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Protein

Thyroid hormone receptor alpha

Gene

THRA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.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

  • chromatin DNA binding Source: Ensembl
  • protein domain specific binding Source: UniProtKB
  • sequence-specific DNA binding Source: InterPro
  • sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • steroid hormone receptor activity Source: InterPro
  • steroid receptor RNA activator RNA binding Source: Ensembl
  • TBP-class protein binding Source: UniProtKB
  • thyroid hormone binding Source: UniProtKB
  • thyroid hormone receptor activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: BHF-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

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.
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 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:11796. THRA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Hypothyroidism, congenital, non-goitrous, 6 (CHNG6)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:614450

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.

Chemistry

DrugBankiDB00509. Dextrothyroxine.
DB00451. Levothyroxine.
DB00279. Liothyronine.
DB01583. Liotrix.

Polymorphism and mutation databases

BioMutaiTHRA.
DMDMi135705.

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

MaxQBiP10827.
PaxDbiP10827.
PRIDEiP10827.

PTM databases

PhosphoSiteiP10827.

Expressioni

Gene expression databases

BgeeiP10827.
CleanExiHS_THRA.
ExpressionAtlasiP10827. baseline and differential.
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
AMOTL2Q9Y2J4-43EBI-286285,EBI-10187270
L3MBTL3Q96JM73EBI-286285,EBI-2686809
MED1Q156485EBI-286285,EBI-394459
Ncoa6Q9JLI42EBI-286285,EBI-286271From a different organism.

Protein-protein interaction databases

BioGridi112923. 76 interactions.
DIPiDIP-31452N.
IntActiP10827. 19 interactions.
MINTiMINT-267914.
STRINGi9606.ENSP00000264637.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 50-402.
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.
GeneTreeiENSGT00780000121834.
HOGENOMiHOG000010313.
HOVERGENiHBG005606.
InParanoidiP10827.
KOiK05547.
OMAiSSMSGYI.
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. AlignAdd to basket

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

        10         20         30         40         50
MEQKPSKVEC GSDPEENSAR SPDGKRKRKN GQCSLKTSMS GYIPSYLDKD
60 70 80 90 100
EQCVVCGDKA TGYHYRCITC EGCKGFFRRT IQKNLHPTYS CKYDSCCVID
110 120 130 140 150
KITRNQCQLC RFKKCIAVGM AMDLVLDDSK RVAKRKLIEQ NRERRRKEEM
160 170 180 190 200
IRSLQQRPEP TPEEWDLIHI ATEAHRSTNA QGSHWKQRRK FLPDDIGQSP
210 220 230 240 250
IVSMPDGDKV DLEAFSEFTK IITPAITRVV DFAKKLPMFS ELPCEDQIIL
260 270 280 290 300
LKGCCMEIMS LRAAVRYDPE SDTLTLSGEM AVKREQLKNG GLGVVSDAIF
310 320 330 340 350
ELGKSLSAFN LDDTEVALLQ AVLLMSTDRS GLLCVDKIEK SQEAYLLAFE
360 370 380 390 400
HYVNHRKHNI PHFWPKLLMK EREVQSSILY KGAAAEGRPG GSLGVHPEGQ
410 420 430 440 450
QLLGMHVVQG PQVRQLEQQL GEAGSLQGPV LQHQSPKSPQ QRLLELLHRS
460 470 480 490
GILHARAVCG EDDSSEADSP SSSEEEPEVC EDLAGNAASP
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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 50-402.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112923. 76 interactions.
DIPiDIP-31452N.
IntActiP10827. 19 interactions.
MINTiMINT-267914.
STRINGi9606.ENSP00000264637.

Chemistry

BindingDBiP10827.
ChEMBLiCHEMBL2111462.
DrugBankiDB00509. Dextrothyroxine.
DB00451. Levothyroxine.
DB00279. Liothyronine.
DB01583. Liotrix.
GuidetoPHARMACOLOGYi588.

PTM databases

PhosphoSiteiP10827.

Polymorphism and mutation databases

BioMutaiTHRA.
DMDMi135705.

Proteomic databases

MaxQBiP10827.
PaxDbiP10827.
PRIDEiP10827.

Protocols and materials databases

DNASUi7067.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi7067.
GeneCardsiGC17P038219.
HGNCiHGNC:11796. THRA.
HPAiCAB023349.
HPA009654.
MIMi190120. gene.
614450. phenotype.
neXtProtiNX_P10827.
Orphaneti97927. Peripheral resistance to thyroid hormones.
PharmGKBiPA36507.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG272726.
GeneTreeiENSGT00780000121834.
HOGENOMiHOG000010313.
HOVERGENiHBG005606.
InParanoidiP10827.
KOiK05547.
OMAiSSMSGYI.
PhylomeDBiP10827.
TreeFamiTF328382.

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
SignaLinkiP10827.

Miscellaneous databases

ChiTaRSiTHRA. human.
EvolutionaryTraceiP10827.
GeneWikiiThyroid_hormone_receptor_alpha.
GenomeRNAii7067.
NextBioi27631.
PROiP10827.
SOURCEiSearch...

Gene expression databases

BgeeiP10827.
CleanExiHS_THRA.
ExpressionAtlasiP10827. baseline and differential.
GenevestigatoriP10827.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: May 27, 2015
This is version 191 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.