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Q14995

- NR1D2_HUMAN

UniProt

Q14995 - NR1D2_HUMAN

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Protein

Nuclear receptor subfamily 1 group D member 2

Gene
NR1D2
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 ARNTL/BMAL1 and CLOCK. Also regulates genes involved in metabolic functions, including lipid metabolism and the 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 nuclegotides (RevDR-2). Acts as a potent competitive repressor of ROR alpha (RORA) function and also negatively regulates the expression of NR1D1. Regulates lipid and energy homeostasis in the skeletal muscle via repression of genes involved in lipid metabolism and myogenesis including: CD36, FABP3, FABP4, UCP3, SCD1 and MSTN. Regulates hepatic lipid metabolism via the repression of APOC3. Represses gene expression at a distance in macrophages by inhibiting the transcription of enhancer-derived RNAs (eRNAs). In addition to its activity as a repressor, can also act as a transcriptional activator. Acts as a transcriptional activator of the sterol regulatory element-binding protein 1 (SREBF1) and the inflammatory mediator interleukin-6 (IL6) in the skeletal muscle.2 Publications

Enzyme regulationi

The heme-bound form can bind gaseous signaling molecules such as CO and nitric oxide (NO) and NO can reverse its transcriptional repressor activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei384 – 3841Heme
Binding sitei568 – 5681Heme

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi100 – 17677Nuclear receptorAdd
BLAST
Zinc fingeri103 – 12321NR C4-typeAdd
BLAST
Zinc fingeri140 – 16425NR C4-typeAdd
BLAST

GO - Molecular functioni

  1. core promoter sequence-specific DNA binding Source: UniProtKB
  2. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. steroid hormone receptor activity Source: InterPro
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. gene expression Source: Reactome
  2. intracellular receptor signaling pathway Source: GOC
  3. lipid homeostasis Source: UniProtKB
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
  5. positive regulation of transcription, DNA-templated Source: UniProtKB
  6. regulation of circadian rhythm Source: UniProtKB
  7. regulation of energy homeostasis Source: UniProtKB
  8. regulation of inflammatory response Source: UniProtKB
  9. regulation of lipid metabolic process Source: UniProtKB
  10. regulation of skeletal muscle cell differentiation Source: UniProtKB
  11. regulation of transcription, DNA-templated Source: UniProtKB
  12. rhythmic process Source: UniProtKB-KW
  13. transcription initiation from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor, Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor subfamily 1 group D member 2
Alternative name(s):
Orphan nuclear hormone receptor BD73
Rev-erb alpha-related receptor
Short name:
RVR
Rev-erb-beta
V-erbA-related protein 1-related
Short name:
EAR-1R
Gene namesi
Name:NR1D2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:7963. NR1D2.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31749.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 579579Nuclear receptor subfamily 1 group D member 2PRO_0000053501Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461Phosphoserine; by GSK3-beta By similarity
Modified residuei162 – 1621N6-acetyllysine; by KAT51 Publication
Modified residuei163 – 1631N6-acetyllysine; by KAT51 Publication
Disulfide bondi337 ↔ 3431 Publication
Disulfide bondi374 ↔ 3841 Publication

Post-translational modificationi

Deacetylated by HDAC1. Acetylation and deacetylation regulate its transcriptional regulatory activity.1 Publication
Under more reducing intracellular redox conditions, Cys-384 is in its heme-bound state, which is optimal for recruitment of the NCOR1/HDAC3 corepressor complex and repression of target genes. When subjected to oxidative stress conditions, Cys-384 undergoes oxidation to form a disulfide bridge with Cys-374, also triggering a ligand switch that results in release of bound heme and derepression of target genes.

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ14995.
PRIDEiQ14995.

PTM databases

PhosphoSiteiQ14995.

Expressioni

Tissue specificityi

Widely expressed. Expressed at high levels in the liver, adipose tissue, skeletal muscle and brain. Expression oscillates diurnally in the suprachiasmatic nucleus (SCN) of the hypothalamus as well as in peripheral tissues.

Gene expression databases

ArrayExpressiQ14995.
BgeeiQ14995.
CleanExiHS_NR1D2.
GenevestigatoriQ14995.

Organism-specific databases

HPAiHPA053868.
HPA054798.

Interactioni

Subunit structurei

Binds DNA as a monomer or a homodimer. Interacts with NCOA5 coactivator, leading to a strong increase of transcription of target genes. Interacts (via N-terminus) with KAT5. Interacts (via C-terminus) with HDAC1. Interacts with ZNHIT1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ClockO087852EBI-6144053,EBI-79859From a different organism.
PRMT6Q96LA82EBI-6144053,EBI-912440

Protein-protein interaction databases

BioGridi115299. 12 interactions.
IntActiQ14995. 7 interactions.
MINTiMINT-8417705.
STRINGi9606.ENSP00000310006.

