Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P27540

- ARNT_HUMAN

UniProt

P27540 - ARNT_HUMAN

Protein

Aryl hydrocarbon receptor nuclear translocator

Gene

ARNT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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. The heterodimer with HIF1A or EPAS1/HIF2A functions as a transcriptional regulator of the adaptive response to hypoxia.

    GO - Molecular functioni

    1. aryl hydrocarbon receptor activity Source: Ensembl
    2. aryl hydrocarbon receptor binding Source: BHF-UCL
    3. enhancer binding Source: MGI
    4. protein binding Source: IntAct
    5. protein heterodimerization activity Source: BHF-UCL
    6. sequence-specific DNA binding transcription factor activity Source: ProtInc
    7. transcription coactivator activity Source: ProtInc
    8. transcription factor binding Source: BHF-UCL

    GO - Biological processi

    1. cell differentiation Source: Ensembl
    2. cellular response to hypoxia Source: Reactome
    3. embryonic placenta development Source: Ensembl
    4. mRNA transcription from RNA polymerase II promoter Source: BHF-UCL
    5. positive regulation of endothelial cell proliferation Source: BHF-UCL
    6. positive regulation of erythrocyte differentiation Source: BHF-UCL
    7. positive regulation of glycolytic process Source: BHF-UCL
    8. positive regulation of hormone biosynthetic process Source: BHF-UCL
    9. positive regulation of protein sumoylation Source: Ensembl
    10. positive regulation of transcription, DNA-templated Source: BHF-UCL
    11. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    12. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
    13. positive regulation vascular endothelial growth factor production Source: BHF-UCL
    14. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
    15. regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: BHF-UCL
    16. response to hypoxia Source: BHF-UCL
    17. transcription, DNA-templated Source: ProtInc

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
    SignaLinkiP27540.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aryl hydrocarbon receptor nuclear translocator
    Short name:
    ARNT protein
    Alternative name(s):
    Class E basic helix-loop-helix protein 2
    Short name:
    bHLHe2
    Dioxin receptor, nuclear translocator
    Hypoxia-inducible factor 1-beta
    Short name:
    HIF-1-beta
    Short name:
    HIF1-beta
    Gene namesi
    Name:ARNT
    Synonyms:BHLHE2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:700. ARNT.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nucleoplasm Source: Reactome
    3. nucleus Source: BHF-UCL
    4. transcription factor complex Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi91 – 911R → A: Diminishes DNA interaction. 1 Publication
    Mutagenesisi93 – 931N → A: Diminishes DNA interaction. 1 Publication
    Mutagenesisi94 – 941H → A: Severely diminishes DNA interaction. 1 Publication
    Mutagenesisi98 – 981E → A: Severely diminishes DNA interaction. 1 Publication
    Mutagenesisi99 – 991R → A: Diminishes DNA interaction. 1 Publication
    Mutagenesisi101 – 1011R → A: Severely diminishes DNA interaction. 1 Publication
    Mutagenesisi102 – 1021R → A: Severely diminishes DNA interaction. 1 Publication

    Organism-specific databases

    PharmGKBiPA24994.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 789788Aryl hydrocarbon receptor nuclear translocatorPRO_0000127118Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei77 – 771Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP27540.
    PaxDbiP27540.
    PRIDEiP27540.

    PTM databases

    PhosphoSiteiP27540.

    Expressioni

    Gene expression databases

    ArrayExpressiP27540.
    BgeeiP27540.
    CleanExiHS_ARNT.
    GenevestigatoriP27540.

    Organism-specific databases

    HPAiCAB004318.
    HPA001759.

    Interactioni

    Subunit structurei

    Efficient DNA binding requires dimerization with another bHLH protein. Forms a heterodimer with AHR, AHRR, HIF1A and EPAS1/HIF2A as well as with other bHLH proteins. Interacts with TACC3 By similarity. Interacts with NOCA7. Heterodimer with HIF1A.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AHRP358695EBI-80809,EBI-80780
    HIF1AQ166659EBI-80809,EBI-447269
    NCOA7Q8NI082EBI-80809,EBI-80799
    NCOR2Q9Y6182EBI-80809,EBI-80830

    Protein-protein interaction databases

    BioGridi106898. 39 interactions.
    DIPiDIP-30886N.
    IntActiP27540. 18 interactions.
    MINTiMINT-1196758.
    STRINGi9606.ENSP00000351407.

