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Bile acid receptor (Farnesoid X-activated receptor) (Farnesol receptor HRR-1) (Nuclear receptor subfamily 1 group H member 4) (Retinoid X receptor-interacting protein 14) (RXR-interacting protein 14)

 NR1H4_HUMAN             Reviewed;         486 AA.
Q96RI1; A1L4K5; B7Z412; B7ZM06; F8VYG8; Q8NFP5; Q8NFP6; Q92943;
27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
26-APR-2004, sequence version 2.
22-APR-2020, entry version 200.
RecName: Full=Bile acid receptor;
AltName: Full=Farnesoid X-activated receptor;
AltName: Full=Farnesol receptor HRR-1;
AltName: Full=Nuclear receptor subfamily 1 group H member 4;
AltName: Full=Retinoid X receptor-interacting protein 14;
Short=RXR-interacting protein 14;
Name=NR1H4; Synonyms=BAR, FXR, HRR1, RIP14;
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 4).
Papetti M., Wood N., Lohmar P.D., Bowman M.R.;
"The identification of the cDNA coding for HRR-1, a novel human farnesol
receptor.";
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Han J.-I., Bok S.-H., Jeong T.-S.;
"Functional analysis of human farnesol receptor (NR1H4) splicing variant.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE SPLICING
(ISOFORMS 3 AND 4).
PubMed=12062799; DOI=10.1016/s0378-1119(02)00557-7;
Huber R.M., Murphy K., Miao B., Link J.R., Cunningham M.R., Rupar M.J.,
Gunyuzlu P.L., Haws T.F. Jr., Kassam A., Powell F., Hollis G.F.,
Young P.R., Mukherjee R., Burn T.C.;
"Generation of multiple farnesoid-X-receptor isoforms through the use of
alternative promoters.";
Gene 290:35-43(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
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=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., 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.,
Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(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] (ISOFORMS 3 AND 5).
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]
FUNCTION IN BA HOMEOSTASIS.
PubMed=10514450; DOI=10.1074/jbc.274.42.29749;
Grober J., Zaghini I., Fujii H., Jones S.A., Kliewer S.A., Willson T.M.,
Ono T., Besnard P.;
"Identification of a bile acid-responsive element in the human ileal bile
acid-binding protein gene. Involvement of the farnesoid X receptor/9-cis-
retinoic acid receptor heterodimer.";
J. Biol. Chem. 274:29749-29754(1999).
[9]
FUNCTION IN BA HOEMOSTASIS.
PubMed=10334992; DOI=10.1126/science.284.5418.1362;
Makishima M., Okamoto A.Y., Repa J.J., Tu H., Learned R.M., Luk A.,
Hull M.V., Lustig K.D., Mangelsdorf D.J., Shan B.;
"Identification of a nuclear receptor for bile acids.";
Science 284:1362-1365(1999).
[10]
FUNCTION IN BA HOEMOSTASIS.
PubMed=10334993; DOI=10.1126/science.284.5418.1365;
Parks D.J., Blanchard S.G., Bledsoe R.K., Chandra G., Consler T.G.,
Kliewer S.A., Stimmel J.B., Willson T.M., Zavacki A.M., Moore D.D.,
Lehmann J.M.;
"Bile acids: natural ligands for an orphan nuclear receptor.";
Science 284:1365-1368(1999).
[11]
FUNCTION IN LIPID HOMEOSTASIS.
PubMed=11579204; DOI=10.1210/mend.15.10.0712;
Kast H.R., Nguyen C.M., Sinal C.J., Jones S.A., Laffitte B.A., Reue K.,
Gonzalez F.J., Willson T.M., Edwards P.A.;
"Farnesoid X-activated receptor induces apolipoprotein C-II transcription:
a molecular mechanism linking plasma triglyceride levels to bile acids.";
Mol. Endocrinol. 15:1720-1728(2001).
[12]
FUNCTION IN LIPID HOMEOSTASIS.