Structurei

Secondary structure

1
579
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi398 – 42124
Helixi424 – 4285
Helixi431 – 44919
Helixi451 – 4533
Turni456 – 4594
Beta strandi460 – 4623
Beta strandi468 – 4703
Helixi471 – 4766
Helixi481 – 49414
Helixi500 – 51213
Helixi516 – 5183
Helixi522 – 54322
Helixi549 – 57325

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V0VX-ray2.40A/B/C/D387-579[»]
2V7CX-ray2.40A/B387-579[»]
3CQVX-ray1.90A381-579[»]
4N73X-ray1.87A381-578[»]
ProteinModelPortaliQ14995.
SMRiQ14995. Positions 98-577.

Miscellaneous databases

EvolutionaryTraceiQ14995.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9999ModulatingAdd
BLAST
Regioni124 – 249126HingeAdd
BLAST
Regioni250 – 570321Ligand-bindingAdd
BLAST
Regioni397 – 579183Interaction with ZNHIT1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 208Poly-Ser
Compositional biasi35 – 395Poly-Ser

Domaini

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

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri103 – 12321NR C4-typeAdd
BLAST
Zinc fingeri140 – 16425NR C4-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG324222.
HOGENOMiHOG000261691.
HOVERGENiHBG106790.
InParanoidiQ14995.
KOiK08531.
OMAiPGMTKSH.
OrthoDBiEOG776SQ0.
PhylomeDBiQ14995.
TreeFamiTF328382.

Family and domain databases

Gene3Di1.10.565.10. 3 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.

Q14995-1 [UniParc]FASTAAdd to Basket

« Hide

MEVNAGGVIA YISSSSSASS PASCHSEGSE NSFQSSSSSV PSSPNSSNSD    50
TNGNPKNGDL ANIEGILKND RIDCSMKTSK SSAPGMTKSH SGVTKFSGMV 100
LLCKVCGDVA SGFHYGVHAC EGCKGFFRRS IQQNIQYKKC LKNENCSIMR 150
MNRNRCQQCR FKKCLSVGMS RDAVRFGRIP KREKQRMLIE MQSAMKTMMN 200
SQFSGHLQND TLVEHHEQTA LPAQEQLRPK PQLEQENIKS SSPPSSDFAK 250
EEVIGMVTRA HKDTFMYNQE QQENSAESMQ PQRGERIPKN MEQYNLNHDH 300
CGNGLSSHFP CSESQQHLNG QFKGRNIMHY PNGHAICIAN GHCMNFSNAY 350
TQRVCDRVPI DGFSQNENKN SYLCNTGGRM HLVCPLSKSP YVDPHKSGHE 400
IWEEFSMSFT PAVKEVVEFA KRIPGFRDLS QHDQVNLLKA GTFEVLMVRF 450
ASLFDAKERT VTFLSGKKYS VDDLHSMGAG DLLNSMFEFS EKLNALQLSD 500
EEMSLFTAVV LVSADRSGIE NVNSVEALQE TLIRALRTLI MKNHPNEASI 550
FTKLLLKLPD LRSLNNMHSE ELLAFKVHP 579
Length:579
Mass (Da):64,625
Last modified:November 25, 2008 - v3
Checksum:i39BDDCD323BD14BF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211P → H.1 Publication
Corresponds to variant rs17854365 [ dbSNP | Ensembl ].
VAR_047377
Natural varianti282 – 2821Q → K.1 Publication
Corresponds to variant rs17857305 [ dbSNP | Ensembl ].
VAR_047378
Natural varianti288 – 2881P → R.1 Publication
Corresponds to variant rs17857306 [ dbSNP | Ensembl ].
VAR_047379
Natural varianti386 – 3861L → M.3 Publications
Corresponds to variant rs4858097 [ dbSNP | Ensembl ].
VAR_047380

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti519 – 5202IE → NRK in AAA65937. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16815 mRNA. Translation: BAA20088.1.
AK313464 mRNA. Translation: BAG36250.1.
AC124914 Genomic DNA. No translation available.
BC045613 mRNA. Translation: AAH45613.1.
L31785 mRNA. Translation: AAA65937.1.
CCDSiCCDS33718.1.
PIRiA57057.
RefSeqiNP_005117.3. NM_005126.4.
UniGeneiHs.37288.

Genome annotation databases

EnsembliENST00000312521; ENSP00000310006; ENSG00000174738.
GeneIDi9975.
KEGGihsa:9975.

Polymorphism databases

DMDMi215274122.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16815 mRNA. Translation: BAA20088.1 .
AK313464 mRNA. Translation: BAG36250.1 .
AC124914 Genomic DNA. No translation available.
BC045613 mRNA. Translation: AAH45613.1 .
L31785 mRNA. Translation: AAA65937.1 .
CCDSi CCDS33718.1.
PIRi A57057.
RefSeqi NP_005117.3. NM_005126.4.
UniGenei Hs.37288.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V0V X-ray 2.40 A/B/C/D 387-579 [» ]
2V7C X-ray 2.40 A/B 387-579 [» ]
3CQV X-ray 1.90 A 381-579 [» ]
4N73 X-ray 1.87 A 381-578 [» ]
ProteinModelPortali Q14995.
SMRi Q14995. Positions 98-577.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115299. 12 interactions.
IntActi Q14995. 7 interactions.
MINTi MINT-8417705.
STRINGi 9606.ENSP00000310006.

