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Thyroid hormone receptor beta (Nuclear receptor subfamily 1 group A member 2) (c-erbA-2) (c-erbA-beta)

 THB_HUMAN               Reviewed;         461 AA.
P10828; B3KU79; P37243; Q13986; Q3KP35; Q6WGL2; Q9UD41;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 2.
28-MAR-2018, entry version 220.
RecName: Full=Thyroid hormone receptor beta;
AltName: Full=Nuclear receptor subfamily 1 group A member 2;
AltName: Full=c-erbA-2;
AltName: Full=c-erbA-beta;
Name=THRB; Synonyms=ERBA2, NR1A2, THR1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1), AND VARIANT ILE-337.
PubMed=3034496;
Weinberger C., Giguere V., Hollenberg S., Rosenfeld M.G., Evans R.M.;
"Human steroid receptors and erbA proto-oncogene products: members of
a new superfamily of enhancer binding proteins.";
Cold Spring Harb. Symp. Quant. Biol. 51:759-772(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1), AND VARIANT ILE-337.
TISSUE=Placenta;
PubMed=2879243; DOI=10.1038/324641a0;
Weinberger C., Thompson C.C., Ong E.S., Lebo R., Gruol D.J.,
Evans R.M.;
"The c-erb-A gene encodes a thyroid hormone receptor.";
Nature 324:641-646(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION.
PubMed=1973914; DOI=10.1016/0303-7207(90)90245-4;
Sakurai A., Nakai A., Degroot L.J.;
"Structural analysis of human thyroid hormone receptor beta gene.";
Mol. Cell. Endocrinol. 71:83-91(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
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.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-122 (ISOFORM BETA-1).
TISSUE=Brain, Kidney, Placenta, and Testis;
PubMed=15105435; DOI=10.1210/me.2003-0346;
Frankton S., Harvey C.B., Gleason L.M., Fadel A., Williams G.R.;
"Multiple messenger ribonucleic acid variants regulate cell-specific
expression of human thyroid hormone receptor beta1.";
Mol. Endocrinol. 18:1631-1642(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-122 (ISOFORM BETA-2).
TISSUE=Pituitary;
Damm K., Berning B.;
"Differential expression and transcriptional regulatory properties of
the thyroid hormone receptor Beta1 and Beta2.";
Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 417-432, AND VARIANT PRTH
GLN-429.
PubMed=7528740;
Flynn T.R., Hollenberg A.N., Cohen O., Menke J.B., Usala S.J.,
Tollin S., Hegarty M.K., Wondisford F.E.;
"A novel C-terminal domain in the thyroid hormone receptor selectively
mediates thyroid hormone inhibition.";
J. Biol. Chem. 269:32713-32716(1994).
[11]
SUBUNIT, AND INTERACTION WITH NR2F6.
PubMed=10713182; DOI=10.1128/MCB.20.7.2604-2618.2000;
Zhu X.G., Park K.S., Kaneshige M., Bhat M.K., Zhu Q., Mariash C.N.,
McPhie P., Cheng S.Y.;
"The orphan nuclear receptor Ear-2 is a negative coregulator for
thyroid hormone nuclear receptor function.";
Mol. Cell. Biol. 20:2604-2618(2000).
[12]
INTERACTION WITH PRMT2.
PubMed=12039952; DOI=10.1074/jbc.M201053200;
Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
"Identification of protein arginine methyltransferase 2 as a
coactivator for estrogen receptor alpha.";
J. Biol. Chem. 277:28624-28630(2002).
[13]
INTERACTION WITH NCOA7.
PubMed=11971969; DOI=10.1128/MCB.22.10.3358-3372.2002;
Shao W., Halachmi S., Brown M.;
"ERAP140, a conserved tissue-specific nuclear receptor coactivator.";
Mol. Cell. Biol. 22:3358-3372(2002).
[14]
INTERACTION WITH THRSP, AND FUNCTION.
PubMed=17418816; DOI=10.1016/j.bbrc.2007.03.103;
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.;
"Human spot 14 protein interacts physically and functionally with the
thyroid receptor.";
Biochem. Biophys. Res. Commun. 357:133-138(2007).
[15]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 104-204 IN COMPLEX WITH ZINC
IONS.
PubMed=7746322; DOI=10.1038/375203a0;
Rastinejad F., Perlmann T., Evans R.M., Sigler P.B.;
"Structural determinants of nuclear receptor assembly on DNA direct
repeats.";
Nature 375:203-211(1995).
[16]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 209-460 IN COMPLEX WITH
SYNTHETIC AGONIST, AND FUNCTION.
PubMed=12699376; DOI=10.1021/jm021080f;
Ye L., Li Y.L., Mellstrom K., Mellin C., Bladh L.G., Koehler K.,
Garg N., Garcia Collazo A.M., Litten C., Husman B., Persson K.,
Ljunggren J., Grover G., Sleph P.G., George R., Malm J.;
"Thyroid receptor ligands. 1. Agonist ligands selective for the
thyroid receptor beta1.";
J. Med. Chem. 46:1580-1588(2003).
[17]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 202-461 OF VARIANT GTHR
THR-234, CHARACTERIZATION OF VARIANT GTHR THR-234, AND MUTAGENESIS OF
ARG-243.
