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Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)

 RXRA_HUMAN              Reviewed;         462 AA.
P19793; B3KY83; Q2NL52; Q2V504;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
11-DEC-2019, entry version 232.
RecName: Full=Retinoic acid receptor RXR-alpha;
AltName: Full=Nuclear receptor subfamily 2 group B member 1;
AltName: Full=Retinoid X receptor alpha;
Name=RXRA; Synonyms=NR2B1;
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 1), AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=2159111; DOI=10.1038/345224a0;
Mangelsdorf D.J., Ong E.S., Dyck J.A., Evans R.M.;
"Nuclear receptor that identifies a novel retinoic acid response pathway.";
Nature 345:224-229(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DNA-BINDING.
PubMed=18619963; DOI=10.1016/j.febslet.2008.07.003;
Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T.;
"DNA-binding profiling of human hormone nuclear receptors via fluorescence
correlation spectroscopy in a cell-free system.";
FEBS Lett. 582:2737-2744(2008).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
TISSUE=Amygdala;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-462.
NIEHS SNPs program;
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, AND IDENTIFICATION OF LIGAND.
PubMed=1310260; DOI=10.1016/0092-8674(92)90479-v;
Heyman R.A., Mangelsdorf D.J., Dyck J.A., Stein R.B., Eichele G.,
Evans R.M., Thaller C.;
"9-cis retinoic acid is a high affinity ligand for the retinoid X
receptor.";
Cell 68:397-406(1992).
[9]
FUNCTION, AND INTERACTION WITH NCOA3.
PubMed=9267036; DOI=10.1016/s0092-8674(00)80516-4;
Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L.,
Privalsky M.L., Nakatani Y., Evans R.M.;
"Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and
forms a multimeric activation complex with P/CAF and CBP/p300.";
Cell 90:569-580(1997).
[10]
INTERACTION WITH NCOA6.
PubMed=10567404; DOI=10.1074/jbc.274.48.34283;
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.;
"A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator
essential for ligand-dependent transactivation by nuclear receptors in
vivo.";
J. Biol. Chem. 274:34283-34293(1999).
[11]
FUNCTION, AND HETERODIMERIZATION WITH PPARA.
PubMed=10195690; DOI=10.1016/s0303-7207(98)00217-2;
Gorla-Bajszczak A., Juge-Aubry C., Pernin A., Burger A.G., Meier C.A.;
"Conserved amino acids in the ligand-binding and tau(i) domains of the
peroxisome proliferator-activated receptor alpha are necessary for
heterodimerization with RXR.";
Mol. Cell. Endocrinol. 147:37-47(1999).
[12]
FUNCTION, PHOSPHORYLATION AT SER-27, AND MUTAGENESIS OF SER-27.
PubMed=11162439; DOI=10.1006/bbrc.2000.4043;
Harish S., Ashok M.S., Khanam T., Rangarajan P.N.;
"Serine 27, a human retinoid X receptor alpha residue, phosphorylated by
protein kinase A is essential for cyclicAMP-mediated downregulation of
RXRalpha function.";
Biochem. Biophys. Res. Commun. 279:853-857(2000).
[13]
INTERACTION WITH SFPQ.
PubMed=11259580; DOI=10.1128/mcb.21.7.2298-2311.2001;
Mathur M., Tucker P.W., Samuels H.H.;
"PSF is a novel corepressor that mediates its effect through Sin3A and the
DNA binding domain of nuclear hormone receptors.";
Mol. Cell. Biol. 21:2298-2311(2001).
[14]
INTERACTION WITH HCV CORE PROTEIN (MICROBIAL INFECTION) AND PPARA,
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=11915042; DOI=10.1053/jhep.2002.32470;
Tsutsumi T., Suzuki T., Shimoike T., Suzuki R., Moriya K., Shintani Y.,
Fujie H., Matsuura Y., Koike K., Miyamura T.;
"Interaction of hepatitis C virus core protein with retinoid X receptor
alpha modulates its transcriptional activity.";
Hepatology 35:937-946(2002).
[15]
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).
[16]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 158-PHE-PHE-159 AND
160-LYS--LYS-165.
PubMed=12145331; DOI=10.1210/me.2001-0345;
Pruefer K., Barsony J.;
"Retinoid X receptor dominates the nuclear import and export of the
unliganded vitamin D receptor.";
Mol. Endocrinol. 16:1738-1751(2002).
[17]
INTERACTION WITH DNTTIP2.
PubMed=15047147; DOI=10.1016/j.bbrc.2004.02.179;
Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M.,
Zhu Y.-J.;
"ERBP, a novel estrogen receptor binding protein enhancing the activity of
estrogen receptor.";
Biochem. Biophys. Res. Commun. 317:54-59(2004).
[18]
INTERACTION WITH RNF8.
PubMed=14981089; DOI=10.1074/jbc.m309148200;
Takano Y., Adachi S., Okuno M., Muto Y., Yoshioka T.,
Matsushima-Nishiwaki R., Tsurumi H., Ito K., Friedman S.L., Moriwaki H.,
Kojima S., Okano Y.;
"The RING finger protein, RNF8, interacts with retinoid X receptor alpha
and enhances its transcription-stimulating activity.";
J. Biol. Chem. 279:18926-18934(2004).
[19]
INTERACTION WITH RARA AND NR4A1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
357-MET--MET-360 AND 418-LEU--LEU-430.
PubMed=15509776; DOI=10.1128/mcb.24.22.9705-9725.2004;
Cao X., Liu W., Lin F., Li H., Kolluri S.K., Lin B., Han Y.H., Dawson M.I.,
Zhang X.K.;
"Retinoid X receptor regulates Nur77/TR3-dependent apoptosis [corrected] by
modulating its nuclear export and mitochondrial targeting.";
Mol. Cell. Biol. 24:9705-9725(2004).
[20]
INTERACTION WITH PELP1.
PubMed=16574651; DOI=10.1074/jbc.m601593200;
Singh R.R., Gururaj A.E., Vadlamudi R.K., Kumar R.;
"9-cis-retinoic acid up-regulates expression of transcriptional coregulator
PELP1, a novel coactivator of the retinoid X receptor alpha pathway.";
J. Biol. Chem. 281:15394-15404(2006).
[21]
SUMOYLATION AT LYS-108, AND INTERACTION WITH SENP6.
PubMed=16912044; DOI=10.1074/jbc.m604033200;
Choi S.J., Chung S.S., Rho E.J., Lee H.W., Lee M.H., Choi H.S., Seol J.H.,
Baek S.H., Bang O.S., Chung C.H.;
"Negative modulation of RXRalpha transcriptional activity by small
ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-
specific protease SUSP1.";
J. Biol. Chem. 281:30669-30677(2006).
[22]
SUBUNIT, INTERACTION WITH EP300 AND NR4A1, SUBCELLULAR LOCATION,
ACETYLATION AT LYS-145 BY EP300, AND MUTAGENESIS OF 133-HIS--LYS-156;
LYS-145; 206-GLN--ASN-216 AND 352-GLU--THR-462.
PubMed=17761950; DOI=10.1210/me.2007-0107;
Zhao W.X., Tian M., Zhao B.X., Li G.D., Liu B., Zhan Y.Y., Chen H.Z.,
Wu Q.;
"Orphan receptor TR3 attenuates the p300-induced acetylation of retinoid X
receptor-alpha.";
Mol. Endocrinol. 21:2877-2889(2007).
[23]
HETERODIMERIZATION WITH RARA.
PubMed=17205979; DOI=10.1074/mcp.m600223-mcp200;
Huq M.D., Tsai N.-P., Khan S.A., Wei L.-N.;
"Lysine trimethylation of retinoic acid receptor-alpha: a novel means to
regulate receptor function.";
Mol. Cell. Proteomics 6:677-688(2007).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[25]
INTERACTION WITH BHLHE40/DEC1; BHLHE41/DEC2; NCOA1; MED1; NCOR1 AND NCOR2.
