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Q8WYA1

- BMAL2_HUMAN

UniProt

Q8WYA1 - BMAL2_HUMAN

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Protein
Aryl hydrocarbon receptor nuclear translocator-like protein 2
Gene
ARNTL2, BHLHE6, BMAL2, CLIF, MOP9, PASD9
Organism
Homo sapiens (Human)
Status
Reviewed - 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, NR1D2, RORA, RORB and RORG, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. The CLOCK-ARNTL2/BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1.3 Publications

GO - Molecular functioni

  1. E-box binding Source: UniProtKB
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  3. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  4. signal transducer activity Source: InterPro

GO - Biological processi

  1. circadian rhythm Source: MGI
  2. entrainment of circadian clock Source: UniProtKB
  3. positive regulation of circadian rhythm Source: UniProtKB
  4. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  5. positive regulation of transcription, DNA-templated Source: UniProtKB
  6. regulation of transcription from RNA polymerase II promoter Source: MGI
  7. regulation of transcription, DNA-templated Source: UniProtKB
  8. transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Aryl hydrocarbon receptor nuclear translocator-like protein 2
Alternative name(s):
Basic-helix-loop-helix-PAS protein MOP9
Brain and muscle ARNT-like 2
CYCLE-like factor
Short name:
CLIF
Class E basic helix-loop-helix protein 6
Short name:
bHLHe6
Member of PAS protein 9
PAS domain-containing protein 9
Gene namesi
Name:ARNTL2
Synonyms:BHLHE6, BMAL2, CLIF, MOP9, PASD9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:18984. ARNTL2.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: InterPro
  2. nucleolus Source: HPA
  3. nucleus Source: UniProtKB
  4. transcription factor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134896555.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 636636Aryl hydrocarbon receptor nuclear translocator-like protein 2
PRO_0000273631Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki287 – 287Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3) By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ8WYA1.
PaxDbiQ8WYA1.
PRIDEiQ8WYA1.

PTM databases

PhosphoSiteiQ8WYA1.

Expressioni

Tissue specificityi

Expressed in fetal brain. Highly expressed in brain and placenta. Lower levels in heart, liver, thymus, kidney and lung. Located to endothelial cells and neuronal cells of the suprachiasmatic nucleus (SCN). Also detected in endothelial cells of the heart, lung and kidney. In the brain, specifically expressed in the thalamus, hippocampus and amygdala.3 Publications

Inductioni

Constitutively expressed. Has no circadian rhythm expression pattern.1 Publication

Gene expression databases

BgeeiQ8WYA1.
CleanExiHS_ARNTL2.
GenevestigatoriQ8WYA1.

Organism-specific databases

HPAiHPA059074.

Interactioni

Subunit structurei

Component of the circadian core oscillator, which includes the CRY proteins, CLOCK, or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Interacts directly with CLOCK to form the ARNTL2/BMAL2-CLOCK transactivator. Can form heterodimers or homodimers which interact directly with CLOCK to form the transcription activator. Also interacts with NPAS2 and HIF1A. Interacts with PER2.2 Publications

Protein-protein interaction databases

BioGridi121263. 2 interactions.
IntActiQ8WYA1. 3 interactions.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi368 – 3758
Beta strandi379 – 3846
Helixi387 – 3915
Turni396 – 3983
Turni404 – 4074
Beta strandi410 – 4123
Helixi413 – 42412
Beta strandi426 – 4283
Beta strandi430 – 4389
Beta strandi440 – 4423
Beta strandi444 – 45512
Beta strandi458 – 4603
Beta strandi462 – 4709

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KDKNMR-A360-477[»]
ProteinModelPortaliQ8WYA1.
SMRiQ8WYA1. Positions 104-477.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini107 – 16054bHLH
Add
BLAST
Domaini178 – 25073PAS 1
Add
BLAST
Domaini357 – 42771PAS 2
Add
BLAST
Domaini432 – 47544PAC
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 258213Interaction with PER2 By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi49 – 546Nuclear localization signal By similarity
Motifi177 – 18711Nuclear export signal 1 By similarity
Add
BLAST
Motifi392 – 4009Nuclear export signal 2 By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG288887.
HOVERGENiHBG107503.
InParanoidiQ8WYA1.
KOiK09099.
OMAiSAMIPQC.
OrthoDBiEOG7V1FQ8.
PhylomeDBiQ8WYA1.
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 (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8WYA1-1) [UniParc]FASTAAdd to Basket

