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P20393

- NR1D1_HUMAN

UniProt

P20393 - NR1D1_HUMAN

Protein

Nuclear receptor subfamily 1 group D member 1

Gene

NR1D1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Transcriptional repressor which coordinates circadian rhythm and metabolic pathways in a heme-dependent manner. Integral component of the complex transcription machinery that governs circadian rhythmicity and forms a critical negative limb of the circadian clock by directly repressing the expression of core clock components ARTNL/BMAL1, CLOCK and CRY1. Also regulates genes involved in metabolic functions, including lipid and bile acid metabolism, adipogenesis, gluconeogenesis and the macrophage inflammatory response. Acts as a receptor for heme which stimulates its interaction with the NCOR1/HDAC3 corepressor complex, enhancing transcriptional repression. Recognizes two classes of DNA response elements within the promoter of its target genes and can bind to DNA as either monomers or homodimers, depending on the nature of the response element. Binds as a monomer to a response element composed of the consensus half-site motif 5'-[A/G]GGTCA-3' preceded by an A/T-rich 5' sequence (RevRE), or as a homodimer to a direct repeat of the core motif spaced by two nucleotides (RevDR-2). Acts as a potent competitive repressor of ROR alpha (RORA) function and regulates the levels of its ligand heme by repressing the expression of PPARGC1A, a potent inducer of heme synthesis. Regulates lipid metabolism by repressing the expression of APOC3 and by influencing the activity of sterol response element binding proteins (SREBPs); represses INSIG2 which interferes with the proteolytic activation of SREBPs which in turn govern the rhythmic expression of enzymes with key functions in sterol and fatty acid synthesis. Regulates gluconeogenesis via repression of G6PC and PEPCK and adipocyte differentiation via repression of PPARG. Regulates glucagon release in pancreatic alpha-cells via the AMPK-NAMPT-SIRT1 pathway and the proliferation, glucose-induced insulin secretion and expression of key lipogenic genes in pancreatic-beta cells. Positively regulates bile acid synthesis by increasing hepatic expression of CYP7A1 via repression of NR0B2 and NFIL3 which are negative regulators of CYP7A1. Modulates skeletal muscle oxidative capacity by regulating mitochondrial biogenesis and autophagy; controls mitochondrial biogenesis and respiration by interfering with the STK11-PRKAA1/2-SIRT1-PPARGC1A signaling pathway. Represses the expression of SERPINE1/PAI1, an important modulator of cardiovascular disease and the expression of inflammatory cytokines and chemokines in macrophages. Represses gene expression at a distance in macrophages by inhibiting the transcription of enhancer-derived RNAs (eRNAs). Plays a role in the circadian regulation of body temperature and negatively regulates thermogenic transcriptional programs in brown adipose tissue (BAT); imposes a circadian oscillation in BAT activity, increasing body temperature when awake and depressing thermogenesis during sleep. In concert with NR2E3, regulates transcriptional networks critical for photoreceptor development and function. In addition to its activity as a repressor, can also act as a transcriptional activator. In the ovarian granulosa cells acts as a transcriptional activator of STAR which plays a role in steroid biosynthesis. In collaboration with SP1, activates GJA1 transcription in a heme-independent manner.9 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei418 – 4181HemeBy similarity
    Binding sitei602 – 6021Heme