PubMed=12511610; DOI=10.1210/me.2002-0097;
Huber B.R., Desclozeaux M., West B.L., Cunha-Lima S.T., Nguyen H.T.,
Baxter J.D., Ingraham H.A., Fletterick R.J.;
"Thyroid hormone receptor-beta mutations conferring hormone resistance
and reduced corepressor release exhibit decreased stability in the N-
terminal ligand-binding domain.";
Mol. Endocrinol. 17:107-116(2003).
[18]
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, AND CHARACTERIZATION OF VARIANT GTHR THR-317.
PubMed=12554782; DOI=10.1210/me.2002-0095;
Huber B.R., Sandler B., West B.L., Cunha Lima S.T., Nguyen H.T.,
Apriletti J.W., Baxter J.D., Fletterick R.J.;
"Two resistance to thyroid hormone mutants with impaired hormone
binding.";
Mol. Endocrinol. 17:643-652(2003).
[19]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 209-461 IN COMPLEX WITH
SYNTHETIC AGONIST, FUNCTION, INTERACTION WITH NCOA1; NCOA2; MED1 AND
NCOR1, AND MUTAGENESIS OF ASN-331.
PubMed=14673100; DOI=10.1073/pnas.2136689100;
Borngraeber S., Budny M.J., Chiellini G., Cunha-Lima S.T., Togashi M.,
Webb P., Baxter J.D., Scanlan T.S., Fletterick R.J.;
"Ligand selectivity by seeking hydrophobicity in thyroid hormone
receptor.";
Proc. Natl. Acad. Sci. U.S.A. 100:15358-15363(2003).
[20]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 202-461 IN COMPLEX WITH
SYNTHETIC AGONIST, AND INTERACTION WITH NCOA2; MED1 AND NCOR1.
PubMed=15466465; DOI=10.1074/jbc.M410124200;
Sandler B., Webb P., Apriletti J.W., Huber B.R., Togashi M.,
Cunha Lima S.T., Juric S., Nilsson S., Wagner R., Fletterick R.J.,
Baxter J.D.;
"Thyroxine-thyroid hormone receptor interactions.";
J. Biol. Chem. 279:55801-55808(2004).
[21]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 202-460 IN COMPLEX WITH
SYNTHETIC AGONIST, FUNCTION, DNA-BINDING, SUBUNIT, AND MUTAGENESIS OF
207-SER-ILE-208.
PubMed=16781732; DOI=10.1016/j.jmb.2006.05.008;
Nascimento A.S., Dias S.M., Nunes F.M., Aparicio R., Ambrosio A.L.,
Bleicher L., Figueira A.C., Santos M.A., de Oliveira Neto M.,
Fischer H., Togashi M., Craievich A.F., Garratt R.C., Baxter J.D.,
Webb P., Polikarpov I.;
"Structural rearrangements in the thyroid hormone receptor hinge
domain and their putative role in the receptor function.";
J. Mol. Biol. 360:586-598(2006).
[22]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 202-461 IN COMPLEX WITH
SYNTHETIC AGONIST, AND FUNCTION.
PubMed=18237438; DOI=10.1186/1472-6807-8-8;
Bleicher L., Aparicio R., Nunes F.M., Martinez L., Gomes Dias S.M.,
Figueira A.C., Santos M.A., Venturelli W.H., da Silva R., Donate P.M.,
Neves F.A., Simeoni L.A., Baxter J.D., Webb P., Skaf M.S.,
Polikarpov I.;
"Structural basis of GC-1 selectivity for thyroid hormone receptor
isoforms.";
BMC Struct. Biol. 8:8-8(2008).
[23]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 202-461, FUNCTION, AND
MUTAGENESIS OF ASN-331.
PubMed=19926848; DOI=10.1073/pnas.0911024106;
Martinez L., Nascimento A.S., Nunes F.M., Phillips K., Aparicio R.,
Dias S.M., Figueira A.C., Lin J.H., Nguyen P., Apriletti J.W.,
Neves F.A., Baxter J.D., Webb P., Skaf M.S., Polikarpov I.;
"Gaining ligand selectivity in thyroid hormone receptors via
entropy.";
Proc. Natl. Acad. Sci. U.S.A. 106:20717-20722(2009).
[24]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 209-460, FUNCTION, SUBUNIT,
AND MUTAGENESIS OF ASP-355.
PubMed=18798561; DOI=10.1002/prot.22225;
Jouravel N., Sablin E., Togashi M., Baxter J.D., Webb P.,
Fletterick R.J.;
"Molecular basis for dimer formation of TRbeta variant D355R.";
Proteins 75:111-117(2009).
[25]
VARIANT GTHR ARG-345.
