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P20393

- NR1D1_HUMAN

UniProt

P20393 - NR1D1_HUMAN

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Protein
Nuclear receptor subfamily 1 group D member 1
Gene
NR1D1, EAR1, HREV, THRAL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 4181Heme By similarity
Binding sitei602 – 6021Heme

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi129 – 20577Nuclear receptor
Add
BLAST
Zinc fingeri132 – 15221NR C4-type
Add
BLAST
Zinc fingeri169 – 19325NR C4-type
Add
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. steroid hormone receptor activity Source: ProtInc
  6. transcription corepressor activity Source: ProtInc
  7. transcription corepressor binding Source: UniProtKB
  8. transcription regulatory region DNA binding Source: BHF-UCL
  9. 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 from RNA polymerase II promoter Source: BHF-UCL
  11. negative regulation of transcription, DNA-templated Source: UniProtKB
  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
Complete GO annotation...

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
Complete GO annotation...

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 1
PRO_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 KAT5 By similarity
Modified residuei192 – 1921N6-acetyllysine; by KAT5 By 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. 1 interaction.
STRINGi9606.ENSP00000246672.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP20393.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 128128Modulating
Add
BLAST
Regioni49 – 284236Crucial for activation of GJA1 By similarity
Add
BLAST
Regioni206 – 28479Hinge
Add
BLAST
Regioni285 – 614330Ligand-binding
Add
BLAST

Compositional bias

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

Domaini

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

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471H → L in CAB53540. 1 Publication
Sequence conflicti564 – 5641E → Q1 Publication

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. 1 interaction.
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 166 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

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