O00327 (BMAL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aryl hydrocarbon receptor nuclear translocator-like protein 1

Alternative name(s):
Basic-helix-loop-helix-PAS protein MOP3
Brain and muscle ARNT-like 1
Class E basic helix-loop-helix protein 5
Short name=bHLHe5
Member of PAS protein 3
PAS domain-containing protein 3
bHLH-PAS protein JAP3

Gene names

Name:	ARNTL
Synonyms:	BHLHE5, BMAL1, MOP3, PASD3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	626 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	ARNTL-CLOCK heterodimers activate E-box element (5'-CACGTG-3') transcription of a number of proteins of the circadian clock. This transcription is inhibited in a feedback loop by PER, and also by CRY proteins By similarity.
Subunit structure	Interacts with CRY2 By similarity. Component of the circadian clock oscillator which includes the CRY proteins, CLOCK or NPAS2, ARNTL or ARNTL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Efficient DNA binding requires dimerization with another bHLH protein. Heterodimerization with CLOCK is required for E-box-dependent transactivation, for CLOCK nuclear translocation and degradation, and, for phosphorylation of both CLOCK and ARNTL. Interaction with PER and CRY proteins requires translocation to the nucleus. Interaction of the CLOCK-ARNTL heterodimer with PER or CRY inhibits transcription activation. Interacts with HSP90; with AHR in vitro, but not in vivo. Part of a nuclear complex which also includes GNB2L1/RACK1 and PRKCA; GNB2L1 and PRKCA are recruited to the complex in a circadian manner. Ref.2 Ref.10
Subcellular location	Nucleus By similarity.
Tissue specificity	Highly expressed in the adult brain, skeletal muscle and heart.
Post-translational modification	Acetylated on Lys-538 upon dimerization with CLOCK. Acetylation facilitates CRY1-mediated repression By similarity. Phosphorylated upon dimerization with CLOCK By similarity. Sumoylated on Lys-259 upon dimerization with CLOCK By similarity.
Miscellaneous	CLOCK-ARNTL double mutations within the PAS domains result in syngernistic desensitization to high levels of CRY on repression of CLOCK-ARNTL transcriptional activity of PER1 and, disrupt circadian rhythmicity.
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.

Ontologies

Keywords
Biological process	Biological rhythms Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	DNA-binding
Molecular function	Activator
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	circadian regulation of gene expression Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 20093779. Source: BHF-UCL protein import into nucleus, translocation Inferred from electronic annotation. Source: Compara regulation of protein catabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro nuclear body Inferred from electronic annotation. Source: Compara transcription factor complex Inferred from physical interaction Ref.4. Source: MGI
Molecular_function	DNA binding Inferred from genetic interaction Ref.4. Source: MGI Hsp90 protein binding Inferred from direct assay Ref.2. Source: BHF-UCL RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity Inferred from sequence or structural similarity. Source: BHF-UCL RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Inferred from electronic annotation. Source: Compara signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform BMAL1B (identifier: O00327-2)

Also known as: JAP3;

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 BMAL1A (identifier: O00327-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: MADQRMDISSTISDFMSPGPTDLLSSSLGTSGVDCNRKRKGSSTDYQ → MINI

Isoform BMAL1C (identifier: O00327-3)

The sequence of this isoform differs from the canonical sequence as follows:
     224-224: T → R
     225-626: Missing.

Isoform BMAL1D (identifier: O00327-4)

The sequence of this isoform differs from the canonical sequence as follows:
     274-391: Missing.

Isoform BMAL1E (identifier: O00327-5)

The sequence of this isoform differs from the canonical sequence as follows:
     278-301: SFCTIHSTGYLKSWPPTKMGLDED → AFCTIHSTGYFGIFTTRTSRHIVL
     302-626: Missing.

Isoform BMAL1F (identifier: O00327-6)

The sequence of this isoform differs from the canonical sequence as follows:
     443-526: ANVLEGGDPT...CGSSPLNITS → SRVDTGHLGQ...QGEPGLGQEK
     527-626: Missing.