PubMed=2510172; DOI=10.1073/pnas.86.22.8977;
Sakurai A., Takeda K., Ain K., Ceccarelli P., Nakai A., Seino S.,
Bell G.I., Refetoff S., Degroot L.;
"Generalized resistance to thyroid hormone associated with a mutation
in the ligand-binding domain of the human thyroid hormone receptor
beta.";
Proc. Natl. Acad. Sci. U.S.A. 86:8977-8981(1989).
[26]
VARIANT GTHR HIS-453.
PubMed=2153155; DOI=10.1172/JCI114438;
Usala S.J., Tennyson G.E., Bale A.E., Lash R.W., Gesundheit N.,
Wondisford F.E., Accili D., Hauser P., Weintraub B.D.;
"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.";
J. Clin. Invest. 85:93-100(1990).
[27]
VARIANT GTHR HIS-340.
PubMed=1846005; DOI=10.1210/jcem-72-1-32;
Usala S.J., Menke J.B., Watson T.L., Berard J., Bradley W.E.C.,
Bale A.E., Lash R.W., Weintraub B.D.;
"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.";
J. Clin. Endocrinol. Metab. 72:32-38(1991).
[28]
VARIANTS GTHR THR-317; ARG-332; VAL-345; GLU-347; VAL-442 AND THR-453.
PubMed=1661299; DOI=10.1172/JCI115542;
Parrilla R., Mixson A.J., McPherson J.A., McClaskey J.H.,
Weintraub B.D.;
"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.";
J. Clin. Invest. 88:2123-2130(1991).
[29]
VARIANT GTHRAR THR-337 DEL.
PubMed=1653889; DOI=10.1210/mend-5-3-327;
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.;
"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.";
Mol. Endocrinol. 5:327-335(1991).
[30]
VARIANT GTHR SER-345.
PubMed=1563081; DOI=10.1111/j.1365-2265.1992.tb01444.x;
Adams M., Nagaya T., Tone Y., Jameson J.L., Chatterjee V.K.K.;
"Functional properties of a novel mutant thyroid hormone receptor in a
family with generalized thyroid hormone resistance syndrome.";
Clin. Endocrinol. (Oxf.) 36:281-289(1992).
[31]
VARIANT GTHR HIS-320.
PubMed=1314846; DOI=10.1210/jcem.74.5.1314846;
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.;
"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.";
J. Clin. Endocrinol. Metab. 74:1164-1170(1992).
[32]
VARIANT GTHR THR-453.
PubMed=1619012; DOI=10.1210/jcem.75.1.1619012;
Shuto Y., Wakabayashi I., Amuro N., Minami S., Okazaki T.;
"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.";
J. Clin. Endocrinol. Metab. 75:213-217(1992).
[33]
VARIANT GTHR GLU-443.
PubMed=1587388; DOI=10.1016/0303-7207(92)90026-3;
Sasaki S., Nakamura H., Tagami T., Miyoshi Y., Tanaka K., Imura H.;
"A point mutation of the T3 receptor beta 1 gene in a kindred of
generalized resistance to thyroid hormone.";
Mol. Cell. Endocrinol. 84:159-166(1992).
[34]
VARIANT GTHR THR-234.
PubMed=1324420; DOI=10.1210/mend.6.7.1324420;
Behr M., Loos U.;
"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.";
Mol. Endocrinol. 6:1119-1126(1992).
[35]
VARIANT PRTH HIS-316.
PubMed=8381821; DOI=10.1172/JCI116233;
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.;
"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.";
J. Clin. Invest. 91:538-546(1993).
[36]
VARIANTS GTHR THR-317; CYS-320; HIS-320; TRP-338; HIS-438 AND THR-453.
PubMed=8514853; DOI=10.1172/JCI116474;
Weiss R.E., Weinberg M., Refetoff S.;
"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.";
J. Clin. Invest. 91:2408-2415(1993).
[37]
VARIANT GTHR ARG-446.
PubMed=8175986; DOI=10.1210/jcem.78.5.8175986;
Weiss R.E., Chyna B., Duell P.B., Hayashi Y., Sunthornthepvarakul T.,
Refetoff S.;
"A new point mutation (C446R) in the thyroid hormone receptor-beta
gene of a family with resistance to thyroid hormone.";
J. Clin. Endocrinol. Metab. 78:1253-1256(1994).
[38]
VARIANT GTHR SER-453.
PubMed=7833659; DOI=10.1089/thy.1994.4.249;
Refetoff S., Weiss R.E., Wing J.R., Sarne D., Chyna B., Hayashi Y.;
"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.";
Thyroid 4:249-254(1994).
[39]
VARIANT GTHR TRP-243.
PubMed=8664910;
DOI=10.1002/(SICI)1098-1004(1996)7:1<79::AID-HUMU15>3.0.CO;2-P;
Pohlenz J., Schoenberger W., Wemme H., Winterpacht A., Wirth S.,
Zabel B.;
"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.";
Hum. Mutat. 7:79-81(1996).
