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UniProtKB - Q9WTL8 (BMAL1_MOUSE)

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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. 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. The preferred binding motif for the CLOCK-ARNTL/BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking Ala residue in addition to the canonical 6-nucleotide E-box sequence (By similarity). CLOCK specifically binds to the half-site 5'-CAC-3', while ARNTL binds to the half-site 5'-GTGA-3' (By similarity). The CLOCK-ARNTL/BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3' (By similarity). Essential for the rhythmic interaction of CLOCK with ASS1 and plays a critical role in positively regulating CLOCK-mediated acetylation of ASS1 (PubMed:28985504).By similarity39 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei132Important for interaction with CLOCKBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding
Biological processBiological rhythms, Transcription, Transcription regulation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Aryl hydrocarbon receptor nuclear translocator-like protein 1
Alternative name(s):
Arnt3
Brain and muscle ARNT-like 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Arntl
Synonyms:Bmal1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:1096381 Arntl

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi38 – 39KR → AA: Loss of nuclear localization. 1 Publication2
Mutagenesisi97S → A: Impaired nuclear accumulation, decreased interaction with CLOCK and disruption of circadian 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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001271581 – 632Aryl hydrocarbon receptor nuclear translocator-like protein 1Add BLAST632

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei17Phosphoserine; by GSK3-beta1 Publication1
Modified residuei21Phosphothreonine; by GSK3-beta1 Publication1
Modified residuei85PhosphoserineBy similarity1
Modified residuei97Phosphoserine; by CK21 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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); alternate1 Publication
Cross-linki266Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei544N6-acetyllysine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Ubiquitinated, leading to its proteasomal degradation (PubMed:16980631, PubMed:18644859, PubMed:23185022). Deubiquitinated by USP9X (PubMed:29626158).4 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. Dephosphorylation at Ser-85 is important for dimerization with CLOCK and transcriptional activity (By similarity).By similarity6 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
Undergoes lysosome-mediated degradation in a time-dependent manner in the liver.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q9WTL8

PRoteomics IDEntifications database

More...PRIDEi		Q9WTL8

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9WTL8

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q9WTL8

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in liver and testis (at protein level). Expressed in the suprachiasmatic nucleus (SCN) in a circadian manner (PubMed:29138967).6 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expressed in a circadian manner in the liver.4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000055116 Expressed in 268 organ(s), highest expression level in zygote

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9WTL8 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9WTL8 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 (PubMed:11779462). Forms a heterodimer with CLOCK (PubMed:9616112, PubMed:16717091, PubMed:16980631, PubMed:18662546, PubMed:19946213, PubMed:19330005, PubMed:21613214, PubMed:23970558, PubMed:22653727). The CLOCK-ARNTL/BMAL1 heterodimer is required for E-box-dependent transactivation, for CLOCK nuclear translocation and degradation, and, for phosphorylation of both CLOCK and ARNTL/BMAL1 (PubMed:11779462). Part of a nuclear complex which also includes RACK1 and PRKCA; RACK1 and PRKCA are recruited to the complex in a circadian manner (PubMed:20093473). Interacts with NPAS2 (PubMed:16628007). Interacts with EZH2 (PubMed:16717091, PubMed:23970558). Interacts with SUMO3 (PubMed:18644859). Interacts with SIRT1 (PubMed:18662546, PubMed:18662547, PubMed:19299583). Interacts with AHR (PubMed:20106950). Interacts with ID1, ID2 and ID3 (PubMed:20861012). Interacts with DDX4 (PubMed:22900038). Interacts with OGT (PubMed:23337503). Interacts with EED and SUZ12 (PubMed:23970558). Interacts with MTA1 (PubMed:24089055). Interacts with CIART (PubMed:24385426, PubMed:24736997). Interacts with HSP90 (By similarity). Interacts with KAT2B and EP300 (By similarity). Interacts with BHLHE40/DEC1 and BHLHE41/DEC2 (PubMed:12397359). Interacts with RELB and the interaction is enhanced in the presence of CLOCK (PubMed:22894897). Interacts with PER1, PER2, CRY1 and CRY2 and this interaction requires a translocation to the nucleus (PubMed:18430226, PubMed:19605937, PubMed:20840750, PubMed:21613214, PubMed:24154698). Interaction of the CLOCK-ARNTL/BMAL1 heterodimer with PER or CRY inhibits transcription activation (PubMed:21613214). Interaction of the CLOCK-ARNTL/BMAL1 with CRY1 is independent of DNA but with PER2 is off DNA (PubMed:21613214). The CLOCK-ARNTL/BMAL1 heterodimer interacts with GSK3B (PubMed:19946213, PubMed:20049328). Interacts with KDM5A (PubMed:21960634). Interacts with KMT2A; in a circadian manner (PubMed:21113167). Interacts with UBE3A (By similarity). Interacts with PRKCG (PubMed:23185022). Interacts with MAGEL2 (PubMed:22208286). Interacts with NCOA2 (PubMed:24529706). Interacts with THRAP3 (PubMed:24043798). The CLOCK-ARNTL/BMAL1 heterodimer interacts with PASD1 (By similarity). Interacts with PASD1 (By similarity). Interacts with USP9X (PubMed:29626158).By similarity35 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei84Interaction with E-box DNABy similarity1
Sitei87Interaction with E-box DNABy similarity1
Sitei88Interaction with E-box DNABy similarity1
Sitei92Interaction with E-box DNABy similarity1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		198207, 17 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3225 CLOCK-BMAL1 transcription complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9WTL8