Also known as: BMAL2a

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

MAAEEEAAAG GKVLREENQC IAPVVSSRVS PGTRPTAMGS FSSHMTEFPR    50
KRKGSDSDPS QSGIMTEKVV EKLSQNPLTY LLSTRIEISA SSGSRVEDGE 100
HQVKMKAFRE AHSQTEKRRR DKMNNLIEEL SAMIPQCNPM ARKLDKLTVL 150
RMAVQHLRSL KGLTNSYVGS NYRPSFLQDN ELRHLILKTA EGFLFVVGCE 200
RGKILFVSKS VSKILNYDQA SLTGQSLFDF LHPKDVAKVK EQLSSFDISP 250
REKLIDAKTG LQVHSNLHAG RTRVYSGSRR SFFCRIKSCK ISVKEEHGCL 300
PNSKKKEHRK FYTIHCTGYL RSWPPNIVGM EEERNSKKDN SNFTCLVAIG 350
RLQPYIVPQN SGEINVKPTE FITRFAVNGK FVYVDQRATA ILGYLPQELL 400
GTSCYEYFHQ DDHNNLTDKH KAVLQSKEKI LTDSYKFRAK DGSFVTLKSQ 450
WFSFTNPWTK ELEYIVSVNT LVLGHSEPGE ASFLPCSSQS SEESSRQSCM 500
SVPGMSTGTV LGAGSIGTDI ANEILDLQRL QSSSYLDDSS PTGLMKDTHT 550
VNCRSMSNKE LFPPSPSEMG ELEATRQNQS TVAVHSHEPL LSDGAQLDFD 600
ALCDNDDTAM AAFMNYLEAE GGLGDPGDFS DIQWTL 636
Length:636
Mass (Da):70,887
Last modified:January 23, 2007 - v2
Checksum:i972CE2BC5B05B1F3
GO
Isoform 2 (identifier: Q8WYA1-2) [UniParc]FASTAAdd to Basket

Also known as: BMAL2b

The sequence of this isoform differs from the canonical sequence as follows:
     96-109: Missing.

Show »
Length:622
Mass (Da):69,231
Checksum:iEE042DBFFB87BC63
GO
Isoform 3 (identifier: Q8WYA1-3) [UniParc]FASTAAdd to Basket

Also known as: BMAL2c

The sequence of this isoform differs from the canonical sequence as follows:
     11-11: G → GEVAGGEATAPG
     62-95: Missing.
     96-109: Missing.

Show »
Length:599
Mass (Da):66,493
Checksum:iA5B1B84DBC4B5B40
GO
Isoform 4 (identifier: Q8WYA1-4) [UniParc]FASTAAdd to Basket

Also known as: BMAL2d

The sequence of this isoform differs from the canonical sequence as follows:
     62-95: Missing.
     96-109: Missing.

Show »
Length:588
Mass (Da):65,553
Checksum:i3D49ACC111064FD8
GO
Isoform 5 (identifier: Q8WYA1-5) [UniParc]FASTAAdd to Basket

Also known as: CLIF

The sequence of this isoform differs from the canonical sequence as follows:
     62-95: Missing.

Show »
Length:602
Mass (Da):67,209
Checksum:iAD8937DD526D8B45
GO
Isoform 6 (identifier: Q8WYA1-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: Missing.
     62-95: Missing.
     96-109: Missing.

Show »
Length:551
Mass (Da):61,788
Checksum:iF845E3F54FFA39B0
GO
Isoform 7 (identifier: Q8WYA1-7) [UniParc]FASTAAdd to Basket

Also known as: MOP9 long form

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: Missing.
     96-109: Missing.