[40]
VARIANTS GTHR THR-317; TRP-338; ILE-342 AND GLU-348.
PubMed=8889584;
DOI=10.1002/(SICI)1098-1004(1996)8:3<247::AID-HUMU8>3.3.CO;2-C;
Seto D., Weintraub B.D.;
"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.";
Hum. Mutat. 8:247-257(1996).
[41]
VARIANT GTHR ILE-426.
PubMed=10660344;
Menzaghi C., di Paola R., Corrias A., Einaudi S., Trischitta V.,
de Sanctis C., de Filippis V.;
"T426I a new mutation in the thyroid hormone receptor gene in a
sporadic patient with resistance to thyroid hormone and dysmorphism.";
Hum. Mutat. 12:289-289(1998).
[42]
VARIANT GTHR TRP-338.
PubMed=16804041; DOI=10.1210/jc.2006-0727;
Mamanasiri S., Yesil S., Dumitrescu A.M., Liao X.-H., Demir T.,
Weiss R.E., Refetoff S.;
"Mosaicism of a thyroid hormone receptor-beta gene mutation in
resistance to thyroid hormone.";
J. Clin. Endocrinol. Metab. 91:3471-3477(2006).
[43]
VARIANTS GTHR GLY-268; ASP-331; PRO-335; PRO-341; PHE-346; MET-431;
THR-447; LEU-453; THR-453 AND CYS-459.
PubMed=19268523; DOI=10.1016/j.mcp.2009.02.002;
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.;
"Genotyping of resistance to thyroid hormone in South American
population. Identification of seven novel missense mutations in the
human thyroid hormone receptor beta gene.";
Mol. Cell. Probes 23:148-153(2009).
-!- FUNCTION: Nuclear hormone receptor that can act as a repressor or
activator of transcription. High affinity receptor for thyroid
hormones, including triiodothyronine and thyroxine.
{ECO:0000269|PubMed:12699376, ECO:0000269|PubMed:14673100,
ECO:0000269|PubMed:16781732, ECO:0000269|PubMed:17418816,
ECO:0000269|PubMed:18237438, ECO:0000269|PubMed:18798561,
ECO:0000269|PubMed:19926848}.
-!- SUBUNIT: 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. {ECO:0000250,
ECO:0000269|PubMed:10713182, ECO:0000269|PubMed:11971969,
ECO:0000269|PubMed:12039952, ECO:0000269|PubMed:12699376,
ECO:0000269|PubMed:14673100, ECO:0000269|PubMed:15466465,
ECO:0000269|PubMed:16781732, ECO:0000269|PubMed:17418816,
ECO:0000269|PubMed:18237438, ECO:0000269|PubMed:18798561,
ECO:0000269|PubMed:7746322}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Beta-1;
IsoId=P10828-1; Sequence=Displayed;
Name=Beta-2;
IsoId=P10828-2, P37243-1;
Sequence=VSP_031077;
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain.
-!- DISEASE: 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).
{ECO:0000269|PubMed:10660344, ECO:0000269|PubMed:12511610,
ECO:0000269|PubMed:12554782, ECO:0000269|PubMed:1314846,
ECO:0000269|PubMed:1324420, ECO:0000269|PubMed:1563081,
ECO:0000269|PubMed:1587388, ECO:0000269|PubMed:1619012,
ECO:0000269|PubMed:1661299, ECO:0000269|PubMed:16804041,
ECO:0000269|PubMed:1846005, ECO:0000269|PubMed:19268523,
ECO:0000269|PubMed:2153155, ECO:0000269|PubMed:2510172,
ECO:0000269|PubMed:7833659, ECO:0000269|PubMed:8175986,
ECO:0000269|PubMed:8514853, ECO:0000269|PubMed:8664910,
ECO:0000269|PubMed:8889584}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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. {ECO:0000269|PubMed:1653889}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:7528740, ECO:0000269|PubMed:8381821}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA35677.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA28412.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M26747; AAA35677.1; ALT_INIT; mRNA.
EMBL; X04707; CAA28412.1; ALT_INIT; mRNA.
EMBL; AK096628; BAG53341.1; -; mRNA.
EMBL; AC012087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC098971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC099054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC112217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW64345.1; -; Genomic_DNA.
EMBL; BC106929; AAI06930.1; -; mRNA.
EMBL; BC106930; AAI06931.1; -; mRNA.
EMBL; AY286465; AAQ23704.1; -; mRNA.
EMBL; AY286466; AAQ23705.1; -; mRNA.
EMBL; AY286467; AAQ23706.1; -; mRNA.
EMBL; AY286468; AAQ23707.1; -; mRNA.
EMBL; AY286469; AAQ23708.1; -; mRNA.
EMBL; AY286470; AAQ23709.1; -; mRNA.
EMBL; AY286471; AAQ23710.1; -; mRNA.
EMBL; X74497; CAA52606.1; -; mRNA.
CCDS; CCDS2641.1; -. [P10828-1]
PIR; A25237; TVHUAR.
