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P10828

- THB_HUMAN

UniProt

P10828 - THB_HUMAN

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Protein

Thyroid hormone receptor beta

Gene

THRB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. sequence-specific DNA binding Source: InterPro
  5. sequence-specific DNA binding transcription factor activity Source: ProtInc
  6. steroid hormone receptor activity Source: InterPro
  7. thyroid hormone binding Source: UniProtKB
  8. thyroid hormone receptor activity Source: UniProtKB
  9. transcription corepressor activity Source: ProtInc
  10. 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
Complete GO annotation...

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. nuclear chromatin Source: Ensembl
  3. nucleoplasm Source: Reactome
  4. nucleus Source: ProtInc
Complete GO annotation...

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. 1 Publication
Mutagenesisi331 – 3311N → S: No effect on thyroid hormone binding. 2 Publications
Mutagenesisi355 – 3551D → R: Stabilizes homodimer. 1 Publication

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

MaxQBiP10828.
PaxDbiP10828.
PRIDEiP10828.

PTM databases

PhosphoSiteiP10828.

Expressioni

Gene expression databases

BgeeiP10828.
CleanExiHS_THRB.
ExpressionAtlasiP10828. baseline and differential.
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. 51 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.
GeneTreeiENSGT00760000118837.
HOGENOMiHOG000010313.
HOVERGENiHBG005606.
InParanoidiP10828.
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

        10         20         30         40         50
MTPNSMTENG LTAWDKPKHC PDREHDWKLV GMSEACLHRK SHSERRSTLK
60 70 80 90 100
NEQSSPHLIQ TTWTSSIFHL DHDDVNDQSV SSAQTFQTEE KKCKGYIPSY
110 120 130 140 150
LDKDELCVVC GDKATGYHYR CITCEGCKGF FRRTIQKNLH PSYSCKYEGK
160 170 180 190 200
CVIDKVTRNQ CQECRFKKCI YVGMATDLVL DDSKRLAKRK LIEENREKRR
210 220 230 240 250
REELQKSIGH KPEPTDEEWE LIKTVTEAHV ATNAQGSHWK QKRKFLPEDI
260 270 280 290 300
GQAPIVNAPE GGKVDLEAFS HFTKIITPAI TRVVDFAKKL PMFCELPCED
310 320 330 340 350
QIILLKGCCM EIMSLRAAVR YDPESETLTL NGEMAVTRGQ LKNGGLGVVS
360 370 380 390 400
DAIFDLGMSL SSFNLDDTEV ALLQAVLLMS SDRPGLACVE RIEKYQDSFL
410 420 430 440 450
LAFEHYINYR KHHVTHFWPK LLMKVTDLRM IGACHASRFL HMKVECPTEL
460
FPPLFLEVFE D
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. 51 interactions.
DIPi DIP-5991N.
IntActi P10828. 10 interactions.
MINTi MINT-1508903.
STRINGi 9606.ENSP00000348827.

Chemistry

BindingDBi P10828.
ChEMBLi CHEMBL1947.
DrugBanki DB00509. Dextrothyroxine.
DB00451. Levothyroxine.
DB00279. Liothyronine.
DB01583. Liotrix.
GuidetoPHARMACOLOGYi 589.

PTM databases

PhosphoSitei P10828.

Polymorphism databases

DMDMi 586092.

Proteomic databases

MaxQBi P10828.
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.
GeneTreei ENSGT00760000118837.
HOGENOMi HOG000010313.
HOVERGENi HBG005606.
InParanoidi P10828.
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

Bgeei P10828.
CleanExi HS_THRB.
ExpressionAtlasi P10828. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 185 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