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi129 – 20577Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri132 – 15221NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri169 – 19325NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. core promoter sequence-specific DNA binding Source: UniProtKB
    2. heme binding Source: UniProtKB
    3. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: ProtInc
    4. protein binding Source: UniProtKB
    5. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
    7. steroid hormone receptor activity Source: ProtInc
    8. transcription corepressor activity Source: ProtInc
    9. transcription corepressor binding Source: UniProtKB
    10. transcription regulatory region DNA binding Source: BHF-UCL
    11. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. cellular response to lipopolysaccharide Source: BHF-UCL
    3. circadian regulation of gene expression Source: UniProtKB
    4. circadian temperature homeostasis Source: UniProtKB
    5. gene expression Source: Reactome
    6. glycogen biosynthetic process Source: UniProtKB
    7. intracellular receptor signaling pathway Source: GOC
    8. negative regulation of receptor biosynthetic process Source: BHF-UCL
    9. negative regulation of toll-like receptor 4 signaling pathway Source: BHF-UCL
    10. negative regulation of transcription, DNA-templated Source: UniProtKB
    11. negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    12. positive regulation of bile acid biosynthetic process Source: UniProtKB
    13. positive regulation of transcription, DNA-templated Source: UniProtKB
    14. proteasomal protein catabolic process Source: UniProtKB
    15. regulation of cholesterol homeostasis Source: UniProtKB
    16. regulation of circadian rhythm Source: UniProtKB
    17. regulation of fat cell differentiation Source: UniProtKB
    18. regulation of gluconeogenesis by regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    19. regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
    20. regulation of lipid metabolic process Source: UniProtKB
    21. regulation of type B pancreatic cell proliferation Source: UniProtKB
    22. response to leptin Source: UniProtKB
    23. transcription initiation from RNA polymerase II promoter Source: Reactome

    Keywords - Molecular functioni

    Activator, Receptor, Repressor

    Keywords - Biological processi

    Biological rhythms, Differentiation, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Heme, Iron, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_15525. Nuclear Receptor transcription pathway.
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_24941. Circadian Clock.
    SignaLinkiP20393.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor subfamily 1 group D member 1
    Alternative name(s):
    Rev-erbA-alpha
    V-erbA-related protein 1
    Short name:
    EAR-1
    Gene namesi
    Name:NR1D1
    Synonyms:EAR1, HREV, THRAL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:7962. NR1D1.

    Subcellular locationi

    Nucleus. Cytoplasm By similarity. Cell projectiondendrite By similarity. Cell projectiondendritic spine By similarity
    Note: Localizes to the cytoplasm, dendrites and dendritic spine in the presence of OPHN1.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. dendrite Source: UniProtKB
    3. dendritic spine Source: UniProtKB
    4. nuclear chromatin Source: BHF-UCL
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31748.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 614614Nuclear receptor subfamily 1 group D member 1PRO_0000053499Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551Phosphoserine; by GSK3-beta1 Publication
    Modified residuei59 – 591Phosphoserine; by GSK3-beta1 Publication
    Modified residuei191 – 1911N6-acetyllysine; by KAT5By similarity
    Modified residuei192 – 1921N6-acetyllysine; by KAT5By similarity

    Post-translational modificationi

    Ubiquitinated, leading to its proteasomal degradation.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP20393.
    PaxDbiP20393.
    PRIDEiP20393.

    PTM databases

    PhosphoSiteiP20393.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed at high levels in the liver, adipose tissue, skeletal muscle and brain. Also expressed in endothelial cells (ECs), vascular smooth muscle cells (VSMCs) and macrophages. Expression oscillates diurnally in the suprachiasmatic nucleus (SCN) of the hypothalamus as well as in peripheral tissues. Expression increases during the differentiation of pre-adipocytes into mature adipocytes. Expressed at high levels in some squamous carcinoma cell lines.1 Publication

    Gene expression databases

    ArrayExpressiP20393.
    BgeeiP20393.
    CleanExiHS_NR1D1.
    GenevestigatoriP20393.

    Organism-specific databases

    HPAiHPA007935.

    Interactioni

    Subunit structurei

    Binds DNA as a monomer or a homodimer. Interacts with C1D, NR2E3 and SP1. Interacts with OPHN1 (via C-terminus). Interacts with ZNHIT1. Interacts with PER2; the interaction associates PER2 to ARNTL promoter region. Interacts with CRY1.3 Publications

    Protein-protein interaction databases

    BioGridi114941. 9 interactions.
    DIPiDIP-48396N.
    IntActiP20393. 2 interactions.
    STRINGi9606.ENSP00000246672.