PIR; S40152; S40152.
RefSeq; NP_000452.2; NM_000461.4. [P10828-1]
RefSeq; NP_001121648.1; NM_001128176.2. [P10828-1]
RefSeq; NP_001121649.1; NM_001128177.1. [P10828-1]
RefSeq; NP_001239563.1; NM_001252634.1. [P10828-1]
RefSeq; XP_005265478.1; XM_005265421.4.
RefSeq; XP_005265480.1; XM_005265423.4.
RefSeq; XP_005265481.1; XM_005265424.3.
RefSeq; XP_006713380.1; XM_006713317.3.
RefSeq; XP_006713381.1; XM_006713318.3. [P10828-1]
RefSeq; XP_011532348.1; XM_011534046.2. [P10828-1]
RefSeq; XP_011532349.1; XM_011534047.2. [P10828-1]
RefSeq; XP_011532350.1; XM_011534048.2. [P10828-1]
RefSeq; XP_011532351.1; XM_011534049.2.
RefSeq; XP_011532352.1; XM_011534050.2. [P10828-1]
RefSeq; XP_011532353.1; XM_011534051.2.
RefSeq; XP_011532354.1; XM_011534052.2. [P10828-1]
RefSeq; XP_016862597.1; XM_017007108.1. [P10828-1]
RefSeq; XP_016862598.1; XM_017007109.1. [P10828-1]
RefSeq; XP_016862599.1; XM_017007110.1. [P10828-1]
RefSeq; XP_016862600.1; XM_017007111.1. [P10828-1]
RefSeq; XP_016862601.1; XM_017007112.1. [P10828-1]
UniGene; Hs.187861; -.
UniGene; Hs.713754; -.
PDB; 1BSX; X-ray; 3.70 A; A/B=202-461.
PDB; 1N46; X-ray; 2.20 A; A/B=204-461.
PDB; 1NAX; X-ray; 2.70 A; A=209-460.
PDB; 1NQ0; X-ray; 2.40 A; A=202-461.
PDB; 1NQ1; X-ray; 2.90 A; A=202-461.
PDB; 1NQ2; X-ray; 2.40 A; A=202-461.
PDB; 1NUO; X-ray; 3.10 A; A=202-461.
PDB; 1Q4X; X-ray; 2.80 A; A=209-461.
PDB; 1R6G; X-ray; 3.00 A; A=203-461.
PDB; 1XZX; X-ray; 2.50 A; X=202-461.
PDB; 1Y0X; X-ray; 3.10 A; X=202-461.
PDB; 2J4A; X-ray; 2.20 A; A=209-461.
PDB; 2NLL; X-ray; 1.90 A; B=104-204.
PDB; 2PIN; X-ray; 2.30 A; A/B=209-461.
PDB; 3D57; X-ray; 2.20 A; A/B=209-460.
PDB; 3GWS; X-ray; 2.20 A; X=202-460.
PDB; 3IMY; X-ray; 2.55 A; A=202-461.
PDB; 3JZC; X-ray; 2.50 A; A=202-461.
PDB; 4ZO1; X-ray; 3.22 A; X=210-461.
PDBsum; 1BSX; -.
PDBsum; 1N46; -.
PDBsum; 1NAX; -.
PDBsum; 1NQ0; -.
PDBsum; 1NQ1; -.
PDBsum; 1NQ2; -.
PDBsum; 1NUO; -.
PDBsum; 1Q4X; -.
PDBsum; 1R6G; -.
PDBsum; 1XZX; -.
PDBsum; 1Y0X; -.
PDBsum; 2J4A; -.
PDBsum; 2NLL; -.
PDBsum; 2PIN; -.
PDBsum; 3D57; -.
PDBsum; 3GWS; -.
PDBsum; 3IMY; -.
PDBsum; 3JZC; -.
PDBsum; 4ZO1; -.
ProteinModelPortal; P10828; -.
SMR; P10828; -.
BioGrid; 112924; 55.
CORUM; P10828; -.
DIP; DIP-5991N; -.
IntAct; P10828; 12.
MINT; P10828; -.
STRING; 9606.ENSP00000348827; -.
BindingDB; P10828; -.
ChEMBL; CHEMBL1947; -.
DrugBank; DB08085; 1-(4-HEXYLPHENYL)PROP-2-EN-1-ONE.
DrugBank; DB00509; Dextrothyroxine.
DrugBank; DB03788; GC-24.
DrugBank; DB05035; KB2115.
DrugBank; DB00451; Levothyroxine.
DrugBank; DB00279; Liothyronine.
DrugBank; DB01583; Liotrix.
DrugBank; DB05192; MB07811.
GuidetoPHARMACOLOGY; 589; -.
iPTMnet; P10828; -.
PhosphoSitePlus; P10828; -.
BioMuta; THRB; -.
DMDM; 586092; -.
MaxQB; P10828; -.
PaxDb; P10828; -.
PeptideAtlas; P10828; -.
PRIDE; P10828; -.
