Reviewed, UniProtKB/Swiss-Prot P10828 (THB_HUMAN)

Names and origin

Protein names

Recommended name:
    Thyroid hormone receptor beta
Alternative name(s):
    Nuclear receptor subfamily 1 group A member 2

Gene names

Name:	THRB
Synonyms:	ERBA2, NR1A2, THR1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	High affinity receptor for triiodothyronine.
Subunit structure	Interacts with NOCA7 in a ligand-inducible manner. Interacts with C1D By similarity.
Subcellular location	Nucleus.
Domain	Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal steroid-binding domain.
Involvement in disease	Defects in THRB are the cause of generalized thyroid hormone resistance (GTHR) [MIM:188570, 274300]. GTHR is transmitted as an autosomal dominant trait, but an autosomal recessive form also exists. The disease is 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). Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Defects in THRB are the cause of selective pituitary thyroid hormone resistance (PRTH) [MIM:145650]; also called familial hyperthyroidism due to inappropriate thyrotropin secretion. PRTH is a 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. Ref.10
Sequence similarities	Belongs to the nuclear hormone receptor family. NR1 subfamily. Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Deafness Disease mutation
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Receptor
Technical term	3D-structure
Gene Ontology (GO)
Biological process	sensory perception of sound Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Traceable author statement. Source: ProtInc
Cellular component	nucleus Traceable author statement. Source: ProtInc
Molecular function	sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro thyroid hormone receptor activity Traceable author statement. Source: ProtInc transcription corepressor activity Traceable author statement. Source: ProtInc transcription factor activity Non-traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRMT2	P55345	1	EBI-78558,EBI-78458

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Beta-1 (identifier: P10828-1)

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.

Isoform Beta-2 (identifier: P10828-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 461

461

Thyroid hormone receptor beta

PRO_0000053446

Regions

DNA binding

107 – 181

75

Nuclear receptor

Zinc finger

107 – 127

21

NR C4-type

Zinc finger

145 – 169

25

NR C4-type

Region

1 – 106

106

Modulating

Region

244 – 461

218

Ligand-binding

Natural variations

Alternative sequence

1 – 93

93

MTPNS…EEKKC → MNYCMQEIYEVHPAAGSNCY MQSTDYYAYFEDSPGYSGCD AQAVPSNNIYMEQAWAVNQP YTCSYPGNMFKSKDSDLDMA LNQYSQPEYFTEEKPTFSQV QSPSYSQK in isoform Beta-2.

VSP_031077

Natural variant

216

1

D → G: dbSNP rs9865746.

VAR_050577

Natural variant

234

1

A → T in GTHR. Ref.9

VAR_004632

Natural variant

243

1

R → W in GTHR. Ref.23

VAR_004633

Natural variant

316

1

R → H in PRTH. Ref.10

VAR_004634

Natural variant

317

1

A → T in GTHR. Ref.11 Ref.12 Ref.24

VAR_004635

Natural variant

320

1

R → C in GTHR. Ref.11 Ref.13

VAR_004636

Natural variant

320

1

R → H in GTHR. Ref.11 Ref.13

VAR_004637

Natural variant

332

1

G → R in GTHR. Ref.12

VAR_004638

Natural variant

337

1

T → I: dbSNP rs1054624. Ref.14 Ref.1 Ref.2

VAR_011784

Natural variant

337

1

Missing in GTHR. Ref.14

VAR_004639

Natural variant

338

1

R → W in GTHR. Ref.11 Ref.24 Ref.26

VAR_004640

Natural variant

340

1

Q → H in GTHR. Ref.15

VAR_004641

Natural variant

342

1

K → I in GTHR. Ref.24

VAR_004642

Natural variant

345

1

G → R in GTHR. Ref.12 Ref.16 Ref.17

VAR_004645

Natural variant

345

1

G → S in GTHR. Ref.12 Ref.16 Ref.17

VAR_004644

Natural variant

345

1

G → V in GTHR. Ref.12 Ref.16 Ref.17

VAR_004643

Natural variant

347

1

G → E in GTHR. Ref.12

VAR_004646

Natural variant

348

1

V → E in GTHR. Ref.24

VAR_004647

Natural variant

426

1

T → I in GTHR. Ref.25

VAR_004648

Natural variant

438

1

R → H in GTHR. Ref.11

VAR_004649

Natural variant

442

1

M → V in GTHR. Ref.12

VAR_004650

Natural variant

443

1

K → E in GTHR. Ref.18

VAR_004651

Natural variant

446

1

C → R in GTHR. Ref.19

VAR_004652

Natural variant

453

1

P → H in GTHR. Ref.11 Ref.12 Ref.20 Ref.21 Ref.22

VAR_004653

Natural variant

453

1

P → S in GTHR. Ref.11 Ref.12 Ref.20 Ref.21 Ref.22

VAR_004654

Natural variant

453

1

P → T in GTHR. dbSNP rs28933408. Ref.11 Ref.12 Ref.20 Ref.21 Ref.22

VAR_004655

Experimental info

Sequence conflict

243

1

R → P in CAA28412. Ref.1

Sequence conflict

243

1

R → P in AAA35677. Ref.2

Sequence conflict

451

1

F → L in CAA28412. Ref.1

Sequence conflict

451

1

F → L in AAA35677. Ref.2

Secondary structure

1

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461

Helix Strand Turn

Details...

