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Q14995

- NR1D2_HUMAN

UniProt

Q14995 - NR1D2_HUMAN

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
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      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 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 receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri103 – 12321NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri140 – 16425NR C4-typePROSITE-ProRule annotationAdd
    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

    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 PublicationsPROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: UniProtKB

    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-betaBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

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

    Zinc finger

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti519 – 5202IE → NRK in AAA65937. (PubMed:7997240)Curated

    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 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

    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: October 1, 2014
    This is version 141 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