P27540 (ARNT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ARNT
Synonyms:	BHLHE2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	789 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.10 Ref.13
Subcellular location	Nucleus.
Sequence similarities	Contains 1 basic helix-loop-helix (bHLH) 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	DNA-binding
Molecular function	Activator
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	mRNA transcription from RNA polymerase II promoter Inferred by curator Ref.8. Source: BHF-UCL positive regulation of endothelial cell proliferation Inferred by curator. Source: BHF-UCL positive regulation of erythrocyte differentiation Inferred by curator. Source: BHF-UCL positive regulation of glycolysis Inferred by curator. Source: BHF-UCL positive regulation of hormone biosynthetic process Inferred from direct assay. Source: BHF-UCL positive regulation of vascular endothelial growth factor receptor signaling pathway Inferred by curator. Source: BHF-UCL positive regulation vascular endothelial growth factor production Inferred from direct assay. Source: BHF-UCL regulation of transcription from RNA polymerase II promoter in response to oxidative stress Inferred from direct assay. Source: BHF-UCL response to hypoxia Inferred from direct assay. Source: BHF-UCL
Molecular function	aryl hydrocarbon receptor binding Inferred from physical interaction. Source: BHF-UCL protein heterodimerization activity Inferred from physical interaction. Source: BHF-UCL sequence-specific DNA binding transcription factor activity Traceable author statement. Source: ProtInc signal transducer activity Inferred from electronic annotation. Source: InterPro transcription coactivator activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AHR	P35869	5	EBI-80809,EBI-80780
HIF1A	Q16665	7	EBI-80809,EBI-447269
NCOA7	Q8NI08	2	EBI-80809,EBI-80799
NCOR2	Q9Y618	2	EBI-80809,EBI-80830

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 789

788

Aryl hydrocarbon receptor nuclear translocator

PRO_0000127118

Regions

Domain

103 – 143

41

Helix-loop-helix motif

Domain

161 – 235

75

PAS 1

Domain

349 – 419

71

PAS 2

Domain

424 – 467

44

PAC

DNA binding

90 – 102

13

Basic motif

Compositional bias

99 – 102

4

Poly-Arg

Compositional bias

503 – 507

5

Poly-Gln

Compositional bias

710 – 769

60

Gln-rich

Compositional bias

738 – 741

4

Poly-Ser

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.12

Modified residue

77

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

1 – 9

9

Missing in isoform 3.

VSP_036532

Alternative sequence

77 – 91

15

Missing in isoform 2.

VSP_002092

Alternative sequence

319 – 323

5

Missing in isoform 3.

VSP_036533

Natural variant

430

1

R → Q.
Corresponds to variant rs2229175 [ dbSNP | Ensembl ].

VAR_024280

Natural variant

435

1

E → K.
Corresponds to variant rs2229176 [ dbSNP | Ensembl ].

VAR_049537

Natural variant

511

1

D → N.
Corresponds to variant rs1805133 [ dbSNP | Ensembl ].

VAR_014819

Natural variant

517

1

D → E. Ref.5
Corresponds to variant rs10305741 [ dbSNP | Ensembl ].

VAR_018906

Natural variant

706

1

P → L.
Corresponds to variant rs2275237 [ dbSNP | Ensembl ].

VAR_020189

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

789

Helix Strand Turn

Details...