PubMed=11927623; DOI=10.1172/jci14505;
Claudel T., Sturm E., Duez H., Torra I.P., Sirvent A., Kosykh V.,
Fruchart J.C., Dallongeville J., Hum D.W., Kuipers F., Staels B.;
"Bile acid-activated nuclear receptor FXR suppresses apolipoprotein A-I
transcription via a negative FXR response element.";
J. Clin. Invest. 109:961-971(2002).
[13]
FUNCTION IN BA HOMEOSTASIS.
PubMed=12815072; DOI=10.1101/gad.1083503;
Holt J.A., Luo G., Billin A.N., Bisi J., McNeill Y.Y., Kozarsky K.F.,
Donahee M., Wang D.Y., Mansfield T.A., Kliewer S.A., Goodwin B.,
Jones S.A.;
"Definition of a novel growth factor-dependent signal cascade for the
suppression of bile acid biosynthesis.";
Genes Dev. 17:1581-1591(2003).
[14]
FUNCTION IN BA HOMEOSTASIS.
PubMed=12806625; DOI=10.1016/s0016-5085(03)00388-3;
Barbier O., Torra I.P., Sirvent A., Claudel T., Blanquart C.,
Duran-Sandoval D., Kuipers F., Kosykh V., Fruchart J.C., Staels B.;
"FXR induces the UGT2B4 enzyme in hepatocytes: a potential mechanism of
negative feedback control of FXR activity.";
Gastroenterology 124:1926-1940(2003).
[15]
FUNCTION IN LIPID HOMEOSTASIS.
PubMed=12891557; DOI=10.1016/s0016-5085(03)00896-5;
Claudel T., Inoue Y., Barbier O., Duran-Sandoval D., Kosykh V.,
Fruchart J., Fruchart J.C., Gonzalez F.J., Staels B.;
"Farnesoid X receptor agonists suppress hepatic apolipoprotein CIII
expression.";
Gastroenterology 125:544-555(2003).
[16]
FUNCTION IN LIPID HOMEOSTASIS.
PubMed=12660231; DOI=10.1074/jbc.m302505200;
Anisfeld A.M., Kast-Woelbern H.R., Meyer M.E., Jones S.A., Zhang Y.,
Williams K.J., Willson T., Edwards P.A.;
"Syndecan-1 expression is regulated in an isoform-specific manner by the
farnesoid-X receptor.";
J. Biol. Chem. 278:20420-20428(2003).
[17]
FUNCTION IN BA HOMEOSTASIS.
PubMed=12754200; DOI=10.1074/jbc.m302128200;
Pircher P.C., Kitto J.L., Petrowski M.L., Tangirala R.K., Bischoff E.D.,
Schulman I.G., Westin S.K.;
"Farnesoid X receptor regulates bile acid-amino acid conjugation.";
J. Biol. Chem. 278:27703-27711(2003).
[18]
FUNCTION IN LIPID HOMEOSTASIS.
PubMed=12554753; DOI=10.1210/me.2002-0120;
Pineda Torra I., Claudel T., Duval C., Kosykh V., Fruchart J.C., Staels B.;
"Bile acids induce the expression of the human peroxisome proliferator-
activated receptor alpha gene via activation of the farnesoid X receptor.";
Mol. Endocrinol. 17:259-272(2003).
[19]
INTERACTION WITH PPARGC1A.
PubMed=15202934; DOI=10.1042/bj20040432;
Kanaya E., Shiraki T., Jingami H.;
"The nuclear bile acid receptor FXR is activated by PGC-1alpha in a ligand-
dependent manner.";
Biochem. J. 382:913-921(2004).
[20]
INTERACTION WITH NCOA1, AND LIGAND-BINDING.
PubMed=14684751; DOI=10.1074/jbc.m306422200;
Lew J.L., Zhao A., Yu J., Huang L., De Pedro N., Pelaez F., Wright S.D.,
Cui J.;
"The farnesoid X receptor controls gene expression in a ligand- and
promoter-selective fashion.";
J. Biol. Chem. 279:8856-8861(2004).
[21]
FUNCTION IN BA HOEMOSTASIS.