    Structurei

    Secondary structure

    1
    789
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi356 – 3583
    Beta strandi362 – 3676
    Beta strandi371 – 3766
    Helixi380 – 3845
    Helixi388 – 3903
    Turni391 – 3933
    Helixi396 – 3994
    Turni402 – 4043
    Helixi405 – 41511
    Turni416 – 4205
    Beta strandi423 – 4308
    Beta strandi436 – 44611
    Turni449 – 4513
    Beta strandi456 – 4638

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D7Gmodel-C87-145[»]
    1X0ONMR-A356-470[»]
    2A24NMR-B358-465[»]
    2ARNmodel-A335-462[»]
    2B02X-ray1.50A354-470[»]
    2HV1NMR-A/B356-470[»]
    2K7SNMR-A356-470[»]
    3F1NX-ray1.48B356-470[»]
    3F1OX-ray1.60B356-470[»]
    3F1PX-ray1.17B356-470[»]
    3H7WX-ray1.65B356-470[»]
    3H82X-ray1.50B356-470[»]
    4EQ1X-ray1.60A/B357-464[»]
    4GHIX-ray1.50B356-470[»]
    4GS9X-ray1.72B356-470[»]
    4H6JX-ray1.52B357-470[»]
    ProteinModelPortaliP27540.
    SMRiP27540. Positions 90-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27540.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini89 – 14254bHLHPROSITE-ProRule annotationAdd
    BLAST
    Domaini161 – 23575PAS 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini349 – 41971PAS 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini424 – 46744PACAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi99 – 1024Poly-Arg
    Compositional biasi503 – 5075Poly-Gln
    Compositional biasi710 – 76960Gln-richAdd
    BLAST
    Compositional biasi738 – 7414Poly-Ser

    Sequence similaritiesi

    Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation
    Contains 2 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG293303.
    HOGENOMiHOG000234380.
    HOVERGENiHBG000164.
    KOiK09097.
    OMAiIVEFCHP.
    OrthoDBiEOG7V1FQ8.
    PhylomeDBiP27540.
    TreeFamiTF319983.

    Family and domain databases

    Gene3Di4.10.280.10. 1 hit.
    InterProiIPR011598. bHLH_dom.
    IPR001067. Nuc_translocat.
    IPR001610. PAC.
    IPR000014. PAS.
    IPR013767. PAS_fold.
    [Graphical view]
    PfamiPF00010. HLH. 1 hit.
    PF00989. PAS. 1 hit.
    [Graphical view]
    PRINTSiPR00785. NCTRNSLOCATR.
    SMARTiSM00353. HLH. 1 hit.
    SM00086. PAC. 1 hit.
    SM00091. PAS. 2 hits.
    [Graphical view]
    SUPFAMiSSF47459. SSF47459. 1 hit.
    SSF55785. SSF55785. 4 hits.
    TIGRFAMsiTIGR00229. sensory_box. 1 hit.
    PROSITEiPS50888. BHLH. 1 hit.
    PS50112. PAS. 2 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P27540-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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.