Isoform MOP3 (identifier: O00327-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: MADQRMDISS...MDTDKDDPHG → MSKEAVSLWA...CFYLLLFPPP

Isoform 8 (identifier: O00327-8)

The sequence of this isoform differs from the canonical sequence as follows:
     274-274: Missing.

Isoform 9 (identifier: O00327-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: MADQRMDISSTISDFMSPGPTDLLSSSLGTSGVDCNRKRKGSSTDYQ → MINI
     274-274: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 626

626

Aryl hydrocarbon receptor nuclear translocator-like protein 1

PRO_0000127156

Regions

Domain

72 – 125

54

bHLH

Domain

143 – 215

73

PAS 1

Domain

326 – 396

71

PAS 2

Domain

401 – 444

44

PAC

Amino acid modifications

Modified residue

538

1

N6-acetyllysine By similarity

Cross-link

259

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence

1 – 59

59

MADQR…DDPHG → MSKEAVSLWALTVSLQPPVP LCVCREMTGSGRRKQQCVTL PFISRELCFYLLLFPPP in isoform MOP3.

VSP_002095

Alternative sequence

1 – 47

47

MADQR…STDYQ → MINI in isoform BMAL1A and isoform 9.

VSP_002094

Alternative sequence

224

1

T → R in isoform BMAL1C.

VSP_002096

Alternative sequence

225 – 626

402

Missing in isoform BMAL1C.

VSP_002097

Alternative sequence

274 – 391

118

Missing in isoform BMAL1D.

VSP_002098

Alternative sequence

274

1

Missing in isoform 8 and isoform 9.

VSP_035457

Alternative sequence

278 – 301

24

SFCTI…GLDED → AFCTIHSTGYFGIFTTRTSR HIVL in isoform BMAL1E.

VSP_002099

Alternative sequence

302 – 626

325

Missing in isoform BMAL1E.

VSP_002100

Alternative sequence

443 – 526

84

ANVLE…LNITS → SRVDTGHLGQVERCTVLSRP NSRFLIAGMFTEPTSWKAGT QPSHSSQHPPTAWTACCPLE KVAQRGPTPLFQGFQGEPGL GQEK in isoform BMAL1F.

VSP_002101

Alternative sequence

527 – 626

100

Missing in isoform BMAL1F.

VSP_002102

Experimental info

Mutagenesis

9

1

S → A or E: Enhanced PER1 reporter activity by CLOCK-ARNTL. Ref.11

Mutagenesis

9

1

S → F: 2-2.5-fold increase in CLOCK-BMAL1 transcriptional activity in the absence of CRY1. No change in repression activity in the presence of CRY1. Ref.11

Mutagenesis

10

1

S → A or E: Enhanced PER1 reporter activity by CLOCK-ARNTL. Ref.11

Mutagenesis

10

1

S → L: 2-2.5-fold increase in CLOCK-ARNTL transcriptional activity in the absence of CRY1. No change in repression activity in the presence of CRY1. Ref.11

Mutagenesis

611

1

A → S or T: Increased desensitization to CRY1, in the presence of CLOCK. Approximately 2-fold increase in CLOCK-ARNTL transcriptional activity in the absence of CRY1; when associated with E-407. Ref.11

Mutagenesis

612

1

G → E: Increased desensitization to CRY1, in the presence of CLOCK. Approximately 2-fold increase in CLOCK-ARNTL transcriptional activity in the absence of CRY1. Ref.11

Sequence conflict

69

1

R → G in AAC51213. Ref.2

Sequence conflict

123

1

K → R in BAA19935. Ref.1

Sequence conflict

173

1

S → P in BAA19939. Ref.1

Sequence conflict

259

1

K → N in BAA19938. Ref.1

Sequence conflict

264

1

D → N in BAA19938. Ref.1

Sequence conflict

418

1

S → N in BAA19937. Ref.1

Sequence conflict

513 – 514

2

SP → LR in AAC51213. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

626

Helix Strand Turn

Details...