Beta strand

355 – 359

5

Beta strand

362 – 367

6

Beta strand

372 – 376

5

Helix

380 – 384

5

Helix

388 – 390

3

Turn

391 – 393

3

Helix

396 – 399

4

Helix

402 – 404

3

Helix

405 – 417

13

Beta strand

422 – 430

9

Beta strand

436 – 447

12

Turn

449 – 451

3

Beta strand

454 – 463

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 2E278F8E62BFBF6D	FASTA	789	86,636
	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
	Isoform 2 (Short) [UniParc]. Checksum: 0653070528296044	FASTA	774	84,948
	10 20 30 40 50 60 MAATTANPEM TSDVPSLGPA IASGNSGPGI QGGGAIVQRA IKRRPGLDFD DDGEGNSKFL 70 80 90 100 110 120 RCDDDQMSND KERFARENHS EIERRRRNKM TAYITELSDM VPTCSALARK PDKLTILRMA 130 140 150 160 170 180 VSHMKSLRGT GNTSTDGSYK PSFLTDQELK HLILEAADGF LFIVSCETGR VVYVSDSVTP 190 200 210 220 230 240 VLNQPQSEWF GSTLYDQVHP DDVDKLREQL STSENALTGR ILDLKTGTVK KEGQQSSMRM 250 260 270 280 290 300 CMGSRRSFIC RMRCGSSSVD PVSVNRLSFV RNRCRNGLGS VKDGEPHFVV VHCTGYIKAW 310 320 330 340 350 360 PPAGVSLPDD DPEAGQGSKF CLVAIGRLQV TSSPNCTDMS NVCQPTEFIS RHNIEGIFTF 370 380 390 400 410 420 VDHRCVATVG YQPQELLGKN IVEFCHPEDQ QLLRDSFQQV VKLKGQVLSV MFRFRSKNQE 430 440 450 460 470 480 WLWMRTSSFT FQNPYSDEIE YIICTNTNVK NSSQEPRPTL SNTIQRPQLG PTANLPLEMG 490 500 510 520 530 540 SGQLAPRQQQ QQTELDMVPG RDGLASYNHS QVVQPVTTTG PEHSKPLEKS DGLFAQDRDP 550 560 570 580 590 600 RFSEIYHNIN ADQSKGISSS TVPATQQLFS QGNTFPPTPR PAENFRNSGL APPVTIVQPS 610 620 630 640 650 660 ASAGQMLAQI SRHSNPTQGA TPTWTPTTRS GFSAQQVATQ ATAKTRTSQF GVGSFQTPSS 670 680 690 700 710 720 FSSMSLPGAP TASPGAAAYP SLTNRGSNFA PETGQTAGQF QTRTAEGVGV WPQWQGQQPH 730 740 750 760 770 HRSSSSEQHV QQPPAQQPGQ PEVFQEMLSM LGDQSNSYNN EEFPDLTMFP PFSE
	Isoform 3 [UniParc]. Checksum: 74839AACC350CB6B	FASTA	775	85,296
	10 20 30 40 50 60 MTSDVPSLGP AIASGNSGPG IQGGGAIVQR AIKRRPGLDF DDDGEGNSKF LRCDDDQMSN 70 80 90 100 110 120 DKERFARSDD EQSSADKERL ARENHSEIER RRRNKMTAYI TELSDMVPTC SALARKPDKL 130 140 150 160 170 180 TILRMAVSHM KSLRGTGNTS TDGSYKPSFL TDQELKHLIL EAADGFLFIV SCETGRVVYV 190 200 210 220 230 240 SDSVTPVLNQ PQSEWFGSTL YDQVHPDDVD KLREQLSTSE NALTGRILDL KTGTVKKEGQ 250 260 270 280 290 300 QSSMRMCMGS RRSFICRMRC GSSSVDPVSV NRLSFVRNRC RNGLGSVKDG EPHFVVVHCT 310 320 330 340 350 360 GYIKAWPPAD DDPEAGQGSK FCLVAIGRLQ VTSSPNCTDM SNVCQPTEFI SRHNIEGIFT 370 380 390 400 410 420 FVDHRCVATV GYQPQELLGK NIVEFCHPED QQLLRDSFQQ VVKLKGQVLS VMFRFRSKNQ 430 440 450 460 470 480 EWLWMRTSSF TFQNPYSDEI EYIICTNTNV KNSSQEPRPT LSNTIQRPQL GPTANLPLEM 490 500 510 520 530 540 GSGQLAPRQQ QQQTELDMVP GRDGLASYNH SQVVQPVTTT GPEHSKPLEK SDGLFAQDRD 550 560 570 580 590 600 PRFSEIYHNI NADQSKGISS STVPATQQLF SQGNTFPPTP RPAENFRNSG LAPPVTIVQP 610 620 630 640 650 660 SASAGQMLAQ ISRHSNPTQG ATPTWTPTTR SGFSAQQVAT QATAKTRTSQ FGVGSFQTPS 670 680 690 700 710 720 SFSSMSLPGA PTASPGAAAY PSLTNRGSNF APETGQTAGQ FQTRTAEGVG VWPQWQGQQP 730 740 750 760 770 HHRSSSSEQH VQQPPAQQPG QPEVFQEMLS MLGDQSNSYN NEEFPDLTMF PPFSE