PubMed=19786558; DOI=10.1124/mol.109.057000;
Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K., Kato Y.,
Makishima M.;
"The basic helix-loop-helix proteins differentiated embryo chondrocyte
(DEC) 1 and DEC2 function as corepressors of retinoid X receptors.";
Mol. Pharmacol. 76:1360-1369(2009).
[26]
INTERACTION WITH TACC1.
PubMed=20078863; DOI=10.1186/1471-2199-11-3;
Guyot R., Vincent S., Bertin J., Samarut J., Ravel-Chapuis P.;
"The transforming acidic coiled coil (TACC1) protein modulates the
transcriptional activity of the nuclear receptors TR and RAR.";
BMC Mol. Biol. 11:3-3(2010).
[27]
FUNCTION, HETERODIMERIZATION WITH RARA, AND MUTAGENESIS OF SER-27.
PubMed=20215566; DOI=10.1210/en.2009-1338;
Santos N.C., Kim K.H.;
"Activity of retinoic acid receptor-alpha is directly regulated at its
protein kinase A sites in response to follicle-stimulating hormone
signaling.";
Endocrinology 151:2361-2372(2010).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS], AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[31]
FUNCTION.
PubMed=25417649; DOI=10.1038/ncomms6494;
Ma F., Liu S.Y., Razani B., Arora N., Li B., Kagechika H., Tontonoz P.,
Nunez V., Ricote M., Cheng G.;
"Retinoid X receptor alpha attenuates host antiviral response by
suppressing type I interferon.";
Nat. Commun. 5:5494-5494(2014).
[32]
FUNCTION, TISSUE SPECIFICITY, AND REPRESSION BY AGING.
PubMed=26463675; DOI=10.1093/brain/awv289;
Natrajan M.S., de la Fuente A.G., Crawford A.H., Linehan E., Nunez V.,
Johnson K.R., Wu T., Fitzgerald D.C., Ricote M., Bielekova B.,
Franklin R.J.;
"Retinoid X receptor activation reverses age-related deficiencies in myelin
debris phagocytosis and remyelination.";
Brain 138:3581-3597(2015).
[33]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[34]
FUNCTION, INTERACTION WITH RARA, SUBCELLULAR LOCATION, AND INDUCTION BY
PULSATILE SHEAR STRESS.
PubMed=28167758; DOI=10.1073/pnas.1621425114;
Lee D.Y., Lin T.E., Lee C.I., Zhou J., Huang Y.H., Lee P.L., Shih Y.T.,
Chien S., Chiu J.J.;
"MicroRNA-10a is crucial for endothelial response to different flow
patterns via interaction of retinoid acid receptors and histone
deacetylases.";
Proc. Natl. Acad. Sci. U.S.A. 114:2072-2077(2017).
[35]
INTERACTION WITH VDR.
PubMed=28698609; DOI=10.1038/s41598-017-05081-x;
Tamura M., Ishizawa M., Isojima T., Oezen S., Oka A., Makishima M.,
Kitanaka S.;
"Functional analyses of a novel missense and other mutations of the vitamin
D receptor in association with alopecia.";
Sci. Rep. 7:5102-5102(2017).
[36]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=30216632; DOI=10.1111/acel.12831;
Ma X., Warnier M., Raynard C., Ferrand M., Kirsh O., Defossez P.A.,
Martin N., Bernard D.;
"The nuclear receptor RXRA controls cellular senescence by regulating
calcium signaling.";
Aging Cell 17:E12831-E12831(2018).
[37]
STRUCTURE BY NMR OF 130-223.
PubMed=7925381; DOI=10.1111/j.1432-1033.1994.00639.x;
Lee M.S., Sem D.S., Kliewer S.A., Provencal J., Evans R.M., Wright P.E.;
"NMR assignments and secondary structure of the retinoid X receptor alpha
DNA-binding domain. Evidence for the novel C-terminal helix.";
Eur. J. Biochem. 224:639-650(1994).
[38]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 130-209.
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).
[39]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 225-462.
PubMed=7760929; DOI=10.1038/375377a0;
Bourguet W., Ruff M., Chambon P., Gronemeyer H., Moras D.;
"Crystal structure of the ligand-binding domain of the human nuclear
receptor RXR-alpha.";
Nature 375:377-382(1995).
[40]
STRUCTURE BY NMR OF 130-212.
PubMed=9698548; DOI=10.1006/jmbi.1998.1908;
Holmbeck S.M., Foster M.P., Casimiro D.R., Sem D.S., Dyson H.J.,
Wright P.E.;
"High-resolution solution structure of the retinoid X receptor DNA-binding
domain.";
J. Mol. Biol. 281:271-284(1998).
[41]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 129-209 IN COMPLEX WITH RARA AND
DNA.
PubMed=10698945; DOI=10.1093/emboj/19.5.1045;
Rastinejad F., Wagner T., Zhao Q., Khorasanizadeh S.;
"Structure of the RXR-RAR DNA-binding complex on the retinoic acid response
element DR1.";
EMBO J. 19:1045-1054(2000).
[42]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 224-462 OF APO AND HOLO FORMS.
PubMed=10835357; DOI=10.1093/emboj/19.11.2592;
Egea P.F., Mitschler A., Rochel N., Ruff M., Chambon P., Moras D.;
"Crystal structure of the human RXRalpha ligand-binding domain bound to its
natural ligand: 9-cis retinoic acid.";
EMBO J. 19:2592-2601(2000).
[43]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 225-462 OF APO AND HOLO FORMS.
PubMed=10970886; DOI=10.1101/gad.802300;
Gampe R.T. Jr., Montana V.G., Lambert M.H., Wisely G.B., Milburn M.V.,
Xu H.E.;
"Structural basis for autorepression of retinoid X receptor by tetramer
formation and the AF-2 helix.";
Genes Dev. 14:2229-2241(2000).
[44] {ECO:0000244|PDB:1BY4}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 129-209 IN COMPLEX WITH ZINC AND
DNA, AND SUBUNIT.
PubMed=10669605; DOI=10.1006/jmbi.1999.3457;
Zhao Q., Chasse S.A., Devarakonda S., Sierk M.L., Ahvazi B., Rastinejad F.;
"Structural basis of RXR-DNA interactions.";
J. Mol. Biol. 296:509-520(2000).
[45]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 225-462 IN COMPLEX WITH PPARG;
COACTIVATOR NCOA1; RETINOIC ACID AND SYNTHETIC ANTIDIABETIC AGONISTS
ROSIGLITAZONE AND GI262570.
PubMed=10882139; DOI=10.1016/s1097-2765(00)80448-7;
Gampe R.T. Jr., Montana V.G., Lambert M.H., Miller A.B., Bledsoe R.K.,
Milburn M.V., Kliewer S.A., Willson T.M., Xu H.E.;
"Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the
molecular basis of heterodimerization among nuclear receptors.";
Mol. Cell 5:545-555(2000).
[46]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 225-462 IN COMPLEX WITH PPARA OR
PPARG; 9-CIS RETINOIC ACID; COACTIVATOR NCOA1 AND PPAR SYNTHETIC AGONIST
GW409544.
PubMed=11698662; DOI=10.1073/pnas.241410198;
Xu H.E., Lambert M.H., Montana V.G., Plunket K.D., Moore L.B.,
Collins J.L., Oplinger J.A., Kliewer S.A., Gampe R.T. Jr., McKee D.D.,
Moore J.T., Willson T.M.;
"Structural determinants of ligand binding selectivity between the
peroxisome proliferator-activated receptors.";
Proc. Natl. Acad. Sci. U.S.A. 98:13919-13924(2001).
[47]
X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 227-458 IN COMPLEX WITH
M.MUSCULUS NR1I13; R.NORVEGICUS NCOA2 AND AGONIST INSECTICIDE CONTAMINANT
TCPOBOP.
PubMed=15610733; DOI=10.1016/S1097-2765(04)00727-0;
Suino K., Peng L., Reynolds R., Li Y., Cha J.Y., Repa J.J., Kliewer S.A.,
Xu H.E.;
"The nuclear xenobiotic receptor CAR: structural determinants of
constitutive activation and heterodimerization.";
Mol. Cell 16:893-905(2004).