PubMed=15239098; DOI=10.1002/hep.20295;
Neimark E., Chen F., Li X., Shneider B.L.;
"Bile acid-induced negative feedback regulation of the human ileal bile
acid transporter.";
Hepatology 40:149-156(2004).
[22]
INTERACTION WITH MED1.
PubMed=15187081; DOI=10.1074/jbc.m405126200;
Pineda Torra I., Freedman L.P., Garabedian M.J.;
"Identification of DRIP205 as a coactivator for the Farnesoid X receptor.";
J. Biol. Chem. 279:36184-36191(2004).
[23]
FUNCTION IN LIPID HOMEOSTASIS.
PubMed=15337761; DOI=10.1074/jbc.m404255200;
Hirokane H., Nakahara M., Tachibana S., Shimizu M., Sato R.;
"Bile acid reduces the secretion of very low density lipoprotein by
repressing microsomal triglyceride transfer protein gene expression
mediated by hepatocyte nuclear factor-4.";
J. Biol. Chem. 279:45685-45692(2004).
[24]
FUNCTION IN BA HOMEOSTASIS, AND INTERACTION WITH CARM1.
PubMed=15471871; DOI=10.1074/jbc.m410021200;
Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J., Walsh M.J.;
"Ligand-dependent activation of the farnesoid X-receptor directs arginine
methylation of histone H3 by CARM1.";
J. Biol. Chem. 279:54348-54357(2004).
[25]
INTERACTION WITH PRMT1.
PubMed=15911693; DOI=10.1124/mol.105.012104;
Rizzo G., Renga B., Antonelli E., Passeri D., Pellicciari R., Fiorucci S.;
"The methyl transferase PRMT1 functions as co-activator of farnesoid X
receptor (FXR)/9-cis retinoid X receptor and regulates transcription of FXR
responsive genes.";
Mol. Pharmacol. 68:551-558(2005).
[26]
FUNCTION IN BA HOEMOSTASIS.
PubMed=16269519; DOI=10.1152/ajpgi.00430.2005;
Landrier J.-F., Eloranta J.J., Vavricka S.R., Kullak-Ublick G.A.;
"The nuclear receptor for bile acids, FXR, transactivates human organic
solute transporter-alpha and -beta genes.";
Am. J. Physiol. 290:G476-G485(2006).
[27]
FUNCTION IN BA HOEMOSTASIS.
PubMed=16946559; DOI=10.2133/dmpk.21.315;
Miyata M., Matsuda Y., Tsuchiya H., Kitada H., Akase T., Shimada M.,
Nagata K., Gonzalez F.J., Yamazoe Y.;
"Chenodeoxycholic acid-mediated activation of the farnesoid X receptor
negatively regulates hydroxysteroid sulfotransferase.";
Drug Metab. Pharmacokinet. 21:315-323(2006).
[28]
POSSIBLE INVOLVEMENT IN INTRAHEPATIC CHOLESTASIS OF PREGNANCY.
PubMed=17681172; DOI=10.1053/j.gastro.2007.05.015;
Van Mil S.W., Milona A., Dixon P.H., Mullenbach R., Geenes V.L.,
Chambers J., Shevchuk V., Moore G.E., Lammert F., Glantz A.G.,
Mattsson L.A., Whittaker J., Parker M.G., White R., Williamson C.;
"Functional variants of the central bile acid sensor FXR identified in
intrahepatic cholestasis of pregnancy.";
Gastroenterology 133:507-516(2007).
[29]
FUNCTION IN BA HEMOSTASIS, AND INTERACTION WITH GPS2.
PubMed=17895379; DOI=10.1073/pnas.0706736104;
Sanyal S., Baavner A., Haroniti A., Nilsson L.M., Lundaasen T.,
Rehnmark S., Witt M.R., Einarsson C., Talianidis I., Gustafsson J.A.,
Treuter E.;
"Involvement of corepressor complex subunit GPS2 in transcriptional
pathways governing human bile acid biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 104:15665-15670(2007).