Database of interacting proteins

More...DIPi		DIP-43977N

Protein interaction database and analysis system

More...IntActi		Q9WTL8, 31 interactors

Molecular INTeraction database

More...MINTi		Q9WTL8

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000046235

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1632
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q9WTL8

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q9WTL8

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni514 – 594Interaction with CIARTAdd BLAST81

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi36 – 41Nuclear localization signal1 Publication6
Motifi149 – 159Nuclear export signal 11 PublicationAdd BLAST11
Motifi367 – 375Nuclear export signal 21 Publication9

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3561 Eukaryota
ENOG410XRJI LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157523

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000234379

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG107503

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9WTL8

KEGG Orthology (KO)

More...KOi		K02296

Identification of Orthologs from Complete Genome Data

More...OMAi		EKINTNC

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9WTL8

TreeFam database of animal gene trees

More...TreeFami		TF319983

Family and domain databases

Conserved Domains Database

More...CDDi		cd00083 HLH, 1 hit
cd00130 PAS, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		4.10.280.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011598 bHLH_dom
IPR036638 HLH_DNA-bd_sf
IPR001067 Nuc_translocat
IPR001610 PAC
IPR000014 PAS
IPR035965 PAS-like_dom_sf
IPR013767 PAS_fold

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00010 HLH, 1 hit
PF00989 PAS, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00785 NCTRNSLOCATR

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00353 HLH, 1 hit
SM00086 PAC, 1 hit
SM00091 PAS, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47459 SSF47459, 1 hit
SSF55785 SSF55785, 2 hits

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00229 sensory_box, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50888 BHLH, 1 hit
PS50112 PAS, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 5 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 5 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1B0GS77A0A1B0GS77_MOUSE
Aryl hydrocarbon receptor nuclear t...
Arntl
633Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti254F → L in BAA76414 (PubMed:10403839).Curated1
Sequence conflicti254F → L in BAA81898 (PubMed:10403839).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS40092.1 [Q9WTL8-4]
CCDS85390.1 [Q9WTL8-3]

Protein sequence database of the Protein Information Resource

More...PIRi		JE0270

NCBI Reference Sequences

More...RefSeqi		NP_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
XP_017177439.1, XM_017321950.1 [Q9WTL8-2]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Mm.33970
Mm.440371

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000047321; ENSMUSP00000046235; ENSMUSG00000055116 [Q9WTL8-4]
ENSMUST00000210074; ENSMUSP00000147764; ENSMUSG00000055116 [Q9WTL8-3]
ENSMUST00000210238; ENSMUSP00000147989; ENSMUSG00000055116 [Q9WTL8-4]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		11865

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:11865

UCSC genome browser

More...UCSCi		uc009jhf.2 mouse [Q9WTL8-3]
uc009jhi.2 mouse [Q9WTL8-2]
uc009jhj.2 mouse [Q9WTL8-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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]
CCDS85390.1 [Q9WTL8-3]
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
XP_017177439.1, XM_017321950.1 [Q9WTL8-2]
UniGeneiMm.33970
Mm.440371

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F3LX-ray2.27B69-453[»]
ProteinModelPortaliQ9WTL8
SMRiQ9WTL8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198207, 17 interactors
ComplexPortaliCPX-3225 CLOCK-BMAL1 transcription complex
CORUMiQ9WTL8
DIPiDIP-43977N
IntActiQ9WTL8, 31 interactors
MINTiQ9WTL8
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

Comparative Toxicogenomics Database

More...CTDi		406
MGIiMGI:1096381 Arntl

Phylogenomic databases

eggNOGiKOG3561 Eukaryota
ENOG410XRJI LUCA
GeneTreeiENSGT00940000157523
HOGENOMiHOG000234379
HOVERGENiHBG107503
InParanoidiQ9WTL8
KOiK02296
OMAiEKINTNC
PhylomeDBiQ9WTL8
TreeFamiTF319983

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q9WTL8

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000055116 Expressed in 268 organ(s), highest expression level in zygote
ExpressionAtlasiQ9WTL8 baseline and differential
GenevisibleiQ9WTL8 MM

Family and domain databases

CDDicd00083 HLH, 1 hit
cd00130 PAS, 2 hits
Gene3Di4.10.280.10, 1 hit
InterProiView protein in InterPro
IPR011598 bHLH_dom
IPR036638 HLH_DNA-bd_sf
IPR001067 Nuc_translocat
IPR001610 PAC
IPR000014 PAS
IPR035965 PAS-like_dom_sf
IPR013767 PAS_fold
PfamiView protein in Pfam
PF00010 HLH, 1 hit
PF00989 PAS, 1 hit
PRINTSiPR00785 NCTRNSLOCATR
SMARTiView protein in SMART
SM00353 HLH, 1 hit
SM00086 PAC, 1 hit
SM00091 PAS, 2 hits
SUPFAMiSSF47459 SSF47459, 1 hit
SSF55785 SSF55785, 2 hits
TIGRFAMsiTIGR00229 sensory_box, 1 hit
PROSITEiView protein in PROSITE
PS50888 BHLH, 1 hit
PS50112 PAS, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiBMAL1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9WTL8
Secondary accession number(s): O88295
, Q921S4, Q9R0U2, Q9WTL9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: August 15, 2003
Last modified: December 5, 2018
This is version 171 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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