[48] {ECO:0000244|PDB:2ACL}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 225-462 IN COMPLEX WITH 9-CIS
RETINOIC ACID, AND FUNCTION.
PubMed=16107141; DOI=10.1021/jm050532w;
Jaye M.C., Krawiec J.A., Campobasso N., Smallwood A., Qiu C., Lu Q.,
Kerrigan J.J., De Los Frailes Alvaro M., Laffitte B., Liu W.S.,
Marino J.P. Jr., Meyer C.R., Nichols J.A., Parks D.J., Perez P.,
Sarov-Blat L., Seepersaud S.D., Steplewski K.M., Thompson S.K., Wang P.,
Watson M.A., Webb C.L., Haigh D., Caravella J.A., Macphee C.H.,
Willson T.M., Collins J.L.;
"Discovery of substituted maleimides as liver X receptor agonists and
determination of a ligand-bound crystal structure.";
J. Med. Chem. 48:5419-5422(2005).
[49] {ECO:0000244|PDB:3FAL}
X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 225-462 IN COMPLEX WITH 9-CIS
RETINOIC ACID, AND FUNCTION.
PubMed=18800767; DOI=10.1021/jm800612u;
Chao E.Y., Caravella J.A., Watson M.A., Campobasso N., Ghisletti S.,
Billin A.N., Galardi C., Wang P., Laffitte B.A., Iannone M.A.,
Goodwin B.J., Nichols J.A., Parks D.J., Stewart E., Wiethe R.W.,
Williams S.P., Smallwood A., Pearce K.H., Glass C.K., Willson T.M.,
Zuercher W.J., Collins J.L.;
"Structure-guided design of N-phenyl tertiary amines as transrepression-
selective liver X receptor modulators with anti-inflammatory activity.";
J. Med. Chem. 51:5758-5765(2008).
[50] {ECO:0000244|PDB:3FC6}
X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 225-462 IN COMPLEX WITH 9-CIS
RETINOIC ACID, AND FUNCTION.
PubMed=19167885; DOI=10.1016/j.bmcl.2009.01.004;
Washburn D.G., Hoang T.H., Campobasso N., Smallwood A., Parks D.J.,
Webb C.L., Frank K.A., Nord M., Duraiswami C., Evans C., Jaye M.,
Thompson S.K.;
"Synthesis and SAR of potent LXR agonists containing an indole
pharmacophore.";
Bioorg. Med. Chem. Lett. 19:1097-1100(2009).
[51] {ECO:0000244|PDB:5UAN}
X-RAY CRYSTALLOGRAPHY (3.51 ANGSTROMS) OF 98-462 IN COMPLEX WITH RARB AND
DNA, AND FUNCTION.
PubMed=29021580; DOI=10.1038/s41467-017-00981-y;
Chandra V., Wu D., Li S., Potluri N., Kim Y., Rastinejad F.;
"The quaternary architecture of RARbeta-RXRalpha heterodimer facilitates
domain-domain signal transmission.";
Nat. Commun. 8:868-868(2017).
[52] {ECO:0000244|PDB:6A5Y}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 225-462 IN COMPLEX WITH NR1H4;
NCOA1 PEPTIDE AND 9-CIS-RETINOIC ACID, AND MUTAGENESIS OF GLU-434.
PubMed=30275017; DOI=10.1074/jbc.ra118.004652;
Wang N., Zou Q., Xu J., Zhang J., Liu J.;
"Ligand binding and heterodimerization with retinoid X receptor alpha
(RXRalpha) induce farnesoid X receptor (FXR) conformational changes
affecting coactivator binding.";
J. Biol. Chem. 293:18180-18191(2018).
-!- FUNCTION: Receptor for retinoic acid that acts as a transcription
factor (PubMed:11162439, PubMed:11915042). Forms homo- or heterodimers
with retinoic acid receptors (RARs) and binds to target response
elements in response to their ligands, all-trans or 9-cis retinoic
acid, to regulate gene expression in various biological processes
(PubMed:10195690, PubMed:11162439, PubMed:11915042, PubMed:28167758,
PubMed:17761950, PubMed:16107141, PubMed:18800767, PubMed:19167885).
The RAR/RXR heterodimers bind to the retinoic acid response elements
(RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to
regulate transcription (PubMed:10195690, PubMed:11162439,
PubMed:11915042, PubMed:17761950, PubMed:28167758). The high affinity
ligand for retinoid X receptors (RXRs) is 9-cis retinoic acid
(PubMed:1310260). In the absence of ligand, the RXR-RAR heterodimers
associate with a multiprotein complex containing transcription
corepressors that induce histone deacetylation, chromatin condensation
and transcriptional suppression (PubMed:20215566). On ligand binding,
the corepressors dissociate from the receptors and coactivators are
recruited leading to transcriptional activation (PubMed:20215566,
PubMed:9267036). Serves as a common heterodimeric partner for a number
of nuclear receptors, such as RARA, RARB and PPARA (PubMed:10195690,
PubMed:11915042, PubMed:28167758, PubMed:29021580). The RXRA/RARB
heterodimer can act as a transcriptional repressor or transcriptional
activator, depending on the RARE DNA element context (PubMed:29021580).
The RXRA/PPARA heterodimer is required for PPARA transcriptional
activity on fatty acid oxidation genes such as ACOX1 and the P450
system genes (PubMed:10195690). Together with RARA, positively
regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1
signaling response to pulsatile shear stress in vascular endothelial
cells (PubMed:28167758). Acts as an enhancer of RARA binding to RARE
DNA element (PubMed:28167758). May facilitate the nuclear import of
heterodimerization partners such as VDR and NR4A1 (PubMed:12145331,
PubMed:15509776). Promotes myelin debris phagocytosis and remyelination
by macrophages (PubMed:26463675). Plays a role in the attenuation of
the innate immune system in response to viral infections, possibly by
negatively regulating the transcription of antiviral genes such as type
I IFN genes (PubMed:25417649). Involved in the regulation of calcium
signaling by repressing ITPR2 gene expression, thereby controlling
cellular senescence (PubMed:30216632). {ECO:0000269|PubMed:10195690,
ECO:0000269|PubMed:11162439, ECO:0000269|PubMed:11915042,
ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:1310260,
ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:16107141,
ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:18800767,
ECO:0000269|PubMed:19167885, ECO:0000269|PubMed:20215566,
ECO:0000269|PubMed:25417649, ECO:0000269|PubMed:26463675,
ECO:0000269|PubMed:28167758, ECO:0000269|PubMed:29021580,
ECO:0000269|PubMed:30216632, ECO:0000269|PubMed:9267036}.
-!- SUBUNIT: Homodimer (PubMed:10669605, PubMed:17761950). Heterodimer (via
C-terminus) with RARA; required for ligand-dependent retinoic acid
receptor transcriptional activity; association with RARA is enhanced by
pulsatile shear stress (PubMed:28167758, PubMed:10698945,
PubMed:15509776). Heterodimer with PPARA (via the leucine-like zipper
in the LBD); the interaction is required for PPARA transcriptional
activity (PubMed:10195690, PubMed:11915042, PubMed:11698662).
Heterodimerizes with PPARG (PubMed:10882139, PubMed:11698662).
Heterodimerizes (via NR LBD) with RARB (PubMed:29021580).
Heterodimerizes with NR1H4; the heterodimerization enhances the binding
affinity for LXXLL motifs from coactivators (PubMed:30275017).
Interacts with NCOA3 and NCOA6 coactivators (PubMed:9267036,
PubMed:10567404). Interacts with coactivator FAM120B (By similarity).
