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P10827

- THA_HUMAN

UniProt

P10827 - THA_HUMAN

Protein

Thyroid hormone receptor alpha

Gene

THRA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 184 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei228 – 2281Thyroid hormone
    Binding sitei277 – 2771Thyroid hormone; via amide nitrogen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi53 – 12775Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri53 – 7321NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri91 – 11525NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin DNA binding Source: Ensembl
    2. protein binding Source: UniProtKB
    3. protein domain specific binding Source: UniProtKB
    4. sequence-specific DNA binding Source: InterPro
    5. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    6. steroid hormone receptor activity Source: InterPro
    7. steroid receptor RNA activator RNA binding Source: Ensembl
    8. TBP-class protein binding Source: UniProtKB
    9. thyroid hormone binding Source: UniProtKB
    10. thyroid hormone receptor activity Source: UniProtKB
    11. transcription factor binding Source: UniProtKB
    12. transcription regulatory region DNA binding Source: BHF-UCL
    13. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cartilage condensation Source: Ensembl
    2. cytoplasmic sequestering of transcription factor Source: Ensembl
    3. erythrocyte differentiation Source: Ensembl
    4. female courtship behavior Source: Ensembl
    5. gene expression Source: Reactome
    6. hormone-mediated signaling pathway Source: BHF-UCL
    7. learning or memory Source: Ensembl
    8. negative regulation of DNA-templated transcription, initiation Source: UniProtKB
    9. negative regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: UniProtKB
    10. negative regulation of transcription, DNA-templated Source: UniProtKB
    11. ossification Source: Ensembl
    12. positive regulation of female receptivity Source: Ensembl
    13. positive regulation of myotube differentiation Source: Ensembl
    14. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    15. regulation of heart contraction Source: Ensembl
    16. regulation of lipid catabolic process Source: Ensembl
    17. regulation of myeloid cell apoptotic process Source: Ensembl
    18. regulation of thyroid hormone mediated signaling pathway Source: Ensembl
    19. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    20. response to cold Source: Ensembl
    21. thyroid gland development Source: Ensembl
    22. transcription from RNA polymerase II promoter Source: UniProtKB
    23. transcription initiation from RNA polymerase II promoter Source: Reactome
    24. Type I pneumocyte differentiation Source: Ensembl

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
    SignaLinkiP10827.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thyroid hormone receptor alpha
    Alternative name(s):
    Nuclear receptor subfamily 1 group A member 1
    V-erbA-related protein 7
    Short name:
    EAR-7
    c-erbA-1
    c-erbA-alpha
    Gene namesi
    Name:THRA
    Synonyms:EAR7, ERBA1, NR1A1, THRA1, THRA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:11796. THRA.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Hypothyroidism, congenital, non-goitrous, 6 (CHNG6) [MIM:614450]: A disease characterized by growth retardation, developmental retardation, skeletal dysplasia, borderline low thyroxine levels and high triiodothyronine levels. There is differential sensitivity to thyroid hormone action, with retention of hormone responsiveness in the hypothalamic pituitary axis and liver but skeletal, gastrointestinal, and myocardial resistance.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi277 – 2771S → N: No effect on thyroid hormone binding. 2 Publications

    Keywords - Diseasei

    Congenital hypothyroidism

    Organism-specific databases

    MIMi614450. phenotype.
    Orphaneti97927. Peripheral resistance to thyroid hormones.
    PharmGKBiPA36507.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 490490Thyroid hormone receptor alphaPRO_0000053424Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki190 – 190Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    PaxDbiP10827.
    PRIDEiP10827.

    PTM databases

    PhosphoSiteiP10827.

    Expressioni

    Gene expression databases

    ArrayExpressiP10827.
    BgeeiP10827.
    CleanExiHS_THRA.
    GenevestigatoriP10827.

    Organism-specific databases

    HPAiCAB023349.
    HPA009654.

    Interactioni

    Subunit structurei

    Binds DNA as a dimer; homodimer and heterodimer with RXRB. Interacts with NCOA3 and NCOA6 coactivators, leading to a strong increase of transcription of target genes. Probably interacts with SFPQ. Interacts with C1D. Interacts with AKAP13. Interacts with TP53INP2. Interacts with PER2.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MED1Q156485EBI-286285,EBI-394459
    Ncoa6Q9JLI42EBI-286285,EBI-286271From a different organism.

    Protein-protein interaction databases

    BioGridi112923. 70 interactions.
    IntActiP10827. 14 interactions.
    MINTiMINT-267914.
    STRINGi9606.ENSP00000264637.

    Structurei

    Secondary structure

    1
    490
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi148 – 1514
    Turni152 – 1543
    Helixi162 – 17615
    Turni180 – 1845
    Turni186 – 1883
    Beta strandi189 – 1913
    Beta strandi196 – 1983
    Helixi212 – 23423
    Helixi237 – 2404
    Helixi244 – 26421
    Turni269 – 2724
    Beta strandi273 – 2764
    Turni277 – 2793
    Beta strandi280 – 2823
    Helixi284 – 2896
    Turni290 – 2934
    Helixi294 – 30613
    Helixi307 – 3093
    Helixi313 – 32412
    Beta strandi329 – 3313
    Helixi335 – 35622
    Helixi363 – 3708

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NAVX-ray2.50A148-370[»]
    2H77X-ray2.33A148-370[»]
    2H79X-ray1.87A148-370[»]
    3HZFX-ray2.50A148-370[»]
    3ILZX-ray1.85A148-370[»]
    3JZBX-ray2.01A148-370[»]
    4LNWX-ray1.90A148-370[»]
    4LNXX-ray2.05A148-370[»]
    ProteinModelPortaliP10827.
    SMRiP10827. Positions 50-378.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10827.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 5252ModulatingAdd
    BLAST
    Regioni190 – 370181Ligand-bindingAdd
    BLAST

    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 fingeri53 – 7321NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri91 – 11525NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG272726.
    HOGENOMiHOG000010313.
    HOVERGENiHBG005606.
    InParanoidiP10827.
    KOiK05547.
    OMAiWLNGPKR.
    PhylomeDBiP10827.
    TreeFamiTF328382.

    Family and domain databases

    Gene3Di1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR001723. Str_hrmn_rcpt.
    IPR001728. ThyrH_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.
    PR00546. THYROIDHORMR.
    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]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform Alpha-2 (identifier: P10827-1) [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

    MEQKPSKVEC GSDPEENSAR SPDGKRKRKN GQCSLKTSMS GYIPSYLDKD    50
    EQCVVCGDKA TGYHYRCITC EGCKGFFRRT IQKNLHPTYS CKYDSCCVID 100
    KITRNQCQLC RFKKCIAVGM AMDLVLDDSK RVAKRKLIEQ NRERRRKEEM 150
    IRSLQQRPEP TPEEWDLIHI ATEAHRSTNA QGSHWKQRRK FLPDDIGQSP 200
    IVSMPDGDKV DLEAFSEFTK IITPAITRVV DFAKKLPMFS ELPCEDQIIL 250
    LKGCCMEIMS LRAAVRYDPE SDTLTLSGEM AVKREQLKNG GLGVVSDAIF 300
    ELGKSLSAFN LDDTEVALLQ AVLLMSTDRS GLLCVDKIEK SQEAYLLAFE 350
    HYVNHRKHNI PHFWPKLLMK EREVQSSILY KGAAAEGRPG GSLGVHPEGQ 400
    QLLGMHVVQG PQVRQLEQQL GEAGSLQGPV LQHQSPKSPQ QRLLELLHRS 450
    GILHARAVCG EDDSSEADSP SSSEEEPEVC EDLAGNAASP 490
    Length:490
    Mass (Da):54,816
    Last modified:July 1, 1989 - v1
    Checksum:iC87C7D2F67B1AE49
    GO
    Isoform Alpha-1 (identifier: P10827-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         371-490: EREVQSSILY...EDLAGNAASP → VTDLRMIGAC...FLEVFEDQEV

    Show »
    Length:410
    Mass (Da):46,813
    Checksum:iB9FD7BFAC16D6882
    GO
    Isoform Alpha-3 (identifier: P10827-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         371-409: Missing.

    Show »
    Length:451
    Mass (Da):50,747
    Checksum:i1495A3F2EE6601DD
    GO
    Isoform Alpha-4 (identifier: P10827-4) [UniParc]FASTAAdd to Basket

    Also known as: Alpha3

    The sequence of this isoform differs from the canonical sequence as follows:
         371-412: Missing.

    Show »
    Length:448
    Mass (Da):50,465
    Checksum:i15FD778790B4D26B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371T → S in CAA68539. (PubMed:3684612)Curated
    Sequence conflicti119 – 1191G → A in CAA68539. (PubMed:3684612)Curated
    Sequence conflicti285 – 2851E → A in CAB57886. (PubMed:1850510)Curated
    Sequence conflicti285 – 2851E → A in CAA38899. (PubMed:1850510)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei371 – 490120EREVQ…NAASP → VTDLRMIGACHASRFLHMKV ECPTELFPPLFLEVFEDQEV in isoform Alpha-1. 2 PublicationsVSP_003621Add
    BLAST
    Alternative sequencei371 – 41242Missing in isoform Alpha-4. 1 PublicationVSP_003623Add
    BLAST
    Alternative sequencei371 – 40939Missing in isoform Alpha-3. 1 PublicationVSP_003622Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55074
    , X55073, X55070, X55071, X55004, X55069, X55068, X55066 Genomic DNA. Translation: CAB57886.1.
    X55005 mRNA. Translation: CAA38749.1.
    X55074
    , X55073, X55070, X55071, X55004, X55069, X55068 Genomic DNA. Translation: CAA38899.1.
    M24899 mRNA. Translation: AAA35783.1.
    M24900 mRNA. Translation: AAA52333.1.
    J03239 mRNA. Translation: AAA61176.1.
    Y00479 mRNA. Translation: CAA68539.1.
    M24748 Genomic DNA. Translation: AAA66021.1.
    AK290530 mRNA. Translation: BAF83219.1.
    CH471152 Genomic DNA. Translation: EAW60632.1.
    BC000261 mRNA. Translation: AAH00261.1.
    BC002728 mRNA. Translation: AAH02728.1.
    BC035137 mRNA. Translation: AAH35137.1.
    AF522368 mRNA. Translation: AAM77692.1.
    CCDSiCCDS11360.1. [P10827-1]
    CCDS42316.1. [P10827-2]
    CCDS58546.1. [P10827-3]
    PIRiA30893.
    A40917.
    S06163.
    RefSeqiNP_001177847.1. NM_001190918.1. [P10827-3]
    NP_001177848.1. NM_001190919.1. [P10827-1]
    NP_003241.2. NM_003250.5. [P10827-1]
    NP_955366.1. NM_199334.3. [P10827-2]
    UniGeneiHs.724.

    Genome annotation databases

    EnsembliENST00000264637; ENSP00000264637; ENSG00000126351. [P10827-1]
    ENST00000394121; ENSP00000377679; ENSG00000126351. [P10827-1]
    ENST00000450525; ENSP00000395641; ENSG00000126351. [P10827-2]
    ENST00000546243; ENSP00000443972; ENSG00000126351. [P10827-2]
    ENST00000584985; ENSP00000463466; ENSG00000126351. [P10827-3]
    GeneIDi7067.
    KEGGihsa:7067.
    UCSCiuc002htw.3. human. [P10827-1]
    uc002htx.3. human. [P10827-3]

    Polymorphism databases

    DMDMi135705.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55074
    , X55073 , X55070 , X55071 , X55004 , X55069 , X55068 , X55066 Genomic DNA. Translation: CAB57886.1 .
    X55005 mRNA. Translation: CAA38749.1 .
    X55074
    , X55073 , X55070 , X55071 , X55004 , X55069 , X55068 Genomic DNA. Translation: CAA38899.1 .
    M24899 mRNA. Translation: AAA35783.1 .
    M24900 mRNA. Translation: AAA52333.1 .
    J03239 mRNA. Translation: AAA61176.1 .
    Y00479 mRNA. Translation: CAA68539.1 .
    M24748 Genomic DNA. Translation: AAA66021.1 .
    AK290530 mRNA. Translation: BAF83219.1 .
    CH471152 Genomic DNA. Translation: EAW60632.1 .
    BC000261 mRNA. Translation: AAH00261.1 .
    BC002728 mRNA. Translation: AAH02728.1 .
    BC035137 mRNA. Translation: AAH35137.1 .
    AF522368 mRNA. Translation: AAM77692.1 .
    CCDSi CCDS11360.1. [P10827-1 ]
    CCDS42316.1. [P10827-2 ]
    CCDS58546.1. [P10827-3 ]
    PIRi A30893.
    A40917.
    S06163.
    RefSeqi NP_001177847.1. NM_001190918.1. [P10827-3 ]
    NP_001177848.1. NM_001190919.1. [P10827-1 ]
    NP_003241.2. NM_003250.5. [P10827-1 ]
    NP_955366.1. NM_199334.3. [P10827-2 ]
    UniGenei Hs.724.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NAV X-ray 2.50 A 148-370 [» ]
    2H77 X-ray 2.33 A 148-370 [» ]
    2H79 X-ray 1.87 A 148-370 [» ]
    3HZF X-ray 2.50 A 148-370 [» ]
    3ILZ X-ray 1.85 A 148-370 [» ]
    3JZB X-ray 2.01 A 148-370 [» ]
    4LNW X-ray 1.90 A 148-370 [» ]
    4LNX X-ray 2.05 A 148-370 [» ]
    ProteinModelPortali P10827.
    SMRi P10827. Positions 50-378.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112923. 70 interactions.
    IntActi P10827. 14 interactions.
    MINTi MINT-267914.
    STRINGi 9606.ENSP00000264637.

    Chemistry

    BindingDBi P10827.
    ChEMBLi CHEMBL2111462.
    DrugBanki DB00451. Levothyroxine.
    DB00279. Liothyronine.
    GuidetoPHARMACOLOGYi 588.

    PTM databases

    PhosphoSitei P10827.

    Polymorphism databases

    DMDMi 135705.

    Proteomic databases

    PaxDbi P10827.
    PRIDEi P10827.

    Protocols and materials databases

    DNASUi 7067.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264637 ; ENSP00000264637 ; ENSG00000126351 . [P10827-1 ]
    ENST00000394121 ; ENSP00000377679 ; ENSG00000126351 . [P10827-1 ]
    ENST00000450525 ; ENSP00000395641 ; ENSG00000126351 . [P10827-2 ]
    ENST00000546243 ; ENSP00000443972 ; ENSG00000126351 . [P10827-2 ]
    ENST00000584985 ; ENSP00000463466 ; ENSG00000126351 . [P10827-3 ]
    GeneIDi 7067.
    KEGGi hsa:7067.
    UCSCi uc002htw.3. human. [P10827-1 ]
    uc002htx.3. human. [P10827-3 ]

    Organism-specific databases

    CTDi 7067.
    GeneCardsi GC17P038219.
    HGNCi HGNC:11796. THRA.
    HPAi CAB023349.
    HPA009654.
    MIMi 190120. gene.
    614450. phenotype.
    neXtProti NX_P10827.
    Orphaneti 97927. Peripheral resistance to thyroid hormones.
    PharmGKBi PA36507.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG272726.
    HOGENOMi HOG000010313.
    HOVERGENi HBG005606.
    InParanoidi P10827.
    KOi K05547.
    OMAi WLNGPKR.
    PhylomeDBi P10827.
    TreeFami TF328382.

    Enzyme and pathway databases

    Reactomei REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinki P10827.

    Miscellaneous databases

    ChiTaRSi THRA. human.
    EvolutionaryTracei P10827.
    GeneWikii Thyroid_hormone_receptor_alpha.
    GenomeRNAii 7067.
    NextBioi 27631.
    PROi P10827.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10827.
    Bgeei P10827.
    CleanExi HS_THRA.
    Genevestigatori P10827.

    Family and domain databases

    Gene3Di 1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR001723. Str_hrmn_rcpt.
    IPR001728. ThyrH_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.
    PR00546. THYROIDHORMR.
    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. "Genomic organization of the human thyroid hormone receptor alpha (c-erbA-1) gene."
      Laudet V., Begue A., Henry C., Joubel A., Martin P., Stehelin D., Saule S.
      Nucleic Acids Res. 19:1105-1112(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
    2. "Two erbA homologs encoding proteins with different T3 binding capacities are transcribed from opposite DNA strands of the same genetic locus."
      Miyajima N., Horiuchi R., Shibuya Y., Fukushige S., Matsubara K., Toyoshima K., Yamamoto T.
      Cell 57:31-39(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
    3. "Characterization of a thyroid hormone receptor expressed in human kidney and other tissues."
      Nakai A., Seino S., Sakurai A., Szilak I., Bell G.I., Degroot L.J.
      Proc. Natl. Acad. Sci. U.S.A. 85:2781-2785(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2).
      Tissue: Kidney.
    4. "Nucleotide sequence of cDNA encoding a novel human thyroid hormone receptor."
      Pfahl M., Benbrook D.
      Nucleic Acids Res. 15:9613-9613(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2).
      Tissue: Testis.
    5. "Characterization of a third human thyroid hormone receptor coexpressed with other thyroid hormone receptors in several tissues."
      Nakai A., Sakurai A., Bell G.I., Degroot L.J.
      Mol. Endocrinol. 2:1087-1092(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-1).
    6. "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 ALPHA-2).
      Tissue: Brain.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS ALPHA-2 AND ALPHA-3).
      Tissue: Brain, Hippocampus and Muscle.
    9. "A novel thyroid hormone receptor encoded by a cDNA clone from a human testis library."
      Benbrook D., Pfahl M.
      Science 238:788-791(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-370.
    10. Liu C., Li L., Liu B., Zang X.
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 280-451 (ISOFORM ALPHA-4).
      Tissue: Brain cortex.
    11. "Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300."
      Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L., Privalsky M.L., Nakatani Y., Evans R.M.
      Cell 90:569-580(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA3.
    12. "Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action."
      Rubino D., Driggers P., Arbit D., Kemp L., Miller B., Coso O., Pagliai K., Gray K., Gutkind S., Segars J.
      Oncogene 16:2513-2526(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AKAP13.
    13. "A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo."
      Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.
      J. Biol. Chem. 274:34283-34293(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA6.
    14. Cited for: FUNCTION, MUTAGENESIS OF SER-277.
    15. Cited for: INTERACTION WITH TP53INP2.
    16. "Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells."
      Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.
      Proteomics 8:2885-2896(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-190.
      Tissue: Cervix carcinoma.
    17. Cited for: INVOLVEMENT IN CHNG6.
    18. Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 148-370 IN COMPLEX WITH SYNTHETIC AGONIST, FUNCTION.
    19. Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 148-370 IN COMPLEX WITH TRIIODOTHYRONINE, SUBUNIT.
    20. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 148-370 IN COMPLEX WITH SYNTHETIC AGONIST, FUNCTION.
    21. Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 148-370 IN COMPLEX WITH SYNTHETIC AGONIST, FUNCTION, MUTAGENESIS OF SER-277.

    Entry informationi

    Entry nameiTHA_HUMAN
    AccessioniPrimary (citable) accession number: P10827
    Secondary accession number(s): A8K3B5
    , P21205, Q8N6A1, Q96H73
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 184 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3