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P49116

- NR2C2_HUMAN

UniProt

P49116 - NR2C2_HUMAN

Protein

Nuclear receptor subfamily 2 group C member 2

Gene

NR2C2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Orphan nuclear receptor that can act as a repressor or activator of transcription. An important repressor of nuclear receptor signaling pathways such as retinoic acid receptor, retinoid X, vitamin D3 receptor, thyroid hormone receptor and estrogen receptor pathways. May regulate gene expression during the late phase of spermatogenesis. Together with NR2C1, forms the core of the DRED (direct repeat erythroid-definitive) complex that represses embryonic and fetal globin transcription including that of GATA1. Binds to hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half site direct repeat consensus sequences. Plays a fundamental role in early embryonic development and embryonic stem cells. Required for normal spermatogenesis and cerebellum development. Appears to be important for neurodevelopmentally regulated behavior By similarity. Activates transcriptional activity of LHCG. Antagonist of PPARA-mediated transactivation.By similarity5 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi114 – 18976Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri117 – 13721NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri153 – 17725NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. cerebellum development Source: Ensembl
    3. gene expression Source: Reactome
    4. meiotic cell cycle Source: Ensembl
    5. nervous system development Source: ProtInc
    6. positive regulation of behavior Source: Ensembl
    7. positive regulation of embryonic development Source: Ensembl
    8. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    9. regulation of transcription, DNA-templated Source: ProtInc
    10. spermatogenesis Source: UniProtKB-KW
    11. transcription initiation from RNA polymerase II promoter Source: Reactome

    Keywords - Molecular functioni

    Activator, Receptor, Repressor

    Keywords - Biological processi

    Differentiation, Spermatogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
    SignaLinkiP49116.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor subfamily 2 group C member 2
    Alternative name(s):
    Orphan nuclear receptor TAK1
    Orphan nuclear receptor TR4
    Testicular receptor 4
    Gene namesi
    Name:NR2C2
    Synonyms:TAK1, TR4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:7972. NR2C2.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31755.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 596596Nuclear receptor subfamily 2 group C member 2PRO_0000053588Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Phosphoserine; by MAPK2 Publications
    Modified residuei46 – 461Phosphoserine2 Publications
    Modified residuei55 – 551Phosphoserine; by MAPKBy similarity
    Modified residuei68 – 681Phosphoserine; by MAPK1 Publication
    Modified residuei98 – 981Phosphoserine1 Publication
    Modified residuei219 – 2191Phosphoserine2 Publications
    Modified residuei231 – 2311N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylation on Ser-19 and Ser-68 is an important regulator of NR2C2-mediated transcriptional activity. Phosphorylation on these residues recruits the corepressor, NRIP1, leading to transcripional repression, whereas the non-phosphorylated form preferentially recruits the coactivator, PCAF By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP49116.
    PaxDbiP49116.
    PRIDEiP49116.

    PTM databases

    PhosphoSiteiP49116.

    Expressioni

    Developmental stagei

    Transiently repressed during the meiotic phase of spermatogenesis.

    Inductioni

    Induced by oxidative stress via FOXO3 activation.1 Publication

    Gene expression databases

    ArrayExpressiP49116.
    BgeeiP49116.
    CleanExiHS_NR2C2.
    GenevestigatoriP49116.

    Organism-specific databases

    HPAiHPA006313.

    Interactioni

    Subunit structurei

    Homodimer; can bind DNA as homodimer By similarity. Heterodimer; binds DNA as a heterodimer with NR2C1 required for chromatin remodeling and for binding to promoter regions such as globin DR1 repeats. Interacts with PCAF; the interaction preferentially occurs on the non-phosphorylated form and induces NR2C2-mediated transactivation activity and does not require the ligand-binding domain. Interacts (MAPK-mediated phosphorylated form) with NRIP1; the interaction promotes repression of NR2C2-mediated activity By similarity. Interacts with NR2C2AP; the interaction represses selective NR2C2-mediated transcriptional activity. Interacts with NLRP10.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi113034. 32 interactions.
    DIPiDIP-5999N.
    IntActiP49116. 4 interactions.
    MINTiMINT-7004540.
    STRINGi9606.ENSP00000320447.

    Structurei

    Secondary structure

    1
    596
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi354 – 3574
    Helixi386 – 40217
    Turni405 – 4073
    Helixi408 – 4103
    Helixi412 – 4209
    Helixi423 – 43311
    Turni434 – 4363
    Helixi468 – 48417
    Helixi489 – 50012
    Helixi512 – 53221
    Turni533 – 5353
    Helixi539 – 5446
    Helixi547 – 5515
    Helixi555 – 5628
    Helixi567 – 5704
    Helixi572 – 5798

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3P0UX-ray3.00A/B348-596[»]
    ProteinModelPortaliP49116.
    SMRiP49116. Positions 115-582.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49116.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni388 – 554167Ligand-bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri117 – 13721NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri153 – 17725NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG297520.
    HOGENOMiHOG000013058.
    HOVERGENiHBG008596.
    KOiK08544.
    OMAiYVQKTYP.
    OrthoDBiEOG7FJH0K.
    PhylomeDBiP49116.
    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 1 (identifier: P49116-1) [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