Interacts with coactivator PELP1, SENP6, SFPQ, DNTTIP2 and RNF8
(PubMed:16574651, PubMed:16912044, PubMed:11259580, PubMed:15047147,
PubMed:14981089). Interacts with PRMT2 (PubMed:12039952). Interacts
with ASXL1 (By similarity). Interacts with BHLHE40/DEC1, BHLHE41/DEC2,
NCOR1 and NCOR2 (PubMed:19786558). Interacts in a ligand-dependent
fashion with MED1 and NCOA1 (PubMed:19786558, PubMed:10882139,
PubMed:11698662). Interacts with VDR (PubMed:28698609). Interacts with
EP300; the interaction is decreased by 9-cis retinoic acid
(PubMed:17761950). Heterodimer (via C-terminus) with NR4A1 (via DNA-
binding domain); DNA-binding of the heterodimer is enhanced by 9-cis
retinoic acid (PubMed:17761950, PubMed:15509776). NR4A1 competes with
EP300 for interaction with RXRA and thereby attenuates EP300 mediated
acetylation of RXRA (PubMed:17761950). In the absence of hormonal
ligand, interacts with TACC1 (PubMed:20078863).
{ECO:0000250|UniProtKB:P28700, ECO:0000269|PubMed:10195690,
ECO:0000269|PubMed:10567404, ECO:0000269|PubMed:10669605,
ECO:0000269|PubMed:10698945, ECO:0000269|PubMed:10882139,
ECO:0000269|PubMed:11259580, ECO:0000269|PubMed:11698662,
ECO:0000269|PubMed:11915042, ECO:0000269|PubMed:12039952,
ECO:0000269|PubMed:14981089, ECO:0000269|PubMed:15047147,
ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:16574651,
ECO:0000269|PubMed:16912044, ECO:0000269|PubMed:17761950,
ECO:0000269|PubMed:19786558, ECO:0000269|PubMed:20078863,
ECO:0000269|PubMed:28167758, ECO:0000269|PubMed:28698609,
ECO:0000269|PubMed:29021580, ECO:0000269|PubMed:30275017,
ECO:0000269|PubMed:9267036}.
-!- SUBUNIT: (Microbial infection) Interacts (via the DNA binding domain)
with HCV core protein; the interaction enhances the transcriptional
activities of the RXRA/RARA and the RXRA/PPARA heterodimers.
{ECO:0000269|PubMed:11915042}.
-!- INTERACTION:
Q03463:- (xeno); NbExp=3; IntAct=EBI-78598, EBI-9159704;
O14503:BHLHE40; NbExp=4; IntAct=EBI-78598, EBI-711810;
P97792-1:Cxadr (xeno); NbExp=2; IntAct=EBI-78598, EBI-15903843;
Q15648:MED1; NbExp=6; IntAct=EBI-78598, EBI-394459;
Q71SY5:MED25; NbExp=4; IntAct=EBI-78598, EBI-394558;
Q15788:NCOA1; NbExp=14; IntAct=EBI-78598, EBI-455189;
Q15596:NCOA2; NbExp=5; IntAct=EBI-78598, EBI-81236;
Q9JLI4:Ncoa6 (xeno); NbExp=2; IntAct=EBI-78598, EBI-286271;
P55055-1:NR1H2; NbExp=2; IntAct=EBI-78598, EBI-21458417;
Q13133:NR1H3; NbExp=8; IntAct=EBI-78598, EBI-781356;
P27986:PIK3R1; NbExp=8; IntAct=EBI-78598, EBI-79464;
P37231-1:PPARG; NbExp=6; IntAct=EBI-78598, EBI-15664691;
P10276:RARA; NbExp=14; IntAct=EBI-78598, EBI-413374;
P42224:STAT1; NbExp=2; IntAct=EBI-78598, EBI-1057697;
P04625:THRA (xeno); NbExp=4; IntAct=EBI-78598, EBI-286261;
P11473:VDR; NbExp=6; IntAct=EBI-78598, EBI-286357;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
ECO:0000269|PubMed:11915042, ECO:0000269|PubMed:12145331,
ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:17761950,
ECO:0000269|PubMed:28167758}. Cytoplasm {ECO:0000269|PubMed:12145331,
ECO:0000269|PubMed:15509776}. Mitochondrion
{ECO:0000269|PubMed:17761950}. Note=Localization to the nucleus is
enhanced by vitamin D3 (PubMed:15509776). Nuclear localization may be
enhanced by the interaction with heterodimerization partner VDR
(PubMed:12145331). Translocation to the mitochondrion upon interaction
with NR4A1 (PubMed:17761950, PubMed:15509776). Increased nuclear
localization upon pulsatile shear stress (PubMed:28167758).
{ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:15509776,
ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:28167758}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P19793-1; Sequence=Displayed;
Name=2;
IsoId=P19793-2; Sequence=VSP_056565;
-!- TISSUE SPECIFICITY: Expressed in lung fibroblasts (at protein level)
(PubMed:30216632). Expressed in monocytes (PubMed:26463675). Highly
expressed in liver, also found in kidney and brain (PubMed:24275569,
PubMed:2159111, PubMed:14702039). {ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:2159111, ECO:0000269|PubMed:24275569,
ECO:0000269|PubMed:26463675, ECO:0000269|PubMed:30216632}.
-!- INDUCTION: Down-regulated by aging (PubMed:26463675). Induced by
pulsatile shear stress (PubMed:28167758). {ECO:0000269|PubMed:26463675,
ECO:0000269|PubMed:28167758}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain (AF1
domain), a DNA-binding domain and a C-terminal ligand-binding domain
(AF2 domain).
-!- PTM: Acetylated by EP300; acetylation enhances DNA binding and
transcriptional activity. {ECO:0000269|PubMed:17761950}.
-!- PTM: Phosphorylated on serine and threonine residues mainly in the N-
terminal modulating domain (By similarity). Constitutively
phosphorylated on Ser-21 in the presence or absence of ligand (By
similarity). Under stress conditions, hyperphosphorylated by activated
JNK on Ser-56, Ser-70, Thr-82 and Ser-260 (By similarity).
Phosphorylated on Ser-27, in vitro, by PKA (PubMed:11162439). This
phosphorylation is required for repression of cAMP-mediated
transcriptional activity of RARA (PubMed:11162439).
{ECO:0000250|UniProtKB:P28700, ECO:0000269|PubMed:11162439}.
-!- PTM: Sumoylation negatively regulates transcriptional activity.
Desumoylated specifically by SENP6. {ECO:0000269|PubMed:16912044}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/rxra/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Retinoid X receptor entry;
URL="https://en.wikipedia.org/wiki/Retinoid_X_receptor";
---------------------------------------------------------------------------
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EMBL; X52773; CAA36982.1; -; mRNA.
EMBL; AB307705; BAH02296.1; -; mRNA.
EMBL; AK131192; BAG54745.1; -; mRNA.
EMBL; AC156789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL354796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL669970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL683798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW88123.1; -; Genomic_DNA.
EMBL; BC110998; AAI10999.1; -; mRNA.
EMBL; DQ303444; ABB96254.1; -; Genomic_DNA.
CCDS; CCDS35172.1; -. [P19793-1]
PIR; S09592; S09592.
RefSeq; NP_001278850.1; NM_001291921.1. [P19793-2]
RefSeq; NP_002948.1; NM_002957.5. [P19793-1]
PDB; 1BY4; X-ray; 2.10 A; A/B/C/D=129-209.
PDB; 1DSZ; X-ray; 1.70 A; B=129-212.
PDB; 1FBY; X-ray; 2.25 A; A/B=224-462.
PDB; 1FM6; X-ray; 2.10 A; A/U=225-462.
PDB; 1FM9; X-ray; 2.10 A; A=225-462.
PDB; 1G1U; X-ray; 2.50 A; A/B/C/D=225-462.
PDB; 1G5Y; X-ray; 2.00 A; A/B/C/D=225-462.
PDB; 1K74; X-ray; 2.30 A; A=225-462.
PDB; 1MV9; X-ray; 1.90 A; A=223-462.
PDB; 1MVC; X-ray; 1.90 A; A=223-462.
PDB; 1MZN; X-ray; 1.90 A; A/C/E/G=223-462.
PDB; 1R0N; X-ray; 2.60 A; A=130-206.
PDB; 1RDT; X-ray; 2.40 A; A=225-462.
PDB; 1RXR; NMR; -; A=130-212.
PDB; 1XLS; X-ray; 2.96 A; A/B/C/D=227-458.
PDB; 1XV9; X-ray; 2.70 A; A/C=227-462.
