AC T00851
XX
ID T00851
XX
DT 15.10.1992 (created); ewi.
DT 05.08.2015 (updated); jmh.
CO Copyright (C), QIAGEN.
XX
FA T3R-beta1
XX
SY c-ErbA; ERBA2; NR1A2; Nuclear receptor subfamily 1 group A member 2; T3R-beta; THR1; THRB; thyroid hormone receptor beta-1; thyroid hormone receptor-beta; thyroid receptor beta 1; TR; TR-beta.
XX
OS human, Homo sapiens
OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; primates
XX
GE G002740 THRB; HGNC: THRB.
XX
CL C0002; CC (rec); 2.1.2.2.2.1.
XX
SZ 461 AA; 52.8 kDa (cDNA) (calc.).
XX
SQ MTPNSMTENGLTAWDKPKHCPDREHDWKLVGMSEACLHRKSHSERRSTLKNEQSSPHLIQ
SQ TTWTSSIFHLDHDDVNDQSVSSAQTFQTEEKKCKGYIPSYLDKDELCVVCGDKATGYHYR
SQ CITCEGCKGFFRRTIQKNLHPSYSCKYEGKCVIDKVTRNQCQECRFKKCIYVGMATDLVL
SQ DDSKRLAKRKLIEENREKRRREELQKSIGHKPEPTDEEWELIKTVTEAHVATNAQGSHWK
SQ QKRKFLPEDIGQAPIVNAPEGGKVDLEAFSHFTKIITPAITRVVDFAKKLPMFCELPCED
SQ QIILLKGCCMEIMSLRAAVRYDPESETLTLNGEMAVTRGQLKNGGLGVVSDAIFDLGMSL
SQ SSFNLDDTEVALLQAVLLMSSDRPGLACVERIEKYQDSFLLAFEHYINYRKHHVTHFWPK
SQ LLMKVTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFED
XX
SC translated from EMBL #X04707; amino acids 1-5 added and positions 243, 337 and 451 edited according to ref. [15]
XX
FT 1 5 
not present in EMBL #X04707 [15].
FT 68 383 
PF00478; IMP dehydrogenase / GMP reductase domai.
FT 75 93 
AF-1 [20].
FT 100 175 
DNA-binding domain [10].
FT 104 177 
SM00399; c4gold.
FT 104 181 
PS51030; NUCLEAR_REC_DBD_2.
FT 105 182 
PF00105; Zinc finger, C4 type (two domains).
FT 107 127 
zinc finger 1 (C-X2-C-X13-C-X2-C) [10].
FT 125 129 
P-box [10].
FT 145 164 
zinc finger 2 (C-X5-C-X9-C-X2-C) [10].
FT 175 182 T region [17].
FT 211 240 CoR box [13].
FT 211 240 nuclear co-repressor T04688 binding domain [13].
FT 212 222 tau2 [19].
FT 214 461 ligand-binding domain [16].
FT 274 432 SM00430; holi.
FT 277 458 PF00104; Ligand-binding domain of nuclear hormon.
FT 344 373 tau3 [19].
XX
SF DNA-binding domain is approximately 180 deg rotated with respect to dimerization interface (in contrast to RXR and steroid receptors);
SF DNA-binding domain, 1st zinc finger (DR-box) are required for heterodimerization with RXR-alpha = determinant of half-site spacing favoring 4bp in direct repeats;
SF P-box determines DNA-binding specificity for different everted repeat binding sites (type ER6) and their flanking sequences [10] [11];
XX
FF dominant negative mutants causing thyroid hormone resistance syndrome: G345R , P453H , delta453-461 (as in v-ErbA) bind to TRE but do not mediate positive or negative T3 response;
FF DNA-binding is antagonized by AP-1, dependent on the C-terminal 17 amino acid residues;
FF the particular structure of the DBD leads to preferential binding of heterodimers to direct repeats (downstream half-site), but of homodimers to palindromes;
XX
IN T08437 ADA2-isoform1; human, Homo sapiens.
IN T02285 ctcf; mouse, Mus musculus.
IN T02763 EAR2; human, Homo sapiens.
IN T08972 EAR2; human, Homo sapiens.
IN T09602 ER; Mammalia.
IN T17995 GATA-2; Mammalia.
IN T01686 GCN5; human, Homo sapiens.
IN T08893 hdac2; mouse, Mus musculus.
IN T04451 LXR-beta; rat, Rattus norvegicus.
IN T08641 NCOR1-isoform1; mouse, Mus musculus.
IN T04687 NCOR1; human, Homo sapiens.
IN T04688 NCOR1; mouse, Mus musculus.
IN T05295 PGC-1-isoform1; human, Homo sapiens.