    MTSPSPRIQI ISTDSAVASP QRIQIVTDQQ TGQKIQIVTA VDASGSPKQQ    50
    FILTSPDGAG TGKVILASPE TSSAKQLIFT TSDNLVPGRI QIVTDSASVE 100
    RLLGKTDVQR PQVVEYCVVC GDKASGRHYG AVSCEGCKGF FKRSVRKNLT 150
    YSCRSNQDCI INKHHRNRCQ FCRLKKCLEM GMKMESVQSE RKPFDVQREK 200
    PSNCAASTEK IYIRKDLRSP LIATPTFVAD KDGARQTGLL DPGMLVNIQQ 250
    PLIREDGTVL LATDSKAETS QGALGTLANV VTSLANLSES LNNGDTSEIQ 300
    PEDQSASEIT RAFDTLAKAL NTTDSSSSPS LADGIDTSGG GSIHVISRDQ 350
    STPIIEVEGP LLSDTHVTFK LTMPSPMPEY LNVHYICESA SRLLFLSMHW 400
    ARSIPAFQAL GQDCNTSLVR ACWNELFTLG LAQCAQVMSL STILAAIVNH 450
    LQNSIQEDKL SGDRIKQVME HIWKLQEFCN SMAKLDIDGY EYAYLKAIVL 500
    FSPDHPGLTS TSQIEKFQEK AQMELQDYVQ KTYSEDTYRL ARILVRLPAL 550
    RLMSSNITEE LFFTGLIGNV SIDSIIPYIL KMETAEYNGQ ITGASL 596
    Length:596
    Mass (Da):65,414
    Last modified:February 1, 1996 - v1
    Checksum:i5180BDC3F3C8BD79
    GO
    Isoform 2 (identifier: P49116-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         24-24: Q → QGSEPASGPLSVFTSLNKEK

    Show »
    Length:615
    Mass (Da):67,345
    Checksum:i5D557E04602C1BAB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti108 – 1081V → A in BAH02299. (PubMed:18619963)Curated
    Sequence conflicti156 – 1561N → S in AAA21474. (PubMed:8016112)Curated
    Sequence conflicti326 – 3261S → F in BAH02299. (PubMed:18619963)Curated
    Sequence conflicti400 – 4001W → R in AAA21474. (PubMed:8016112)Curated
    Sequence conflicti409 – 4091A → G in AAA21474. (PubMed:8016112)Curated
    Sequence conflicti484 – 4852KL → NW in AAA21474. (PubMed:8016112)Curated
    Sequence conflicti594 – 5941A → V in AAA21474. (PubMed:8016112)Curated
    Sequence conflicti594 – 5941A → V in BAH02299. (PubMed:18619963)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei24 – 241Q → QGSEPASGPLSVFTSLNKEK in isoform 2. 1 PublicationVSP_039522

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10990 mRNA. Translation: AAC50118.1.
    L27586 mRNA. Translation: AAA21474.1.
    AB307708 mRNA. Translation: BAH02299.1.
    AK290590 mRNA. Translation: BAF83279.1.
    AC090937 Genomic DNA. No translation available.
    AC090954 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64215.1.
    CCDSiCCDS2621.1. [P49116-2]
    PIRiA57031.
    I59309.
    RefSeqiNP_001278623.1. NM_001291694.1. [P49116-1]
    NP_003289.2. NM_003298.4. [P49116-2]
    UniGeneiHs.555973.

    Genome annotation databases

    EnsembliENST00000323373; ENSP00000320447; ENSG00000177463. [P49116-2]
    ENST00000393102; ENSP00000376814; ENSG00000177463. [P49116-1]
    ENST00000406272; ENSP00000384463; ENSG00000177463. [P49116-1]
    ENST00000425241; ENSP00000388387; ENSG00000177463. [P49116-1]
    GeneIDi7182.
    KEGGihsa:7182.
    UCSCiuc003bzj.4. human. [P49116-1]

    Polymorphism databases

    DMDMi1351190.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10990 mRNA. Translation: AAC50118.1 .
    L27586 mRNA. Translation: AAA21474.1 .
    AB307708 mRNA. Translation: BAH02299.1 .
    AK290590 mRNA. Translation: BAF83279.1 .
    AC090937 Genomic DNA. No translation available.
    AC090954 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64215.1 .
    CCDSi CCDS2621.1. [P49116-2 ]
    PIRi A57031.
    I59309.
    RefSeqi NP_001278623.1. NM_001291694.1. [P49116-1 ]
    NP_003289.2. NM_003298.4. [P49116-2 ]
    UniGenei Hs.555973.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3P0U X-ray 3.00 A/B 348-596 [» ]
    ProteinModelPortali P49116.
    SMRi P49116. Positions 115-582.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113034. 32 interactions.
    DIPi DIP-5999N.
    IntActi P49116. 4 interactions.
    MINTi MINT-7004540.
    STRINGi 9606.ENSP00000320447.