    « Hide

    MAATTANPEM TSDVPSLGPA IASGNSGPGI QGGGAIVQRA IKRRPGLDFD    50
    DDGEGNSKFL RCDDDQMSND KERFARSDDE QSSADKERLA RENHSEIERR 100
    RRNKMTAYIT ELSDMVPTCS ALARKPDKLT ILRMAVSHMK SLRGTGNTST 150
    DGSYKPSFLT DQELKHLILE AADGFLFIVS CETGRVVYVS DSVTPVLNQP 200
    QSEWFGSTLY DQVHPDDVDK LREQLSTSEN ALTGRILDLK TGTVKKEGQQ 250
    SSMRMCMGSR RSFICRMRCG SSSVDPVSVN RLSFVRNRCR NGLGSVKDGE 300
    PHFVVVHCTG YIKAWPPAGV SLPDDDPEAG QGSKFCLVAI GRLQVTSSPN 350
    CTDMSNVCQP TEFISRHNIE GIFTFVDHRC VATVGYQPQE LLGKNIVEFC 400
    HPEDQQLLRD SFQQVVKLKG QVLSVMFRFR SKNQEWLWMR TSSFTFQNPY 450
    SDEIEYIICT NTNVKNSSQE PRPTLSNTIQ RPQLGPTANL PLEMGSGQLA 500
    PRQQQQQTEL DMVPGRDGLA SYNHSQVVQP VTTTGPEHSK PLEKSDGLFA 550
    QDRDPRFSEI YHNINADQSK GISSSTVPAT QQLFSQGNTF PPTPRPAENF 600
    RNSGLAPPVT IVQPSASAGQ MLAQISRHSN PTQGATPTWT PTTRSGFSAQ 650
    QVATQATAKT RTSQFGVGSF QTPSSFSSMS LPGAPTASPG AAAYPSLTNR 700
    GSNFAPETGQ TAGQFQTRTA EGVGVWPQWQ GQQPHHRSSS SEQHVQQPPA 750
    QQPGQPEVFQ EMLSMLGDQS NSYNNEEFPD LTMFPPFSE 789
    Length:789
    Mass (Da):86,636
    Last modified:August 1, 1992 - v1
    Checksum:i2E278F8E62BFBF6D
    GO
    Isoform 2 (identifier: P27540-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         77-91: Missing.

    Show »
    Length:774
    Mass (Da):84,948
    Checksum:i0653070528296044
    GO
    Isoform 3 (identifier: P27540-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-9: Missing.
         319-323: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:775
    Mass (Da):85,296
    Checksum:i74839AACC350CB6B
    GO
    Isoform 4 (identifier: P27540-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         601-602: Missing.

    Show »
    Length:787
    Mass (Da):86,366
    Checksum:i956940ABFFF1E71A
    GO

    Sequence cautioni

    The sequence BAD93114.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAD38953.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti627 – 6271R → H in BAG36518. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti430 – 4301R → Q.
    Corresponds to variant rs2229175 [ dbSNP | Ensembl ].
    VAR_024280
    Natural varianti435 – 4351E → K.
    Corresponds to variant rs2229176 [ dbSNP | Ensembl ].
    VAR_049537
    Natural varianti511 – 5111D → N.
    Corresponds to variant rs1805133 [ dbSNP | Ensembl ].
    VAR_014819
    Natural varianti517 – 5171D → E.1 Publication
    Corresponds to variant rs10305741 [ dbSNP | Ensembl ].
    VAR_018906
    Natural varianti706 – 7061P → L.
    Corresponds to variant rs2275237 [ dbSNP | Ensembl ].
    VAR_020189

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 99Missing in isoform 3. 1 PublicationVSP_036532
    Alternative sequencei77 – 9115Missing in isoform 2. 1 PublicationVSP_002092Add
    BLAST
    Alternative sequencei319 – 3235Missing in isoform 3. 1 PublicationVSP_036533
    Alternative sequencei601 – 6022Missing in isoform 4. 1 PublicationVSP_055030

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69238 mRNA. Translation: AAA51777.1.
    Y18859
    , AJ251863, AJ404851, AJ404852, AJ404853, AJ404854 Genomic DNA. Translation: CAC21446.1.
    AK290177 mRNA. Translation: BAF82866.1.
    AK293027 mRNA. Translation: BAF85716.1.
    AK313780 mRNA. Translation: BAG36518.1.
    AB209877 mRNA. Translation: BAD93114.1. Different initiation.
    AL834279 mRNA. Translation: CAD38953.1. Different initiation.
    AY430083 Genomic DNA. Translation: AAQ96598.1.
    AL355860 Genomic DNA. No translation available.
    CH471121 Genomic DNA. Translation: EAW53510.1.
    CH471121 Genomic DNA. Translation: EAW53513.1.
    CCDSiCCDS65641.1. [P27540-3]
    CCDS65642.1. [P27540-4]
    CCDS970.1. [P27540-1]
    CCDS971.1. [P27540-2]
    PIRiI59550.
    RefSeqiNP_001184254.1. NM_001197325.1.
    NP_001272964.1. NM_001286035.1. [P27540-3]
    NP_001272965.1. NM_001286036.1.
    NP_001659.1. NM_001668.3. [P27540-1]
    NP_848514.1. NM_178427.2. [P27540-2]
    UniGeneiHs.632446.