Helix

71 – 98

28

Helix

100 – 103

4

Helix

111 – 125

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform BMAL1B (JAP3) [UniParc]. Last modified August 15, 2003. Version 2. Checksum: 820F0E07DC6265A6	FASTA	626	68,762
	10 20 30 40 50 60 MADQRMDISS TISDFMSPGP TDLLSSSLGT SGVDCNRKRK GSSTDYQESM DTDKDDPHGR 70 80 90 100 110 120 LEYTEHQGRI KNAREAHSQI EKRRRDKMNS FIDELASLVP TCNAMSRKLD KLTVLRMAVQ 130 140 150 160 170 180 HMKTLRGATN PYTEANYKPT FLSDDELKHL ILRAADGFLF VVGCDRGKIL FVSESVFKIL 190 200 210 220 230 240 NYSQNDLIGQ SLFDYLHPKD IAKVKEQLSS SDTAPRERLI DAKTGLPVKT DITPGPSRLC 250 260 270 280 290 300 SGARRSFFCR MKCNRPSVKV EDKDFPSTCS KKKADRKSFC TIHSTGYLKS WPPTKMGLDE 310 320 330 340 350 360 DNEPDNEGCN LSCLVAIGRL HSHVVPQPVN GEIRVKSMEY VSRHAIDGKF VFVDQRATAI 370 380 390 400 410 420 LAYLPQELLG TSCYEYFHQD DIGHLAECHR QVLQTREKIT TNCYKFKIKD GSFITLRSRW 430 440 450 460 470 480 FSFMNPWTKE VEYIVSTNTV VLANVLEGGD PTFPQLTASP HSMDSMLPSG EGGPKRTHPT 490 500 510 520 530 540 VPGIPGGTRA GAGKIGRMIA EEIMEIHRIR GSSPSSCGSS PLNITSTPPP DASSPGGKKI 550 560 570 580 590 600 LNGGTPDIPS SGLLSGQAQE NPGYPYSDSS SILGENPHIG IDMIDNDQGS SSPSNDEAAM 610 620 AVIMSLLEAD AGLGGPVDFS DLPWPL
	Isoform BMAL1A [UniParc]. Checksum: 2AA8E7EEB4A71119	FASTA	583	64,207
	10 20 30 40 50 60 MINIESMDTD KDDPHGRLEY TEHQGRIKNA REAHSQIEKR RRDKMNSFID ELASLVPTCN 70 80 90 100 110 120 AMSRKLDKLT VLRMAVQHMK TLRGATNPYT EANYKPTFLS DDELKHLILR AADGFLFVVG 130 140 150 160 170 180 CDRGKILFVS ESVFKILNYS QNDLIGQSLF DYLHPKDIAK VKEQLSSSDT APRERLIDAK 190 200 210 220 230 240 TGLPVKTDIT PGPSRLCSGA RRSFFCRMKC NRPSVKVEDK DFPSTCSKKK ADRKSFCTIH 250 260 270 280 290 300 STGYLKSWPP TKMGLDEDNE PDNEGCNLSC LVAIGRLHSH VVPQPVNGEI RVKSMEYVSR 310 320 330 340 350 360 HAIDGKFVFV DQRATAILAY LPQELLGTSC YEYFHQDDIG HLAECHRQVL QTREKITTNC 370 380 390 400 410 420 YKFKIKDGSF ITLRSRWFSF MNPWTKEVEY IVSTNTVVLA NVLEGGDPTF PQLTASPHSM 430 440 450 460 470 480 DSMLPSGEGG PKRTHPTVPG IPGGTRAGAG KIGRMIAEEI MEIHRIRGSS PSSCGSSPLN 490 500 510 520 530 540 ITSTPPPDAS SPGGKKILNG GTPDIPSSGL LSGQAQENPG YPYSDSSSIL GENPHIGIDM 550 560 570 580 IDNDQGSSSP SNDEAAMAVI MSLLEADAGL GGPVDFSDLP WPL
	Isoform BMAL1C [UniParc]. Checksum: 0A0580AEDC5A45A0	FASTA	224	25,353
	10 20 30 40 50 60 MADQRMDISS TISDFMSPGP TDLLSSSLGT SGVDCNRKRK GSSTDYQESM DTDKDDPHGR 70 80 90 100 110 120 LEYTEHQGRI KNAREAHSQI EKRRRDKMNS FIDELASLVP TCNAMSRKLD KLTVLRMAVQ 130 140 150 160 170 180 HMKTLRGATN PYTEANYKPT FLSDDELKHL ILRAADGFLF VVGCDRGKIL FVSESVFKIL 190 200 210 220 NYSQNDLIGQ SLFDYLHPKD IAKVKEQLSS SDTAPRERLI DAKR
	Isoform BMAL1D [UniParc]. Checksum: 5FAB2403FD8AAB32	FASTA	508	55,462
