFTFQNPYSDEIEYIICTNTNVKNSSQEPRPTLSNTIPRSQLGPTANLSLEMGTGQLPSRQQQQQHTELDMVPGRDGLASYNHSQVSVQPVASAGSEHSKPLEKSEGLFAQDRDPRFPEIYPSITADQSKGISSSTVPATQQLFSQGSSFPPNPRPAENFRNSGLTPPVTIVQPSSSAGQILAQISRHSNPAQGSAPTWTSSSRPGFAAQQVPTQATAKTRSSQFGVNNFQTSSSFSAMSLPGAPTASSGTAAYPALPNRGSNFPPETGQTTGQFQARTAEGVGVWPQWQGQQPHHRSSSSEQHVQQTQAQAPSQPEVFQEMLSMLGDQSNTYNNEEFPDLTMFPPFSE | ||||||
Cross-link | 58 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 77 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Monomer (PubMed:28602820).
Homodimer only upon binding to a DNA (PubMed:26245371, PubMed:28602820).
Efficient DNA binding requires dimerization with another bHLH protein (By similarity).
Interacts with TACC3 (PubMed:11025203).
Interacts with HIF1A, EPAS1, NPAS1 and NPAS3; forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:26245371, PubMed:27782878).
Forms a heterodimer with AHRR, as well as with other bHLH proteins (PubMed:9887096).
Interacts with NOCA7 (By similarity).
Interacts with AHR; 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:27782878, PubMed:28602820).
Interacts with SIM1 and NPAS4 (PubMed:27782878).
Homodimer only upon binding to a DNA (PubMed:26245371, PubMed:28602820).
Efficient DNA binding requires dimerization with another bHLH protein (By similarity).
Interacts with TACC3 (PubMed:11025203).
Interacts with HIF1A, EPAS1, NPAS1 and NPAS3; forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:26245371, PubMed:27782878).
Forms a heterodimer with AHRR, as well as with other bHLH proteins (PubMed:9887096).
Interacts with NOCA7 (By similarity).
Interacts with AHR; 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:27782878, PubMed:28602820).
Interacts with SIM1 and NPAS4 (PubMed:27782878).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P53762 | Ahr P30561 | 2 | EBI-78852, EBI-78863 | |
BINARY | P53762 | Epas1 P97481 | 5 | EBI-78852, EBI-15704570 | |
BINARY | P53762 | Hif1a Q61221 | 6 | EBI-78852, EBI-298954 | |
BINARY | P53762 | Hif1a Q61221-1 | 5 | EBI-78852, EBI-8549331 | |
BINARY | P53762 | Sim1 Q61045 | 4 | EBI-78852, EBI-78890 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-19 | Polar residues | ||||
Sequence: MAATTANPEMTSDVPSLGP | ||||||
Region | 1-33 | Disordered | ||||
Sequence: MAATTANPEMTSDVPSLGPTIASGNPGPGIQGG | ||||||
Region | 73-97 | Disordered | ||||
Sequence: RFARSDDEQSSADKERLARENHSEI | ||||||
Region | 88-128 | DNA-binding | ||||
Sequence: RLARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDK | ||||||
Domain | 89-142 | bHLH | ||||
Sequence: LARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSL | ||||||
Region | 112-168 | Required for heterodimer formation with HIF1A | ||||
Sequence: LSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKPSFLTDQELKHLI | ||||||
Region | 112-264 | Required for heterodimer formation with EPAS1 | ||||
Sequence: LSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKPSFLTDQELKHLILEAADGFLFIVSCETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGRVLDLKTGTVKKEGQQSSMRMCMGSRRSFI | ||||||
Domain | 161-235 | PAS 1 | ||||
Sequence: DQELKHLILEAADGFLFIVSCETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGR | ||||||
Region | 167-171 | Mediates the transcription activity and dimerization of the AHR:ARNT complex | ||||
Sequence: LILEA | ||||||
Domain | 349-419 | PAS 2 | ||||
Sequence: PNCTDMSNICQPTEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQVVKLK | ||||||
Domain | 424-467 | PAC | ||||
Sequence: SVMFRFRSKTREWLWMRTSSFTFQNPYSDEIEYIICTNTNVKNS | ||||||
Region | 465-508 | Disordered | ||||
Sequence: KNSSQEPRPTLSNTIPRSQLGPTANLSLEMGTGQLPSRQQQQQH | ||||||
Region | 530-554 | Disordered | ||||
Sequence: VQPVASAGSEHSKPLEKSEGLFAQD | ||||||
Region | 631-667 | Disordered | ||||
Sequence: SNPAQGSAPTWTSSSRPGFAAQQVPTQATAKTRSSQF | ||||||
Compositional bias | 682-698 | Polar residues | ||||
Sequence: SLPGAPTASSGTAAYPA | ||||||
Region | 682-715 | Disordered | ||||
Sequence: SLPGAPTASSGTAAYPALPNRGSNFPPETGQTTG | ||||||
Region | 730-791 | Disordered | ||||
Sequence: QWQGQQPHHRSSSSEQHVQQTQAQAPSQPEVFQEMLSMLGDQSNTYNNEEFPDLTMFPPFSE | ||||||
Compositional bias | 733-780 | Polar residues | ||||
Sequence: GQQPHHRSSSSEQHVQQTQAQAPSQPEVFQEMLSMLGDQSNTYNNEEF |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P53762-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameLong
- Length791
- Mass (Da)86,963
- Last updated2011-07-27 v3
- ChecksumBDEC0991CD57D402
P53762-2
- NameShort
- Differences from canonical
- 77-100: SDDEQSSADKERLARENHSEIERR → TKFL
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-19 | Polar residues | ||||
Sequence: MAATTANPEMTSDVPSLGP | ||||||
Alternative sequence | VSP_002093 | 77-100 | in isoform Short | |||
Sequence: SDDEQSSADKERLARENHSEIERR → TKFL | ||||||
Sequence conflict | 411 | in Ref. 2; AAA61732 | ||||
Sequence: S → T | ||||||
Sequence conflict | 534 | in Ref. 2; AAA61732 | ||||
Sequence: A → R | ||||||
Sequence conflict | 644 | in Ref. 1; AAA56717 | ||||
Sequence: S → T | ||||||
Sequence conflict | 650 | in Ref. 2; AAA61732 | ||||
Sequence: A → C | ||||||
Compositional bias | 682-698 | Polar residues | ||||
Sequence: SLPGAPTASSGTAAYPA | ||||||
Compositional bias | 733-780 | Polar residues | ||||
Sequence: GQQPHHRSSSSEQHVQQTQAQAPSQPEVFQEMLSMLGDQSNTYNNEEF |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U10325 EMBL· GenBank· DDBJ | AAA56717.1 EMBL· GenBank· DDBJ | mRNA | ||
U14333 EMBL· GenBank· DDBJ | AAA61732.1 EMBL· GenBank· DDBJ | mRNA | ||
AK153355 EMBL· GenBank· DDBJ | BAE31928.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466620 EMBL· GenBank· DDBJ | EDL38816.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC012870 EMBL· GenBank· DDBJ | AAH12870.1 EMBL· GenBank· DDBJ | mRNA |