[30]
PHOSPHORYLATION AT THR-456, AND MUTAGENESIS OF THR-456.
PubMed=18668687; DOI=10.1002/hep.22431;
Frankenberg T., Miloh T., Chen F.Y., Ananthanarayanan M., Sun A.Q.,
Balasubramaniyan N., Arias I., Setchell K.D., Suchy F.J., Shneider B.L.;
"The membrane protein ATPase class I type 8B member 1 signals through
protein kinase C zeta to activate the farnesoid X receptor.";
Hepatology 48:1896-1905(2008).
[31]
POSSIBLE INVOLVEMENT IN CHOLESTEROL CHOLELITHIASIS.
PubMed=17931734; DOI=10.1016/j.jhep.2007.07.027;
Kovacs P., Kress R., Rocha J., Kurtz U., Miquel J.F., Nervi F.,
Mendez-Sanchez N., Uribe M., Bock H.H., Schirin-Sokhan R., Stumvoll M.,
Moessner J., Lammert F., Wittenburg H.;
"Variation of the gene encoding the nuclear bile salt receptor FXR and
gallstone susceptibility in mice and humans.";
J. Hepatol. 48:116-124(2008).
[32]
PHOSPHORYLATION AT SER-145 AND SER-164, INTERACTION WITH PPARGC1A, AND
MUTAGENESIS OF SER-145 AND SER-164.
PubMed=18755856; DOI=10.1210/me.2008-0092;
Gineste R., Sirvent A., Paumelle R., Helleboid S., Aquilina A., Darteil R.,
Hum D.W., Fruchart J.C., Staels B.;
"Phosphorylation of farnesoid X receptor by protein kinase C promotes its
transcriptional activity.";
Mol. Endocrinol. 22:2433-2447(2008).
[33]
INTERACTION WITH XRCC5 AND XRCC6.
PubMed=19833092; DOI=10.1016/j.bbrc.2009.10.040;
Ohno M., Kunimoto M., Nishizuka M., Osada S., Imagawa M.;
"Ku proteins function as corepressors to regulate farnesoid X receptor-
mediated gene expression.";
Biochem. Biophys. Res. Commun. 390:738-742(2009).
[34]
TISSUE SPECIFICITY.
PubMed=19393742; DOI=10.1016/j.bbadis.2009.04.004;
Renga B., Migliorati M., Mencarelli A., Fiorucci S.;
"Reciprocal regulation of the bile acid-activated receptor FXR and the
interferon-gamma-STAT-1 pathway in macrophages.";
Biochim. Biophys. Acta 1792:564-573(2009).
[35]
ACETYLATION AT LYS-167 AND LYS-227 BY EP300.
PubMed=19883617; DOI=10.1016/j.cmet.2009.09.009;
Kemper J.K., Xiao Z., Ponugoti B., Miao J., Fang S., Kanamaluru D.,
Tsang S., Wu S.Y., Chiang C.M., Veenstra T.D.;
"FXR acetylation is normally dynamically regulated by p300 and SIRT1 but
constitutively elevated in metabolic disease states.";
Cell Metab. 10:392-404(2009).
[36]
FUNCTION IN INTESTINAL INNATE IMMUNITY, TISSUE SPECIFICITY, SUBCELLULAR
LOCATION, AND SUMOYLATION.
PubMed=19864602; DOI=10.4049/jimmunol.0803978;
Vavassori P., Mencarelli A., Renga B., Distrutti E., Fiorucci S.;
"The bile acid receptor FXR is a modulator of intestinal innate immunity.";
J. Immunol. 183:6251-6261(2009).
[37]
FUNCTION IN BA HOMEOSTASIS.
PubMed=19085950; DOI=10.1002/hep.22627;
Song K.H., Li T., Owsley E., Strom S., Chiang J.Y.;
"Bile acids activate fibroblast growth factor 19 signaling in human
hepatocytes to inhibit cholesterol 7alpha-hydroxylase gene expression.";
Hepatology 49:297-305(2009).
[38]
INTERACTION WITH SMARCA4.