	10 20 30 40 50 60 MADQRMDISS TISDFMSPGP TDLLSSSLGT SGVDCNRKRK GSSTDYQESM DTDKDDPHGR 70 80 90 100 110 120 LEYTEHQGRI KNAREAHSQI EKRRRDKMNS FIDELASLVP TCNAMSRKLD KLTVLRMAVQ 130 140 150 160 170 180 HMKTLRGATN PYTEANYKPT FLSDDELKHL ILRAADGFLF VVGCDRGKIL FVSESVFKIL 190 200 210 220 230 240 NYSQNDLIGQ SLFDYLHPKD IAKVKEQLSS SDTAPRERLI DAKTGLPVKT DITPGPSRLC 250 260 270 280 290 300 SGARRSFFCR MKCNRPSVKV EDKDFPSTCS KKKVLQTREK ITTNCYKFKI KDGSFITLRS 310 320 330 340 350 360 RWFSFMNPWT KEVEYIVSTN TVVLANVLEG GDPTFPQLTA SPHSMDSMLP SGEGGPKRTH 370 380 390 400 410 420 PTVPGIPGGT RAGAGKIGRM IAEEIMEIHR IRGSSPSSCG SSPLNITSTP PPDASSPGGK 430 440 450 460 470 480 KILNGGTPDI PSSGLLSGQA QENPGYPYSD SSSILGENPH IGIDMIDNDQ GSSSPSNDEA 490 500 AMAVIMSLLE ADAGLGGPVD FSDLPWPL
	Isoform BMAL1E [UniParc]. Checksum: EC942D8A9C9219B3	FASTA	301	33,922
	10 20 30 40 50 60 MADQRMDISS TISDFMSPGP TDLLSSSLGT SGVDCNRKRK GSSTDYQESM DTDKDDPHGR 70 80 90 100 110 120 LEYTEHQGRI KNAREAHSQI EKRRRDKMNS FIDELASLVP TCNAMSRKLD KLTVLRMAVQ 130 140 150 160 170 180 HMKTLRGATN PYTEANYKPT FLSDDELKHL ILRAADGFLF VVGCDRGKIL FVSESVFKIL 190 200 210 220 230 240 NYSQNDLIGQ SLFDYLHPKD IAKVKEQLSS SDTAPRERLI DAKTGLPVKT DITPGPSRLC 250 260 270 280 290 300 SGARRSFFCR MKCNRPSVKV EDKDFPSTCS KKKADRKAFC TIHSTGYFGI FTTRTSRHIV L
	Isoform BMAL1F [UniParc]. Checksum: ED01AF63A26CE4E0	FASTA	526	59,242
	10 20 30 40 50 60 MADQRMDISS TISDFMSPGP TDLLSSSLGT SGVDCNRKRK GSSTDYQESM DTDKDDPHGR 70 80 90 100 110 120 LEYTEHQGRI KNAREAHSQI EKRRRDKMNS FIDELASLVP TCNAMSRKLD KLTVLRMAVQ 130 140 150 160 170 180 HMKTLRGATN PYTEANYKPT FLSDDELKHL ILRAADGFLF VVGCDRGKIL FVSESVFKIL 190 200 210 220 230 240 NYSQNDLIGQ SLFDYLHPKD IAKVKEQLSS SDTAPRERLI DAKTGLPVKT DITPGPSRLC 250 260 270 280 290 300 SGARRSFFCR MKCNRPSVKV EDKDFPSTCS KKKADRKSFC TIHSTGYLKS WPPTKMGLDE 310 320 330 340 350 360 DNEPDNEGCN LSCLVAIGRL HSHVVPQPVN GEIRVKSMEY VSRHAIDGKF VFVDQRATAI 370 380 390 400 410 420 LAYLPQELLG TSCYEYFHQD DIGHLAECHR QVLQTREKIT TNCYKFKIKD GSFITLRSRW 430 440 450 460 470 480 FSFMNPWTKE VEYIVSTNTV VLSRVDTGHL GQVERCTVLS RPNSRFLIAG MFTEPTSWKA 490 500 510 520 GTQPSHSSQH PPTAWTACCP LEKVAQRGPT PLFQGFQGEP GLGQEK
	Isoform MOP3 [UniParc]. Checksum: 7A3FD8FAE5E496D7	FASTA	624	68,828
