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Protein

Aryl hydrocarbon receptor nuclear translocator-like protein 1

Gene

Arntl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. ARNTL/BMAL1 positively regulates myogenesis and negatively regulates adipogenesis via the transcriptional control of the genes of the canonical Wnt signaling pathway. Plays a role in normal pancreatic beta-cell function; regulates glucose-stimulated insulin secretion via the regulation of antioxidant genes NFE2L2/NRF2 and its targets SESN2, PRDX3, CCLC and CCLM. Negatively regulates the mTORC1 signaling pathway; regulates the expression of MTOR and DEPTOR. Controls diurnal oscillations of Ly6C inflammatory monocytes; rhythmic recruitment of the PRC2 complex imparts diurnal variation to chemokine expression that is necessary to sustain Ly6C monocyte rhythms. Regulates the expression of HSD3B2, STAR, PTGS2, CYP11A1, CYP19A1 and LHCGR in the ovary and also the genes involved in hair growth. Plays an important role in adult hippocampal neurogenesis by regulating the timely entry of neural stem/progenitor cells (NSPCs) into the cell cycle and the number of cell divisions that take place prior to cell-cycle exit. Regulates the circadian expression of CIART and KLF11. The CLOCK-ARNTL/BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. May play a role in spermatogenesis; contributes to the chromatoid body assembly and physiology. The NPAS2-ARNTL/BMAL1 heterodimer positively regulates the expression of MAOA, F7 and LDHA and modulates the circadian rhythm of daytime contrast sensitivity by regulating the rhythmic expression of adenylate cyclase type 1 (ADCY1) in the retina.38 Publications

Enzyme regulationi

The redox state of the cell can modulate the transcriptional activity of the CLOCK-ARNTL/BMAL1 and NPAS2-ARNTL/BMAL1 heterodimers; NADH and NADPH enhance the DNA-binding activity of the heterodimers.By similarity

GO - Molecular functioni

  • aryl hydrocarbon receptor binding Source: MGI
  • bHLH transcription factor binding Source: BHF-UCL
  • core promoter binding Source: UniProtKB
  • core promoter sequence-specific DNA binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • E-box binding Source: UniProtKB
  • Hsp90 protein binding Source: MGI
  • protein heterodimerization activity Source: BHF-UCL
  • repressing transcription factor binding Source: MGI
  • sequence-specific DNA binding Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: BHF-UCL
  • transcriptional activator activity, RNA polymerase II transcription factor binding Source: BHF-UCL
  • transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: BHF-UCL
  • transcription factor activity, sequence-specific DNA binding Source: MGI
  • transcription factor binding Source: MGI
  • transcription regulatory region sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • circadian regulation of gene expression Source: UniProtKB
  • circadian rhythm Source: UniProtKB
  • maternal process involved in parturition Source: CACAO
  • negative regulation of fat cell differentiation Source: UniProtKB
  • negative regulation of glucocorticoid receptor signaling pathway Source: UniProtKB
  • negative regulation of TOR signaling Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • oxidative stress-induced premature senescence Source: UniProtKB
  • positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  • positive regulation of circadian rhythm Source: UniProtKB
  • positive regulation of skeletal muscle cell differentiation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein import into nucleus, translocation Source: MGI
  • regulation of cell cycle Source: UniProtKB
  • regulation of cellular senescence Source: UniProtKB
  • regulation of hair cycle Source: UniProtKB
  • regulation of insulin secretion Source: UniProtKB
  • regulation of neurogenesis Source: UniProtKB
  • regulation of protein catabolic process Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of type B pancreatic cell development Source: UniProtKB
  • response to redox state Source: UniProtKB
  • spermatogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1368082. RORA activates gene expression.
R-MMU-1368092. Rora activates gene expression.
R-MMU-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-MMU-1368110. Bmal1:Clock,Npas2 activates circadian gene expression.
R-MMU-1989781. PPARA activates gene expression.
R-MMU-400253. Circadian Clock.
R-MMU-508751. Circadian Clock.

Names & Taxonomyi

Protein namesi
Recommended name:
Aryl hydrocarbon receptor nuclear translocator-like protein 1
Alternative name(s):
Arnt3
Brain and muscle ARNT-like 1
Gene namesi
Name:Arntl
Synonyms:Bmal1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1096381. Arntl.