IN T01331 RXR-alpha; mouse, Mus musculus.
IN T01345 RXR-alpha; human, Homo sapiens.
IN T01359 RXR-alpha; clawed frog, Xenopus laevis.
IN T01349 RXR-beta; rat, Rattus norvegicus.
IN T04689 SMRT; human, Homo sapiens.
IN T21552 SRC-1; Mammalia.
IN T08256 SRC-1A; human, Homo sapiens.
IN T04640 SRC3; human, Homo sapiens.
IN T02482 TIF2; mouse, Mus musculus.
IN T01355 TRAP; human, Homo sapiens.
IN T05150 ZAC-1b; mouse, Mus musculus.
XX
MX M02119 V$T3RBETA_Q6_01.
MX M00963 V$T3R_Q6.
XX
BS R03564.
BS R03941.
BS R01465.
BS R03565.
BS R03952.
BS R03953.
BS R03954.
BS R03980.
BS R03982.
BS R03983.
BS R03984.
BS R04404.
BS R04508.
BS R04633.
BS R04765.
BS R04766.
BS R04767.
BS R04777.
BS R04803.
BS R01673.
BS R26500.
BS R29380.
BS R65777.
BS R65778.
BS R36133.
BS R03960.
BS R69093.
BS R03958.
BS R61647.
BS R61648.
BS R03942.
BS R29384.
BS R69095.
BS R03102.
BS R04771.
BS R30850.
BS R72407.
BS R02595.
BS R41589.
BS R27625.
BS R30860.
BS R27896.
BS R20554.
BS R00618.
BS R01617.
BS R01169.
BS R03523.
BS R01906.
XX
DR TRANSPATH: MO000021670.
DR TRANSCOMPEL: C00361.
DR PATHODB: MT010692.
DR PATHODB: MT010702.
DR PATHODB: MT010703.
DR PATHODB: MT010704.
DR PATHODB: MT010705.
DR PATHODB: MT010706.
DR PATHODB: MT010707.
DR PATHODB: MT010708.
DR PATHODB: MT010709.
DR PATHODB: MT010710.
DR PATHODB: MT010711.
DR PATHODB: MT010712.
DR PATHODB: MT010713.
DR PATHODB: MT010714.
DR PATHODB: MT010715.
DR PATHODB: MT010716.
DR PATHODB: MT010717.
DR PATHODB: MT010718.
DR PATHODB: MT010719.
DR PATHODB: MT010720.
DR PATHODB: MT010721.
DR PATHODB: MT010722.
DR PATHODB: MT010723.
DR PATHODB: MT010724.
DR PATHODB: MT010725.
DR PATHODB: MT010726.
DR PATHODB: MT010727.
DR PATHODB: MT010728.
DR PATHODB: MT010729.
DR PATHODB: MT010730.
DR PATHODB: MT010731.
DR PATHODB: MT010732.
DR PATHODB: MT010733.
DR PATHODB: MT010734.
DR PATHODB: MT010735.
DR PATHODB: MT010736.
DR PATHODB: MT010737.
DR PATHODB: MT010738.
DR PATHODB: MT010739.
DR PATHODB: MT010740.
DR PATHODB: MT010741.
DR PATHODB: MT010742.
DR PATHODB: MT010743.
DR PATHODB: MT010744.
DR PATHODB: MT010745.
DR PATHODB: MT010746.
DR PATHODB: MT010747.
DR PATHODB: MT010748.
DR PATHODB: MT010749.
DR PATHODB: MT010750.
DR PATHODB: MT010751.
DR PATHODB: MT010752.
DR PATHODB: MT010753.
DR PATHODB: MT010754.
DR PATHODB: MT010755.
DR PATHODB: MT010756.
DR PATHODB: MT010757.
DR PATHODB: MT010758.
DR PATHODB: MT010759.
DR PATHODB: MT010760.
DR PATHODB: MT010761.
DR PATHODB: MT010762.
DR PATHODB: MT010763.
DR PATHODB: MT010764.
DR PATHODB: MT010765.
DR PATHODB: MT010766.
DR PATHODB: MT010767.
DR PATHODB: MT010785.
DR PATHODB: MT010786.
DR PATHODB: MT010787.
DR PATHODB: MT010788.
DR PATHODB: MT010797.
DR PATHODB: MT010800.
DR EMBL: X04707;
DR UniProtKB: P10828-1;
XX
RN [1]; RE0000792.
RX PUBMED: 8392479.
RA Kurokawa R., Yu V. C., Naeaer A., Kyakumoto S., Han Z., Silverman S., Rosenfeld M. G., Glass C. K.