DNASU; 7068; -.
Ensembl; ENST00000280696; ENSP00000280696; ENSG00000151090. [P10828-2]
Ensembl; ENST00000356447; ENSP00000348827; ENSG00000151090. [P10828-1]
Ensembl; ENST00000396671; ENSP00000379904; ENSG00000151090. [P10828-1]
Ensembl; ENST00000416420; ENSP00000414444; ENSG00000151090. [P10828-1]
GeneID; 7068; -.
KEGG; hsa:7068; -.
UCSC; uc003ccx.5; human. [P10828-1]
CTD; 7068; -.
DisGeNET; 7068; -.
EuPathDB; HostDB:ENSG00000151090.17; -.
GeneCards; THRB; -.
HGNC; HGNC:11799; THRB.
HPA; CAB002008; -.
HPA; CAB002009; -.
HPA; HPA061035; -.
MalaCards; THRB; -.
MIM; 145650; phenotype.
MIM; 188570; phenotype.
MIM; 190160; gene.
MIM; 274300; phenotype.
neXtProt; NX_P10828; -.
OpenTargets; ENSG00000151090; -.
Orphanet; 3221; Generalized resistance to thyroid hormone.
Orphanet; 97927; Peripheral resistance to thyroid hormones.
Orphanet; 165994; Selective pituitary resistance to thyroid hormone.
PharmGKB; PA36508; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00870000136372; -.
HOGENOM; HOG000010313; -.
HOVERGEN; HBG005606; -.
InParanoid; P10828; -.
KO; K08362; -.
OMA; QEWELIK; -.
OrthoDB; EOG091G0GC1; -.
PhylomeDB; P10828; -.
TreeFam; TF328382; -.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
SignaLink; P10828; -.
SIGNOR; P10828; -.
ChiTaRS; THRB; human.
EvolutionaryTrace; P10828; -.
GeneWiki; Thyroid_hormone_receptor_beta; -.
GenomeRNAi; 7068; -.
PRO; PR:P10828; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000151090; -.
CleanEx; HS_THRB; -.
ExpressionAtlas; P10828; baseline and differential.
Genevisible; P10828; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0003700; F:DNA binding transcription factor activity; NAS:ProtInc.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISM:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0070324; F:thyroid hormone binding; IDA:UniProtKB.
GO; GO:0004887; F:thyroid hormone receptor activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
GO; GO:0008050; P:female courtship behavior; IEA:Ensembl.
GO; GO:0007621; P:negative regulation of female receptivity; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0008016; P:regulation of heart contraction; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; TAS:ProtInc.
GO; GO:0060509; P:Type I pneumocyte differentiation; IEA:Ensembl.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR001728; ThyrH_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
PRINTS; PR00546; THYROIDHORMR.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Deafness;
Disease mutation; DNA-binding; Metal-binding; Nucleus; Polymorphism;
Receptor; Reference proteome; Transcription; Transcription regulation;
Zinc; Zinc-finger.
CHAIN 1 461 Thyroid hormone receptor beta.
/FTId=PRO_0000053446.
DOMAIN 217 461 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 107 181 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 107 127 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 145 169 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 106 Modulating.
REGION 244 461 Interaction with NR2F6.
{ECO:0000269|PubMed:10713182}.
BINDING 282 282 Thyroid hormone.
BINDING 320 320 Thyroid hormone.
BINDING 331 331 Thyroid hormone; via amide nitrogen.
BINDING 435 435 Thyroid hormone.
VAR_SEQ 1 93 MTPNSMTENGLTAWDKPKHCPDREHDWKLVGMSEACLHRKS
HSERRSTLKNEQSSPHLIQTTWTSSIFHLDHDDVNDQSVSS
AQTFQTEEKKC -> MNYCMQEIYEVHPAAGSNCYMQSTDY
YAYFEDSPGYSGCDAQAVPSNNIYMEQAWAVNQPYTCSYPG
NMFKSKDSDLDMALNQYSQPEYFTEEKPTFSQVQSPSYSQK
(in isoform Beta-2). {ECO:0000303|Ref.9}.
/FTId=VSP_031077.
VARIANT 216 216 D -> G (in dbSNP:rs9865746).
/FTId=VAR_050577.
VARIANT 234 234 A -> T (in GTHR; impairs hormone binding
and ligand-dependent conformational
changes; dbSNP:rs121918694).
{ECO:0000269|PubMed:12511610,
ECO:0000269|PubMed:1324420}.
/FTId=VAR_004632.
VARIANT 243 243 R -> W (in GTHR; dbSNP:rs121918707).
{ECO:0000269|PubMed:8664910}.
/FTId=VAR_004633.
VARIANT 268 268 A -> G (in GTHR).
{ECO:0000269|PubMed:19268523}.
/FTId=VAR_059041.
VARIANT 316 316 R -> H (in PRTH; impairs hormone binding;
dbSNP:rs121918695).
{ECO:0000269|PubMed:12554782,
ECO:0000269|PubMed:8381821}.