PDB; 1XVP; X-ray; 2.60 A; A/C=227-462.
PDB; 1YNW; X-ray; 3.00 A; B=130-228.
PDB; 2ACL; X-ray; 2.80 A; A/C/E/G=225-462.
PDB; 2NLL; X-ray; 1.90 A; A=135-200.
PDB; 2P1T; X-ray; 1.80 A; A=223-462.
PDB; 2P1U; X-ray; 2.20 A; A=223-462.
PDB; 2P1V; X-ray; 2.20 A; A=223-462.
PDB; 2ZXZ; X-ray; 3.00 A; A=223-462.
PDB; 2ZY0; X-ray; 2.90 A; A/C=223-462.
PDB; 3DZU; X-ray; 3.20 A; A=11-462.
PDB; 3DZY; X-ray; 3.10 A; A=11-462.
PDB; 3E00; X-ray; 3.10 A; A=11-462.
PDB; 3E94; X-ray; 1.90 A; A=223-462.
PDB; 3FAL; X-ray; 2.36 A; A/C=225-462.
PDB; 3FC6; X-ray; 2.06 A; A/C=225-462.
PDB; 3FUG; X-ray; 2.00 A; A=223-462.
PDB; 3H0A; X-ray; 2.10 A; A=228-455.
PDB; 3KWY; X-ray; 2.30 A; A=223-462.
PDB; 3NSP; X-ray; 2.90 A; A/B=223-462.
PDB; 3NSQ; X-ray; 2.60 A; A/B=223-462.
PDB; 3OAP; X-ray; 2.05 A; A=228-458.
PDB; 3OZJ; X-ray; 2.10 A; A/C=225-462.
PDB; 3PCU; X-ray; 2.00 A; A=229-458.
PDB; 3R29; X-ray; 2.90 A; A/B=223-462.
PDB; 3R2A; X-ray; 3.00 A; A/B/C/D=223-462.
PDB; 3R5M; X-ray; 2.80 A; A/C=223-462.
PDB; 3UVV; X-ray; 2.95 A; B=225-462.
PDB; 4CN2; X-ray; 2.07 A; C/D=130-212.
PDB; 4CN3; X-ray; 2.35 A; A/B/C=130-212, D=130-173, D=175-212.
PDB; 4CN5; X-ray; 2.00 A; A/B=130-212.
PDB; 4CN7; X-ray; 2.34 A; A/B/E/F=130-212.
PDB; 4J5W; X-ray; 2.80 A; C/D=227-462.
PDB; 4J5X; X-ray; 2.80 A; C/D=227-462.
PDB; 4K4J; X-ray; 2.00 A; A=228-458.
PDB; 4K6I; X-ray; 2.10 A; A=228-458.
PDB; 4M8E; X-ray; 2.40 A; A=228-458.
PDB; 4M8H; X-ray; 2.20 A; A=228-458.
PDB; 4N5G; X-ray; 2.11 A; A/B/C/D=223-462.
PDB; 4N8R; X-ray; 2.03 A; A/B/C/D=223-462.
PDB; 4NQA; X-ray; 3.10 A; A/H=98-462.
PDB; 4OC7; X-ray; 2.50 A; A=223-462.
PDB; 4POH; X-ray; 2.30 A; A=228-458.
PDB; 4POJ; X-ray; 2.00 A; A=228-458.
PDB; 4PP3; X-ray; 2.00 A; A=228-458.
PDB; 4PP5; X-ray; 2.00 A; A=228-458.
PDB; 4RFW; X-ray; 2.40 A; A=228-458.
PDB; 4RMC; X-ray; 2.70 A; A=228-458.
PDB; 4RMD; X-ray; 1.90 A; A=228-462.
PDB; 4RME; X-ray; 2.30 A; A=228-462.
PDB; 4ZO1; X-ray; 3.22 A; B=231-455.
PDB; 4ZSH; X-ray; 1.80 A; A=223-462.
PDB; 5EC9; X-ray; 2.30 A; A=229-456.
PDB; 5GYM; X-ray; 2.60 A; A/B/C/D/E/F/G/H=227-462.
PDB; 5JI0; X-ray; 1.98 A; A=223-462.
PDB; 5LYQ; X-ray; 2.17 A; A=223-462.
PDB; 5MJ5; X-ray; 1.90 A; A=229-457.
PDB; 5MK4; X-ray; 2.00 A; A/C=229-457.
PDB; 5MKJ; X-ray; 2.50 A; A=229-458.
PDB; 5MKU; X-ray; 1.78 A; A=229-456.
PDB; 5MMW; X-ray; 2.70 A; A=229-457.
PDB; 5TBP; X-ray; 2.60 A; A/B/C/D=223-462.
PDB; 5UAN; X-ray; 3.51 A; A=98-462.
PDB; 5Z12; X-ray; 2.75 A; B/C=228-458.
PDB; 5ZQU; X-ray; 2.60 A; A/B/C/D=224-462.
PDB; 6A5Y; X-ray; 2.10 A; D=225-462.
PDB; 6A5Z; X-ray; 2.95 A; D/L=225-462.
PDB; 6A60; X-ray; 3.05 A; D=225-462.
PDB; 6FBQ; X-ray; 1.60 A; A/B=130-212.
PDB; 6FBR; X-ray; 2.10 A; A/B=130-212.
PDB; 6HN6; X-ray; 2.71 A; A=201-462.
PDB; 6SJM; X-ray; 2.52 A; A=229-456.
PDBsum; 1BY4; -.
PDBsum; 1DSZ; -.
PDBsum; 1FBY; -.
PDBsum; 1FM6; -.
PDBsum; 1FM9; -.
PDBsum; 1G1U; -.
PDBsum; 1G5Y; -.
PDBsum; 1K74; -.
PDBsum; 1MV9; -.
PDBsum; 1MVC; -.
PDBsum; 1MZN; -.
PDBsum; 1R0N; -.
PDBsum; 1RDT; -.
PDBsum; 1RXR; -.
PDBsum; 1XLS; -.
PDBsum; 1XV9; -.
PDBsum; 1XVP; -.
PDBsum; 1YNW; -.
PDBsum; 2ACL; -.
PDBsum; 2NLL; -.
PDBsum; 2P1T; -.
PDBsum; 2P1U; -.
PDBsum; 2P1V; -.
PDBsum; 2ZXZ; -.
PDBsum; 2ZY0; -.
PDBsum; 3DZU; -.
PDBsum; 3DZY; -.
PDBsum; 3E00; -.
PDBsum; 3E94; -.
PDBsum; 3FAL; -.
PDBsum; 3FC6; -.
PDBsum; 3FUG; -.
PDBsum; 3H0A; -.
PDBsum; 3KWY; -.
PDBsum; 3NSP; -.
PDBsum; 3NSQ; -.
PDBsum; 3OAP; -.
PDBsum; 3OZJ; -.
PDBsum; 3PCU; -.
PDBsum; 3R29; -.
PDBsum; 3R2A; -.
PDBsum; 3R5M; -.
PDBsum; 3UVV; -.
PDBsum; 4CN2; -.
PDBsum; 4CN3; -.
PDBsum; 4CN5; -.
PDBsum; 4CN7; -.
PDBsum; 4J5W; -.
PDBsum; 4J5X; -.
PDBsum; 4K4J; -.
PDBsum; 4K6I; -.
PDBsum; 4M8E; -.
PDBsum; 4M8H; -.
PDBsum; 4N5G; -.
PDBsum; 4N8R; -.
PDBsum; 4NQA; -.
PDBsum; 4OC7; -.
PDBsum; 4POH; -.
PDBsum; 4POJ; -.
PDBsum; 4PP3; -.
PDBsum; 4PP5; -.
PDBsum; 4RFW; -.
PDBsum; 4RMC; -.
PDBsum; 4RMD; -.
PDBsum; 4RME; -.
PDBsum; 4ZO1; -.
PDBsum; 4ZSH; -.
PDBsum; 5EC9; -.
PDBsum; 5GYM; -.
PDBsum; 5JI0; -.