	10 20 30 40 50 60 MSKEAVSLWA LTVSLQPPVP LCVCREMTGS GRRKQQCVTL PFISRELCFY LLLFPPPRLE 70 80 90 100 110 120 YTEHQGRIKN AREAHSQIEK RRRDKMNSFI DELASLVPTC NAMSRKLDKL TVLRMAVQHM 130 140 150 160 170 180 KTLRGATNPY TEANYKPTFL SDDELKHLIL RAADGFLFVV GCDRGKILFV SESVFKILNY 190 200 210 220 230 240 SQNDLIGQSL FDYLHPKDIA KVKEQLSSSD TAPRERLIDA KTGLPVKTDI TPGPSRLCSG 250 260 270 280 290 300 ARRSFFCRMK CNRPSVKVED KDFPSTCSKK KADRKSFCTI HSTGYLKSWP PTKMGLDEDN 310 320 330 340 350 360 EPDNEGCNLS CLVAIGRLHS HVVPQPVNGE IRVKSMEYVS RHAIDGKFVF VDQRATAILA 370 380 390 400 410 420 YLPQELLGTS CYEYFHQDDI GHLAECHRQV LQTREKITTN CYKFKIKDGS FITLRSRWFS 430 440 450 460 470 480 FMNPWTKEVE YIVSTNTVVL ANVLEGGDPT FPQLTASPHS MDSMLPSGEG GPKRTHPTVP 490 500 510 520 530 540 GIPGGTRAGA GKIGRMIAEE IMEIHRIRGS SPSSCGSSPL NITSTPPPDA SSPGGKKILN 550 560 570 580 590 600 GGTPDIPSSG LLSGQAQENP GYPYSDSSSI LGENPHIGID MIDNDQGSSS PSNDEAAMAV 610 620 IMSLLEADAG LGGPVDFSDL PWPL
	Isoform 8 [UniParc]. Checksum: 3F3F7D5688A6FFE2	FASTA	625	68,691
	10 20 30 40 50 60 MADQRMDISS TISDFMSPGP TDLLSSSLGT SGVDCNRKRK GSSTDYQESM DTDKDDPHGR 70 80 90 100 110 120 LEYTEHQGRI KNAREAHSQI EKRRRDKMNS FIDELASLVP TCNAMSRKLD KLTVLRMAVQ 130 140 150 160 170 180 HMKTLRGATN PYTEANYKPT FLSDDELKHL ILRAADGFLF VVGCDRGKIL FVSESVFKIL 190 200 210 220 230 240 NYSQNDLIGQ SLFDYLHPKD IAKVKEQLSS SDTAPRERLI DAKTGLPVKT DITPGPSRLC 250 260 270 280 290 300 SGARRSFFCR MKCNRPSVKV EDKDFPSTCS KKKDRKSFCT IHSTGYLKSW PPTKMGLDED 310 320 330 340 350 360 NEPDNEGCNL SCLVAIGRLH SHVVPQPVNG EIRVKSMEYV SRHAIDGKFV FVDQRATAIL 370 380 390 400 410 420 AYLPQELLGT SCYEYFHQDD IGHLAECHRQ VLQTREKITT NCYKFKIKDG SFITLRSRWF 430 440 450 460 470 480 SFMNPWTKEV EYIVSTNTVV LANVLEGGDP TFPQLTASPH SMDSMLPSGE GGPKRTHPTV 490 500 510 520 530 540 PGIPGGTRAG AGKIGRMIAE EIMEIHRIRG SSPSSCGSSP LNITSTPPPD ASSPGGKKIL 550 560 570 580 590 600 NGGTPDIPSS GLLSGQAQEN PGYPYSDSSS ILGENPHIGI DMIDNDQGSS SPSNDEAAMA 610 620 VIMSLLEADA GLGGPVDFSD LPWPL
	Isoform 9 [UniParc]. Checksum: E8D6943E4DD24037	FASTA	582	64,136
	10 20 30 40 50 60 MINIESMDTD KDDPHGRLEY TEHQGRIKNA REAHSQIEKR RRDKMNSFID ELASLVPTCN 70 80 90 100 110 120 AMSRKLDKLT VLRMAVQHMK TLRGATNPYT EANYKPTFLS DDELKHLILR AADGFLFVVG 130 140 150 160 170 180 CDRGKILFVS ESVFKILNYS QNDLIGQSLF DYLHPKDIAK VKEQLSSSDT APRERLIDAK 190 200 210 220 230 240 TGLPVKTDIT PGPSRLCSGA RRSFFCRMKC NRPSVKVEDK DFPSTCSKKK DRKSFCTIHS 250 260 270 280 290 300 TGYLKSWPPT KMGLDEDNEP DNEGCNLSCL VAIGRLHSHV VPQPVNGEIR VKSMEYVSRH 310 320 330 340 350 360 AIDGKFVFVD QRATAILAYL PQELLGTSCY EYFHQDDIGH LAECHRQVLQ TREKITTNCY 370 380 390 400 410 420 KFKIKDGSFI TLRSRWFSFM NPWTKEVEYI VSTNTVVLAN VLEGGDPTFP QLTASPHSMD 430 440 450 460 470 480 SMLPSGEGGP KRTHPTVPGI PGGTRAGAGK IGRMIAEEIM EIHRIRGSSP SSCGSSPLNI 490 500 510 520 530 540 TSTPPPDASS PGGKKILNGG TPDIPSSGLL SGQAQENPGY PYSDSSSILG ENPHIGIDMI 550 560 570 580 DNDQGSSSPS NDEAAMAVIM SLLEADAGLG GPVDFSDLPW PL