Subcellular locationi

GO - Cellular componenti

  • chromatoid body Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • intracellular membrane-bounded organelle Source: MGI
  • nuclear body Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB-SubCell
  • transcription factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice are characterized by reduced lifespan, and the presence of a number of pathologies characteristic of pre-mature aging and increased oxidative stress. They show impaired functional connectivity, increased oxidative damage and severe astrogliosis in the brain. They also exhibit accelerated thrombosis with elevated levels of thrombogenic factors, including VWF, SERPINE1/PAI1, and fibrinogen. Both male and female mice are infertile and male mice have low testosterone and high luteinizing hormone serum levels and a significant decrease in sperm count.4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi38 – 39KR → AA: Loss of nuclear localization. 1 Publication2
Mutagenesisi97S → A: Impaired nuclear accumulation, decreased interaction with CLOCK and disruption of circadain clock function. 1 Publication1
Mutagenesisi102L → E: Reduced CLOCK binding. Abolishes transcriptional activation by the CLOCK-ARNTL/BMAL1 heterodimer. 1 Publication1
Mutagenesisi122L → E: Reduced CLOCK binding. Abolishes transcriptional activation by the CLOCK-ARNTL/BMAL1 heterodimer. 1 Publication1
Mutagenesisi154L → A: Significant reduction in nucleocytoplasmic shuttling; when associated with A-157. 1 Publication1
Mutagenesisi157L → A: Significant reduction in nucleocytoplasmic shuttling; when associated with A-154. 1 Publication1
Mutagenesisi230K → R: No effect on sumoylation. 1 Publication1
Mutagenesisi236K → R: No effect on sumoylation. 1 Publication1
Mutagenesisi259K → R: Significant decrease in; transcriptional activity, localization in PML body, ubiquitination and proteasome-mediated proteolysis. 1 Publication1
Mutagenesisi266K → R: Abolishes sumoylation. 1 Publication1
Mutagenesisi279K → R: No effect on sumoylation. 1 Publication1
Mutagenesisi323I → D: Reduced CLOCK binding. Slightly reduced transcriptional activation by the CLOCK-ARNTL/BMAL1 heterodimer. Impairs regulation of circadian clock. 1 Publication1
Mutagenesisi370L → A: Significant reduction in nucleocytoplasmic shuttling; when associated with A-374. 1 Publication1
Mutagenesisi374L → A: Significant reduction in nucleocytoplasmic shuttling; when associated with A-370. 1 Publication1
Mutagenesisi418S → A: Decreases without abolishing O-GlcNAcylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001271581 – 632Aryl hydrocarbon receptor nuclear translocator-like protein 1Add BLAST632

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17Phosphoserine; by GSK3-beta1 Publication1
Modified residuei21Phosphothreonine; by GSK3-beta1 Publication1
Modified residuei97Phosphoserine; by CK21 Publication1
Cross-linki259Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3)1 Publication
Cross-linki266Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei544N6-acetyllysine1 Publication1

Post-translational modificationi

Ubiquitinated, leading to its proteasomal degradation.3 Publications
O-glycosylated; contains O-GlcNAc. O-glycosylation by OGT prevents protein degradation by inhibiting ubiquitination. It also stabilizes the CLOCK-ARNTL/BMAL1 heterodimer thereby increasing CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2/3 and CRY1/2.2 Publications
Acetylated on Lys-544 upon dimerization with CLOCK. Acetylation facilitates CRY1-mediated repression. Deacetylated by SIRT1, which may result in decreased protein stability.2 Publications
Phosphorylated upon dimerization with CLOCK. Phosphorylation enhances the transcriptional activity, alters the subcellular localization and decreases the stability of the CLOCK-ARNTL/BMAL1 heterodimer by promoting its degradation. Phosphorylation shows circadian variations in the liver with a peak between CT10 to CT14. Phosphorylation at Ser-97 by CK2 is essential for its nuclear localization, its interaction with CLOCK and controls CLOCK nuclear entry.6 Publications
Sumoylated on Lys-266 upon dimerization with CLOCK. Predominantly conjugated to poly-SUMO2/3 rather than SUMO1 and the level of these conjugates undergo rhythmic variation, peaking at CT9-CT12. Sumoylation localizes it exclusively to the PML body and promotes its ubiquitination in the PML body, ubiquitin-dependent proteasomal degradation and the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer.2 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9WTL8.
PRIDEiQ9WTL8.

PTM databases

iPTMnetiQ9WTL8.
PhosphoSitePlusiQ9WTL8.

Expressioni

Tissue specificityi

Expressed in liver and testis (at protein level).5 Publications

Inductioni

Expressed in a circadian manner in the liver.4 Publications

Gene expression databases

BgeeiENSMUSG00000055116.
ExpressionAtlasiQ9WTL8. baseline and differential.
GenevisibleiQ9WTL8. MM.