    Structurei

    Secondary structure

    1
    614
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni133 – 1353
    Beta strandi136 – 1383
    Beta strandi141 – 1433
    Beta strandi146 – 1483
    Helixi150 – 16011
    Beta strandi170 – 1734
    Turni179 – 1835
    Helixi186 – 1938
    Turni194 – 1974
    Helixi200 – 2023
    Helixi285 – 29915
    Helixi434 – 45623
    Helixi460 – 4623
    Helixi465 – 48622
    Helixi509 – 5113
    Helixi514 – 52916
    Helixi534 – 54613
    Helixi556 – 57722
    Helixi584 – 5896
    Helixi591 – 60212
    Beta strandi606 – 6105

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A6YX-ray2.30A/B123-216[»]
    1EF6model-A281-301[»]
    B430-614[»]
    1GA5X-ray2.40A/B/E/F123-216[»]
    1HLZX-ray2.80A/B123-216[»]
    3N00X-ray2.60A281-614[»]
    ProteinModelPortaliP20393.
    SMRiP20393. Positions 127-613.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20393.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 128128ModulatingAdd
    BLAST
    Regioni49 – 284236Crucial for activation of GJA1By similarityAdd
    BLAST
    Regioni206 – 28479HingeAdd
    BLAST
    Regioni285 – 614330Ligand-bindingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi82 – 9312Poly-SerAdd
    BLAST

    Domaini

    Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

    Sequence similaritiesi

    Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri132 – 15221NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri169 – 19325NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG324222.
    HOGENOMiHOG000261691.
    HOVERGENiHBG106790.
    InParanoidiP20393.
    KOiK03728.
    OMAiGTSPGNF.
    OrthoDBiEOG776SQ0.
    PhylomeDBiP20393.
    TreeFamiTF328382.

    Family and domain databases

    Gene3Di1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view]
    PfamiPF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view]
    PRINTSiPR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTiSM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view]
    SUPFAMiSSF48508. SSF48508. 1 hit.
    PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P20393-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTLDSNNNT GGVITYIGSS GSSPSRTSPE SLYSDNSNGS FQSLTQGCPT    50
    YFPPSPTGSL TQDPARSFGS IPPSLSDDGS PSSSSSSSSS SSSFYNGSPP 100
    GSLQVAMEDS SRVSPSKSTS NITKLNGMVL LCKVCGDVAS GFHYGVHACE 150
    GCKGFFRRSI QQNIQYKRCL KNENCSIVRI NRNRCQQCRF KKCLSVGMSR 200
    DAVRFGRIPK REKQRMLAEM QSAMNLANNQ LSSQCPLETS PTQHPTPGPM 250
    GPSPPPAPVP SPLVGFSQFP QQLTPPRSPS PEPTVEDVIS QVARAHREIF 300
    TYAHDKLGSS PGNFNANHAS GSPPATTPHR WENQGCPPAP NDNNTLAAQR 350
    HNEALNGLRQ APSSYPPTWP PGPAHHSCHQ SNSNGHRLCP THVYAAPEGK 400
    APANSPRQGN SKNVLLACPM NMYPHGRSGR TVQEIWEDFS MSFTPAVREV 450
    VEFAKHIPGF RDLSQHDQVT LLKAGTFEVL MVRFASLFNV KDQTVMFLSR 500
    TTYSLQELGA MGMGDLLSAM FDFSEKLNSL ALTEEELGLF TAVVLVSADR 550
    SGMENSASVE QLQETLLRAL RALVLKNRPL ETSRFTKLLL KLPDLRTLNN 600
    MHSEKLLSFR VDAQ 614
    Length:614
    Mass (Da):66,805
    Last modified:February 1, 1991 - v1
    Checksum:i67C71758E166508A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471H → L in CAB53540. (PubMed:1971514)Curated
    Sequence conflicti564 – 5641E → Q(PubMed:1971514)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24898 mRNA. Translation: AAA52335.1.
    M24900 mRNA. Translation: AAA52332.1.
    X55066 Genomic DNA. No translation available.
    X55067 Genomic DNA. No translation available.
    X72631 mRNA. Translation: CAB53540.1.
    BC047875 mRNA. Translation: AAH47875.1.
    BC056148 mRNA. Translation: AAH56148.1.
    M34339 mRNA. Translation: AAA36561.1.
    M34340 mRNA. Translation: AAA36562.2.
    CCDSiCCDS11361.1.
    PIRiA32286. A32608.
    RefSeqiNP_068370.1. NM_021724.4.
    UniGeneiHs.592130.
    Hs.724.

    Genome annotation databases

    EnsembliENST00000246672; ENSP00000246672; ENSG00000126368.
    GeneIDi9572.
    KEGGihsa:9572.
    UCSCiuc002htz.3. human.

