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Q505F1

- NR2C1_MOUSE

UniProt

Q505F1 - NR2C1_MOUSE

Protein

Nuclear receptor subfamily 2 group C member 1

Gene

Nr2c1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Orphan nuclear receptor. Binds the IR7 element in the promoter of its own gene in an autoregulatory negative feedback mechanism. Primarily repressor of a broad range of genes including ESR1 and RARB. Together with NR2C2, forms the core of the DRED (direct repeat erythroid-definitive) complex that represses embryonic and fetal globin transcription. Binds to hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half site direct repeat consensus sequences By similarity. Also activator of OCT4 gene expression. Plays a fundamental role in early embryogenesis and regulates embryonic stem cell proliferation and differentiation. Mediator of retinoic acid-regulated preadipocyte proliferation.By similarity13 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi98 – 17376Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri101 – 12121NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri137 – 15620NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. histone deacetylase binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB
    5. sequence-specific DNA binding Source: InterPro
    6. sequence-specific DNA binding transcription factor activity Source: InterPro
    7. steroid hormone receptor activity Source: InterPro
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. negative regulation of transcription, DNA-templated Source: UniProtKB
    2. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    3. positive regulation of retinoic acid receptor signaling pathway Source: UniProtKB
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Receptor, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor subfamily 2 group C member 1
    Alternative name(s):
    Orphan nuclear receptor TR2
    Testicular receptor 2
    Short name:
    mTR2
    Gene namesi
    Name:Nr2c1Imported
    Synonyms:Tr2, Tr2-11Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1352465. Nr2c1.

    Subcellular locationi

    Nucleus. NucleusPML body
    Note: Recruited by HDAC3, after all-trans retinoic acid stimulated MAPK1-mediated Thr-210 phosphorylation, to PML bodies for subsequent sumoylation.

    GO - Cellular componenti

    1. nucleus Source: UniProtKB
    2. PML body Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. Mice exhibit normal spermatogenesis and testis development, as well as normal central nervous system development. NR2C1 and NR2C2 double null mutants result in early embryonic lethality and increased apoptosis. Embryos die around 7.5 dpc.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi167 – 1671K → A: No effect on sumoylation. 1 Publication
    Mutagenesisi170 – 1701S → A: No effect on sumoylation nor on DNA-binding and little effect on binding KAT2B. Greatly reduced DNA-binding, binding to KAT2B and activation of the RARB promoter; when associated with A-185. 2 Publications
    Mutagenesisi185 – 1851S → A: No effect on sumoylation and little effect on binding KAT2B. Some reduced DNA-binding. Greatly reduced DNA-binding, binding to KAT2B and activation of the RARB promoter; when associated with A-170. 2 Publications
    Mutagenesisi203 – 2031S → A: No effect on sumoylation. 1 Publication
    Mutagenesisi208 – 2081T → A: No effect on sumoylation. 1 Publication
    Mutagenesisi210 – 2101T → A: Abolishes sumoylation. No repression of OCT4 gene expression with or without retinoic acid and enhanced interaction with KAT2B and HDAC3. Abolishes interaction with HDAC3 and PML association; when associated with R-238. 1 Publication
    Mutagenesisi210 – 2101T → E: Sumoylated. Repressed OCT4 gene expression. Enhanced interaction with KAT2B; when associated with R-238. 1 Publication
    Mutagenesisi238 – 2381K → A: Abolishes sumoylation. Strongly associated with PML nuclear bodies. No effect on activation of OCT4 but activation not suppressed by additional SUMO1. Increased binding to KAT2B and reduced binding to NRIP1. Abolishes PML association; when associated with A-210. 2 Publications
    Mutagenesisi238 – 2381K → R: Abolishes sumoylation. No effect on activation of OCT4 but activation not suppressed by additional SUMO1. Enhanced interaction with KAT2B; when associated with A-210 or E-210. 2 Publications
    Mutagenesisi240 – 2401E → A: Abolishes sumoylation. 1 Publication
    Mutagenesisi461 – 4611S → A: Little effect on PKC-stimulated protein stability nor on activation of RARB reporter. 1 Publication
    Mutagenesisi461 – 4611S → A: No effect on sumoylation. 1 Publication
    Mutagenesisi568 – 5681S → A: Greatly reduced PKC-stimulated protein stability and activation of RARB reporter. 1 Publication
    Mutagenesisi568 – 5681S → A: No effect on sumoylation. 1 Publication
    Mutagenesisi575 – 5751K → R: No effect on sumoylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 590590Nuclear receptor subfamily 2 group C member 1PRO_0000053587Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei185 – 1851Phosphoserine1 Publication
    Modified residuei203 – 2031Phosphoserine1 Publication
    Modified residuei208 – 2081Phosphothreonine1 Publication
    Modified residuei210 – 2101Phosphothreonine; by MAPK11 Publication
    Cross-linki238 – 238Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei461 – 4611Phosphoserine; by PKC1 Publication
    Modified residuei568 – 5681Phosphoserine; by PKC1 Publication