PubMed=19805516; DOI=10.1128/mcb.00825-09;
Miao J., Fang S., Lee J., Comstock C., Knudsen K.E., Kemper J.K.;
"Functional specificities of Brm and Brg-1 Swi/Snf ATPases in the feedback
regulation of hepatic bile acid biosynthesis.";
Mol. Cell. Biol. 29:6170-6181(2009).
[39]
INTERACTION WITH PAGR1 AND NCOA6.
PubMed=19556342; DOI=10.1210/me.2009-0099;
Kim D.H., Lee J., Lee B., Lee J.W.;
"ASCOM controls farnesoid X receptor transactivation through its associated
histone H3 lysine 4 methyltransferase activity.";
Mol. Endocrinol. 23:1556-1562(2009).
[40]
FUNCTION IN GLUCOSE HOMEOSTASIS, AND TISSUE SPECIFICITY.
PubMed=20447400; DOI=10.1016/j.febslet.2010.04.068;
Popescu I.R., Helleboid-Chapman A., Lucas A., Vandewalle B., Dumont J.,
Bouchaert E., Derudas B., Kerr-Conte J., Caron S., Pattou F., Staels B.;
"The nuclear receptor FXR is expressed in pancreatic beta-cells and
protects human islets from lipotoxicity.";
FEBS Lett. 584:2845-2851(2010).
[41]
REVIEW.
PubMed=21383957; DOI=10.1621/nrs.08005;
Modica S., Gadaleta R.M., Moschetta A.;
"Deciphering the nuclear bile acid receptor FXR paradigm.";
Nucl. Recept. Signal. 8:E005-E005(2010).
[42]
FUNCTION IN INTESTINAL INFLAMMATION.
PubMed=21242261; DOI=10.1136/gut.2010.212159;
Gadaleta R.M., van Erpecum K.J., Oldenburg B., Willemsen E.C., Renooij W.,
Murzilli S., Klomp L.W., Siersema P.D., Schipper M.E., Danese S., Penna G.,
Laverny G., Adorini L., Moschetta A., van Mil S.W.;
"Farnesoid X receptor activation inhibits inflammation and preserves the
intestinal barrier in inflammatory bowel disease.";
Gut 60:463-472(2011).
[43]
FUNCTION IN LIPID HOMEOSTASIS.
PubMed=21804189; DOI=10.1172/jci45277;
Chennamsetty I., Claudel T., Kostner K.M., Baghdasaryan A., Kratky D.,
Levak-Frank S., Frank S., Gonzalez F.J., Trauner M., Kostner G.M.;
"Farnesoid X receptor represses hepatic human APOA gene expression.";
J. Clin. Invest. 121:3724-3734(2011).
[44]
REVIEW.
PubMed=22820415; DOI=10.1016/j.bbalip.2012.07.004;
Hollman D.A., Milona A., van Erpecum K.J., van Mil S.W.;
"Anti-inflammatory and metabolic actions of FXR: insights into molecular
mechanisms.";
Biochim. Biophys. Acta 1821:1443-1452(2012).
[45]
METHYLATION AT LYS-220 BY SETD7.
PubMed=22345554; DOI=10.1152/ajpgi.00441.2011;
Balasubramaniyan N., Ananthanarayanan M., Suchy F.J.;
"Direct methylation of FXR by Set7/9, a lysine methyltransferase, regulates
the expression of FXR target genes.";
Am. J. Physiol. 302:G937-G947(2012).
[46]
POSSIBLE INVOLVEMENT IN PRIMARY BILIARY CIRRHOSIS.
PubMed=23235576; DOI=10.1002/14651858.cd000551.pub3;
Rudic J.S., Poropat G., Krstic M.N., Bjelakovic G., Gluud C.;
"Ursodeoxycholic acid for primary biliary cirrhosis.";
Cochrane Database Syst. Rev. 12:CD000551-CD000551(2012).