Show »
Length:585
Mass (Da):65,466
Checksum:iEE2E576065881B01
GO
Isoform 8 (identifier: Q8WYA1-8) [UniParc]FASTAAdd to Basket

Also known as: MOP9 short form

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: Missing.
     61-61: Q → H
     62-74: Missing.
     96-109: Missing.

Note: No experimental confirmation available.

Show »
Length:572
Mass (Da):64,072
Checksum:iFDDF781F6E2FDBC5
GO
Isoform 9 (identifier: Q8WYA1-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     11-11: G → GEVAGGEATAPG
     62-95: Missing.
     96-109: Missing.
     556-635: MSNKELFPPS...PGDFSDIQWT → VMVHSWISMPYVTMMTQPWLH

Note: No experimental confirmation available.

Show »
Length:540
Mass (Da):60,390
Checksum:i9C6DF2CB4CE1BB8A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti340 – 3401N → S.
Corresponds to variant rs1037921 [ dbSNP | Ensembl ].
VAR_030158
Natural varianti574 – 5741A → V.
Corresponds to variant rs11049005 [ dbSNP | Ensembl ].
VAR_030159

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3737Missing in isoform 6, isoform 7 and isoform 8.
VSP_022580Add
BLAST
Alternative sequencei11 – 111G → GEVAGGEATAPG in isoform 3 and isoform 9.
VSP_022585
Alternative sequencei61 – 611Q → H in isoform 8.
VSP_022582
Alternative sequencei62 – 9534Missing in isoform 3, isoform 4, isoform 5, isoform 6 and isoform 9.
VSP_022581Add
BLAST
Alternative sequencei62 – 7413Missing in isoform 8.
VSP_022583Add
BLAST
Alternative sequencei96 – 10914Missing in isoform 2, isoform 3, isoform 4, isoform 6, isoform 7, isoform 8 and isoform 9.
VSP_022584Add
BLAST
Alternative sequencei556 – 63580MSNKE…DIQWT → VMVHSWISMPYVTMMTQPWL H in isoform 9.
VSP_044773Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411F → S1 Publication
Sequence conflicti173 – 1731R → G in BAH12415. 1 Publication
Sequence conflicti257 – 2571A → T1 Publication
Sequence conflicti276 – 2761S → F1 Publication
Sequence conflicti304 – 3041K → R in BAH12415. 1 Publication
Sequence conflicti324 – 3241P → R1 Publication
Sequence conflicti527 – 5271L → I1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB039921 mRNA. Translation: BAB01485.1.
AF256215 mRNA. Translation: AAG34652.1.
AF231338 mRNA. Translation: AAF71306.1.
AF231339 mRNA. Translation: AAF71307.1.
AF246960 mRNA. Translation: AAL50339.1.
AF246961 mRNA. Translation: AAL50340.1.
AF246962 mRNA. Translation: AAL50341.1.
AF246963 mRNA. Translation: AAL50342.1.
AK296706 mRNA. Translation: BAH12415.1.
AC068794 Genomic DNA. No translation available.
AC092829 Genomic DNA. No translation available.
BC000172 mRNA. Translation: AAH00172.3.
BC125061 mRNA. Translation: AAI25062.1.
BC125062 mRNA. Translation: AAI25063.1.
CCDSiCCDS58219.1. [Q8WYA1-2]
CCDS58220.1. [Q8WYA1-4]
CCDS58221.1. [Q8WYA1-3]
CCDS58222.1. [Q8WYA1-9]
CCDS8712.1. [Q8WYA1-1]
RefSeqiNP_001234931.1. NM_001248002.1. [Q8WYA1-2]
NP_001234932.1. NM_001248003.1. [Q8WYA1-3]
NP_001234933.1. NM_001248004.1. [Q8WYA1-4]
NP_001234934.1. NM_001248005.1. [Q8WYA1-9]
NP_064568.3. NM_020183.4. [Q8WYA1-1]
UniGeneiHs.445447.

