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P27540

- ARNT_HUMAN

UniProt

P27540 - ARNT_HUMAN

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Protein

Aryl hydrocarbon receptor nuclear translocator

Gene
ARNT, BHLHE2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. DNA binding Source: UniProtKB-KW
  4. enhancer binding Source: MGI
  5. protein binding Source: IntAct
  6. protein heterodimerization activity Source: BHF-UCL
  7. sequence-specific DNA binding transcription factor activity Source: InterPro
  8. signal transducer activity Source: InterPro
  9. transcription coactivator activity Source: ProtInc
  10. 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: UniProtKB-KW
Complete GO annotation...

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: InterPro
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
  4. transcription factor complex Source: InterPro
Complete GO annotation...

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.2 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.

Miscellaneous databases

EvolutionaryTraceiP27540.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini89 – 14254bHLHAdd
BLAST
Domaini161 – 23575PAS 1Add
BLAST
Domaini349 – 41971PAS 2Add
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

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.

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. VSP_036532
Alternative sequencei77 – 9115Missing in isoform 2. VSP_002092Add
BLAST
Alternative sequencei319 – 3235Missing in isoform 3. VSP_036533
Alternative sequencei601 – 6022Missing in isoform 4. VSP_055030

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti627 – 6271R → H in BAG36518. 1 Publication

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]
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.
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 ]
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 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 162 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

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