    Post-translational modificationi

    Sumoylation requires both PIAS1 and UBE2I. Sumoylation appears to dissociate NR2C1 from the PML nuclear bodies. Enhances the interaction with NRIP1 but inhibits interaction with KAT2B. In proliferating cells, stimulation by all-trans retinoic acid, activation of MAPK1-mediated phosphorylation and recruitment to PML bodies with subsequent sumoylation, suppresses OCT4 expression.
    Phosphorylated on several serine and threonine residues. Phosphorylation on Thr-210, stimulated by all-trans retinoic acid (atRA) mediates PML location and sumoylation in proliferating cells which then modulates its association with effector molecules, KAT2B and NRIP1. Phosphorylation on Ser-568 by PKC is important for protein stability and function as activator of RARB.2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ505F1.
    PRIDEiQ505F1.

    PTM databases

    PhosphoSiteiQ505F1.

    Expressioni

    Tissue specificityi

    Isoform 1 is highly expressed in the adlumenal compartment of the seminiferous tubule of adult testes (at protein level) and in the eyes of newborn animals. Weakly expressed in other adult organs including the seminal vesicle, prostate, ovary, adrenal gland, heart, thymus, placenta and brain. Expressed during embryonic stages in developing eyes, brain and cartilage primordia (at protein level). Also expressed in the developing spinal motor neurons and in the sympathetic-, parasympathetic- and sensory ganglia of the embryonic PNS. Expressed in the developing neural epithelia of the inner ear, nasal cavity, tongue and retina. At day 16.5, expressed in various tissues including kidney and intestine. In contrast, isoform 2 is widely expressed at a low level throughout the adult testis.7 Publications

    Developmental stagei

    Isoform 1 is highly expressed in early to midgestation embryos, with expression leveling off at 15 dpc. Expressed in yolk sac erythrocytes at 9.5 dpc. After birth, expression in the testes remains at a basal level until puberty, begins to increase at postnatal day 16 (P16) and peaks at P20 to P24. Expression is maintained at a high level throughout adulthood. Isoform 2 peaks transiently at P24.4 Publications

    Inductioni

    By ciliary neurotrophic factor (CNTF). Repressed by vitamin A. Induced by retinoic acid.2 Publications

    Gene expression databases

    BgeeiQ505F1.
    CleanExiMM_NR2C1.
    GenevestigatoriQ505F1.

    Interactioni

    Subunit structurei

    Homodimer. Heterodimer; with NR2C2 which is required for chromatin remodeling and for binding to promoter regions such as globin DR1 repeats. Interacts with ESR1; the interaction prevents homodimerization of ESR1 and suppresses its transcriptional activity and cell growth By similarity. Interacts with NRIP1 (via its LXXLL motifs); the interaction provides corepressor activity. Interacts with HDAC3 (via the DNA-binding domain); the interaction recruits phosphorylated NR2C1 to PML bodies for sumoylation. Interacts with HDAC4 (via the DNA-binding domain). Interacts with PIAS1; the interaction is required for sumoylation of NR2C1. Interacts with UBE2I; the interaction is required for sumoylation of NR2C1. Interacts with KAT2B; the interaction acts as a corepressor of gene expression.By similarity6 Publications

    Protein-protein interaction databases

    BioGridi204299. 1 interaction.
    DIPiDIP-29275N.