Turn

108 – 110

3

Beta strand

116 – 118

3

Helix

125 – 136

12

Helix

140 – 142

3

Turn

155 – 159

5

Helix

162 – 171

10

Helix

176 – 178

3

Helix

182 – 195

14

Helix

203 – 208

6

Helix

216 – 230

15

Turn

248 – 251

4

Beta strand

260 – 263

4

Helix

266 – 273

8

Helix

276 – 288

13

Helix

293 – 295

3

Helix

298 – 319

22

Turn

323 – 326

4

Beta strand

327 – 330

4

Turn

331 – 333

3

Beta strand

334 – 336

3

Helix

338 – 343

6

Turn

344 – 348

5

Helix

349 – 360

12

Helix

361 – 363

3

Helix

367 – 378

12

Helix

389 – 410

22

Helix

417 – 445

29

Helix

448 – 450

3

Helix

453 – 459

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform Beta-1 [UniParc]. Last modified October 1, 1994. Version 2. Checksum: 6770BB0D372A7CAA	FASTA	461	52,788
	10 20 30 40 50 60 MTPNSMTENG LTAWDKPKHC PDREHDWKLV GMSEACLHRK SHSERRSTLK NEQSSPHLIQ 70 80 90 100 110 120 TTWTSSIFHL DHDDVNDQSV SSAQTFQTEE KKCKGYIPSY LDKDELCVVC GDKATGYHYR 130 140 150 160 170 180 CITCEGCKGF FRRTIQKNLH PSYSCKYEGK CVIDKVTRNQ CQECRFKKCI YVGMATDLVL 190 200 210 220 230 240 DDSKRLAKRK LIEENREKRR REELQKSIGH KPEPTDEEWE LIKTVTEAHV ATNAQGSHWK 250 260 270 280 290 300 QKRKFLPEDI GQAPIVNAPE GGKVDLEAFS HFTKIITPAI TRVVDFAKKL PMFCELPCED 310 320 330 340 350 360 QIILLKGCCM EIMSLRAAVR YDPESETLTL NGEMAVTRGQ LKNGGLGVVS DAIFDLGMSL 370 380 390 400 410 420 SSFNLDDTEV ALLQAVLLMS SDRPGLACVE RIEKYQDSFL LAFEHYINYR KHHVTHFWPK 430 440 450 460 LLMKVTDLRM IGACHASRFL HMKVECPTEL FPPLFLEVFE D
	Isoform Beta-2 [UniParc] [UniParc]. Checksum: 21755292507335D8	FASTA	476	54,449
	10 20 30 40 50 60 MNYCMQEIYE VHPAAGSNCY MQSTDYYAYF EDSPGYSGCD AQAVPSNNIY MEQAWAVNQP 70 80 90 100 110 120 YTCSYPGNMF KSKDSDLDMA LNQYSQPEYF TEEKPTFSQV QSPSYSQKKG YIPSYLDKDE 130 140 150 160 170 180 LCVVCGDKAT GYHYRCITCE GCKGFFRRTI QKNLHPSYSC KYEGKCVIDK VTRNQCQECR 190 200 210 220 230 240 FKKCIYVGMA TDLVLDDSKR LAKRKLIEEN REKRRREELQ KSIGHKPEPT DEEWELIKTV 250 260 270 280 290 300 TEAHVATNAQ GSHWKQKRKF LPEDIGQAPI VNAPEGGKVD LEAFSHFTKI ITPAITRVVD 310 320 330 340 350 360 FAKKLPMFCE LPCEDQIILL KGCCMEIMSL RAAVRYDPES ETLTLNGEMA VTRGQLKNGG 370 380 390 400 410 420 LGVVSDAIFD LGMSLSSFNL DDTEVALLQA VLLMSSDRPG LACVERIEKY QDSFLLAFEH 430 440 450 460 470 YINYRKHHVT HFWPKLLMKV TDLRMIGACH ASRFLHMKVE CPTELFPPLF LEVFED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 2879243] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1), VARIANT ILE-337. Tissue: Placenta.
[2]	"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: 3034496] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1), VARIANT ILE-337.
[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: 1973914] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1).
[5]	"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.
[6]	"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: 15105435] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-122 (ISOFORM BETA-1). Tissue: Brain, Kidney, Placenta and Testis.
[7]	"ERAP140, a conserved tissue-specific nuclear receptor coactivator." Shao W., Halachmi S., Brown M. Mol. Cell. Biol. 22:3358-3372(2002) [PubMed: 11971969] [Abstract] Cited for: INTERACTION WITH NOCA7.
[8]	"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: 7746322] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 102-212.
[9]	"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: 1324420] [Abstract] Cited for: VARIANT GTHR THR-234.
[10]	"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: 8381821] [Abstract] Cited for: VARIANT PRTH HIS-316.
[11]	"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: 8514853] [Abstract] Cited for: VARIANTS GTHR THR-317; CYS-320; HIS-320; TRP-338; HIS-438 AND THR-453.
[12]	"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: 1661299] [Abstract] Cited for: VARIANTS GTHR THR-317; ARG-332; VAL-345; GLU-347; VAL-442 AND THR-453.
[13]	"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: 1314846] [Abstract] Cited for: VARIANT GTHR HIS-320.
[14]	"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: 1653889] [Abstract] Cited for: VARIANT GTHR THR-337 DEL.
[15]	"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: 1846005] [Abstract] Cited for: VARIANT GTHR HIS-340.
[16]	"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: 1563081] [Abstract] Cited for: VARIANT GTHR SER-345.
[17]	"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: 2510172] [Abstract] Cited for: VARIANT GTHR ARG-345.
[18]	"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: 1587388] [Abstract] Cited for: VARIANT GTHR GLU-443.
[19]	"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: 8175986] [Abstract] Cited for: VARIANT GTHR ARG-446.
[20]	"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: 2153155] [Abstract] Cited for: VARIANT GTHR HIS-453.
[21]	"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: 1619012] [Abstract] Cited for: VARIANT GTHR THR-453.
[22]	"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: 7833659] [Abstract] Cited for: VARIANT GTHR SER-453.
[23]	"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: 8664910] [Abstract] Cited for: VARIANT GTHR TRP-243.
[24]	"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: 8889584] [Abstract] Cited for: VARIANTS GTHR THR-317; TRP-338; ILE-342 AND GLU-348.
[25]	"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: 10660344] [Abstract] Cited for: VARIANT GTHR ILE-426.
[26]	"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: 16804041] [Abstract] Cited for: VARIANT GTHR TRP-338.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

