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Q8WYA1

- BMAL2_HUMAN

UniProt

Q8WYA1 - BMAL2_HUMAN

Protein

Aryl hydrocarbon receptor nuclear translocator-like protein 2

Gene

ARNTL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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, DNA-templated Source: UniProtKB
    5. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    6. regulation of transcription, DNA-templated Source: UniProtKB
    7. regulation of transcription from RNA polymerase II promoter Source: MGI
    8. transcription from RNA polymerase II promoter Source: GOC

    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 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

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

    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 2PRO_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

    1
    636
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini107 – 16054bHLHPROSITE-ProRule annotationAdd
    BLAST
    Domaini178 – 25073PAS 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini357 – 42771PAS 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini432 – 47544PACAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni46 – 258213Interaction with PER2By similarityAdd
    BLAST

    Motif

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

    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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti41 – 411F → S(PubMed:10964693)Curated
    Sequence conflicti173 – 1731R → G in BAH12415. (PubMed:14702039)Curated
    Sequence conflicti257 – 2571A → T(PubMed:10864977)Curated
    Sequence conflicti276 – 2761S → F(PubMed:10864977)Curated
    Sequence conflicti304 – 3041K → R in BAH12415. (PubMed:14702039)Curated
    Sequence conflicti324 – 3241P → R(PubMed:10964693)Curated
    Sequence conflicti527 – 5271L → I(PubMed:10964693)Curated

    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. 2 PublicationsVSP_022580Add
    BLAST
    Alternative sequencei11 – 111G → GEVAGGEATAPG in isoform 3 and isoform 9. 3 PublicationsVSP_022585
    Alternative sequencei61 – 611Q → H in isoform 8. 1 PublicationVSP_022582
    Alternative sequencei62 – 9534Missing in isoform 3, isoform 4, isoform 5, isoform 6 and isoform 9. 5 PublicationsVSP_022581Add
    BLAST
    Alternative sequencei62 – 7413Missing in isoform 8. 1 PublicationVSP_022583Add
    BLAST
    Alternative sequencei96 – 10914Missing in isoform 2, isoform 3, isoform 4, isoform 6, isoform 7, isoform 8 and isoform 9. 5 PublicationsVSP_022584Add
    BLAST
    Alternative sequencei556 – 63580MSNKE…DIQWT → VMVHSWISMPYVTMMTQPWL H in isoform 9. 1 PublicationVSP_044773Add
    BLAST

    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

    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: October 1, 2014
    This is version 113 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