    Structurei

    3D structure databases

    ProteinModelPortaliQ505F1.
    SMRiQ505F1. Positions 100-576.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 166166Required for interaction with KAT2BAdd
    BLAST
    Regioni571 – 59020Required for interaction with NRIP1Add
    BLAST

    Sequence similaritiesi

    Belongs to the nuclear hormone receptor family. NR2 subfamily.Sequence Analysis
    Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri101 – 12121NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri137 – 15620NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG297520.
    GeneTreeiENSGT00740000115010.
    HOVERGENiHBG008596.
    InParanoidiQ0VGP8.
    KOiK08543.
    OMAiEKAYMEF.
    OrthoDBiEOG7FJH0K.
    TreeFamiTF316650.

    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. 2 hits.
    PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 13 Publications (identifier: Q505F1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MATIEEIAHQ IIDQQMGEIV TEQQTGQKIQ IVTALDHSTQ GKQFILANHE    50
    GSTPGKVFLT TPDAAGVNQL FFTSPDLSAP HLQLLTEKSP DQGPNKVFDL 100
    CVVCGDKASG RHYGAITCEG CKGFFKRSIR KNLVYSCRGS KDCVINKHHR 150
    NRCQYCRLQR CIAFGMKQDS VQCERKPIEV SREKSSNCAA STEKIYIRKD 200
    LRSPLAATPT FVTDSETARS AGLLDSGMFV NIHPSGIKTE PAMLMAPDKA 250
    ESCQGDLSTL ASVVTSLANL GKAKDLSHCG GDMPVVQSLR NGDTSFGAFH 300
    HDIQTNGDVS RAFDTLAKAL TPGESSACQS PEEGMEGSPH LIAGEPSFVE 350
    KEGPLLSESH VAFRLTMPSP MPEYLNVHYI GESASRLLFL SMHWALSIPS 400
    FQALGQENSI SLVKAYWNEL FTLGLAQCWQ VMNVATILAT FVNCLHSSLQ 450
    QDKMSPERRK SLMEHIFKLQ EFCNSMVKLC IDGHEYAYLK AIVLFSPDHP 500
    GLENMELIER FQEKAYVEFQ DYITRTYPDD TYRLSRLLLR LPALRLMNAT 550
    ITEELFFKGL IGNVRIDSVI PHILKMEPAD YNSQIIGHSL 590
    Length:590
    Mass (Da):65,476
    Last modified:July 27, 2011 - v3
    Checksum:iE639AF3E5312918D
    GO
    Isoform 21 Publication (identifier: Q505F1-2) [UniParc]FASTAAdd to Basket

    Also known as: TR2-11-t1 Publication

    , TR2-11-truncated1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         220-256: SAGLLDSGMFVNIHPSGIKTEPAMLMAPDKAESCQGD → CPAAISASFASLPRSTETKTCASFVAGQLDCWIQECL
         257-590: Missing.

    Note: Due to intron retention.1 Publication

    Show »
    Length:256
    Mass (Da):28,225
    Checksum:i53064D53EEB1C54A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti88 – 881K → N in CAA72244. (PubMed:9504722)Curated
    Sequence conflicti88 – 881K → N in AAC29502. (PubMed:9694834)Curated
    Sequence conflicti88 – 881K → N in AAL31315. 1 PublicationCurated
    Sequence conflicti200 – 2001D → N in AAC29502. (PubMed:9694834)Curated
    Sequence conflicti200 – 2001D → N in AAL31315. 1 PublicationCurated
    Sequence conflicti273 – 2731A → T in AAC29502. (PubMed:9694834)Curated
    Sequence conflicti273 – 2731A → T in AAL31315. 1 PublicationCurated
    Sequence conflicti326 – 3272SA → TS in AAC52787. (PubMed:8595902)Curated
    Sequence conflicti326 – 3272SA → TS in AAC53253. (PubMed:8595902)Curated
    Sequence conflicti326 – 3272SA → TS in CAA72244. (PubMed:9504722)Curated
    Sequence conflicti326 – 3272SA → TS in AAL31315. 1 PublicationCurated
    Sequence conflicti331 – 3311P → S in AAC29502. (PubMed:9694834)Curated
    Sequence conflicti331 – 3311P → S in AAL31315. 1 PublicationCurated
    Sequence conflicti529 – 5291D → N in BAE27509. (PubMed:16141072)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti29 – 291I → M in strain: CD-1. 2 Publications
    Natural varianti145 – 1451I → M in strain: CD-1. 2 Publications
    Natural varianti296 – 3049FGAFHHDIQ → SVLFIMIFK in strain: CD-1. 2 Publications
    Natural varianti361 – 3611V → I in strain: CD-1. 2 Publications
    Natural varianti377 – 3771V → A in strain: CD-1. 2 Publications
    Natural varianti456 – 4561P → A in strain: CD-1. 2 Publications