    Genome annotation databases

    EnsembliENST00000354396; ENSP00000346372; ENSG00000143437. [P27540-4]
    ENST00000358595; ENSP00000351407; ENSG00000143437. [P27540-1]
    ENST00000505755; ENSP00000427571; ENSG00000143437. [P27540-2]
    ENST00000515192; ENSP00000423851; ENSG00000143437. [P27540-3]
    GeneIDi405.
    KEGGihsa:405.
    UCSCiuc001evr.2. human. [P27540-1]
    uc001evs.2. human. [P27540-2]
    uc009wmb.2. human. [P27540-3]

    Polymorphism databases

    DMDMi114163.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M69238 mRNA. Translation: AAA51777.1 .
    Y18859
    , AJ251863 , AJ404851 , AJ404852 , AJ404853 , AJ404854 Genomic DNA. Translation: CAC21446.1 .
    AK290177 mRNA. Translation: BAF82866.1 .
    AK293027 mRNA. Translation: BAF85716.1 .
    AK313780 mRNA. Translation: BAG36518.1 .
    AB209877 mRNA. Translation: BAD93114.1 . Different initiation.
    AL834279 mRNA. Translation: CAD38953.1 . Different initiation.
    AY430083 Genomic DNA. Translation: AAQ96598.1 .
    AL355860 Genomic DNA. No translation available.
    CH471121 Genomic DNA. Translation: EAW53510.1 .
    CH471121 Genomic DNA. Translation: EAW53513.1 .
    CCDSi CCDS65641.1. [P27540-3 ]
    CCDS65642.1. [P27540-4 ]
    CCDS970.1. [P27540-1 ]
    CCDS971.1. [P27540-2 ]
    PIRi I59550.
    RefSeqi NP_001184254.1. NM_001197325.1.
    NP_001272964.1. NM_001286035.1. [P27540-3 ]
    NP_001272965.1. NM_001286036.1.
    NP_001659.1. NM_001668.3. [P27540-1 ]
    NP_848514.1. NM_178427.2. [P27540-2 ]
    UniGenei Hs.632446.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D7G model - C 87-145 [» ]
    1X0O NMR - A 356-470 [» ]
    2A24 NMR - B 358-465 [» ]
    2ARN model - A 335-462 [» ]
    2B02 X-ray 1.50 A 354-470 [» ]
    2HV1 NMR - A/B 356-470 [» ]
    2K7S NMR - A 356-470 [» ]
    3F1N X-ray 1.48 B 356-470 [» ]
    3F1O X-ray 1.60 B 356-470 [» ]
    3F1P X-ray 1.17 B 356-470 [» ]
    3H7W X-ray 1.65 B 356-470 [» ]
    3H82 X-ray 1.50 B 356-470 [» ]
    4EQ1 X-ray 1.60 A/B 357-464 [» ]
    4GHI X-ray 1.50 B 356-470 [» ]
    4GS9 X-ray 1.72 B 356-470 [» ]
    4H6J X-ray 1.52 B 357-470 [» ]
    ProteinModelPortali P27540.
    SMRi P27540. Positions 90-464.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106898. 39 interactions.
    DIPi DIP-30886N.
    IntActi P27540. 18 interactions.
    MINTi MINT-1196758.
    STRINGi 9606.ENSP00000351407.

    Chemistry

    ChEMBLi CHEMBL5618.

    PTM databases

    PhosphoSitei P27540.

    Polymorphism databases

    DMDMi 114163.

    Proteomic databases

    MaxQBi P27540.
    PaxDbi P27540.
    PRIDEi P27540.