PDBsum; 5LYQ; -.
PDBsum; 5MJ5; -.
PDBsum; 5MK4; -.
PDBsum; 5MKJ; -.
PDBsum; 5MKU; -.
PDBsum; 5MMW; -.
PDBsum; 5TBP; -.
PDBsum; 5UAN; -.
PDBsum; 5Z12; -.
PDBsum; 5ZQU; -.
PDBsum; 6A5Y; -.
PDBsum; 6A5Z; -.
PDBsum; 6A60; -.
PDBsum; 6FBQ; -.
PDBsum; 6FBR; -.
PDBsum; 6HN6; -.
PDBsum; 6SJM; -.
SMR; P19793; -.
BioGrid; 112168; 132.
ComplexPortal; CPX-496; RXRalpha-PXR retinoic acid receptor complex.
ComplexPortal; CPX-508; RXRalpha-RARalpha retinoic acid receptor complex.
ComplexPortal; CPX-631; RXRalpha-VDR nuclear hormone receptor complex.
ComplexPortal; CPX-632; RXRalpha-LXRalpha nuclear hormone receptor complex.
ComplexPortal; CPX-654; RXRalpha-TRbeta nuclear hormone receptor complex.
ComplexPortal; CPX-662; RXRalpha-TRalpha nuclear hormone receptor complex.
ComplexPortal; CPX-664; RXRalpha-RXRalpha retinoic acid receptor complex.
ComplexPortal; CPX-678; RXRalpha-LXRbeta nuclear hormone receptor complex.
ComplexPortal; CPX-816; RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex.
CORUM; P19793; -.
DIP; DIP-641N; -.
ELM; P19793; -.
IntAct; P19793; 51.
MINT; P19793; -.
STRING; 9606.ENSP00000419692; -.
BindingDB; P19793; -.
ChEMBL; CHEMBL2061; -.
DrugBank; DB07557; (5BETA)-PREGNANE-3,20-DIONE.
DrugBank; DB08063; 1-BENZYL-3-(4-METHOXYPHENYLAMINO)-4-PHENYLPYRROLE-2,5-DIONE.
DrugBank; DB08402; 2-[(2,4-DICHLOROBENZOYL)AMINO]-5-(PYRIMIDIN-2-YLOXY)BENZOIC ACID.
DrugBank; DB07863; 2-chloro-5-nitro-N-phenylbenzamide.
DrugBank; DB00459; Acitretin.
DrugBank; DB00210; Adapalene.
DrugBank; DB01436; Alfacalcidol.
DrugBank; DB00523; Alitretinoin.
DrugBank; DB00132; Alpha-Linolenic Acid.
DrugBank; DB04557; Arachidonic Acid.
DrugBank; DB00307; Bexarotene.
DrugBank; DB01393; Bezafibrate.
DrugBank; DB03756; Doconexent.
DrugBank; DB00749; Etodolac.
DrugBank; DB00926; Etretinate.
DrugBank; DB05956; EVT-101.
DrugBank; DB04224; Oleic Acid.
DrugBank; DB02746; Phthalic Acid.
DrugBank; DB00412; Rosiglitazone.
DrugBank; DB00755; Tretinoin.
DrugBank; DB08601; tributylstannanyl.
DrugCentral; P19793; -.
GuidetoPHARMACOLOGY; 610; -.
SwissLipids; SLP:000001552; -.
MoonDB; P19793; Predicted.
iPTMnet; P19793; -.
PhosphoSitePlus; P19793; -.
BioMuta; RXRA; -.
DMDM; 133701; -.
EPD; P19793; -.
jPOST; P19793; -.
MassIVE; P19793; -.
MaxQB; P19793; -.
PaxDb; P19793; -.
PeptideAtlas; P19793; -.
PRIDE; P19793; -.
ProteomicsDB; 3832; -.
ProteomicsDB; 53687; -. [P19793-1]
DNASU; 6256; -.
Ensembl; ENST00000481739; ENSP00000419692; ENSG00000186350. [P19793-1]
GeneID; 6256; -.
KEGG; hsa:6256; -.
UCSC; uc004cfb.3; human. [P19793-1]
CTD; 6256; -.
DisGeNET; 6256; -.
EuPathDB; HostDB:ENSG00000186350.9; -.
GeneCards; RXRA; -.
HGNC; HGNC:10477; RXRA.
HPA; CAB004565; -.
HPA; CAB005352; -.
MIM; 180245; gene.
neXtProt; NX_P19793; -.
OpenTargets; ENSG00000186350; -.
PharmGKB; PA34890; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00940000159789; -.
InParanoid; P19793; -.
KO; K08524; -.
OMA; ESPGPFM; -.
OrthoDB; 912470at2759; -.
PhylomeDB; P19793; -.
TreeFam; TF352097; -.
Reactome; R-HSA-1368082; RORA activates gene expression.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-159418; Recycling of bile acids and salts.
Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-HSA-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
Reactome; R-HSA-211976; Endogenous sterols.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-9029558; NR1H2 & NR1H3 regulate gene expression linked to lipogenesis.
Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
Reactome; R-HSA-9031525; NR1H2 & NR1H3 regulate gene expression to limit cholesterol uptake.
Reactome; R-HSA-9031528; NR1H2 & NR1H3 regulate gene expression linked to triglyceride lipolysis in adipose.
Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
Reactome; R-HSA-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
Reactome; R-HSA-9632974; NR1H2 & NR1H3 regulate gene expression linked to gluconeogenesis.
SignaLink; P19793; -.
SIGNOR; P19793; -.
ChiTaRS; RXRA; human.
EvolutionaryTrace; P19793; -.
GeneWiki; Retinoid_X_receptor_alpha; -.
GenomeRNAi; 6256; -.
Pharos; P19793; Tclin.
PRO; PR:P19793; -.
Proteomes; UP000005640; Chromosome 9.
RNAct; P19793; protein.
Bgee; ENSG00000186350; Expressed in 231 organ(s), highest expression level in liver.
ExpressionAtlas; P19793; baseline and differential.
Genevisible; P19793; HS.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:BHF-UCL.
GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
GO; GO:0050692; F:DBD domain binding; IDA:CAFA.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0003690; F:double-stranded DNA binding; IMP:CAFA.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:MGI.
GO; GO:0050693; F:LBD domain binding; IDA:CAFA.
GO; GO:0004879; F:nuclear receptor activity; IDA:BHF-UCL.
GO; GO:0016922; F:nuclear receptor binding; IPI:CAFA.
GO; GO:0042277; F:peptide binding; IDA:CAFA.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0001972; F:retinoic acid binding; IDA:CAFA.
GO; GO:0044323; F:retinoic acid-responsive element binding; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:AgBase.
GO; GO:0038023; F:signaling receptor activity; TAS:BHF-UCL.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0042809; F:vitamin D receptor binding; IPI:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
GO; GO:0015721; P:bile acid and bile salt transport; TAS:Reactome.
GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0008203; P:cholesterol metabolic process; TAS:BHF-UCL.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
GO; GO:0019048; P:modulation by virus of host morphology or physiology; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045994; P:positive regulation of translational initiation by iron; IEA:Ensembl.
GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; IEA:Ensembl.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0032526; P:response to retinoic acid; IMP:BHF-UCL.
GO; GO:0048384; P:retinoic acid receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; IEA:Ensembl.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
GO; GO:0006766; P:vitamin metabolic process; TAS:ProtInc.
DisProt; DP00062; -.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR-like_dom_sf.