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei220 – 25637SAGLL…SCQGD → CPAAISASFASLPRSTETKT CASFVAGQLDCWIQECL in isoform 2. 1 PublicationVSP_051921Add
    BLAST
    Alternative sequencei257 – 590334Missing in isoform 2. 1 PublicationVSP_051922Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28280
    , U28269, U28270, U28271, U28272, U28273, U28274, U28275, U28276, U28277, U28278, U28279 Genomic DNA. Translation: AAC53253.1.
    U28265 mRNA. Translation: AAC52787.1.
    Y11436 mRNA. Translation: CAA72244.1.
    U30482 mRNA. Translation: AAC29502.1.
    L26957 mRNA. Translation: AAL31315.1.
    AK146891 mRNA. Translation: BAE27509.1.
    AK149374 mRNA. Translation: BAE28842.1.
    AC127596 Genomic DNA. No translation available.
    AC138026 Genomic DNA. No translation available.
    BC090662 mRNA. Translation: AAH90662.1.
    BC094580 mRNA. Translation: AAH94580.1.
    CCDSiCCDS24131.1. [Q505F1-1]
    RefSeqiNP_035759.3. NM_011629.3. [Q505F1-1]
    XP_006513655.1. XM_006513592.1. [Q505F1-1]
    UniGeneiMm.107483.

    Genome annotation databases

    EnsembliENSMUST00000092213; ENSMUSP00000089858; ENSMUSG00000005897. [Q505F1-1]
    ENSMUST00000099343; ENSMUSP00000096945; ENSMUSG00000005897. [Q505F1-1]
    ENSMUST00000105290; ENSMUSP00000100927; ENSMUSG00000005897. [Q505F1-1]
    GeneIDi22025.
    KEGGimmu:22025.
    UCSCiuc007gvo.2. mouse. [Q505F1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U28280
    , U28269 , U28270 , U28271 , U28272 , U28273 , U28274 , U28275 , U28276 , U28277 , U28278 , U28279 Genomic DNA. Translation: AAC53253.1 .
    U28265 mRNA. Translation: AAC52787.1 .
    Y11436 mRNA. Translation: CAA72244.1 .
    U30482 mRNA. Translation: AAC29502.1 .
    L26957 mRNA. Translation: AAL31315.1 .
    AK146891 mRNA. Translation: BAE27509.1 .
    AK149374 mRNA. Translation: BAE28842.1 .
    AC127596 Genomic DNA. No translation available.
    AC138026 Genomic DNA. No translation available.
    BC090662 mRNA. Translation: AAH90662.1 .
    BC094580 mRNA. Translation: AAH94580.1 .
    CCDSi CCDS24131.1. [Q505F1-1 ]
    RefSeqi NP_035759.3. NM_011629.3. [Q505F1-1 ]
    XP_006513655.1. XM_006513592.1. [Q505F1-1 ]
    UniGenei Mm.107483.

    3D structure databases

    ProteinModelPortali Q505F1.
    SMRi Q505F1. Positions 100-576.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204299. 1 interaction.
    DIPi DIP-29275N.

    PTM databases

    PhosphoSitei Q505F1.

    Proteomic databases

    PaxDbi Q505F1.
    PRIDEi Q505F1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000092213 ; ENSMUSP00000089858 ; ENSMUSG00000005897 . [Q505F1-1 ]
    ENSMUST00000099343 ; ENSMUSP00000096945 ; ENSMUSG00000005897 . [Q505F1-1 ]
    ENSMUST00000105290 ; ENSMUSP00000100927 ; ENSMUSG00000005897 . [Q505F1-1 ]
    GeneIDi 22025.
    KEGGi mmu:22025.
    UCSCi uc007gvo.2. mouse. [Q505F1-1 ]

    Organism-specific databases

    CTDi 7181.
    MGIi MGI:1352465. Nr2c1.