    Polymorphism databases

    DMDMi119100.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24898 mRNA. Translation: AAA52335.1 .
    M24900 mRNA. Translation: AAA52332.1 .
    X55066 Genomic DNA. No translation available.
    X55067 Genomic DNA. No translation available.
    X72631 mRNA. Translation: CAB53540.1 .
    BC047875 mRNA. Translation: AAH47875.1 .
    BC056148 mRNA. Translation: AAH56148.1 .
    M34339 mRNA. Translation: AAA36561.1 .
    M34340 mRNA. Translation: AAA36562.2 .
    CCDSi CCDS11361.1.
    PIRi A32286. A32608.
    RefSeqi NP_068370.1. NM_021724.4.
    UniGenei Hs.592130.
    Hs.724.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A6Y X-ray 2.30 A/B 123-216 [» ]
    1EF6 model - A 281-301 [» ]
    B 430-614 [» ]
    1GA5 X-ray 2.40 A/B/E/F 123-216 [» ]
    1HLZ X-ray 2.80 A/B 123-216 [» ]
    3N00 X-ray 2.60 A 281-614 [» ]
    ProteinModelPortali P20393.
    SMRi P20393. Positions 127-613.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114941. 9 interactions.
    DIPi DIP-48396N.
    IntActi P20393. 2 interactions.
    STRINGi 9606.ENSP00000246672.

    Chemistry

    BindingDBi P20393.
    ChEMBLi CHEMBL1961783.
    GuidetoPHARMACOLOGYi 596.

    PTM databases

    PhosphoSitei P20393.

    Polymorphism databases

    DMDMi 119100.

    Proteomic databases

    MaxQBi P20393.
    PaxDbi P20393.
    PRIDEi P20393.

    Protocols and materials databases

    DNASUi 9572.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000246672 ; ENSP00000246672 ; ENSG00000126368 .
    GeneIDi 9572.
    KEGGi hsa:9572.
    UCSCi uc002htz.3. human.

    Organism-specific databases

    CTDi 9572.
    GeneCardsi GC17M038249.
    HGNCi HGNC:7962. NR1D1.
    HPAi HPA007935.
    MIMi 602408. gene.
    neXtProti NX_P20393.
    PharmGKBi PA31748.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG324222.
    HOGENOMi HOG000261691.
    HOVERGENi HBG106790.
    InParanoidi P20393.
    KOi K03728.
    OMAi GTSPGNF.
    OrthoDBi EOG776SQ0.
    PhylomeDBi P20393.
    TreeFami TF328382.

    Enzyme and pathway databases

    Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_15525. Nuclear Receptor transcription pathway.
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_24941. Circadian Clock.
    SignaLinki P20393.

    Miscellaneous databases

    ChiTaRSi NR1D1. human.
    EvolutionaryTracei P20393.
    GeneWikii Rev-ErbA_alpha.
    GenomeRNAii 9572.
    NextBioi 35899.
    PROi P20393.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20393.
    Bgeei P20393.
    CleanExi HS_NR1D1.
    Genevestigatori P20393.