[47]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=23928191; DOI=10.1016/j.bcp.2013.07.022;
Vaquero J., Monte M.J., Dominguez M., Muntane J., Marin J.J.;
"Differential activation of the human farnesoid X receptor depends on the
pattern of expressed isoforms and the bile acid pool composition.";
Biochem. Pharmacol. 86:926-939(2013).
[48]
SUMOYLATION AT LYS-132 AND LYS-289, AND MUTAGENESIS OF LYS-132; LYS-289 AND
GLU-291.
PubMed=23546875; DOI=10.1074/jbc.m112.443937;
Balasubramaniyan N., Luo Y., Sun A.Q., Suchy F.J.;
"SUMOylation of the farnesoid X receptor (FXR) regulates the expression of
FXR target genes.";
J. Biol. Chem. 288:13850-13862(2013).
[49]
MUTAGENESIS OF LYS-132; LYS-167; LYS-220; LYS-227; LYS-353 AND LYS-474, AND
INTERACTION WITH RXRA AND SETD7.
PubMed=23462506; DOI=10.1124/mol.113.084772;
Sun A.Q., Luo Y., Backos D.S., Xu S., Balasubramaniyan N., Reigan P.,
Suchy F.J.;
"Identification of functionally relevant lysine residues that modulate
human farnesoid X receptor activation.";
Mol. Pharmacol. 83:1078-1086(2013).
[50]
INVOLVEMENT IN PFIC5, VARIANT PFIC5 LYS-149 INS, CHARACTERIZATION OF
VARIANT PFIC5 LYS-149 INS (ISOFORM 4), AND FUNCTION (ISOFORM 4).
PubMed=26888176; DOI=10.1038/ncomms10713;
Gomez-Ospina N., Potter C.J., Xiao R., Manickam K., Kim M.S., Kim K.H.,
Shneider B.L., Picarsic J.L., Jacobson T.A., Zhang J., He W., Liu P.,
Knisely A.S., Finegold M.J., Muzny D.M., Boerwinkle E., Lupski J.R.,
Plon S.E., Gibbs R.A., Eng C.M., Yang Y., Washington G.C., Porteus M.H.,
Berquist W.E., Kambham N., Singh R.J., Xia F., Enns G.M., Moore D.D.;
"Mutations in the nuclear bile acid receptor FXR cause progressive familial
intrahepatic cholestasis.";
Nat. Commun. 7:10713-10713(2016).
[51]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 258-476 IN COMPLEX WITH SYNTHETIC
AGONIST FEXARAMINE, FUNCTION, AND INTERACTION WITH NCOA1.
PubMed=12718892; DOI=10.1016/s1097-2765(03)00104-7;
Downes M., Verdecia M.A., Roecker A.J., Hughes R., Hogenesch J.B.,
Kast-Woelbern H.R., Bowman M.E., Ferrer J.L., Anisfeld A.M., Edwards P.A.,
Rosenfeld J.M., Alvarez J.G., Noel J.P., Nicolaou K.C., Evans R.M.;
"A chemical, genetic, and structural analysis of the nuclear bile acid
receptor FXR.";
Mol. Cell 11:1079-1092(2003).
[52]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 241-469 IN COMPLEXES WITH
CHENODEOXYCHOLIC ACID ANALOGS AND NCOA2 COACTIVATOR PEPTIDE.
PubMed=12718893; DOI=10.1016/s1097-2765(03)00112-6;
Mi L.Z., Devarakonda S., Harp J.M., Han Q., Pellicciari R., Willson T.M.,
Khorasanizadeh S., Rastinejad F.;
"Structural basis for bile acid binding and activation of the nuclear
receptor FXR.";
Mol. Cell 11:1093-1100(2003).
[53]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 252-486 IN COMPLEX WITH SYNTHETIC
AGONIST, FUNCTION, AND INTERACTION WITH NCOA1.