Interactioni

Subunit structurei

Component of the circadian clock oscillator which includes the CRY1/2 proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER1/2/3 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/BMAL1. Part of a nuclear complex which also includes RACK1 and PRKCA; RACK1 and PRKCA are recruited to the complex in a circadian manner. Interacts with NPAS2, HSP90, AHR, CIART, DDX4, SUMO3, OGT, EED, EZH2, SUZ12, KAT2B, EP300, BHLHE40/DEC1, BHLHE41/DEC2, ID1, ID2, ID3, MTA1 and SIRT1. Interacts with RELB and the interaction is enhanced in the presence of CLOCK. Interacts with PER1, PER2, CRY1 and CRY2 and this interaction requires a translocation to the nucleus. Interaction of the CLOCK-ARNTL/BMAL1 heterodimer with PER or CRY inhibits transcription activation. Interaction of the CLOCK-ARNTL/BMAL1 with CRY1 is independent of DNA but with PER2 is off DNA. The CLOCK-ARNTL/BMAL1 heterodimer interacts with GSK3B. Interacts with KDM5A. Interacts with KMT2A in a circadian manner. Interacts with UBE3A (By similarity). Interacts with PRKCG. Interacts with MAGEL2. Interacts with NCOA2. Interacts with THRAP3. The CLOCK-ARNTL/BMAL1 heterodimer interacts with PASD1 (By similarity). Interacts with PASD1 (By similarity).By similarity34 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ClockO0878524EBI-644534,EBI-79859
Cry1P9778412EBI-644534,EBI-1266607
Cry2Q99JJ14EBI-644534,EBI-1794634
Cry2Q9R1946EBI-644534,EBI-1266619
Parp1P111037EBI-644534,EBI-642213
Per2O549438EBI-644534,EBI-1266779
Ppp1caP621372EBI-644534,EBI-357187
RORCP514492EBI-644534,EBI-3908771From a different organism.
WDR5P619642EBI-644534,EBI-540834From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198207. 17 interactors.
DIPiDIP-43977N.
IntActiQ9WTL8. 20 interactors.
MINTiMINT-1657344.
STRINGi10090.ENSMUSP00000046235.

Structurei

Secondary structure

1632
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi79 – 105Combined sources27
Helixi107 – 111Combined sources5
Helixi118 – 133Combined sources16
Helixi151 – 160Combined sources10
Beta strandi164 – 170Combined sources7
Turni171 – 173Combined sources3
Beta strandi175 – 179Combined sources5
Helixi183 – 187Combined sources5
Helixi191 – 194Combined sources4
Helixi199 – 202Combined sources4
Helixi205 – 207Combined sources3
Helixi208 – 215Combined sources8
Helixi248 – 250Combined sources3
Beta strandi251 – 259Combined sources9
Beta strandi284 – 295Combined sources12
Beta strandi319 – 326Combined sources8
Beta strandi337 – 339Combined sources3
Beta strandi345 – 350Combined sources6
Beta strandi354 – 359Combined sources6
Helixi362 – 367Combined sources6
Helixi371 – 374Combined sources4
Helixi379 – 381Combined sources3
Helixi385 – 398Combined sources14
Beta strandi410 – 413Combined sources4
Beta strandi419 – 431Combined sources13
Turni432 – 435Combined sources4
Beta strandi436 – 446Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F3LX-ray2.27B69-453[»]
DisProtiDP00735.
ProteinModelPortaliQ9WTL8.
SMRiQ9WTL8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini79 – 132bHLHPROSITE-ProRule annotationAdd BLAST54
Domaini150 – 222PAS 1PROSITE-ProRule annotationAdd BLAST73
Domaini333 – 403PAS 2PROSITE-ProRule annotationAdd BLAST71
Domaini408 – 451PACAdd BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni514 – 594Interaction with CIARTAdd BLAST81

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi36 – 41Nuclear localization signal1 Publication6
Motifi149 – 159Nuclear export signal 11 PublicationAdd BLAST11
Motifi367 – 375Nuclear export signal 21 Publication9

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3561. Eukaryota.
ENOG410XRJI. LUCA.
GeneTreeiENSGT00760000118788.
HOGENOMiHOG000234379.
HOVERGENiHBG107503.
InParanoidiQ9WTL8.
KOiK02296.
OMAiEKINTNC.
PhylomeDBiQ9WTL8.
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. 3 hits.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9WTL8-1) [UniParc]FASTAAdd to basket
Also known as: b'