/FTId=VAR_004634.
VARIANT 317 317 A -> T (in GTHR; impairs hormone binding;
dbSNP:rs121918690).
{ECO:0000269|PubMed:12554782,
ECO:0000269|PubMed:1661299,
ECO:0000269|PubMed:8514853,
ECO:0000269|PubMed:8889584}.
/FTId=VAR_004635.
VARIANT 320 320 R -> C (in GTHR; dbSNP:rs121918696).
{ECO:0000269|PubMed:8514853}.
/FTId=VAR_004636.
VARIANT 320 320 R -> H (in GTHR; dbSNP:rs121918693).
{ECO:0000269|PubMed:1314846,
ECO:0000269|PubMed:8514853}.
/FTId=VAR_004637.
VARIANT 331 331 N -> D (in GTHR).
{ECO:0000269|PubMed:19268523}.
/FTId=VAR_059042.
VARIANT 332 332 G -> R (in GTHR; dbSNP:rs28999969).
{ECO:0000269|PubMed:1661299}.
/FTId=VAR_004638.
VARIANT 335 335 A -> P (in GTHR).
{ECO:0000269|PubMed:19268523}.
/FTId=VAR_059043.
VARIANT 337 337 T -> I (in dbSNP:rs1054624).
{ECO:0000269|PubMed:2879243,
ECO:0000269|PubMed:3034496}.
/FTId=VAR_011784.
VARIANT 337 337 Missing (in GTHRAR).
{ECO:0000269|PubMed:1653889}.
/FTId=VAR_004639.
VARIANT 338 338 R -> W (in GTHR; dbSNP:rs121918697).
{ECO:0000269|PubMed:16804041,
ECO:0000269|PubMed:8514853,
ECO:0000269|PubMed:8889584}.
/FTId=VAR_004640.
VARIANT 340 340 Q -> H (in GTHR; dbSNP:rs121918688).
{ECO:0000269|PubMed:1846005}.
/FTId=VAR_004641.
VARIANT 341 341 L -> P (in GTHR).
{ECO:0000269|PubMed:19268523}.
/FTId=VAR_059044.
VARIANT 342 342 K -> I (in GTHR).
{ECO:0000269|PubMed:8889584}.
/FTId=VAR_004642.
VARIANT 345 345 G -> R (in GTHR; dbSNP:rs121918686).
{ECO:0000269|PubMed:2510172}.
/FTId=VAR_004645.
VARIANT 345 345 G -> S (in GTHR; dbSNP:rs121918686).
{ECO:0000269|PubMed:1563081}.
/FTId=VAR_004644.
VARIANT 345 345 G -> V (in GTHR; dbSNP:rs28999970).
{ECO:0000269|PubMed:1661299}.
/FTId=VAR_004643.
VARIANT 346 346 L -> F (in GTHR).
{ECO:0000269|PubMed:19268523}.
/FTId=VAR_059045.
VARIANT 347 347 G -> E (in GTHR; dbSNP:rs28999971).
{ECO:0000269|PubMed:1661299}.
/FTId=VAR_004646.
VARIANT 348 348 V -> E (in GTHR).
{ECO:0000269|PubMed:8889584}.
/FTId=VAR_004647.
VARIANT 426 426 T -> I (in GTHR).
{ECO:0000269|PubMed:10660344}.
/FTId=VAR_004648.
VARIANT 429 429 R -> Q (in PRTH).
{ECO:0000269|PubMed:7528740}.
/FTId=VAR_058508.
VARIANT 431 431 I -> M (in GTHR).
{ECO:0000269|PubMed:19268523}.
/FTId=VAR_059046.
VARIANT 438 438 R -> H (in GTHR; dbSNP:rs121918698).
{ECO:0000269|PubMed:8514853}.
/FTId=VAR_004649.
VARIANT 442 442 M -> V (in GTHR; dbSNP:rs121918691).
{ECO:0000269|PubMed:1661299}.
/FTId=VAR_004650.
VARIANT 443 443 K -> E (in GTHR; dbSNP:rs121918692).
{ECO:0000269|PubMed:1587388}.
/FTId=VAR_004651.
VARIANT 446 446 C -> R (in GTHR; dbSNP:rs121918703).
{ECO:0000269|PubMed:8175986}.
/FTId=VAR_004652.
VARIANT 447 447 P -> T (in GTHR).
{ECO:0000269|PubMed:19268523}.
/FTId=VAR_059047.
VARIANT 453 453 P -> H (in GTHR; dbSNP:rs121918687).
{ECO:0000269|PubMed:2153155}.
/FTId=VAR_004653.
VARIANT 453 453 P -> L (in GTHR).
{ECO:0000269|PubMed:19268523}.
/FTId=VAR_059048.
VARIANT 453 453 P -> S (in GTHR).
{ECO:0000269|PubMed:7833659}.
/FTId=VAR_004654.
VARIANT 453 453 P -> T (in GTHR; dbSNP:rs28933408).