References

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[1]	"cDNA cloning and tissue-specific expression of a novel basic helix-loop-helix/PAS protein (BMAL1) and identification of alternatively spliced variants with alternative translation initiation site usage." Ikeda M., Nomura M. Biochem. Biophys. Res. Commun. 233:258-264(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING (ISOFORMS BMAL1A; BMAL1B; BMAL1C; BMAL1D; BMAL1E AND BMAL1F). Tissue: Brain.
[2]	"Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway." Hogenesch J.B., Chan W.K., Jackiw V.H., Brown R.C., Gu Y.-Z., Pray-Grant M., Perdew G.H., Bradfield C.A. J. Biol. Chem. 272:8581-8593(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MOP3), INTERACTION WITH HSP90 AND AHR. Tissue: Fetal brain.
[3]	"JAP3: a novel ARNT-like bHLH-PAS protein." Tian H., Russell D.W., McKnight S.L. Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BMAL1B).
[4]	"The basic-helix-loop-helix-PAS orphan MOP3 forms transcriptionally active complexes with circadian and hypoxia factors." Hogenesch J.B., Gu Y.Z., Jain S., Bradfield C.A. Proc. Natl. Acad. Sci. U.S.A. 95:5474-5479(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BMAL1B).
[5]	"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] (ISOFORMS BMAL1B AND 9). Tissue: Brain.
[6]	"ARNTL resequence." Kripke D.F., Klimecki W. Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8 AND BMAL1A). Tissue: Brain and Skin.
[10]	"Role of the CLOCK protein in the mammalian circadian mechanism." Gekakis N., Staknis D., Nguyen H.B., Davis F.C., Wilsbacher L.D., King D.P., Takahashi J.S., Weitz C.J. Science 280:1564-1569(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CLOCK.
[11]	"Feedback repression is required for mammalian circadian clock function." Sato T.K., Yamada R.G., Ukai H., Baggs J.E., Miraglia L.J., Kobayashi T.J., Welsh D.K., Kay S.A., Ueda H.R., Hogenesch J.B. Nat. Genet. 38:312-319(2006) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF SER-9; SER-10; ALA-611 AND GLY-612.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D89722 mRNA. Translation: BAA19968.1.
AB000812 mRNA. Translation: BAA19935.1.
AB000813 Genomic DNA. Translation: BAA19936.1.
AB000814 mRNA. Translation: BAA19937.1.
AB000815 mRNA. Translation: BAA19938.1.
AB000816 mRNA. Translation: BAA19939.1.
U51627 mRNA. Translation: AAC51213.1.
U60415 mRNA. Translation: AAB37248.1.
AF044288 mRNA. Translation: AAC24353.1.
AK095749 mRNA. Translation: BAG53120.1.
AK291510 mRNA. Translation: BAF84199.1.
EF015894 Genomic DNA. Translation: ABM64205.1.
AC016884 Genomic DNA. No translation available.
AC022878 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68504.1.
CH471064 Genomic DNA. Translation: EAW68505.1.
CH471064 Genomic DNA. Translation: EAW68510.1.
CH471064 Genomic DNA. Translation: EAW68511.1.
CH471064 Genomic DNA. Translation: EAW68513.1.
BC016674 mRNA. Translation: AAH16674.1.
BC031214 mRNA. Translation: AAH31214.1.
BC041129 mRNA. Translation: AAH41129.2.