RT Differential orientations of the DNA-binding domain and carboxy-terminal dimerization interface regulate binding site selection by nuclear receptor heterodimers
RL Genes Dev. 7:1423-1435 (1993).
RN [2]; RE0000793.
RX PUBMED: 8392478.
RA Perlmann T., Rangarajan P. N., Umesono K., Evans R. M.
RT Determinants for selective RAR and TR recognition of direct repeat HREs
RL Genes Dev. 7:1411-1422 (1993).
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RA Rosen E. D., Beninghof E. G., Koenig R. J.
RT Dimerization interfaces of thyroid hormone, retinoic acid, vitamin D, and retinoid X receptors
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RA Chatterjee V. K., Nagaya T., Madison L. D., Datta S., Rentoumis A., Jameson J. L.
RT Thyroid hormone resistance syndrome: inhibition of normal receptor function by mutant thyroid hormone receptors
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RT Novel pathway for thyroid hormone receptor action through interaction with jun and fos oncogene activities
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RA Zhang X. K., Hoffmann B., Tran P. B.-V., Graupner G., Pfahl M.
RT Retinoid X receptor is an auxiliary protein for thyroid hormone and retinoic acid receptors
RL Nature 355:441-446 (1992).
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RA Kliewer S. A., Umesono K., Mangelsdorf D. J., Evans R. M.
RT Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signalling
RL Nature 355:446-449 (1992).
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RT Identification of a thyroid hormone response element in the malic enzyme gene
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RA Evans R. M.
RT The steroid and thyroid hormone receptor superfamily
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RA Nelson C. C., Hendy S. C., Romaniuk P. J.
RT Relationship between P-box acid sequence and DNA binding specificity of the thyroid hormone receptor. The effects of half-site sequence in everted repeats
RL J. Biol. Chem. 270:16981-16987 (1995).
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RX PUBMED: 7622519.
RA Nelson C. C., Hendy S. C., Romaniuk P. J.
RT Relationship between P-box acid sequence and DNA binding specificity of the thyroid hormone receptor. The effects of sequences flanking half-sites in thyroid hormone response elements
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RA Tone Y., Collingwood T. N., Adams M., Chatterjee V. K.
RT Functional analysis of a transactivation domain in the thyroid hormone beta receptor
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RA Hoerlein A. J., Naeaer A. M., Heinzel T., Torchia J., Gloss B., Kurokawa R., Ryan A., Kamei Y., Soederstroem M., Glass C. K., Rosenfeld M. G.
RT Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
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RA Nuclear Receptors Nomenclature Committee.
RT A unified nomenclature system for the nuclear receptor superfamily
RL Cell 97:161-163 (1999).
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RX PUBMED: 1973914.
RA Sakurai A., Nakai A., DeGroot L. J.
RT Structural analysis of human thyroid hormone receptor beta gene
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RX PUBMED: 8548460.
RA Wurtz J. M., Bourguet W., Renaud J. P., Vivat V., Chambon P., Moras D., Gronemeyer H.
RT A canonical structure for the ligand-binding domain of nuclear receptors
RL Nat. Struct. Biol. 3:87-94 (1996).
RN [17]; RE0015818.
RX PUBMED: 7746322.
RA Rastinejad F., Perlmann T., Evans R. M., Sigler P. B.
RT Structural determinants of nuclear receptor assembly on DNA direct repeats
RL Nature 375:203-211 (1995).
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RX PUBMED: 8564548.
RA Wurtz J. M., Bourguet W., Renaud J. P., Vivat V., Chambon P., Moras D., Gronemeyer H.
RT A canonical structure for the ligand-binding domain of nuclear receptors
RL Nat. Struct. Biol. 3:206 (1996).
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RX PUBMED: 7799971.
RA Baniahmad A., Leng X., Burris T. P., Tsai S. Y., Tsai M. J., O'Malley B. W.
RT The tau 4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing.
RL Mol. Cell. Biol. 15:76-86 (1995).
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RX PUBMED: 9295330.
RA Wilkinson J. R., Towle H. C.
RT Identification and characterization of the AF-1 transactivation domain of thyroid hormone receptor beta1.
RL J. Biol. Chem. 272:23824-23832 (1997).
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RX PUBMED: 11903058.
RA Krogsdam A. M., Nielsen C. A., Neve S., Holst D., Helledie T., Thomsen B., Bendixen C., Mandrup S., Kristiansen K.
RT Nuclear receptor corepressor-dependent repression of peroxisome-proliferator-activated receptor delta-mediated transactivation.
RL Biochem. J. 363:157-65 (2002).
RN [22]; RE0025766.
RX PUBMED: 12048199.
RA Lin H. M., Zhao L., Cheng S. Y.
