Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P27540 (ARNT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ARNT
Synonyms:BHLHE2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length789 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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

Subunit structure

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. Ref.11 Ref.13

Subcellular location

Nucleus.

Sequence similarities

Contains 1 bHLH (basic helix-loop-helix) domain.

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 2 PAS (PER-ARNT-SIM) domains.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Traceable author statement. Source: Reactome

embryonic placenta development

Inferred from electronic annotation. Source: Ensembl

mRNA transcription from RNA polymerase II promoter

Inferred by curator Ref.8. Source: BHF-UCL

positive regulation of endothelial cell proliferation

Inferred by curator PubMed 8756616. Source: BHF-UCL

positive regulation of erythrocyte differentiation

Inferred by curator PubMed 1448077. Source: BHF-UCL

positive regulation of glycolysis

Inferred by curator PubMed 8089148. Source: BHF-UCL

positive regulation of hormone biosynthetic process

Inferred from direct assay PubMed 1448077. Source: BHF-UCL

positive regulation of protein sumoylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 8089148. Source: BHF-UCL

positive regulation of vascular endothelial growth factor receptor signaling pathway

Inferred by curator PubMed 8756616. Source: BHF-UCL

positive regulation vascular endothelial growth factor production

Inferred from direct assay PubMed 8756616. Source: BHF-UCL

regulation of transcription from RNA polymerase II promoter in response to hypoxia

Traceable author statement. Source: Reactome

regulation of transcription from RNA polymerase II promoter in response to oxidative stress

Inferred from direct assay PubMed 8089148. Source: BHF-UCL

response to hypoxia

Inferred from direct assay PubMed 8756616. Source: BHF-UCL

transcription, DNA-templated

Traceable author statement Ref.9. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 8089148. Source: BHF-UCL

transcription factor complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

aryl hydrocarbon receptor activity

Inferred from electronic annotation. Source: Ensembl

aryl hydrocarbon receptor binding

Inferred from physical interaction PubMed 9079689. Source: BHF-UCL

protein heterodimerization activity

Inferred from physical interaction PubMed 9079689. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 10777486Ref.9. Source: ProtInc

transcription coactivator activity

Traceable author statement Ref.9. Source: ProtInc

transcription factor binding

Inferred from physical interaction PubMed 10692439Ref.8PubMed 9079689. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P27540-1)

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.
Isoform 2 (identifier: P27540-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     77-91: Missing.
Isoform 3 (identifier: P27540-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: Missing.
     319-323: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 789788Aryl hydrocarbon receptor nuclear translocator
PRO_0000127118

Regions

Domain89 – 14254bHLH
Domain161 – 23575PAS 1
Domain349 – 41971PAS 2
Domain424 – 46744PAC
Compositional bias99 – 1024Poly-Arg
Compositional bias503 – 5075Poly-Gln
Compositional bias710 – 76960Gln-rich
Compositional bias738 – 7414Poly-Ser

Amino acid modifications

Modified residue21N-acetylalanine Ref.14
Modified residue771Phosphoserine Ref.12

Natural variations

Alternative sequence1 – 99Missing in isoform 3.
VSP_036532
Alternative sequence77 – 9115Missing in isoform 2.
VSP_002092
Alternative sequence319 – 3235Missing in isoform 3.
VSP_036533
Natural variant4301R → Q.
Corresponds to variant rs2229175 [ dbSNP | Ensembl ].
VAR_024280
Natural variant4351E → K.
Corresponds to variant rs2229176 [ dbSNP | Ensembl ].
VAR_049537
Natural variant5111D → N.
Corresponds to variant rs1805133 [ dbSNP | Ensembl ].
VAR_014819
Natural variant5171D → E. Ref.5
Corresponds to variant rs10305741 [ dbSNP | Ensembl ].
VAR_018906
Natural variant7061P → L.
Corresponds to variant rs2275237 [ dbSNP | Ensembl ].
VAR_020189

Experimental info

Mutagenesis911R → A: Diminishes DNA interaction. Ref.10
Mutagenesis931N → A: Diminishes DNA interaction. Ref.10
Mutagenesis941H → A: Severely diminishes DNA interaction. Ref.10
Mutagenesis981E → A: Severely diminishes DNA interaction. Ref.10
Mutagenesis991R → A: Diminishes DNA interaction. Ref.10
Mutagenesis1011R → A: Severely diminishes DNA interaction. Ref.10
Mutagenesis1021R → A: Severely diminishes DNA interaction. Ref.10

Secondary structure

.......................... 789
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 2E278F8E62BFBF6D

FASTA78986,636
        10         20         30         40         50         60 
MAATTANPEM TSDVPSLGPA IASGNSGPGI QGGGAIVQRA IKRRPGLDFD DDGEGNSKFL 

        70         80         90        100        110        120 
RCDDDQMSND KERFARSDDE QSSADKERLA RENHSEIERR RRNKMTAYIT ELSDMVPTCS 

       130        140        150        160        170        180 
ALARKPDKLT ILRMAVSHMK SLRGTGNTST DGSYKPSFLT DQELKHLILE AADGFLFIVS 

       190        200        210        220        230        240 
CETGRVVYVS DSVTPVLNQP QSEWFGSTLY DQVHPDDVDK LREQLSTSEN ALTGRILDLK 