References

	« Hide 'large scale' referencesShow '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: 1852076] [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: 14702039] [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: 17974005] [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. , 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: 16710414] [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. , 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: 7539918] [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: 1317062] [Abstract] Cited for: CHARACTERIZATION.
[10]	"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: 10395741] [Abstract] Cited for: INTERACTION WITH NOCA7.
[11]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 20699359] [Abstract] Cited for: INTERACTION WITH HIF1A.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M69238 mRNA. Translation: AAA51777.1.
Y18859 , AJ404853, AJ404852, AJ404851, AJ404854, AJ251863 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.

IPI

IPI00218287.
IPI00514749.
IPI00922490.

PIR

I59550.

RefSeq

NP_001184254.1. NM_001197325.1.
NP_001659.1. NM_001668.3.
NP_848514.1. NM_178427.2.

UniGene

Hs.632446.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P27540.

SMR

P27540. Positions 90-145, 171-469.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-30886N.

IntAct

P27540. 18 interactions.

MINT

MINT-1196758.

STRING

P27540.

PTM databases

PhosphoSite

P27540.

Polymorphism databases

DMDM

114163.

Proteomic databases

PRIDE

P27540.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000358595; ENSP00000351407; ENSG00000143437.

GeneID

405.

KEGG

hsa:405.

UCSC

uc001evr.1. human.
uc001evs.1. human.

Organism-specific databases

CTD

405.

GeneCards

GC01M150782.

H-InvDB

HIX0199938.

HGNC

HGNC:700. ARNT.

HPA

CAB004318.
HPA001759.

MIM

126110. gene.

neXtProt

NX_P27540.

PharmGKB

PA24994.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

HBG000164.

OMA

KFCLVAI.

OrthoDB

EOG4R7V9H.

PhylomeDB

P27540.

Enzyme and pathway databases

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.
hif1apathway. Hypoxic and oxygen homeostasis regulation of HIF-1-alpha.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.

Gene expression databases

ArrayExpress

P27540.

Bgee

P27540.

CleanEx

HS_ARNT.

Genevestigator

P27540.

GermOnline

ENSG00000143437. Homo sapiens.

Family and domain databases

InterPro

IPR011598. HLH_DNA-bd.
IPR001067. Nuc_translocat.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR013655. PAS_fold_3.
[Graphical view]

Gene3D

G3DSA:4.10.280.10. HLH_DNA_bd. 1 hit.

KO

K09097.

Pfam

PF00010. HLH. 1 hit.
PF00989. PAS. 1 hit.
PF08447. PAS_3. 1 hit.
[Graphical view]

PRINTS

PR00785. NCTRNSLOCATR.

SMART

SM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]

SUPFAM

SSF47459. HLH_basic. 1 hit.

TIGRFAMs

TIGR00229. Sensory_box. 1 hit.

PROSITE

PS50888. HLH. 1 hit.
PS50113. PAC. False negative.
PS50112. PAS. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

1693.

SOURCE

Search...

Entry information

Entry name

ARNT_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.