    Family and domain databases

    Gene3Di 1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view ]
    Pfami PF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view ]
    PRINTSi PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTi SM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48508. SSF48508. 1 hit.
    PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Two erbA homologs encoding proteins with different T3 binding capacities are transcribed from opposite DNA strands of the same genetic locus."
      Miyajima N., Horiuchi R., Shibuya Y., Fukushige S., Matsubara K., Toyoshima K., Yamamoto T.
      Cell 57:31-39(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Placenta.
    2. "Isolation of a cDNA encoding human Rev-ErbA alpha: transcription from the noncoding DNA strand of a thyroid hormone receptor gene results in a related protein that does not bind thyroid hormone."
      Lazar M.A., Jones K.E., Chin W.W.
      DNA Cell Biol. 9:77-83(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Tissue: Fetal skeletal muscle.
    3. "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].
      Tissue: PNS.
    4. "Genomic organization of the human thyroid hormone receptor alpha (c-erbA-1) gene."
      Laudet V., Begue A., Henry C., Joubel A., Martin P., Stehelin D., Saule S.
      Nucleic Acids Res. 19:1105-1112(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 549-614.
    5. "Orphan nuclear hormone receptor Rev-erbalpha regulates the human apolipoprotein CIII promoter."
      Coste H., Rodriguez J.C.
      J. Biol. Chem. 277:27120-27129(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "The orphan nuclear receptor Rev-erbalpha recruits the N-CoR/histone deacetylase 3 corepressor to regulate the circadian Bmal1 gene."
      Yin L., Lazar M.A.
      Mol. Endocrinol. 19:1452-1459(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The orphan nuclear receptor Rev-erb alpha regulates circadian expression of plasminogen activator inhibitor type 1."
      Wang J., Yin L., Lazar M.A.
      J. Biol. Chem. 281:33842-33848(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Nuclear receptor Rev-erbalpha is a critical lithium-sensitive component of the circadian clock."
      Yin L., Wang J., Klein P.S., Lazar M.A.
      Science 311:1002-1005(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-55 AND SER-59, UBIQUITINATION.
    9. "A zinc finger HIT domain-containing protein, ZNHIT-1, interacts with orphan nuclear hormone receptor Rev-erbbeta and removes Rev-erbbeta-induced inhibition of apoCIII transcription."
      Wang J., Li Y., Zhang M., Liu Z., Wu C., Yuan H., Li Y.Y., Zhao X., Lu H.
      FEBS J. 274:5370-5381(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNHIT1.
    10. "Rev-erbalpha, a heme sensor that coordinates metabolic and circadian pathways."
      Yin L., Wu N., Curtin J.C., Qatanani M., Szwergold N.R., Reid R.A., Waitt G.M., Parks D.J., Pearce K.H., Wisely G.B., Lazar M.A.
      Science 318:1786-1789(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HEME-BINDING.
    11. "Negative feedback maintenance of heme homeostasis by its receptor, Rev-erbalpha."
      Wu N., Yin L., Hanniman E.A., Joshi S., Lazar M.A.
      Genes Dev. 23:2201-2209(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Nuclear receptor Rev-erbalpha: a heme receptor that coordinates circadian rhythm and metabolism."
      Yin L., Wu N., Lazar M.A.
      Nucl. Recept. Signal. 8:E001-E001(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    13. "A circadian clock in hippocampus is regulated by interaction between oligophrenin-1 and Rev-erbalpha."
      Valnegri P., Khelfaoui M., Dorseuil O., Bassani S., Lagneaux C., Gianfelice A., Benfante R., Chelly J., Billuart P., Sala C., Passafaro M.
      Nat. Neurosci. 14:1293-1301(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH OPHN1.
    14. "Cryptochromes mediate rhythmic repression of the glucocorticoid receptor."
      Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H., Jonker J.W., Downes M., Evans R.M.
      Nature 480:552-556(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CRY1 AND PER2.
    15. "Direct regulation of CLOCK expression by REV-ERB."
      Crumbley C., Burris T.P.
      PLoS ONE 6:E17290-E17290(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "REV-ERBs: more than the sum of the individual parts."
      Stratmann M., Schibler U.
      Cell Metab. 15:791-793(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    17. "REV-ERB-erating nuclear receptor functions in circadian metabolism and physiology."
      Ripperger J.A., Albrecht U.
      Cell Res. 22:1319-1321(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    18. "The nuclear receptor REV-ERBalpha mediates circadian regulation of innate immunity through selective regulation of inflammatory cytokines."
      Gibbs J.E., Blaikley J., Beesley S., Matthews L., Simpson K.D., Boyce S.H., Farrow S.N., Else K.J., Singh D., Ray D.W., Loudon A.S.
      Proc. Natl. Acad. Sci. U.S.A. 109:582-587(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Structural elements of an orphan nuclear receptor-DNA complex."
      Zhao Q., Khorasanizadeh S., Miyoshi Y., Lazar M.A., Rastinejad F.
      Mol. Cell 1:849-861(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 123-215.

    Entry informationi

    Entry nameiNR1D1_HUMAN
    AccessioniPrimary (citable) accession number: P20393
    Secondary accession number(s): Q0P5Z4, Q15304
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 167 of the entry and version 1 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 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3