{ECO:0000269|PubMed:1619012,
ECO:0000269|PubMed:1661299,
ECO:0000269|PubMed:19268523,
ECO:0000269|PubMed:8514853}.
/FTId=VAR_004655.
VARIANT 459 459 F -> C (in GTHR; dbSNP:rs121918702).
{ECO:0000269|PubMed:19268523}.
/FTId=VAR_059049.
MUTAGEN 207 208 SI->AA: Modestly inhibits homodimer
formation on a minimal response element
(in vitro).
{ECO:0000269|PubMed:16781732}.
MUTAGEN 207 208 SI->KK: Inhibits homodimer formation on a
minimal response element (in vitro).
{ECO:0000269|PubMed:16781732}.
MUTAGEN 243 243 R->Q: Impairs hormone binding and ligand-
dependent conformational changes.
{ECO:0000269|PubMed:12511610}.
MUTAGEN 331 331 N->S: No effect on thyroid hormone
binding. {ECO:0000269|PubMed:14673100,
ECO:0000269|PubMed:19926848}.
MUTAGEN 355 355 D->R: Stabilizes homodimer.
{ECO:0000269|PubMed:18798561}.
CONFLICT 243 243 R -> P (in Ref. 1; AAA35677 and 2;
CAA28412). {ECO:0000305}.
CONFLICT 451 451 F -> L (in Ref. 1; AAA35677 and 2;
CAA28412). {ECO:0000305}.
TURN 108 110 {ECO:0000244|PDB:2NLL}.
STRAND 116 118 {ECO:0000244|PDB:2NLL}.
HELIX 125 136 {ECO:0000244|PDB:2NLL}.
HELIX 140 142 {ECO:0000244|PDB:2NLL}.
TURN 155 159 {ECO:0000244|PDB:2NLL}.
HELIX 162 171 {ECO:0000244|PDB:2NLL}.
HELIX 176 178 {ECO:0000244|PDB:2NLL}.
HELIX 182 195 {ECO:0000244|PDB:2NLL}.
HELIX 198 205 {ECO:0000244|PDB:2NLL}.
TURN 207 209 {ECO:0000244|PDB:1Y0X}.
HELIX 216 230 {ECO:0000244|PDB:1N46}.
TURN 234 237 {ECO:0000244|PDB:3GWS}.
HELIX 239 242 {ECO:0000244|PDB:2J4A}.
TURN 248 251 {ECO:0000244|PDB:1N46}.
STRAND 260 263 {ECO:0000244|PDB:1N46}.
HELIX 266 273 {ECO:0000244|PDB:1N46}.
HELIX 276 288 {ECO:0000244|PDB:1N46}.
HELIX 293 295 {ECO:0000244|PDB:1N46}.
HELIX 298 319 {ECO:0000244|PDB:1N46}.
TURN 323 326 {ECO:0000244|PDB:1N46}.
STRAND 327 330 {ECO:0000244|PDB:1N46}.
TURN 331 333 {ECO:0000244|PDB:1N46}.
STRAND 334 336 {ECO:0000244|PDB:1N46}.
HELIX 338 343 {ECO:0000244|PDB:1N46}.
TURN 344 348 {ECO:0000244|PDB:1N46}.
HELIX 349 360 {ECO:0000244|PDB:1N46}.
HELIX 361 363 {ECO:0000244|PDB:1N46}.
HELIX 367 378 {ECO:0000244|PDB:1N46}.
HELIX 389 410 {ECO:0000244|PDB:1N46}.
STRAND 413 416 {ECO:0000244|PDB:1R6G}.
HELIX 417 445 {ECO:0000244|PDB:1N46}.
HELIX 448 450 {ECO:0000244|PDB:1N46}.
HELIX 453 459 {ECO:0000244|PDB:1N46}.
SEQUENCE 461 AA; 52788 MW; 6770BB0D372A7CAA CRC64;
MTPNSMTENG LTAWDKPKHC PDREHDWKLV GMSEACLHRK SHSERRSTLK NEQSSPHLIQ
TTWTSSIFHL DHDDVNDQSV SSAQTFQTEE KKCKGYIPSY LDKDELCVVC GDKATGYHYR
CITCEGCKGF FRRTIQKNLH PSYSCKYEGK CVIDKVTRNQ CQECRFKKCI YVGMATDLVL
DDSKRLAKRK LIEENREKRR REELQKSIGH KPEPTDEEWE LIKTVTEAHV ATNAQGSHWK
QKRKFLPEDI GQAPIVNAPE GGKVDLEAFS HFTKIITPAI TRVVDFAKKL PMFCELPCED
QIILLKGCCM EIMSLRAAVR YDPESETLTL NGEMAVTRGQ LKNGGLGVVS DAIFDLGMSL
SSFNLDDTEV ALLQAVLLMS SDRPGLACVE RIEKYQDSFL LAFEHYINYR KHHVTHFWPK
LLMKVTDLRM IGACHASRFL HMKVECPTEL FPPLFLEVFE D


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