    Phylogenomic databases

    eggNOGi NOG297520.
    GeneTreei ENSGT00740000115010.
    HOVERGENi HBG008596.
    InParanoidi Q0VGP8.
    KOi K08543.
    OMAi EKAYMEF.
    OrthoDBi EOG7FJH0K.
    TreeFami TF316650.

    Miscellaneous databases

    NextBioi 301764.
    PROi Q505F1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q505F1.
    CleanExi MM_NR2C1.
    Genevestigatori Q505F1.

    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. 2 hits.
    PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic structure, promoter identification, and chromosomal mapping of a mouse nuclear orphan receptor expressed in embryos and adult testes."
      Lee C.-H., Copeland N.G., Gilbert D.J., Jenkins N.A., Wei L.-N.
      Genomics 30:46-52(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANTS MET-29; MET-145; 296-SER--LYS-304; ILE-361; ALA-377 AND ALA-456.
      Strain: CD-1Imported.
      Tissue: Embryo1 Publication.
    2. "Molecular cloning and characterization of a mouse nuclear orphan receptor expressed in embryos and testes."
      Lee C.-H., Chang L., Wei L.N.
      Mol. Reprod. Dev. 44:305-314(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANTS MET-29; MET-145; 296-SER--LYS-304; ILE-361; ALA-377 AND ALA-456.
      Strain: CD-1Imported.
      Tissue: Embryo1 Publication.
    3. "Distinct expression patterns and biological activities of two isoforms of the mouse orphan receptor TR2."
      Lee C.-H., Chang L., Wei L.-N.
      J. Endocrinol. 152:245-255(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    4. "Polymorphism in the murine Tr2-11 gene encoding an orphan receptor, and its exclusion as a candidate gene for the cataract mutation Cat3."
      Immervoll T., Adamski J., Graw J.
      Biol. Chem. 379:83-85(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Strain: C3H X 1021 Publication.
    5. "A bidirectional regulation between the TR2/TR4 orphan receptors (TR2/TR4) and the ciliary neurotrophic factor (CNTF) signaling pathway."
      Young W.-J., Lee Y.-F., Smith S.M., Chang C.
      J. Biol. Chem. 273:20877-20885(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION.
      Strain: C57BL/6Imported.
      Tissue: TestisImported.
    6. "Cloning, antibody production and immunohistochemical localization of an androgen repressed of mouse and rat TR2 orphan receptors: a member of steroid receptor superfamily."
      Ideta R., Yeh S., Lee Y.-F., Adachi K., Takeda H., Su C., Chang C.
      Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    7. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6JImported.
      Tissue: Embryonic kidney1 Publication and Liver tumorImported.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    9. "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] (ISOFORM 1).
      Strain: C57BL/6Imported.
      Tissue: EyeImported.
    10. "Multiple functions of the TR2-11 orphan receptor in modulating activation of two key cis-acting elements involved in the retinoic acid signal transduction system."
      Lin T.M., Young W.J., Chang C.
      J. Biol. Chem. 270:30121-30128(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, FUNCTION, TISSUE SPECIFICITY.
    11. "The orphan nuclear receptor TR2 suppresses a DR4 hormone response element of the mouse CRABP-I gene promoter."
      Chinpaisal C., Chang L., Hu X., Lee C.-H., Wen W.-N., Wei L.-N.
      Biochemistry 36:14088-14095(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, HOMODIMERIZATION.
    12. "Cloning and characterization of mouse RIP140, a corepressor for nuclear orphan receptor TR2."
      Lee C.-H., Chinpaisal C., Wei L.-N.
      Mol. Cell. Biol. 18:6745-6755(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NRIP1.
    13. "The orphan nuclear receptor TR2 interacts directly with both class I and class II histone deacetylases."
      Franco P.J., Farooqui M., Seto E., Wei L.-N.
      Mol. Endocrinol. 15:1318-1328(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HDAC3 AND HDAC4.