IPI

IPI00217732.
IPI00217734.
IPI00217735.
IPI00217736.
IPI00412162.
IPI00413132.
IPI00783543.
IPI00879656.
IPI00910251.

PIR

JC5405.
JC5407.
PC4288.
PC4289.

RefSeq

NP_001025443.1. NM_001030272.1.
NP_001025444.1. NM_001030273.1.
NP_001169.3. NM_001178.4.

UniGene

Hs.65734.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4H10	X-ray	2.40	A	66-128	[»]

ProteinModelPortal

O00327.

ModBase

Search...

Protein-protein interaction databases

IntAct

O00327. 2 interactions.

PTM databases

PhosphoSite

O00327.

Proteomic databases

PaxDb

O00327.

PRIDE

O00327.

Protocols and materials databases

DNASU

406.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361003; ENSP00000354278; ENSG00000133794.
ENST00000389707; ENSP00000374357; ENSG00000133794.
ENST00000396441; ENSP00000379718; ENSG00000133794.
ENST00000401424; ENSP00000385915; ENSG00000133794.
ENST00000403290; ENSP00000384517; ENSG00000133794.
ENST00000403482; ENSP00000385897; ENSG00000133794.
ENST00000403510; ENSP00000385581; ENSG00000133794.

GeneID

406.

KEGG

hsa:406.

UCSC

uc001mko.3. human.
uc001mkp.3. human.
uc001mkr.3. human.
uc001mks.3. human.
uc001mkx.3. human.
uc009ygm.1. human.

Organism-specific databases

CTD

406.

GeneCards

GC11P013299.

HGNC

HGNC:701. ARNTL.

HPA

CAB045962.

MIM

602550. gene.

neXtProt

NX_O00327.

PharmGKB

PA24996.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG293303.

HOGENOM

HOG000234379.

HOVERGEN

HBG107503.

InParanoid

O00327.

KO

K02296.

OMA

EKINTNC.

OrthoDB

EOG4NS3B2.

Enzyme and pathway databases

Pathway_Interaction_DB

circadianpathway. Circadian rhythm pathway.

Reactome

REACT_24941. Circadian Clock.

Gene expression databases

ArrayExpress

O00327.

Bgee

O00327.

Genevestigator

O00327.

GermOnline

ENSG00000133794. Homo sapiens.

Family and domain databases

Gene3D

4.10.280.10. 1 hit.

InterPro

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

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.
SSF55785. SSF55785. 2 hits.

TIGRFAMs

TIGR00229. sensory_box. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

GenomeRNAi

406.

NextBio

1701.

SOURCE

Search...

Entry information

Entry name

BMAL1_HUMAN

Accession

Primary (citable) accession number: O00327
Secondary accession number(s): A2I2N6 , A8K645, B5ME11, B7WPG7, D3DQW6, O00313, O00314, O00315, O00316, O00317, Q4G136, Q8IUT4, Q99631, Q99649

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 15, 2003
Last modified:	May 29, 2013
This is version 139 of the entry and version 2 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.