Chemistry

BindingDBi Q14995.
ChEMBLi CHEMBL1961784.
GuidetoPHARMACOLOGYi 597.

PTM databases

PhosphoSitei Q14995.

Polymorphism databases

DMDMi 215274122.

Proteomic databases

PaxDbi Q14995.
PRIDEi Q14995.

Protocols and materials databases

DNASUi 9975.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000312521 ; ENSP00000310006 ; ENSG00000174738 .
GeneIDi 9975.
KEGGi hsa:9975.

Organism-specific databases

CTDi 9975.
GeneCardsi GC03P023961.
HGNCi HGNC:7963. NR1D2.
HPAi HPA053868.
HPA054798.
MIMi 602304. gene.
neXtProti NX_Q14995.
PharmGKBi PA31749.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG324222.
HOGENOMi HOG000261691.
HOVERGENi HBG106790.
InParanoidi Q14995.
KOi K08531.
OMAi PGMTKSH.
OrthoDBi EOG776SQ0.
PhylomeDBi Q14995.
TreeFami TF328382.

Enzyme and pathway databases

Reactomei REACT_15525. Nuclear Receptor transcription pathway.

Miscellaneous databases

EvolutionaryTracei Q14995.
GeneWikii Rev-ErbA_beta.
GenomeRNAii 9975.
NextBioi 37672.
PROi Q14995.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14995.
Bgeei Q14995.
CleanExi HS_NR1D2.
Genevestigatori Q14995.

Family and domain databases

Gene3Di 1.10.565.10. 3 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. "Isolation of a novel member of the thyroid/steroid hormone receptor superfamily from human osteoblastic osteosarcoma HOS cell."
    Kamizono A., Shuichiro K., Kohei U.
    Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-386.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Hippocampus.
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANTS HIS-21; LYS-282; ARG-288 AND MET-386.
    Tissue: Brain.
  5. "A new orphan member of the nuclear hormone receptor superfamily closely related to Rev-Erb."
    Dumas B., Harding H.P., Choi H.-S., Lehmann K.A., Chung M., Lazar M.A., Moore D.D.
    Mol. Endocrinol. 8:996-1005(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-579, VARIANT MET-386.
    Tissue: Peripheral blood lymphocyte.
  6. "CIA, a novel estrogen receptor coactivator with a bifunctional nuclear receptor interacting determinant."
    Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F., Giguere V.
    Mol. Cell. Biol. 21:343-353(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA5.
  7. "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: FUNCTION, INTERACTION WITH ZNHIT1, SUBCELLULAR LOCATION.
  8. "The orphan nuclear receptor Rev-erbbeta recruits Tip60 and HDAC1 to regulate apolipoprotein CIII promoter."
    Wang J., Liu N., Liu Z., Li Y., Song C., Yuan H., Li Y.Y., Zhao X., Lu H.
    Biochim. Biophys. Acta 1783:224-236(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KAT5 AND HDAC1, SUBCELLULAR LOCATION, ACETYLATION AT LYS-162 AND LYS-163.
  9. "Thiol-disulfide redox dependence of heme binding and heme ligand switching in nuclear hormone receptor rev-erb{beta}."
    Gupta N., Ragsdale S.W.
    J. Biol. Chem. 286:4392-4403(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: HEME-BINDING, DISULFIDE BONDS.
  10. "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.
  11. "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.
  12. "Structural insight into the constitutive repression function of the nuclear receptor Rev-erbbeta."
    Woo E.-J., Jeong D.G., Lim M.-Y., Jun Kim S., Kim K.-J., Yoon S.-M., Park B.-C., Eon Ryu S.
    J. Mol. Biol. 373:735-744(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 386-579.
  13. "The structural basis of gas-responsive transcription by the human nuclear hormone receptor REV-ERBbeta."
    Pardee K.I., Xu X., Reinking J., Schuetz A., Dong A., Liu S., Zhang R., Tiefenbach J., Lajoie G., Plotnikov A.N., Botchkarev A., Krause H.M., Edwards A.
    PLoS Biol. 7:E43-E43(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 381-579, HEME-BINDING, ENZYME REGULATION.

Entry informationi

Entry nameiNR1D2_HUMAN
AccessioniPrimary (citable) accession number: Q14995
Secondary accession number(s): B2R8Q3, O00402, Q86XD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 25, 2008
Last modified: September 3, 2014
This is version 140 of the entry and version 3 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 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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