    14. "An embryonic/fetal beta-type globin gene repressor contains a nuclear receptor TR2/TR4 heterodimer."
      Tanabe O., Katsuoka F., Campbell A.D., Song W., Yamamoto M., Tanimoto K., Engel J.D.
      EMBO J. 21:3434-3442(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY IN DRED COMPLEX, FUNCTION, SUBCELLULAR LOCATION, HETERODIMERIZATION, DEVELOPMENTAL STAGE.
    15. "Spermatogenesis and testis development are normal in mice lacking testicular orphan nuclear receptor 2."
      Shyr C.R., Collins L.L., Mu X.M., Platt K.A., Chang C.
      Mol. Cell. Biol. 22:4661-4666(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
    16. "Protein kinase C-mediated phosphorylation of orphan nuclear receptor TR2: effects on receptor stability and activity."
      Khan S.A., Park S.W., Huq M., Wei L.N.
      Proteomics 5:3885-3894(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-461 AND SER-568, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "Ligand-independent orphan receptor TR2 activation by phosphorylation at the DNA-binding domain."
      Khan S.A., Park S.W., Huq M.D., Wei L.N.
      Proteomics 6:123-130(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-185, DNA-BINDING, FUNCTION, INTERACTION WITH KAT2B, MUTAGENESIS OF SER-170 AND SER-185.
    18. "Embryonic and fetal beta-globin gene repression by the orphan nuclear receptors, TR2 and TR4."
      Tanabe O., McPhee D., Kobayashi S., Shen Y., Brandt W., Jiang X., Campbell A.D., Chen Y.T., Chang C., Yamamoto M., Tanimoto K., Engel J.D.
      EMBO J. 26:2295-2306(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HETERODIMERIZATION.
    19. "The TR2 and TR4 orphan nuclear receptors repress Gata1 transcription."
      Tanabe O., Shen Y., Liu Q., Campbell A.D., Kuroha T., Yamamoto M., Engel J.D.
      Genes Dev. 21:2832-2844(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: HETERODIMERIZATION, FUNCTION.
    20. "SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells."
      Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.
      Nat. Struct. Mol. Biol. 14:68-75(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-238, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH KAT2B; NRIP1; PIAS1 AND UBE2I, MUTAGENESIS OF LYS-167; LYS-238; GLU-240 AND LYS-575.
    21. "Orphan nuclear receptor TR2, a mediator of preadipocyte proliferation, is differentially regulated by RA through exchange of coactivator PCAF with corepressor RIP140 on a platform molecule GRIP1."
      Gupta P., Park S.W., Farooqui M., Wei L.N.
      Nucleic Acids Res. 35:2269-2282(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "Retinoic acid-stimulated sequential phosphorylation, PML recruitment, and SUMOylation of nuclear receptor TR2 to suppress Oct4 expression."
      Gupta P., Ho P.C., Huq M.M., Ha S.G., Park S.W., Khan A.A., Tsai N.P., Wei L.N.
      Proc. Natl. Acad. Sci. U.S.A. 105:11424-11429(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-203; THR-208 AND THR-210, SUMOYLATION, INTERACTION WITH KAT2B, MUTAGENESIS OF SER-170; SER-185; SER-203; THR-208; THR-210; LYS-238; SER-461 AND SER-568, IDENTIFICATION BY MASS SPECTROMETRY.
    23. "Roles of testicular orphan nuclear receptors 2 and 4 in early embryonic development and embryonic stem cells."
      Shyr C.R., Kang H.Y., Tsai M.Y., Liu N.C., Ku P.Y., Huang K.E., Chang C.
      Endocrinology 150:2454-2462(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, INDUCTION, FUNCTION.
    24. "HDAC3 as a molecular chaperone for shuttling phosphorylated TR2 to PML: a novel deacetylase activity-independent function of HDAC3."
      Gupta P., Ho P.C., Ha S.G., Lin Y.W., Wei L.N.
      PLoS ONE 4:E4363-E4363(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION, INTERACTION WITH HDAC3, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiNR2C1_MOUSE
    AccessioniPrimary (citable) accession number: Q505F1
    Secondary accession number(s): P97763
    , Q0VGP8, Q3UIJ7, Q4U1Z4, Q60927, Q62152, Q8VIJ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 93 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3