InterPro; IPR021780; Nuc_recep-AF1.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR000003; Retinoid-X_rcpt/HNF4.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF11825; Nuc_recep-AF1; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00545; RETINOIDXR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
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; Acetylation; Alternative splicing; Cytoplasm; DNA-binding;
Host-virus interaction; Isopeptide bond; Metal-binding; Mitochondrion;
Nucleus; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1..462
/note="Retinoic acid receptor RXR-alpha"
/id="PRO_0000053566"
DOMAIN 227..458
/note="NR LBD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
DNA_BIND 135..200
/note="Nuclear receptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 135..155
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 171..195
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
REGION 1..134
/note="Modulating"
/evidence="ECO:0000250"
REGION 160..165
/note="Nuclear localization signal"
/evidence="ECO:0000269|PubMed:12145331"
REGION 201..224
/note="Hinge"
REGION 348..368
/note="Required for nuclear export"
/evidence="ECO:0000269|PubMed:15509776"
METAL 135
/note="Zinc 1"
/evidence="ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605"
METAL 138
/note="Zinc 1"
/evidence="ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605"
METAL 152
/note="Zinc 1"
/evidence="ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605"
METAL 155
/note="Zinc 1"
/evidence="ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605"
METAL 171
/note="Zinc 2"
/evidence="ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605"
METAL 177
/note="Zinc 2"
/evidence="ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605"
METAL 187
/note="Zinc 2"
/evidence="ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605"
METAL 190
/note="Zinc 2"
/evidence="ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605"
BINDING 316
/note="9-cis retinoic acid"
/evidence="ECO:0000244|PDB:2ACL, ECO:0000244|PDB:3FAL,
ECO:0000244|PDB:3FC6, ECO:0000269|PubMed:16107141,
ECO:0000269|PubMed:18800767, ECO:0000269|PubMed:19167885"
BINDING 327
/note="9-cis retinoic acid; via amide nitrogen"
/evidence="ECO:0000244|PDB:2ACL, ECO:0000244|PDB:3FAL,
ECO:0000244|PDB:3FC6, ECO:0000269|PubMed:16107141,
ECO:0000269|PubMed:18800767, ECO:0000269|PubMed:19167885"
MOD_RES 21
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P28700"
MOD_RES 27
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:11162439"
MOD_RES 56
/note="Phosphoserine; by MAPK8 and MAPK9"
/evidence="ECO:0000250|UniProtKB:P28700"
MOD_RES 70
/note="Phosphoserine; by MAPK8 and MAPK9"
/evidence="ECO:0000250|UniProtKB:P28700"
MOD_RES 82
/note="Phosphothreonine; by MAPK8 and MAPK9"
/evidence="ECO:0000250|UniProtKB:P28700"
MOD_RES 129
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 145
/note="N6-acetyllysine; by EP300"
/evidence="ECO:0000269|PubMed:17761950"
MOD_RES 259
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 260
/note="Phosphoserine; by MAPK8 and MAPK9"
/evidence="ECO:0000250|UniProtKB:P28700"
CROSSLNK 4
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 108
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO)"
/evidence="ECO:0000269|PubMed:16912044"
VAR_SEQ 1..97
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_056565"
VARIANT 261
/note="P -> L (in dbSNP:rs2234960)"
/id="VAR_014620"
VARIANT 327
/note="A -> S (in dbSNP:rs1805345)"
/id="VAR_050582"
VARIANT 336
/note="S -> I (in dbSNP:rs1805345)"
/id="VAR_014621"
VARIANT 398
/note="A -> V (in dbSNP:rs11542209)"
/id="VAR_050583"
MUTAGEN 27
/note="S->A: Abolishes phosphorylation. No change in
increase of RARA-mediated transcriptional activity."
/evidence="ECO:0000269|PubMed:11162439,
ECO:0000269|PubMed:20215566"
MUTAGEN 27
/note="S->A: Increase in RARA-mediated transcriptional
activity."
/evidence="ECO:0000269|PubMed:11162439,
ECO:0000269|PubMed:20215566"
MUTAGEN 133..156
/note="Missing: Abolishes acetylation by EP300."
/evidence="ECO:0000269|PubMed:17761950"
MUTAGEN 145
/note="K->R: Abolishes acetylation by EP300, DNA binding
and transcriptional activity. Impairs interaction with
EP300."
/evidence="ECO:0000269|PubMed:17761950"
MUTAGEN 158..159
/note="FF->AA: Abolishes nuclear export."
/evidence="ECO:0000269|PubMed:12145331"
MUTAGEN 160..165
/note="KRTVRK->QGTVGQ: Abolishes nuclear localization and
transcriptional activity."
/evidence="ECO:0000269|PubMed:12145331"
MUTAGEN 206..216
/note="Missing: No impact on acetylation by EP300."
/evidence="ECO:0000269|PubMed:17761950"
MUTAGEN 352..462
/note="Missing: No impact on acetylation by EP300."
/evidence="ECO:0000269|PubMed:17761950"
MUTAGEN 357..360
/note="MRDM->ARDA: Abolishes nuclear export."
/evidence="ECO:0000269|PubMed:15509776"
MUTAGEN 418..430
/note="LLLRLPALRSIGL->ALARLPALRSIGA: Abolishes nuclear
localization."
/evidence="ECO:0000269|PubMed:15509776"
MUTAGEN 434
/note="E->N,Q,K,A: As a heterodimer with NR1H4, impairs
interaction with coactivator NCOA1. Impairs transcriptional
activity."
/evidence="ECO:0000269|PubMed:30275017"
STRAND 131..134
/evidence="ECO:0000244|PDB:4CN5"
TURN 136..138
/evidence="ECO:0000244|PDB:6FBQ"
STRAND 141..146
/evidence="ECO:0000244|PDB:6FBQ"
STRAND 149..151
/evidence="ECO:0000244|PDB:6FBQ"
HELIX 153..164
/evidence="ECO:0000244|PDB:6FBQ"
STRAND 172..175
/evidence="ECO:0000244|PDB:2NLL"
TURN 181..185
/evidence="ECO:0000244|PDB:6FBQ"
HELIX 188..198
/evidence="ECO:0000244|PDB:6FBQ"
HELIX 202..204
/evidence="ECO:0000244|PDB:6FBQ"
HELIX 226..229
/evidence="ECO:0000244|PDB:3FC6"
HELIX 232..241
/evidence="ECO:0000244|PDB:5MKU"
HELIX 246..250
/evidence="ECO:0000244|PDB:1MZN"
TURN 251..253
/evidence="ECO:0000244|PDB:1FM9"
STRAND 258..261
/evidence="ECO:0000244|PDB:1XVP"
HELIX 264..284
/evidence="ECO:0000244|PDB:5MKU"
HELIX 289..291
/evidence="ECO:0000244|PDB:5MKU"
HELIX 294..316
/evidence="ECO:0000244|PDB:5MKU"
HELIX 317..319
/evidence="ECO:0000244|PDB:5MKU"
STRAND 320..325
/evidence="ECO:0000244|PDB:5MKU"
TURN 327..329
/evidence="ECO:0000244|PDB:4N8R"
STRAND 331..333
/evidence="ECO:0000244|PDB:2P1T"
HELIX 334..339
/evidence="ECO:0000244|PDB:5MKU"
TURN 340..342
/evidence="ECO:0000244|PDB:3UVV"
HELIX 343..352
/evidence="ECO:0000244|PDB:5MKU"
HELIX 354..360
/evidence="ECO:0000244|PDB:5MKU"
HELIX 364..375
/evidence="ECO:0000244|PDB:5MKU"
STRAND 380..382
/evidence="ECO:0000244|PDB:3DZU"
HELIX 386..407
/evidence="ECO:0000244|PDB:5MKU"
HELIX 414..419
/evidence="ECO:0000244|PDB:5MKU"
HELIX 422..441