X04707 mRNA. Translation: CAA28412.1. Different initiation.
M26747 mRNA. Translation: AAA35677.1. Different initiation.
BC106929 mRNA. Translation: AAI06930.1.
BC106930 mRNA. Translation: AAI06931.1.
X74497 mRNA. Translation: CAA52606.1.
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.

IPI

IPI00444844.
IPI00446999.

PIR

TVHUAR. A25237.
S40152.

RefSeq

NP_000452.2.
NP_001121648.1.
NP_001121649.1.

UniGene

Hs.187861

3D structure databases

PDBPDBe

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	2.00	X	202-460	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:5991N.

IntAct

P10828. 3 interactions.

PTM databases

PhosphoSite

P10828.

Proteomic databases

PRIDE

P10828.

Genome annotation databases

Ensembl

ENSG00000151090. Homo sapiens. [Contig view]

GeneID

7068.

KEGG

hsa:7068.

Organism-specific databases

GeneCards

GC03M024139.

H-InvDB

HIX0024295.

HGNC

HGNC:11799. THRB.

HPA

CAB002008.
CAB002009.

MIM

145650. phenotype.
188570. phenotype.
190160. gene.
274300. phenotype.

Orphanet

3221. Generalized resistance to thyroid hormone.
165994. Selective pituitary resistance to thyroid hormone.

PharmGKB

PA36508.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P10828.

OMA

P10828. ELYEVHP.

Enzyme and pathway databases

Pathway_Interaction_DB

rxr_vdr_pathway. RXR and RAR hetrodimerization with other nuclear receptor.

Gene expression databases

ArrayExpress

P10828.

Bgee

P10828.

CleanEx

HS_THRB.

GermOnline

ENSG00000151090. Homo sapiens.

Family and domain databases

InterPro

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]

Gene3D

G3DSA:1.10.565.10. Nucl_hrmn_rcpt_lig_bd. 1 hit.
G3DSA:3.30.50.10. Znf_NHR/GATA. 1 hit.

Pfam

PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PRINTS

PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
PR00546. THYROIDHORMR.

ProDom

PD000035. Znf_C4steroid. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

DrugBank

DB00451. Levothyroxine.
DB00279. Liothyronine.

NextBio

27637.

SOURCE

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Entry information

Entry name

THB_HUMAN

Accession

Primary (citable) accession number: P10828
Secondary accession number(s): P37243 , Q13986, Q3KP35, Q6WGL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)