    Protocols and materials databases

    DNASUi 405.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000354396 ; ENSP00000346372 ; ENSG00000143437 . [P27540-4 ]
    ENST00000358595 ; ENSP00000351407 ; ENSG00000143437 . [P27540-1 ]
    ENST00000505755 ; ENSP00000427571 ; ENSG00000143437 . [P27540-2 ]
    ENST00000515192 ; ENSP00000423851 ; ENSG00000143437 . [P27540-3 ]
    GeneIDi 405.
    KEGGi hsa:405.
    UCSCi uc001evr.2. human. [P27540-1 ]
    uc001evs.2. human. [P27540-2 ]
    uc009wmb.2. human. [P27540-3 ]

    Organism-specific databases

    CTDi 405.
    GeneCardsi GC01M150782.
    HGNCi HGNC:700. ARNT.
    HPAi CAB004318.
    HPA001759.
    MIMi 126110. gene.
    neXtProti NX_P27540.
    PharmGKBi PA24994.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG293303.
    HOGENOMi HOG000234380.
    HOVERGENi HBG000164.
    KOi K09097.
    OMAi IVEFCHP.
    OrthoDBi EOG7V1FQ8.
    PhylomeDBi P27540.
    TreeFami TF319983.

    Enzyme and pathway databases

    Reactomei REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
    SignaLinki P27540.

    Miscellaneous databases

    ChiTaRSi ARNT. human.
    EvolutionaryTracei P27540.
    GeneWikii Aryl_hydrocarbon_receptor_nuclear_translocator.
    GenomeRNAii 405.
    NextBioi 1693.
    PROi P27540.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P27540.
    Bgeei P27540.
    CleanExi HS_ARNT.
    Genevestigatori P27540.

    Family and domain databases

    Gene3Di 4.10.280.10. 1 hit.
    InterProi IPR011598. bHLH_dom.
    IPR001067. Nuc_translocat.
    IPR001610. PAC.
    IPR000014. PAS.
    IPR013767. PAS_fold.
    [Graphical view ]
    Pfami PF00010. HLH. 1 hit.
    PF00989. PAS. 1 hit.
    [Graphical view ]
    PRINTSi PR00785. NCTRNSLOCATR.
    SMARTi SM00353. HLH. 1 hit.
    SM00086. PAC. 1 hit.
    SM00091. PAS. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47459. SSF47459. 1 hit.
    SSF55785. SSF55785. 4 hits.
    TIGRFAMsi TIGR00229. sensory_box. 1 hit.
    PROSITEi PS50888. BHLH. 1 hit.
    PS50112. PAS. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a factor required for activity of the Ah (dioxin) receptor."
      Hoffman E.C., Reyes H., Chu F.-F., Sander F., Conley L.H., Brooks B.A., Hankinson O.
      Science 252:954-958(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    2. Scheel J.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis, Thalamus and Uterus.
    4. "Homo sapiens protein coding cDNA."
      Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Aortic endothelium.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    6. NIEHS SNPs program
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-517.
    7. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension."
      Wang G.L., Jiang B.-H., Rue E.A., Semenza G.L.
      Proc. Natl. Acad. Sci. U.S.A. 92:5510-5514(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 186-203 AND 662-694.
    10. "Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor."
      Reyes H., Reisz-Porszasz S., Hankinson O.
      Science 256:1193-1195(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    11. "Functional characterization of DNA-binding domains of the subunits of the heterodimeric aryl hydrocarbon receptor complex imputing novel and canonical basic helix-loop-helix protein-DNA interactions."
      Bacsi S.G., Hankinson O.
      J. Biol. Chem. 271:8843-8850(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, MUTAGENESIS OF ARG-91; ASN-93; HIS-94; GLU-98; ARG-99; ARG-101 AND ARG-102.
    12. "Interactions of nuclear receptor coactivator/corepressor proteins with the aryl hydrocarbon receptor complex."
      Nguyen T.A., Hoivik D., Lee J.-E., Safe S.
      Arch. Biochem. Biophys. 367:250-257(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NOCA7.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Casein kinase 1 regulates human hypoxia-inducible factor HIF-1."
      Kalousi A., Mylonis I., Politou A.S., Chachami G., Paraskeva E., Simos G.
      J. Cell Sci. 123:2976-2986(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIF1A.
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiARNT_HUMAN
    AccessioniPrimary (citable) accession number: P27540
    Secondary accession number(s): B2R9H1
    , C4AMA1, F8WAP6, Q59ED4, Q5QP39, Q8NDC7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 163 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3