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

        10         20         30         40         50
MADQRMDISS TISDFMSPGP TDLLSGSLGT SGVDCNRKRK GSATDYQLDD
60 70 80 90 100
FAFEESMDTD KDDPHGRLEY AEHQGRIKNA REAHSQIEKR RRDKMNSFID
110 120 130 140 150
ELASLVPTCN AMSRKLDKLT VLRMAVQHMK TLRGATNPYT EANYKPTFLS
160 170 180 190 200
DDELKHLILR AADGFLFVVG CDRGKILFVS ESVFKILNYS QNDLIGQSLF
210 220 230 240 250
DYLHPKDIAK VKEQLSSSDT APRERLIDAK TGLPVKTDIT PGPSRLCSGA
260 270 280 290 300
RRSFFCRMKC NRPSVKVEDK DFASTCSKKK DRKSFCTIHS TGYLKSWPPT
310 320 330 340 350
KMGLDEDNEP DNEGCNLSCL VAIGRLHSHM VPQPANGEIR VKSMEYVSRH
360 370 380 390 400
AIDGKFVFVD QRATAILAYL PQELLGTSCY EYFHQDDIGH LAECHRQVLQ
410 420 430 440 450
TREKITTNCY KFKIKDGSFI TLRSRWFSFM NPWTKEVEYI VSTNTVVLAN
460 470 480 490 500
VLEGGDPTFP QLTAPPHSMD SMLPSGEGGP KRTHPTVPGI PGGTRAGAGK
510 520 530 540 550
IGRMIAEEIM EIHRIRGSSP SSCGSSPLNI TSTPPPDASS PGGKKILNGG
560 570 580 590 600
TPDIPSTGLL PGQAQETPGY PYSDSSSILG ENPHIGIDMI DNDQGSSSPS
610 620 630
NDEAAMAVIM SLLEADAGLG GPVDFSDLPW PL
Length:632
Mass (Da):69,452
Last modified:August 15, 2003 - v2
Checksum:i9669C3712A95C2DE
GO
Isoform 2 (identifier: Q9WTL8-2) [UniParc]FASTAAdd to basket
Also known as: b

The sequence of this isoform differs from the canonical sequence as follows:
     48-54: Missing.

Show »
Length:625
Mass (Da):68,614
Checksum:i5A99555F851260CF
GO
Isoform 3 (identifier: Q9WTL8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     49-68: Missing.
     280-280: K → KA

Show »
Length:613
Mass (Da):67,200
Checksum:i24B91BA2E81D1A25
GO
Isoform 4 (identifier: Q9WTL8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     48-54: Missing.
     280-280: K → KA

Show »
Length:626
Mass (Da):68,685
Checksum:i837330EF65406CE4
GO
Isoform 5 (identifier: Q9WTL8-5) [UniParc]FASTAAdd to basket
Also known as: g'

The sequence of this isoform differs from the canonical sequence as follows:
     48-54: Missing.
     161-483: AADGFLFVVG...PSGEGGPKRT → DVTEGRSSLS...PRLDFRLKRI
     484-632: Missing.

Show »
Length:222
Mass (Da):25,061
Checksum:i9AE175BE7F6A446C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti254F → L in BAA76414 (PubMed:10403839).Curated1
Sequence conflicti254F → L in BAA81898 (PubMed:10403839).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00799248 – 54Missing in isoform 2, isoform 4 and isoform 5. 3 Publications7
Alternative sequenceiVSP_00799349 – 68Missing in isoform 3. 1 PublicationAdd BLAST20
Alternative sequenceiVSP_007995161 – 483AADGF…GPKRT → DVTEGRSSLSPSLSSRSSII ARMTLLARACLTTCIQKILP KLRNSYLPRTLRPGSDSLMP RLDFRLKRI in isoform 5. 1 PublicationAdd BLAST323
Alternative sequenceiVSP_007994280K → KA in isoform 3 and isoform 4. 2 Publications1
Alternative sequenceiVSP_007996484 – 632Missing in isoform 5. 1 PublicationAdd BLAST149

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012601 mRNA. Translation: BAA76414.1.
AB015203 mRNA. Translation: BAA81898.1.
AB012602 mRNA. Translation: BAA76415.1.
AB014494 mRNA. Translation: BAA32208.1.
BC025973 mRNA. Translation: AAH25973.1.
BC011080 mRNA. Translation: AAH11080.1.
CCDSiCCDS40092.1. [Q9WTL8-4]
PIRiJE0270.
RefSeqiNP_001229977.1. NM_001243048.1. [Q9WTL8-3]
NP_031515.1. NM_007489.4. [Q9WTL8-4]
XP_006507314.1. XM_006507251.2. [Q9WTL8-1]
XP_017177438.1. XM_017321949.1. [Q9WTL8-2]
XP_017177439.1. XM_017321950.1. [Q9WTL8-2]
UniGeneiMm.33970.
Mm.440371.

Genome annotation databases

EnsembliENSMUST00000047321; ENSMUSP00000046235; ENSMUSG00000055116. [Q9WTL8-4]
ENSMUST00000210074; ENSMUSP00000147764; ENSMUSG00000055116. [Q9WTL8-3]
ENSMUST00000210238; ENSMUSP00000147989; ENSMUSG00000055116. [Q9WTL8-4]
GeneIDi11865.
KEGGimmu:11865.
UCSCiuc009jhf.2. mouse. [Q9WTL8-3]
uc009jhi.2. mouse. [Q9WTL8-2]
uc009jhj.2. mouse. [Q9WTL8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012601 mRNA. Translation: BAA76414.1.
AB015203 mRNA. Translation: BAA81898.1.
AB012602 mRNA. Translation: BAA76415.1.
AB014494 mRNA. Translation: BAA32208.1.
BC025973 mRNA. Translation: AAH25973.1.
BC011080 mRNA. Translation: AAH11080.1.
CCDSiCCDS40092.1. [Q9WTL8-4]
PIRiJE0270.
RefSeqiNP_001229977.1. NM_001243048.1. [Q9WTL8-3]
NP_031515.1. NM_007489.4. [Q9WTL8-4]
XP_006507314.1. XM_006507251.2. [Q9WTL8-1]
XP_017177438.1. XM_017321949.1. [Q9WTL8-2]
XP_017177439.1. XM_017321950.1. [Q9WTL8-2]
UniGeneiMm.33970.
Mm.440371.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F3LX-ray2.27B69-453[»]
DisProtiDP00735.
ProteinModelPortaliQ9WTL8.
SMRiQ9WTL8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198207. 17 interactors.
DIPiDIP-43977N.
IntActiQ9WTL8. 20 interactors.
MINTiMINT-1657344.
STRINGi10090.ENSMUSP00000046235.

PTM databases

iPTMnetiQ9WTL8.
PhosphoSitePlusiQ9WTL8.

Proteomic databases

PaxDbiQ9WTL8.
PRIDEiQ9WTL8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047321; ENSMUSP00000046235; ENSMUSG00000055116. [Q9WTL8-4]
ENSMUST00000210074; ENSMUSP00000147764; ENSMUSG00000055116. [Q9WTL8-3]
ENSMUST00000210238; ENSMUSP00000147989; ENSMUSG00000055116. [Q9WTL8-4]
GeneIDi11865.
KEGGimmu:11865.
UCSCiuc009jhf.2. mouse. [Q9WTL8-3]
uc009jhi.2. mouse. [Q9WTL8-2]
uc009jhj.2. mouse. [Q9WTL8-1]

Organism-specific databases

CTDi406.
MGIiMGI:1096381. Arntl.

Phylogenomic databases

eggNOGiKOG3561. Eukaryota.
ENOG410XRJI. LUCA.
GeneTreeiENSGT00760000118788.
HOGENOMiHOG000234379.
HOVERGENiHBG107503.
InParanoidiQ9WTL8.
KOiK02296.
OMAiEKINTNC.
PhylomeDBiQ9WTL8.
TreeFamiTF319983.

Enzyme and pathway databases

ReactomeiR-MMU-1368082. RORA activates gene expression.
R-MMU-1368092. Rora activates gene expression.
R-MMU-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-MMU-1368110. Bmal1:Clock,Npas2 activates circadian gene expression.
R-MMU-1989781. PPARA activates gene expression.
R-MMU-400253. Circadian Clock.
R-MMU-508751. Circadian Clock.

Miscellaneous databases

PROiQ9WTL8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000055116.
ExpressionAtlasiQ9WTL8. baseline and differential.
GenevisibleiQ9WTL8. MM.

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. 3 hits.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBMAL1_MOUSE
AccessioniPrimary (citable) accession number: Q9WTL8
Secondary accession number(s): O88295
, Q921S4, Q9R0U2, Q9WTL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: August 15, 2003
Last modified: November 2, 2016
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.