    Chemistry

    BindingDBi P49116.
    ChEMBLi CHEMBL5716.
    GuidetoPHARMACOLOGYi 614.

    PTM databases

    PhosphoSitei P49116.

    Polymorphism databases

    DMDMi 1351190.

    Proteomic databases

    MaxQBi P49116.
    PaxDbi P49116.
    PRIDEi P49116.

    Protocols and materials databases

    DNASUi 7182.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000323373 ; ENSP00000320447 ; ENSG00000177463 . [P49116-2 ]
    ENST00000393102 ; ENSP00000376814 ; ENSG00000177463 . [P49116-1 ]
    ENST00000406272 ; ENSP00000384463 ; ENSG00000177463 . [P49116-1 ]
    ENST00000425241 ; ENSP00000388387 ; ENSG00000177463 . [P49116-1 ]
    GeneIDi 7182.
    KEGGi hsa:7182.
    UCSCi uc003bzj.4. human. [P49116-1 ]

    Organism-specific databases

    CTDi 7182.
    GeneCardsi GC03P014989.
    HGNCi HGNC:7972. NR2C2.
    HPAi HPA006313.
    MIMi 601426. gene.
    neXtProti NX_P49116.
    PharmGKBi PA31755.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG297520.
    HOGENOMi HOG000013058.
    HOVERGENi HBG008596.
    KOi K08544.
    OMAi YVQKTYP.
    OrthoDBi EOG7FJH0K.
    PhylomeDBi P49116.
    TreeFami TF316650.

    Enzyme and pathway databases

    Reactomei REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinki P49116.

    Miscellaneous databases

    ChiTaRSi NR2C2. human.
    EvolutionaryTracei P49116.
    GeneWikii Testicular_receptor_4.
    GenomeRNAii 7182.
    NextBioi 28158.
    PROi P49116.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49116.
    Bgeei P49116.
    CleanExi HS_NR2C2.
    Genevestigatori P49116.

    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. "TAK1: molecular cloning and characterization of a new member of the nuclear receptor superfamily."
      Hirose T., Fujimoto W., Yamaai T., Kim K.H., Matsuura H., Jetten A.M.
      Mol. Endocrinol. 8:1667-1680(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    2. "Human and rat TR4 orphan receptors specify a subclass of the steroid receptor superfamily."
      Chang C., da Silva S.L., Ideta R., Lee Y., Yeh S., Burbach J.P.
      Proc. Natl. Acad. Sci. U.S.A. 91:6040-6044(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Prostate and Testis.
    3. "DNA-binding profiling of human hormone nuclear receptors via fluorescence correlation spectroscopy in a cell-free system."
      Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T.
      FEBS Lett. 582:2737-2744(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DNA-BINDING SPECIFICITY.
    4. "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] (ISOFORM 1).
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The orphan receptor TAK1 acts as a repressor of RAR-, RXR- and T3R-mediated signaling pathways."
      Hirose T., Apfel R., Pfahl M., Jetten A.M.
      Biochem. Biophys. Res. Commun. 211:83-91(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, FUNCTION.
    8. "Regulation of peroxisome proliferator-activated receptor alpha-induced transactivation by the nuclear orphan receptor TAK1/TR4."
      Yan Z.H., Karam W.G., Staudinger J.L., Medvedev A., Ghanayem B.I., Jetten A.M.
      J. Biol. Chem. 273:10948-10957(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, INTERACTION WITH NRIP1, FUNCTION.
    9. "Differential regulation of direct repeat 3 vitamin D3 and direct repeat 4 thyroid hormone signaling pathways by the human TR4 orphan receptor."
      Lee Y.F., Young W.J., Lin W.J., Shyr C.R., Chang C.
      J. Biol. Chem. 274:16198-16205(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, FUNCTION.
    10. "Nuclear orphan receptors regulate transcription of the gene for the human luteinizing hormone receptor."
      Zhang Y., Dufau M.L.
      J. Biol. Chem. 275:2763-2770(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "Identification of a novel testicular orphan receptor-4 (TR4)-associated protein as repressor for the selective suppression of TR4-mediated transactivation."
      Yang Y., Wang X., Dong T., Kim E., Lin W.-J., Chang C.
      J. Biol. Chem. 278:7709-7717(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR2C2AP.
    12. "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.
    13. "Oxidative stress stimulates testicular orphan receptor 4 through forkhead transcription factor forkhead box O3a."
      Li G., Lee Y.F., Liu S., Cai Y., Xie S., Liu N.C., Bao B.Y., Chen Z., Chang C.
      Endocrinology 149:3490-3499(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-46; SER-68; SER-98 AND SER-219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: INTERACTION WITH NLRP10.

    Entry informationi

    Entry nameiNR2C2_HUMAN
    AccessioniPrimary (citable) accession number: P49116
    Secondary accession number(s): A8K3H5, B6ZGT8, P55092
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 140 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 3
      Human chromosome 3: 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