Genome annotation databases

EnsembliENST00000261178; ENSP00000261178; ENSG00000029153. [Q8WYA1-4]
ENST00000266503; ENSP00000266503; ENSG00000029153. [Q8WYA1-1]
ENST00000311001; ENSP00000312247; ENSG00000029153. [Q8WYA1-2]
ENST00000395901; ENSP00000379238; ENSG00000029153. [Q8WYA1-3]
ENST00000542388; ENSP00000445836; ENSG00000029153. [Q8WYA1-6]
ENST00000544915; ENSP00000442438; ENSG00000029153. [Q8WYA1-5]
ENST00000546179; ENSP00000438545; ENSG00000029153. [Q8WYA1-9]
GeneIDi56938.
KEGGihsa:56938.
UCSCiuc001rht.2. human. [Q8WYA1-1]
uc001rhu.2. human. [Q8WYA1-2]
uc001rhv.2. human. [Q8WYA1-4]
uc001rhw.3. human. [Q8WYA1-3]
uc009zji.2. human. [Q8WYA1-5]

Polymorphism databases

DMDMi124007121.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB039921 mRNA. Translation: BAB01485.1 .
AF256215 mRNA. Translation: AAG34652.1 .
AF231338 mRNA. Translation: AAF71306.1 .
AF231339 mRNA. Translation: AAF71307.1 .
AF246960 mRNA. Translation: AAL50339.1 .
AF246961 mRNA. Translation: AAL50340.1 .
AF246962 mRNA. Translation: AAL50341.1 .
AF246963 mRNA. Translation: AAL50342.1 .
AK296706 mRNA. Translation: BAH12415.1 .
AC068794 Genomic DNA. No translation available.
AC092829 Genomic DNA. No translation available.
BC000172 mRNA. Translation: AAH00172.3 .
BC125061 mRNA. Translation: AAI25062.1 .
BC125062 mRNA. Translation: AAI25063.1 .
CCDSi CCDS58219.1. [Q8WYA1-2 ]
CCDS58220.1. [Q8WYA1-4 ]
CCDS58221.1. [Q8WYA1-3 ]
CCDS58222.1. [Q8WYA1-9 ]
CCDS8712.1. [Q8WYA1-1 ]
RefSeqi NP_001234931.1. NM_001248002.1. [Q8WYA1-2 ]
NP_001234932.1. NM_001248003.1. [Q8WYA1-3 ]
NP_001234933.1. NM_001248004.1. [Q8WYA1-4 ]
NP_001234934.1. NM_001248005.1. [Q8WYA1-9 ]
NP_064568.3. NM_020183.4. [Q8WYA1-1 ]
UniGenei Hs.445447.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KDK NMR - A 360-477 [» ]
ProteinModelPortali Q8WYA1.
SMRi Q8WYA1. Positions 104-477.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121263. 2 interactions.
IntActi Q8WYA1. 3 interactions.

PTM databases

PhosphoSitei Q8WYA1.

Polymorphism databases

DMDMi 124007121.

Proteomic databases

MaxQBi Q8WYA1.
PaxDbi Q8WYA1.
PRIDEi Q8WYA1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261178 ; ENSP00000261178 ; ENSG00000029153 . [Q8WYA1-4 ]
ENST00000266503 ; ENSP00000266503 ; ENSG00000029153 . [Q8WYA1-1 ]
ENST00000311001 ; ENSP00000312247 ; ENSG00000029153 . [Q8WYA1-2 ]
ENST00000395901 ; ENSP00000379238 ; ENSG00000029153 . [Q8WYA1-3 ]
ENST00000542388 ; ENSP00000445836 ; ENSG00000029153 . [Q8WYA1-6 ]
ENST00000544915 ; ENSP00000442438 ; ENSG00000029153 . [Q8WYA1-5 ]
ENST00000546179 ; ENSP00000438545 ; ENSG00000029153 . [Q8WYA1-9 ]
GeneIDi 56938.
KEGGi hsa:56938.
UCSCi uc001rht.2. human. [Q8WYA1-1 ]
uc001rhu.2. human. [Q8WYA1-2 ]
uc001rhv.2. human. [Q8WYA1-4 ]
uc001rhw.3. human. [Q8WYA1-3 ]
uc009zji.2. human. [Q8WYA1-5 ]