       250        260        270        280        290        300 
TGTVKKEGQQ SSMRMCMGSR RSFICRMRCG SSSVDPVSVN RLSFVRNRCR NGLGSVKDGE 

       310        320        330        340        350        360 
PHFVVVHCTG YIKAWPPAGV SLPDDDPEAG QGSKFCLVAI GRLQVTSSPN CTDMSNVCQP 

       370        380        390        400        410        420 
TEFISRHNIE GIFTFVDHRC VATVGYQPQE LLGKNIVEFC HPEDQQLLRD SFQQVVKLKG 

       430        440        450        460        470        480 
QVLSVMFRFR SKNQEWLWMR TSSFTFQNPY SDEIEYIICT NTNVKNSSQE PRPTLSNTIQ 

       490        500        510        520        530        540 
RPQLGPTANL PLEMGSGQLA PRQQQQQTEL DMVPGRDGLA SYNHSQVVQP VTTTGPEHSK 

       550        560        570        580        590        600 
PLEKSDGLFA QDRDPRFSEI YHNINADQSK GISSSTVPAT QQLFSQGNTF PPTPRPAENF 

       610        620        630        640        650        660 
RNSGLAPPVT IVQPSASAGQ MLAQISRHSN PTQGATPTWT PTTRSGFSAQ QVATQATAKT 

       670        680        690        700        710        720 
RTSQFGVGSF QTPSSFSSMS LPGAPTASPG AAAYPSLTNR GSNFAPETGQ TAGQFQTRTA 

       730        740        750        760        770        780 
EGVGVWPQWQ GQQPHHRSSS SEQHVQQPPA QQPGQPEVFQ EMLSMLGDQS NSYNNEEFPD 


LTMFPPFSE 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 0653070528296044
Show »

FASTA77484,948
Isoform 3 [UniParc].

Checksum: 74839AACC350CB6B
Show »

FASTA77585,296

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: Thalamus and Uterus.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[5]NIEHS SNPs program
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-517.
[6]"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. expand/collapse author list , 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].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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.
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M69238 mRNA. Translation: AAA51777.1.
Y18859 expand/collapse EMBL AC list , AJ251863, AJ404851, AJ404852, AJ404853, AJ404854 Genomic DNA. Translation: CAC21446.1.
AK290177 mRNA. Translation: BAF82866.1.
AK293027 mRNA. Translation: BAF85716.1.
AL834279 mRNA. Translation: CAD38953.1. Different initiation.
AY430083 Genomic DNA. Translation: AAQ96598.1.
AL355860 Genomic DNA. Translation: CAI12797.1.
CH471121 Genomic DNA. Translation: EAW53510.1.
CH471121 Genomic DNA. Translation: EAW53513.1.
PIRI59550.
RefSeqNP_001184254.1. NM_001197325.1.
NP_001272964.1. NM_001286035.1.
NP_001272965.1. NM_001286036.1.
NP_001659.1. NM_001668.3.
NP_848514.1. NM_178427.2.
UniGeneHs.632446.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP27540.
SMRP27540. Positions 90-464.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106898. 39 interactions.
DIPDIP-30886N.
IntActP27540. 18 interactions.
MINTMINT-1196758.
STRING9606.ENSP00000351407.

Chemistry

ChEMBLCHEMBL5618.

PTM databases

PhosphoSiteP27540.

Polymorphism databases

DMDM114163.

Proteomic databases

PaxDbP27540.
PRIDEP27540.

Protocols and materials databases

DNASU405.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358595; ENSP00000351407; ENSG00000143437. [P27540-1]
ENST00000505755; ENSP00000427571; ENSG00000143437. [P27540-2]
ENST00000515192; ENSP00000423851; ENSG00000143437. [P27540-3]
GeneID405.
KEGGhsa:405.
UCSCuc001evr.2. human. [P27540-1]
uc001evs.2. human. [P27540-2]
uc009wmb.2. human. [P27540-3]

Organism-specific databases

CTD405.
GeneCardsGC01M150782.
HGNCHGNC:700. ARNT.
HPACAB004318.
HPA001759.
MIM126110. gene.
neXtProtNX_P27540.
PharmGKBPA24994.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG293303.
HOGENOMHOG000234380.
HOVERGENHBG000164.
KOK09097.
OMAIVEFCHP.
OrthoDBEOG7V1FQ8.
PhylomeDBP27540.
TreeFamTF319983.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
SignaLinkP27540.

Gene expression databases

ArrayExpressP27540.
BgeeP27540.
CleanExHS_ARNT.
GenevestigatorP27540.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
IPR001067. Nuc_translocat.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
[Graphical view]
PfamPF00010. HLH. 1 hit.
PF00989. PAS. 1 hit.
[Graphical view]
PRINTSPR00785. NCTRNSLOCATR.
SMARTSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 4 hits.
TIGRFAMsTIGR00229. sensory_box. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARNT. human.
EvolutionaryTraceP27540.
GeneWikiAryl_hydrocarbon_receptor_nuclear_translocator.
GenomeRNAi405.
NextBio1693.
PROP27540.
SOURCESearch...

Entry information

Entry nameARNT_HUMAN
AccessionPrimary (citable) accession number: P27540
Secondary accession number(s): C4AMA1, Q5QP39, Q8NDC7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM