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P10828

- THB_HUMAN

UniProt

P10828 - THB_HUMAN

Protein

Thyroid hormone receptor beta

Gene

THRB

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 2 (01 Oct 1994)
      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.7 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei282 – 2821Thyroid hormone
    Binding sitei320 – 3201Thyroid hormone
    Binding sitei331 – 3311Thyroid hormone; via amide nitrogen
    Binding sitei435 – 4351Thyroid hormone

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi107 – 18175Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri107 – 12721NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri145 – 16925NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin DNA binding Source: Ensembl
    2. DNA binding Source: ProtInc
    3. enzyme binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. sequence-specific DNA binding Source: InterPro
    6. sequence-specific DNA binding transcription factor activity Source: ProtInc
    7. steroid hormone receptor activity Source: InterPro
    8. thyroid hormone binding Source: UniProtKB
    9. thyroid hormone receptor activity Source: UniProtKB
    10. transcription corepressor activity Source: ProtInc
    11. zinc ion binding Source: InterPro

    GO - Biological processi

    1. female courtship behavior Source: Ensembl
    2. gene expression Source: Reactome
    3. intracellular receptor signaling pathway Source: GOC
    4. negative regulation of female receptivity Source: Ensembl
    5. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. organ morphogenesis Source: Ensembl
    7. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    8. regulation of heart contraction Source: Ensembl
    9. sensory perception of sound Source: Ensembl
    10. transcription, DNA-templated Source: ProtInc
    11. transcription initiation from RNA polymerase II promoter Source: Reactome
    12. 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.
    SignaLinkiP10828.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thyroid hormone receptor beta
    Alternative name(s):
    Nuclear receptor subfamily 1 group A member 2
    c-erbA-2
    c-erbA-beta
    Gene namesi
    Name:THRB
    Synonyms:ERBA2, NR1A2, THR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:11799. THRB.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. nucleoplasm Source: Reactome
    3. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Generalized thyroid hormone resistance (GTHR) [MIM:188570]: A disease characterized by goiter, abnormal mental functions, increased susceptibility to infections, abnormal growth and bone maturation, tachycardia and deafness. Affected individuals may also have attention deficit-hyperactivity disorders (ADHD) and language difficulties. GTHR patients also have high levels of circulating thyroid hormones (T3-T4), with normal or slightly elevated thyroid stimulating hormone (TSH).18 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti234 – 2341A → T in GTHR; impairs hormone binding and ligand-dependent conformational changes. 1 Publication
    VAR_004632
    Natural varianti243 – 2431R → W in GTHR. 1 Publication
    VAR_004633
    Natural varianti268 – 2681A → G in GTHR. 1 Publication
    VAR_059041
    Natural varianti317 – 3171A → T in GTHR; impairs hormone binding. 3 Publications
    VAR_004635
    Natural varianti320 – 3201R → C in GTHR. 1 Publication
    VAR_004636
    Natural varianti320 – 3201R → H in GTHR. 2 Publications
    VAR_004637
    Natural varianti331 – 3311N → D in GTHR. 1 Publication
    VAR_059042
    Natural varianti332 – 3321G → R in GTHR. 1 Publication
    Corresponds to variant rs28999969 [ dbSNP | Ensembl ].
    VAR_004638
    Natural varianti335 – 3351A → P in GTHR. 1 Publication
    VAR_059043
    Natural varianti337 – 3371Missing in GTHR. 1 Publication
    VAR_004639
    Natural varianti338 – 3381R → W in GTHR. 3 Publications
    VAR_004640
    Natural varianti340 – 3401Q → H in GTHR. 1 Publication
    VAR_004641
    Natural varianti341 – 3411L → P in GTHR. 1 Publication
    VAR_059044
    Natural varianti342 – 3421K → I in GTHR. 1 Publication
    VAR_004642
    Natural varianti345 – 3451G → R in GTHR. 1 Publication
    VAR_004645
    Natural varianti345 – 3451G → S in GTHR. 1 Publication
    VAR_004644
    Natural varianti345 – 3451G → V in GTHR. 1 Publication
    Corresponds to variant rs28999970 [ dbSNP | Ensembl ].
    VAR_004643
    Natural varianti346 – 3461L → F in GTHR. 1 Publication
    VAR_059045
    Natural varianti347 – 3471G → E in GTHR. 1 Publication
    Corresponds to variant rs28999971 [ dbSNP | Ensembl ].
    VAR_004646
    Natural varianti348 – 3481V → E in GTHR. 1 Publication
    VAR_004647
    Natural varianti426 – 4261T → I in GTHR. 1 Publication
    VAR_004648
    Natural varianti431 – 4311I → M in GTHR. 1 Publication
    VAR_059046
    Natural varianti438 – 4381R → H in GTHR. 1 Publication
    VAR_004649
    Natural varianti442 – 4421M → V in GTHR. 1 Publication
    VAR_004650
    Natural varianti443 – 4431K → E in GTHR. 1 Publication
    VAR_004651
    Natural varianti446 – 4461C → R in GTHR. 1 Publication
    VAR_004652
    Natural varianti447 – 4471P → T in GTHR. 1 Publication
    VAR_059047
    Natural varianti453 – 4531P → H in GTHR. 1 Publication
    VAR_004653
    Natural varianti453 – 4531P → L in GTHR. 1 Publication
    VAR_059048
    Natural varianti453 – 4531P → S in GTHR. 1 Publication
    VAR_004654
    Natural varianti453 – 4531P → T in GTHR. 4 Publications
    Corresponds to variant rs28933408 [ dbSNP | Ensembl ].
    VAR_004655
    Natural varianti459 – 4591F → C in GTHR. 1 Publication
    VAR_059049
    Generalized thyroid hormone resistance autosomal recessive (GTHRAR) [MIM:274300]: An autosomal recessive disorder characterized by goiter, clinical euthyroidism, end-organ unresponsiveness to thyroid hormone, abnormal growth and bone maturation, and deafness. Patients also have high levels of circulating thyroid hormones, with elevated thyroid stimulating hormone.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Selective pituitary thyroid hormone resistance (PRTH) [MIM:145650]: Variant form of thyroid hormone resistance and is characterized by clinical hyperthyroidism, with elevated free thyroid hormones, but inappropriately normal serum TSH. Unlike GRTH, where the syndrome usually segregates with a dominant allele, the mode of inheritance in PRTH has not been established.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti316 – 3161R → H in PRTH; impairs hormone binding. 1 Publication
    VAR_004634
    Natural varianti429 – 4291R → Q in PRTH. 1 Publication
    VAR_058508

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi207 – 2082SI → AA: Modestly inhibits homodimer formation on a minimal response element (in vitro). 1 Publication
    Mutagenesisi207 – 2082SI → KK: Inhibits homodimer formation on a minimal response element (in vitro). 1 Publication
    Mutagenesisi243 – 2431R → Q: Impairs hormone binding and ligand-dependent conformational changes. 2 Publications
    Mutagenesisi331 – 3311N → S: No effect on thyroid hormone binding. 3 Publications
    Mutagenesisi355 – 3551D → R: Stabilizes homodimer. 2 Publications

    Keywords - Diseasei

    Deafness, Disease mutation

    Organism-specific databases

    MIMi145650. phenotype.
    188570. phenotype.
    274300. phenotype.
    Orphaneti3221. Generalized resistance to thyroid hormone.
    97927. Peripheral resistance to thyroid hormones.
    165994. Selective pituitary resistance to thyroid hormone.
    PharmGKBiPA36508.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Thyroid hormone receptor betaPRO_0000053446Add
    BLAST

    Proteomic databases

    PaxDbiP10828.
    PRIDEiP10828.

    PTM databases

    PhosphoSiteiP10828.

    Expressioni

    Gene expression databases

    ArrayExpressiP10828.
    BgeeiP10828.
    CleanExiHS_THRB.
    GenevestigatoriP10828.

    Organism-specific databases

    HPAiCAB002008.
    CAB002009.

    Interactioni

    Subunit structurei

    Binds DNA as a dimer; homodimer and heterodimer with RXRA. Interacts with the coactivators NCOA1/SRC1, NCOA2/GRIP1, NCOA7 and MED1/TRAP220 in a ligand-inducible manner. Interacts with the corepressor NCOR1 in absence of ligand. Interacts with C1D By similarity. Interacts with NR2F6; the interaction impairs the binding of the THRB homodimer and THRB:RXRB heterodimer to T3 response elements. Interacts with PRMT2 and THRSP.By similarity11 Publications

    Protein-protein interaction databases

    BioGridi112924. 49 interactions.
    DIPiDIP-5991N.
    IntActiP10828. 10 interactions.
    MINTiMINT-1508903.
    STRINGi9606.ENSP00000348827.

    Structurei

    Secondary structure

    1
    461
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni108 – 1103
    Beta strandi116 – 1183
    Helixi125 – 13612
    Helixi140 – 1423
    Turni155 – 1595
    Helixi162 – 17110
    Helixi176 – 1783
    Helixi182 – 19514
    Helixi198 – 2047
    Helixi205 – 2084
    Helixi216 – 23015
    Turni234 – 2374
    Helixi239 – 2424
    Turni248 – 2514
    Beta strandi260 – 2634
    Helixi266 – 2738
    Helixi276 – 28813
    Helixi293 – 2953
    Helixi298 – 31922
    Turni323 – 3264
    Beta strandi327 – 3304
    Turni331 – 3333
    Beta strandi334 – 3363
    Helixi338 – 3436
    Turni344 – 3485
    Helixi349 – 36012
    Helixi361 – 3633
    Helixi367 – 37812
    Helixi389 – 41022
    Beta strandi413 – 4164
    Helixi417 – 44529
    Helixi448 – 4503
    Helixi453 – 4597

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BSXX-ray3.70A/B202-461[»]
    1N46X-ray2.20A/B204-461[»]
    1NAXX-ray2.70A209-460[»]
    1NQ0X-ray2.40A202-461[»]
    1NQ1X-ray2.90A202-461[»]
    1NQ2X-ray2.40A202-461[»]
    1NUOX-ray3.10A202-461[»]
    1Q4XX-ray2.80A209-461[»]
    1R6GX-ray3.00A203-461[»]
    1XZXX-ray2.50X202-461[»]
    1Y0XX-ray3.10X202-461[»]
    2J4AX-ray2.20A209-461[»]
    2NLLX-ray1.90B104-204[»]
    2PINX-ray2.30A/B209-461[»]
    3D57X-ray2.20A/B209-460[»]
    3GWSX-ray2.20X202-460[»]
    3IMYX-ray2.55A202-461[»]
    3JZCX-ray2.50A202-461[»]
    ProteinModelPortaliP10828.
    SMRiP10828. Positions 94-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10828.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 106106ModulatingAdd
    BLAST
    Regioni244 – 461218Interaction with NR2F6Add
    BLAST
    Regioni244 – 461218Ligand-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 fingeri107 – 12721NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri145 – 16925NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG272726.
    HOGENOMiHOG000010313.
    HOVERGENiHBG005606.
    KOiK08362.
    OMAiLYEVHPA.
    OrthoDBiEOG7TBC2V.
    PhylomeDBiP10828.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Beta-1 (identifier: P10828-1) [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

    MTPNSMTENG LTAWDKPKHC PDREHDWKLV GMSEACLHRK SHSERRSTLK    50
    NEQSSPHLIQ TTWTSSIFHL DHDDVNDQSV SSAQTFQTEE KKCKGYIPSY 100
    LDKDELCVVC GDKATGYHYR CITCEGCKGF FRRTIQKNLH PSYSCKYEGK 150
    CVIDKVTRNQ CQECRFKKCI YVGMATDLVL DDSKRLAKRK LIEENREKRR 200
    REELQKSIGH KPEPTDEEWE LIKTVTEAHV ATNAQGSHWK QKRKFLPEDI 250
    GQAPIVNAPE GGKVDLEAFS HFTKIITPAI TRVVDFAKKL PMFCELPCED 300
    QIILLKGCCM EIMSLRAAVR YDPESETLTL NGEMAVTRGQ LKNGGLGVVS 350
    DAIFDLGMSL SSFNLDDTEV ALLQAVLLMS SDRPGLACVE RIEKYQDSFL 400
    LAFEHYINYR KHHVTHFWPK LLMKVTDLRM IGACHASRFL HMKVECPTEL 450
    FPPLFLEVFE D 461
    Length:461
    Mass (Da):52,788
    Last modified:October 1, 1994 - v2
    Checksum:i6770BB0D372A7CAA
    GO
    Isoform Beta-2 (identifier: P10828-2) [UniParc] [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-93: MTPNSMTENG...QTFQTEEKKC → MNYCMQEIYE...QVQSPSYSQK

    Show »
    Length:476
    Mass (Da):54,449
    Checksum:i21755292507335D8
    GO

    Sequence cautioni

    The sequence AAA35677.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA28412.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti243 – 2431R → P in AAA35677. (PubMed:3034496)Curated
    Sequence conflicti243 – 2431R → P in CAA28412. (PubMed:2879243)Curated
    Sequence conflicti451 – 4511F → L in AAA35677. (PubMed:3034496)Curated
    Sequence conflicti451 – 4511F → L in CAA28412. (PubMed:2879243)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti216 – 2161D → G.
    Corresponds to variant rs9865746 [ dbSNP | Ensembl ].
    VAR_050577
    Natural varianti234 – 2341A → T in GTHR; impairs hormone binding and ligand-dependent conformational changes. 1 Publication
    VAR_004632
    Natural varianti243 – 2431R → W in GTHR. 1 Publication
    VAR_004633
    Natural varianti268 – 2681A → G in GTHR. 1 Publication
    VAR_059041
    Natural varianti316 – 3161R → H in PRTH; impairs hormone binding. 1 Publication
    VAR_004634
    Natural varianti317 – 3171A → T in GTHR; impairs hormone binding. 3 Publications
    VAR_004635
    Natural varianti320 – 3201R → C in GTHR. 1 Publication
    VAR_004636
    Natural varianti320 – 3201R → H in GTHR. 2 Publications
    VAR_004637
    Natural varianti331 – 3311N → D in GTHR. 1 Publication
    VAR_059042
    Natural varianti332 – 3321G → R in GTHR. 1 Publication
    Corresponds to variant rs28999969 [ dbSNP | Ensembl ].
    VAR_004638
    Natural varianti335 – 3351A → P in GTHR. 1 Publication
    VAR_059043
    Natural varianti337 – 3371T → I.2 Publications
    Corresponds to variant rs1054624 [ dbSNP | Ensembl ].
    VAR_011784
    Natural varianti337 – 3371Missing in GTHR. 1 Publication
    VAR_004639
    Natural varianti338 – 3381R → W in GTHR. 3 Publications
    VAR_004640
    Natural varianti340 – 3401Q → H in GTHR. 1 Publication
    VAR_004641
    Natural varianti341 – 3411L → P in GTHR. 1 Publication
    VAR_059044
    Natural varianti342 – 3421K → I in GTHR. 1 Publication
    VAR_004642
    Natural varianti345 – 3451G → R in GTHR. 1 Publication
    VAR_004645
    Natural varianti345 – 3451G → S in GTHR. 1 Publication
    VAR_004644
    Natural varianti345 – 3451G → V in GTHR. 1 Publication
    Corresponds to variant rs28999970 [ dbSNP | Ensembl ].
    VAR_004643
    Natural varianti346 – 3461L → F in GTHR. 1 Publication
    VAR_059045
    Natural varianti347 – 3471G → E in GTHR. 1 Publication
    Corresponds to variant rs28999971 [ dbSNP | Ensembl ].
    VAR_004646
    Natural varianti348 – 3481V → E in GTHR. 1 Publication
    VAR_004647
    Natural varianti426 – 4261T → I in GTHR. 1 Publication
    VAR_004648
    Natural varianti429 – 4291R → Q in PRTH. 1 Publication
    VAR_058508
    Natural varianti431 – 4311I → M in GTHR. 1 Publication
    VAR_059046
    Natural varianti438 – 4381R → H in GTHR. 1 Publication
    VAR_004649
    Natural varianti442 – 4421M → V in GTHR. 1 Publication
    VAR_004650
    Natural varianti443 – 4431K → E in GTHR. 1 Publication
    VAR_004651
    Natural varianti446 – 4461C → R in GTHR. 1 Publication
    VAR_004652
    Natural varianti447 – 4471P → T in GTHR. 1 Publication
    VAR_059047
    Natural varianti453 – 4531P → H in GTHR. 1 Publication
    VAR_004653
    Natural varianti453 – 4531P → L in GTHR. 1 Publication
    VAR_059048
    Natural varianti453 – 4531P → S in GTHR. 1 Publication
    VAR_004654
    Natural varianti453 – 4531P → T in GTHR. 4 Publications
    Corresponds to variant rs28933408 [ dbSNP | Ensembl ].
    VAR_004655
    Natural varianti459 – 4591F → C in GTHR. 1 Publication
    VAR_059049

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9393MTPNS…EEKKC → MNYCMQEIYEVHPAAGSNCY MQSTDYYAYFEDSPGYSGCD AQAVPSNNIYMEQAWAVNQP YTCSYPGNMFKSKDSDLDMA LNQYSQPEYFTEEKPTFSQV QSPSYSQK in isoform Beta-2. 1 PublicationVSP_031077Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26747 mRNA. Translation: AAA35677.1. Different initiation.
    X04707 mRNA. Translation: CAA28412.1. Different initiation.
    AK096628 mRNA. Translation: BAG53341.1.
    AC012087 Genomic DNA. No translation available.
    AC093927 Genomic DNA. No translation available.
    AC098971 Genomic DNA. No translation available.
    AC099054 Genomic DNA. No translation available.
    AC112217 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64345.1.
    BC106929 mRNA. Translation: AAI06930.1.
    BC106930 mRNA. Translation: AAI06931.1.
    AY286465 mRNA. Translation: AAQ23704.1.
    AY286466 mRNA. Translation: AAQ23705.1.
    AY286467 mRNA. Translation: AAQ23706.1.
    AY286468 mRNA. Translation: AAQ23707.1.
    AY286469 mRNA. Translation: AAQ23708.1.
    AY286470 mRNA. Translation: AAQ23709.1.
    AY286471 mRNA. Translation: AAQ23710.1.
    X74497 mRNA. Translation: CAA52606.1.
    CCDSiCCDS2641.1. [P10828-1]
    PIRiA25237. TVHUAR.
    S40152.
    RefSeqiNP_000452.2. NM_000461.4. [P10828-1]
    NP_001121648.1. NM_001128176.2. [P10828-1]
    NP_001121649.1. NM_001128177.1. [P10828-1]
    NP_001239563.1. NM_001252634.1. [P10828-1]
    XP_005265477.1. XM_005265420.2. [P10828-2]
    XP_005265478.1. XM_005265421.2. [P10828-1]
    XP_005265480.1. XM_005265423.2. [P10828-1]
    XP_005265481.1. XM_005265424.2. [P10828-1]
    XP_005265482.1. XM_005265425.2. [P10828-1]
    XP_006713380.1. XM_006713317.1. [P10828-1]
    XP_006713381.1. XM_006713318.1. [P10828-1]
    UniGeneiHs.187861.

    Genome annotation databases

    EnsembliENST00000280696; ENSP00000280696; ENSG00000151090. [P10828-2]
    ENST00000356447; ENSP00000348827; ENSG00000151090. [P10828-1]
    ENST00000396671; ENSP00000379904; ENSG00000151090. [P10828-1]
    ENST00000415021; ENSP00000404898; ENSG00000151090.
    ENST00000416420; ENSP00000414444; ENSG00000151090. [P10828-1]
    ENST00000447875; ENSP00000388467; ENSG00000151090.
    GeneIDi7068.
    KEGGihsa:7068.
    UCSCiuc003ccx.4. human. [P10828-1]

    Polymorphism databases

    DMDMi586092.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26747 mRNA. Translation: AAA35677.1 . Different initiation.
    X04707 mRNA. Translation: CAA28412.1 . Different initiation.
    AK096628 mRNA. Translation: BAG53341.1 .
    AC012087 Genomic DNA. No translation available.
    AC093927 Genomic DNA. No translation available.
    AC098971 Genomic DNA. No translation available.
    AC099054 Genomic DNA. No translation available.
    AC112217 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64345.1 .
    BC106929 mRNA. Translation: AAI06930.1 .
    BC106930 mRNA. Translation: AAI06931.1 .
    AY286465 mRNA. Translation: AAQ23704.1 .
    AY286466 mRNA. Translation: AAQ23705.1 .
    AY286467 mRNA. Translation: AAQ23706.1 .
    AY286468 mRNA. Translation: AAQ23707.1 .
    AY286469 mRNA. Translation: AAQ23708.1 .
    AY286470 mRNA. Translation: AAQ23709.1 .
    AY286471 mRNA. Translation: AAQ23710.1 .
    X74497 mRNA. Translation: CAA52606.1 .
    CCDSi CCDS2641.1. [P10828-1 ]
    PIRi A25237. TVHUAR.
    S40152.
    RefSeqi NP_000452.2. NM_000461.4. [P10828-1 ]
    NP_001121648.1. NM_001128176.2. [P10828-1 ]
    NP_001121649.1. NM_001128177.1. [P10828-1 ]
    NP_001239563.1. NM_001252634.1. [P10828-1 ]
    XP_005265477.1. XM_005265420.2. [P10828-2 ]
    XP_005265478.1. XM_005265421.2. [P10828-1 ]
    XP_005265480.1. XM_005265423.2. [P10828-1 ]
    XP_005265481.1. XM_005265424.2. [P10828-1 ]
    XP_005265482.1. XM_005265425.2. [P10828-1 ]
    XP_006713380.1. XM_006713317.1. [P10828-1 ]
    XP_006713381.1. XM_006713318.1. [P10828-1 ]
    UniGenei Hs.187861.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BSX X-ray 3.70 A/B 202-461 [» ]
    1N46 X-ray 2.20 A/B 204-461 [» ]
    1NAX X-ray 2.70 A 209-460 [» ]
    1NQ0 X-ray 2.40 A 202-461 [» ]
    1NQ1 X-ray 2.90 A 202-461 [» ]
    1NQ2 X-ray 2.40 A 202-461 [» ]
    1NUO X-ray 3.10 A 202-461 [» ]
    1Q4X X-ray 2.80 A 209-461 [» ]
    1R6G X-ray 3.00 A 203-461 [» ]
    1XZX X-ray 2.50 X 202-461 [» ]
    1Y0X X-ray 3.10 X 202-461 [» ]
    2J4A X-ray 2.20 A 209-461 [» ]
    2NLL X-ray 1.90 B 104-204 [» ]
    2PIN X-ray 2.30 A/B 209-461 [» ]
    3D57 X-ray 2.20 A/B 209-460 [» ]
    3GWS X-ray 2.20 X 202-460 [» ]
    3IMY X-ray 2.55 A 202-461 [» ]
    3JZC X-ray 2.50 A 202-461 [» ]
    ProteinModelPortali P10828.
    SMRi P10828. Positions 94-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112924. 49 interactions.
    DIPi DIP-5991N.
    IntActi P10828. 10 interactions.
    MINTi MINT-1508903.
    STRINGi 9606.ENSP00000348827.

    Chemistry

    BindingDBi P10828.
    ChEMBLi CHEMBL1947.
    DrugBanki DB00451. Levothyroxine.
    DB00279. Liothyronine.
    GuidetoPHARMACOLOGYi 589.

    PTM databases

    PhosphoSitei P10828.

    Polymorphism databases

    DMDMi 586092.

    Proteomic databases

    PaxDbi P10828.
    PRIDEi P10828.

    Protocols and materials databases

    DNASUi 7068.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000280696 ; ENSP00000280696 ; ENSG00000151090 . [P10828-2 ]
    ENST00000356447 ; ENSP00000348827 ; ENSG00000151090 . [P10828-1 ]
    ENST00000396671 ; ENSP00000379904 ; ENSG00000151090 . [P10828-1 ]
    ENST00000415021 ; ENSP00000404898 ; ENSG00000151090 .
    ENST00000416420 ; ENSP00000414444 ; ENSG00000151090 . [P10828-1 ]
    ENST00000447875 ; ENSP00000388467 ; ENSG00000151090 .
    GeneIDi 7068.
    KEGGi hsa:7068.
    UCSCi uc003ccx.4. human. [P10828-1 ]

    Organism-specific databases

    CTDi 7068.
    GeneCardsi GC03M024158.
    HGNCi HGNC:11799. THRB.
    HPAi CAB002008.
    CAB002009.
    MIMi 145650. phenotype.
    188570. phenotype.
    190160. gene.
    274300. phenotype.
    neXtProti NX_P10828.
    Orphaneti 3221. Generalized resistance to thyroid hormone.
    97927. Peripheral resistance to thyroid hormones.
    165994. Selective pituitary resistance to thyroid hormone.
    PharmGKBi PA36508.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG272726.
    HOGENOMi HOG000010313.
    HOVERGENi HBG005606.
    KOi K08362.
    OMAi LYEVHPA.
    OrthoDBi EOG7TBC2V.
    PhylomeDBi P10828.
    TreeFami TF328382.

    Enzyme and pathway databases

    Reactomei REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinki P10828.

    Miscellaneous databases

    EvolutionaryTracei P10828.
    GeneWikii Thyroid_hormone_receptor_beta.
    GenomeRNAii 7068.
    NextBioi 27637.
    PROi P10828.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10828.
    Bgeei P10828.
    CleanExi HS_THRB.
    Genevestigatori P10828.

    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. "Human steroid receptors and erbA proto-oncogene products: members of a new superfamily of enhancer binding proteins."
      Weinberger C., Giguere V., Hollenberg S., Rosenfeld M.G., Evans R.M.
      Cold Spring Harb. Symp. Quant. Biol. 51:759-772(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1), VARIANT ILE-337.
    2. "The c-erb-A gene encodes a thyroid hormone receptor."
      Weinberger C., Thompson C.C., Ong E.S., Lebo R., Gruol D.J., Evans R.M.
      Nature 324:641-646(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1), VARIANT ILE-337.
      Tissue: Placenta.
    3. "Structural analysis of human thyroid hormone receptor beta gene."
      Sakurai A., Nakai A., Degroot L.J.
      Mol. Cell. Endocrinol. 71:83-91(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION.
    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 BETA-1).
      Tissue: Brain.
    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 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 BETA-1).
    8. "Multiple messenger ribonucleic acid variants regulate cell-specific expression of human thyroid hormone receptor beta1."
      Frankton S., Harvey C.B., Gleason L.M., Fadel A., Williams G.R.
      Mol. Endocrinol. 18:1631-1642(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-122 (ISOFORM BETA-1).
      Tissue: Brain, Kidney, Placenta and Testis.
    9. "Differential expression and transcriptional regulatory properties of the thyroid hormone receptor Beta1 and Beta2."
      Damm K., Berning B.
      Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-122 (ISOFORM BETA-2).
      Tissue: Pituitary.
    10. "A novel C-terminal domain in the thyroid hormone receptor selectively mediates thyroid hormone inhibition."
      Flynn T.R., Hollenberg A.N., Cohen O., Menke J.B., Usala S.J., Tollin S., Hegarty M.K., Wondisford F.E.
      J. Biol. Chem. 269:32713-32716(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 417-432, VARIANT PRTH GLN-429.
    11. "The orphan nuclear receptor Ear-2 is a negative coregulator for thyroid hormone nuclear receptor function."
      Zhu X.G., Park K.S., Kaneshige M., Bhat M.K., Zhu Q., Mariash C.N., McPhie P., Cheng S.Y.
      Mol. Cell. Biol. 20:2604-2618(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH NR2F6.
    12. "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha."
      Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.
      J. Biol. Chem. 277:28624-28630(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRMT2.
    13. "ERAP140, a conserved tissue-specific nuclear receptor coactivator."
      Shao W., Halachmi S., Brown M.
      Mol. Cell. Biol. 22:3358-3372(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA7.
    14. "Human spot 14 protein interacts physically and functionally with the thyroid receptor."
      Chou W.Y., Cheng Y.S., Ho C.L., Liu S.T., Liu P.Y., Kuo C.C., Chang H.P., Chen Y.H., Chang G.G., Huang S.M.
      Biochem. Biophys. Res. Commun. 357:133-138(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THRSP, FUNCTION.
    15. "Structural determinants of nuclear receptor assembly on DNA direct repeats."
      Rastinejad F., Perlmann T., Evans R.M., Sigler P.B.
      Nature 375:203-211(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 104-204 IN COMPLEX WITH ZINC IONS.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 209-460 IN COMPLEX WITH SYNTHETIC AGONIST, FUNCTION.
    17. "Thyroid hormone receptor-beta mutations conferring hormone resistance and reduced corepressor release exhibit decreased stability in the N-terminal ligand-binding domain."
      Huber B.R., Desclozeaux M., West B.L., Cunha-Lima S.T., Nguyen H.T., Baxter J.D., Ingraham H.A., Fletterick R.J.
      Mol. Endocrinol. 17:107-116(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 202-461 OF VARIANT GTHR THR-234, CHARACTERIZATION OF VARIANT GTHR THR-234, MUTAGENESIS OF ARG-243.
    18. Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 202-461 OF VARIANT PTHR HIS-316 AND VARIANT GTHR THR-317, CHARACTERIZATION OF VARIANT PTHR HIS-316, CHARACTERIZATION OF VARIANT GTHR THR-317.
    19. Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 209-461 IN COMPLEX WITH SYNTHETIC AGONIST, FUNCTION, INTERACTION WITH NCOA1; NCOA2; MED1 AND NCOR1, MUTAGENESIS OF ASN-331.
    20. Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 202-461 IN COMPLEX WITH SYNTHETIC AGONIST, INTERACTION WITH NCOA2; MED1 AND NCOR1.
    21. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 202-460 IN COMPLEX WITH SYNTHETIC AGONIST, FUNCTION, DNA-BINDING, SUBUNIT, MUTAGENESIS OF 207-SER-ILE-208.
    22. Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 202-461 IN COMPLEX WITH SYNTHETIC AGONIST, FUNCTION.
    23. Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 202-461, FUNCTION, MUTAGENESIS OF ASN-331.
    24. "Molecular basis for dimer formation of TRbeta variant D355R."
      Jouravel N., Sablin E., Togashi M., Baxter J.D., Webb P., Fletterick R.J.
      Proteins 75:111-117(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 209-460, FUNCTION, SUBUNIT, MUTAGENESIS OF ASP-355.
    25. "Generalized resistance to thyroid hormone associated with a mutation in the ligand-binding domain of the human thyroid hormone receptor beta."
      Sakurai A., Takeda K., Ain K., Ceccarelli P., Nakai A., Seino S., Bell G.I., Refetoff S., Degroot L.
      Proc. Natl. Acad. Sci. U.S.A. 86:8977-8981(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GTHR ARG-345.
    26. "A base mutation of the C-erbA beta thyroid hormone receptor in a kindred with generalized thyroid hormone resistance. Molecular heterogeneity in two other kindreds."
      Usala S.J., Tennyson G.E., Bale A.E., Lash R.W., Gesundheit N., Wondisford F.E., Accili D., Hauser P., Weintraub B.D.
      J. Clin. Invest. 85:93-100(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GTHR HIS-453.
    27. "A new point mutation in the 3,5,3'-triiodothyronine-binding domain of the c-erbA beta thyroid hormone receptor is tightly linked to generalized thyroid hormone resistance."
      Usala S.J., Menke J.B., Watson T.L., Berard J., Bradley W.E.C., Bale A.E., Lash R.W., Weintraub B.D.
      J. Clin. Endocrinol. Metab. 72:32-38(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GTHR HIS-340.
    28. "Characterization of seven novel mutations of the c-erbA beta gene in unrelated kindreds with generalized thyroid hormone resistance. Evidence for two 'hot spot' regions of the ligand binding domain."
      Parrilla R., Mixson A.J., McPherson J.A., McClaskey J.H., Weintraub B.D.
      J. Clin. Invest. 88:2123-2130(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GTHR THR-317; ARG-332; VAL-345; GLU-347; VAL-442 AND THR-453.
    29. "A homozygous deletion in the c-erbA beta thyroid hormone receptor gene in a patient with generalized thyroid hormone resistance: isolation and characterization of the mutant receptor."
      Usala S.J., Menke J.B., Watson T.L., Wondisford F.E., Weintraub B.D., Berard J., Bradley W.E.C., Ono S., Mueller O.T., Bercu B.B.
      Mol. Endocrinol. 5:327-335(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GTHR THR-337 DEL.
    30. "Functional properties of a novel mutant thyroid hormone receptor in a family with generalized thyroid hormone resistance syndrome."
      Adams M., Nagaya T., Tone Y., Jameson J.L., Chatterjee V.K.K.
      Clin. Endocrinol. (Oxf.) 36:281-289(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GTHR SER-345.
    31. "An arginine to histidine mutation in codon 315 of the c-erbA beta thyroid hormone receptor in a kindred with generalized resistance to thyroid hormones results in a receptor with significant 3,5,3'-triiodothyronine binding activity."
      Cugini C.D. Jr., Leidy J.W. Jr., Chertow B.S., Berard J., Bradley W.E.C., Menke J.B., Hao E.-H., Usala S.J.
      J. Clin. Endocrinol. Metab. 74:1164-1170(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GTHR HIS-320.
    32. "A point mutation in the 3,5,3'-triiodothyronine-binding domain of thyroid hormone receptor-beta associated with a family with generalized resistance to thyroid hormone."
      Shuto Y., Wakabayashi I., Amuro N., Minami S., Okazaki T.
      J. Clin. Endocrinol. Metab. 75:213-217(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GTHR THR-453.
    33. "A point mutation of the T3 receptor beta 1 gene in a kindred of generalized resistance to thyroid hormone."
      Sasaki S., Nakamura H., Tagami T., Miyoshi Y., Tanaka K., Imura H.
      Mol. Cell. Endocrinol. 84:159-166(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GTHR GLU-443.
    34. "A point mutation (Ala229 to Thr) in the hinge domain of the c-erbA beta thyroid hormone receptor gene in a family with generalized thyroid hormone resistance."
      Behr M., Loos U.
      Mol. Endocrinol. 6:1119-1126(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GTHR THR-234.
    35. "An arginine to histidine mutation in codon 311 of the C-erbA beta gene results in a mutant thyroid hormone receptor that does not mediate a dominant negative phenotype."
      Geffner M.E., Su F., Ross N.S., Hershman J.M., van Dop C., Menke J.B., Hao E., Stanzak R.K., Eaton T., Samuels H.H., Usala S.J.
      J. Clin. Invest. 91:538-546(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PRTH HIS-316.
    36. "Identical mutations in unrelated families with generalized resistance to thyroid hormone occur in cytosine-guanine-rich areas of the thyroid hormone receptor beta gene. Analysis of 15 families."
      Weiss R.E., Weinberg M., Refetoff S.
      J. Clin. Invest. 91:2408-2415(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GTHR THR-317; CYS-320; HIS-320; TRP-338; HIS-438 AND THR-453.
    37. "A new point mutation (C446R) in the thyroid hormone receptor-beta gene of a family with resistance to thyroid hormone."
      Weiss R.E., Chyna B., Duell P.B., Hayashi Y., Sunthornthepvarakul T., Refetoff S.
      J. Clin. Endocrinol. Metab. 78:1253-1256(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GTHR ARG-446.
    38. "Resistance to thyroid hormone in subjects from two unrelated families is associated with a point mutation in the thyroid hormone receptor beta gene resulting in the replacement of the normal proline 453 with serine."
      Refetoff S., Weiss R.E., Wing J.R., Sarne D., Chyna B., Hayashi Y.
      Thyroid 4:249-254(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GTHR SER-453.
    39. "New point mutation (R243W) in the hormone binding domain of the c-erbA beta 1 gene in a family with generalized resistance to thyroid hormone."
      Pohlenz J., Schoenberger W., Wemme H., Winterpacht A., Wirth S., Zabel B.
      Hum. Mutat. 7:79-81(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GTHR TRP-243.
    40. "Rapid molecular diagnosis of mutations associated with generalized thyroid hormone resistance by PCR-coupled automated direct sequencing of genomic DNA: detection of two novel mutations."
      Seto D., Weintraub B.D.
      Hum. Mutat. 8:247-257(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GTHR THR-317; TRP-338; ILE-342 AND GLU-348.
    41. "T426I a new mutation in the thyroid hormone receptor gene in a sporadic patient with resistance to thyroid hormone and dysmorphism."
      Menzaghi C., di Paola R., Corrias A., Einaudi S., Trischitta V., de Sanctis C., de Filippis V.
      Hum. Mutat. 12:289-289(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GTHR ILE-426.
    42. "Mosaicism of a thyroid hormone receptor-beta gene mutation in resistance to thyroid hormone."
      Mamanasiri S., Yesil S., Dumitrescu A.M., Liao X.-H., Demir T., Weiss R.E., Refetoff S.
      J. Clin. Endocrinol. Metab. 91:3471-3477(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GTHR TRP-338.
    43. "Genotyping of resistance to thyroid hormone in South American population. Identification of seven novel missense mutations in the human thyroid hormone receptor beta gene."
      Rivolta C.M., Olcese M.C., Belforte F.S., Chiesa A., Gruneiro-Papendieck L., Iorcansky S., Herzovich V., Cassorla F., Gauna A., Gonzalez-Sarmiento R., Targovnik H.M.
      Mol. Cell. Probes 23:148-153(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GTHR GLY-268; ASP-331; PRO-335; PRO-341; PHE-346; MET-431; THR-447; LEU-453; THR-453 AND CYS-459.

    Entry informationi

    Entry nameiTHB_HUMAN
    AccessioniPrimary (citable) accession number: P10828
    Secondary accession number(s): B3KU79
    , P37243, Q13986, Q3KP35, Q6WGL2, Q9UD41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 184 of the entry and version 2 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