RT Cyclin D1 Is a Ligand-independent Co-repressor for Thyroid Hormone Receptors.
RL J. Biol. Chem. 277:28733-41 (2002).
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RX PUBMED: 10454579.
RA Kim H. J., Yi J. Y., Sung H. S., Moore D. D., Jhun B. H., Lee Y. C., Lee J. W.
RT Activating signal cointegrator 1, a novel transcription coactivator of nuclear receptors, and its cytosolic localization under conditions of serum deprivation
RL Mol. Cell. Biol. 19:6323-32 (1999).
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RX PUBMED: 11739747.
RA Ko L., Cardona G. R., Henrion-Caude A., Chin W. W.
RT Identification and characterization of a tissue-specific coactivator, GT198, that interacts with the DNA-binding domains of nuclear receptors.
RL Mol. Cell. Biol. 22:357-369 (2002).
RN [25]; RE0047600.
RX PUBMED: 9717844.
RA Lee S. K., Choi H. S., Song M. R., Lee M. O., Lee J. W.
RT Estrogen receptor, a common interaction partner for a subset of nuclear receptors.
RL Mol. Endocrinol. 12:1184-1192 (1998).
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RX PUBMED: 10625678.
RA Perez-Juste G., Garcia-Silva S., Aranda A.
RT An element in the region responsible for premature termination of transcription mediates repression of c-myc gene expression by thyroid hormone in neuroblastoma cells.
RL J. Biol. Chem. 275:1307-1314 (2000).
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RX PUBMED: 9372952.
RA Qi J. S., Desai-Yajnik V., Yuan Y., Samuels H. H.
RT Constitutive activation of gene expression by thyroid hormone receptor results from reversal of p53-mediated repression.
RL Mol. Cell. Biol. 17:7195-7207 (1997).
RN [28]; RE0047707.
RX PUBMED: 10508171.
RA Sasaki S., Lesoon-Wood L. A., Dey A., Kuwata T., Weintraub B. D., Humphrey G., Yang W. M., Seto E., Yen P. M., Howard B. H., Ozato K.
RT Ligand-induced recruitment of a histone deacetylase in the negative-feedback regulation of the thyrotropin beta gene.
RL EMBO J. 18:5389-5398 (1999).
RN [29]; RE0047804.
RX PUBMED: 10713182.
RA Zhu X. G., Park K. S., Kaneshige M., Bhat M. K., Zhu Q., Mariash C. N., McPhie P., Cheng S. Y.
RT The orphan nuclear receptor Ear-2 is a negative coregulator for thyroid hormone nuclear receptor function.
RL Mol. Cell. Biol. 20:2604-2618 (2000).
RN [30]; RE0048488.
RX PUBMED: 15691842.
RA Yu C., Markan K., Temple K. A., Deplewski D., Brady M. J., Cohen R. N.
RT The nuclear receptor corepressors NCoR and SMRT decrease peroxisome proliferator-activated receptor gamma transcriptional activity and repress 3T3-L1 adipogenesis.
RL J. Biol. Chem. 280:13600-13605 (2005).
RN [31]; RE0048879.
RX PUBMED: 11818500.
RA Marimuthu A., Feng W., Tagami T., Nguyen H., Jameson J. L., Fletterick R. J., Baxter J. D., West B. L.
RT TR surfaces and conformations required to bind nuclear receptor corepressor.
RL Mol. Endocrinol. 16:271-286 (2002).
RN [32]; RE0065802.
RX PUBMED: 18653622.
RA Nagayama K., Sasaki S., Matsushita A., Ohba K., Iwaki H., Matsunaga H., Suzuki S., Misawa H., Ishizuka K., Oki Y., Noh J. Y., Nakamura H.
RT Inhibition of GATA2-dependent transactivation of the TSHbeta gene by ligand-bound estrogen receptor alpha.
RL J. Endocrinol. 199:113-125 (2008).
RN [33]; RE0067795.
RX PUBMED: 18187603.
RA Yamauchi M., Kambe F., Cao X., Lu X., Kozaki Y., Oiso Y., Seo H.
RT Thyroid hormone activates adenosine 5'-monophosphate-activated protein kinase via intracellular calcium mobilization and activation of calcium/calmodulin-dependent protein kinase kinase-beta.
RL Mol. Endocrinol. 22:893-903 (2008).
RN [34]; RE0068910.
RX PUBMED: 19487700.
RA Privalsky M. L., Lee S., Hahm J. B., Young B. M., Fong R. N., Chan I. H.
RT The p160 coactivator PAS-B motif stabilizes nuclear receptor binding and contributes to isoform-specific regulation by thyroid hormone receptors.
RL J. Biol. Chem. 284:19554-19563 (2009).
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