/evidence="ECO:0000244|PDB:5MKU"
STRAND 447..449
/evidence="ECO:0000244|PDB:5MKU"
HELIX 450..454
/evidence="ECO:0000244|PDB:5MKU"
HELIX 457..459
/evidence="ECO:0000244|PDB:3NSQ"
SEQUENCE 462 AA; 50811 MW; 7F952B580AD84C42 CRC64;
MDTKHFLPLD FSTQVNSSLT SPTGRGSMAA PSLHPSLGPG IGSPGQLHSP ISTLSSPING
MGPPFSVISS PMGPHSMSVP TTPTLGFSTG SPQLSSPMNP VSSSEDIKPP LGLNGVLKVP
AHPSGNMASF TKHICAICGD RSSGKHYGVY SCEGCKGFFK RTVRKDLTYT CRDNKDCLID
KRQRNRCQYC RYQKCLAMGM KREAVQEERQ RGKDRNENEV ESTSSANEDM PVERILEAEL
AVEPKTETYV EANMGLNPSS PNDPVTNICQ AADKQLFTLV EWAKRIPHFS ELPLDDQVIL
LRAGWNELLI ASFSHRSIAV KDGILLATGL HVHRNSAHSA GVGAIFDRVL TELVSKMRDM
QMDKTELGCL RAIVLFNPDS KGLSNPAEVE ALREKVYASL EAYCKHKYPE QPGRFAKLLL
RLPALRSIGL KCLEHLFFFK LIGDTPIDTF LMEMLEAPHQ MT


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Catalog number Product name Quantity
E2043r ELISA kit Nr2b1,Nuclear receptor subfamily 2 group B member 1,Rat,Rattus norvegicus,Retinoic acid receptor RXR-alpha,Retinoid X receptor alpha,Rxra 96T
U2043r CLIA Nr2b1,Nuclear receptor subfamily 2 group B member 1,Rat,Rattus norvegicus,Retinoic acid receptor RXR-alpha,Retinoid X receptor alpha,Rxra 96T
U2043m CLIA Mouse,Mus musculus,Nr2b1,Nuclear receptor subfamily 2 group B member 1,Retinoic acid receptor RXR-alpha,Retinoid X receptor alpha,Rxra 96T
U2043r CLIA kit Nr2b1,Nuclear receptor subfamily 2 group B member 1,Rat,Rattus norvegicus,Retinoic acid receptor RXR-alpha,Retinoid X receptor alpha,Rxra 96T
E2043m ELISA Mouse,Mus musculus,Nr2b1,Nuclear receptor subfamily 2 group B member 1,Retinoic acid receptor RXR-alpha,Retinoid X receptor alpha,Rxra 96T
E2043r ELISA Nr2b1,Nuclear receptor subfamily 2 group B member 1,Rat,Rattus norvegicus,Retinoic acid receptor RXR-alpha,Retinoid X receptor alpha,Rxra 96T
U2043m CLIA kit Mouse,Mus musculus,Nr2b1,Nuclear receptor subfamily 2 group B member 1,Retinoic acid receptor RXR-alpha,Retinoid X receptor alpha,Rxra 96T
E2043m ELISA kit Mouse,Mus musculus,Nr2b1,Nuclear receptor subfamily 2 group B member 1,Retinoic acid receptor RXR-alpha,Retinoid X receptor alpha,Rxra 96T
U2043h CLIA Homo sapiens,Human,NR2B1,Nuclear receptor subfamily 2 group B member 1,Retinoic acid receptor RXR-alpha,Retinoid X receptor alpha,RXRA 96T
U2043h CLIA kit Homo sapiens,Human,NR2B1,Nuclear receptor subfamily 2 group B member 1,Retinoic acid receptor RXR-alpha,Retinoid X receptor alpha,RXRA 96T
E2043h ELISA Homo sapiens,Human,NR2B1,Nuclear receptor subfamily 2 group B member 1,Retinoic acid receptor RXR-alpha,Retinoid X receptor alpha,RXRA 96T
E2043h ELISA kit Homo sapiens,Human,NR2B1,Nuclear receptor subfamily 2 group B member 1,Retinoic acid receptor RXR-alpha,Retinoid X receptor alpha,RXRA 96T
EIAAB35712 Homo sapiens,Human,NR1F1,Nuclear receptor ROR-alpha,Nuclear receptor RZR-alpha,Nuclear receptor subfamily 1 group F member 1,Retinoid-related orphan receptor-alpha,RORA,RZRA
EIAAB35713 Mouse,Mus musculus,Nr1f1,Nuclear receptor ROR-alpha,Nuclear receptor RZR-alpha,Nuclear receptor subfamily 1 group F member 1,Retinoid-related orphan receptor-alpha,Rora,Rzra
EIAAB36502 Nr2b2,Nuclear receptor coregulator 1,Nuclear receptor subfamily 2 group B member 2,Rat,Rattus norvegicus,Rcor-1,Retinoic acid receptor RXR-beta,Retinoid X receptor beta,Rxrb
E2297m Mouse,Mus musculus,Nr1b1,Nuclear receptor subfamily 1 group B member 1,Rara,RAR-alpha,Retinoic acid receptor alpha
E2297m ELISA kit Mouse,Mus musculus,Nr1b1,Nuclear receptor subfamily 1 group B member 1,Rara,RAR-alpha,Retinoic acid receptor alpha 96T
E2297h Homo sapiens,Human,NR1B1,Nuclear receptor subfamily 1 group B member 1,RARA,RAR-alpha,Retinoic acid receptor alpha
U2297m CLIA Mouse,Mus musculus,Nr1b1,Nuclear receptor subfamily 1 group B member 1,Rara,RAR-alpha,Retinoic acid receptor alpha 96T
E2297m ELISA Mouse,Mus musculus,Nr1b1,Nuclear receptor subfamily 1 group B member 1,Rara,RAR-alpha,Retinoic acid receptor alpha 96T
U2297m CLIA kit Mouse,Mus musculus,Nr1b1,Nuclear receptor subfamily 1 group B member 1,Rara,RAR-alpha,Retinoic acid receptor alpha 96T
U2297h CLIA kit Homo sapiens,Human,NR1B1,Nuclear receptor subfamily 1 group B member 1,RARA,RAR-alpha,Retinoic acid receptor alpha 96T
U2297h CLIA Homo sapiens,Human,NR1B1,Nuclear receptor subfamily 1 group B member 1,RARA,RAR-alpha,Retinoic acid receptor alpha 96T
E2297h ELISA Homo sapiens,Human,NR1B1,Nuclear receptor subfamily 1 group B member 1,RARA,RAR-alpha,Retinoic acid receptor alpha 96T
E2297h ELISA kit Homo sapiens,Human,NR1B1,Nuclear receptor subfamily 1 group B member 1,RARA,RAR-alpha,Retinoic acid receptor alpha 96T
Pathways :
WP1963: The effect of Glucocorticoids on target gene expression
WP566: canonical wnt - zebrafish
WP1284: EPO Receptor Signaling
WP1913: Signaling by Insulin receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP809: TGF-beta Receptor Signaling Pathway
WP57: Signal Transduction of S1P Receptor
WP2272: Pathogenic Escherichia coli infection
WP362: TGF-beta Receptor Signaling Pathway
WP1121: Kit Receptor Signaling Pathway
WP1309: Toll-like receptor signaling pathway
WP26: Signal Transduction of S1P Receptor
WP732: Serotonin Receptor 2 and ELK-SRF/GATA4 signaling
WP474: Endochondral Ossification
WP1011: T Cell Receptor Signaling Pathway
WP926: TGF-beta Receptor Signaling Pathway
WP1618: alpha-Linolenic acid metabolism
WP75: Toll-like receptor signaling pathway
WP1025: B Cell Receptor Signaling Pathway
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1781: Advanced glycosylation endproduct receptor signaling
WP23: B Cell Receptor Signaling Pathway
WP1133: Androgen receptor signaling pathway
WP878: EPO Receptor Signaling
WP1161: TGF-beta Receptor Signaling Pathway

Related Genes :

Bibliography :
[26270486] In Silico Adoption of an Orphan Nuclear Receptor NR4A1.
[17367745] Vitamin D receptor-mediated suppression of RelB in antigen presenting cells: a paradigm for ligand-augmented negative transcriptional regulation.
[16819395] Bile salt excretory pump: biology and pathobiology.
[15707588] Proteasome inhibitors induce peroxisome proliferator-activated receptor transactivation through RXR accumulation and a protein kinase C-dependent pathway.
[9372944] Novel receptor interaction and repression domains in the orphan receptor SHP.
[8530418] Multiple functions of the TR2-11 orphan receptor in modulating activation of two key cis-acting elements involved in the retinoic acid signal transduction system.
[8387200] Retinoic acid is a negative regulator of the Epstein-Barr virus protein (BZLF1) that mediates disruption of latent infection.