Organism-specific databases

CTDi 56938.
GeneCardsi GC12P027485.
H-InvDB HIX0037110.
HGNCi HGNC:18984. ARNTL2.
HPAi HPA059074.
MIMi 614517. gene.
neXtProti NX_Q8WYA1.
PharmGKBi PA134896555.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG288887.
HOVERGENi HBG107503.
InParanoidi Q8WYA1.
KOi K09099.
OMAi SAMIPQC.
OrthoDBi EOG7V1FQ8.
PhylomeDBi Q8WYA1.
TreeFami TF319983.

Enzyme and pathway databases

Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.

Miscellaneous databases

GeneWikii ARNTL2.
GenomeRNAii 56938.
NextBioi 62501.
PROi Q8WYA1.
SOURCEi Search...

Gene expression databases

Bgeei Q8WYA1.
CleanExi HS_ARNTL2.
Genevestigatori Q8WYA1.

Family and domain databases

Gene3Di 4.10.280.10. 1 hit.
InterProi IPR011598. bHLH_dom.
IPR001067. Nuc_translocat.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
[Graphical view ]
Pfami PF00010. HLH. 1 hit.
PF00989. PAS. 1 hit.
[Graphical view ]
PRINTSi PR00785. NCTRNSLOCATR.
SMARTi SM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view ]
SUPFAMi SSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 3 hits.
TIGRFAMsi TIGR00229. sensory_box. 1 hit.
PROSITEi PS50888. BHLH. 1 hit.
PS50112. PAS. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of a novel bHLH-PAS transcription factor superfamily gene, BMAL2; Its mRNA expression, subcellular distribution, and chromosomal localization."
    Ikeda M., Yu W., Hirai M., Ebisawa T., Honma S., Yoshimura K., Honma K., Nomura M.
    Biochem. Biophys. Res. Commun. 275:493-502(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "CLIF, a novel cycle-like factor, regulates the circadian oscillation of plasminogen activator inhibitor-1 gene expression."
    Maemura K., de La Monte S.M., Chin M.T., Layne M.D., Hsieh C.-M., Yet S.-F., Perrella M.A., Lee M.-E.
    J. Biol. Chem. 275:36847-36851(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INDUCTION, TISSUE SPECIFICITY, INTERACTION WITH CLOCK.
    Tissue: Umbilical vein endothelial cell.
  3. "The basic helix-loop-helix-PAS protein MOP9 is a brain-specific heterodimeric partner of circadian and hypoxia factors."
    Hogenesch J.B., Gu Y.-Z., Moran S.M., Shimomura K., Radcliffe L.A., Takahashi J.S., Bradfield C.A.
    J. Neurosci. 20:RC83-RC83(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7 AND 8), TISSUE SPECIFICITY, INTERACTION WITH CLOCK; NPAS2 AND HIF1A.
    Tissue: Brain.
  4. "Chicken pineal clock genes: implication of BMAL2 as a bidirectional regulator in circadian clock oscillation."
    Okano T., Yamamoto K., Okano K., Hirota T., Kasahara T., Sasaki M., Takanaka Y., Fukada Y.
    Genes Cells 6:825-836(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
    Tissue: Embryonic kidney.
  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] (ISOFORM 9).
    Tissue: Tongue.
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 3; 4 AND 5).
    Tissue: Placenta.
  8. "Regulation of the PAI-1 promoter by circadian clock components: differential activation by BMAL1 and BMAL2."
    Schoenhard J.A., Smith L.H., Painter C.A., Eren M., Johnson C.H., Vaughan D.E.
    J. Mol. Cell. Cardiol. 35:473-481(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: FUNCTION.

Entry informationi

Entry nameiBMAL2_HUMAN
AccessioniPrimary (citable) accession number: Q8WYA1
Secondary accession number(s): B7Z429
, F5H402, Q8WYA2, Q8WYA3, Q8WYA4, Q96J63, Q9H2M4, Q9NS70, Q9NYQ4, Q9NYQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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