PubMed=18621523; DOI=10.1016/j.bmcl.2008.06.073;
Akwabi-Ameyaw A., Bass J.Y., Caldwell R.D., Caravella J.A., Chen L.,
Creech K.L., Deaton D.N., Jones S.A., Kaldor I., Liu Y., Madauss K.P.,
Marr H.B., McFadyen R.B., Miller A.B., Iii F.N., Parks D.J., Spearing P.K.,
Todd D., Williams S.P., Wisely G.B.;
"Conformationally constrained farnesoid X receptor (FXR) agonists:
Naphthoic acid-based analogs of GW 4064.";
Bioorg. Med. Chem. Lett. 18:4339-4343(2008).
[54]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 249-486 IN COMPLEX WITH STEROID
ANALOG MFA-1 AND NCOA1 PEPTIDE, INTERACTION WITH NCOA1, AND DOMAIN.
PubMed=18391212; DOI=10.1073/pnas.0710981105;
Soisson S.M., Parthasarathy G., Adams A.D., Sahoo S., Sitlani A.,
Sparrow C., Cui J., Becker J.W.;
"Identification of a potent synthetic FXR agonist with an unexpected mode
of binding and activation.";
Proc. Natl. Acad. Sci. U.S.A. 105:5337-5342(2008).
[55]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 260-486 IN COMPLEX WITH SYNTHETIC
AGONIST, FUNCTION, AND INTERACTION WITH NCOA1.
PubMed=19410460; DOI=10.1016/j.bmcl.2009.04.047;
Bass J.Y., Caldwell R.D., Caravella J.A., Chen L., Creech K.L.,
Deaton D.N., Madauss K.P., Marr H.B., McFadyen R.B., Miller A.B.,
Parks D.J., Todd D., Williams S.P., Wisely G.B.;
"Substituted isoxazole analogs of farnesoid X receptor (FXR) agonist
GW4064.";
Bioorg. Med. Chem. Lett. 19:2969-2973(2009).
[56]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 257-486 IN COMPLEX WITH SYNTHETIC
AGONIST, FUNCTION, AND INTERACTION WITH NCOA1.
PubMed=19586769; DOI=10.1016/j.bmcl.2009.06.062;
Akwabi-Ameyaw A., Bass J.Y., Caldwell R.D., Caravella J.A., Chen L.,
Creech K.L., Deaton D.N., Madauss K.P., Marr H.B., McFadyen R.B.,
Miller A.B., Navas F. III, Parks D.J., Spearing P.K., Todd D.,
Williams S.P., Bruce Wisely G.;
"FXR agonist activity of conformationally constrained analogs of GW 4064.";
Bioorg. Med. Chem. Lett. 19:4733-4739(2009).
[57]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 258-486 IN COMPLEX WITH SYNTHETIC
AGONIST.
PubMed=19159286; DOI=10.1021/jm8014124;
Flatt B., Martin R., Wang T.L., Mahaney P., Murphy B., Gu X.H., Foster P.,
Li J., Pircher P., Petrowski M., Schulman I., Westin S., Wrobel J., Yan G.,
Bischoff E., Daige C., Mohan R.;
"Discovery of XL335 (WAY-362450), a highly potent, selective, and orally
active agonist of the farnesoid X receptor (FXR).";
J. Med. Chem. 52:904-907(2009).
[58]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 248-476 IN COMPLEX WITH SYNTHETIC
AGONIST.
PubMed=20095622; DOI=10.1021/jm901650u;
Lundquist J.T., Harnish D.C., Kim C.Y., Mehlmann J.F., Unwalla R.J.,
Phipps K.M., Crawley M.L., Commons T., Green D.M., Xu W., Hum W.T.,
Eta J.E., Feingold I., Patel V., Evans M.J., Lai K., Borges-Marcucci L.,
Mahaney P.E., Wrobel J.E.;
"Improvement of physiochemical properties of the tetrahydroazepinoindole
series of farnesoid X receptor (FXR) agonists: beneficial modulation of
lipids in primates.";
J. Med. Chem. 53:1774-1787(2010).
[59] {ECO:0000244|PDB:6A5Y}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 258-485 IN COMPLEX WITH RXRA;
SYNTHETIC AGONISTS AND NCOA1 PEPTIDE, AND MUTAGENESIS OF ARG-455.
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: Ligand-activated transcription factor. Receptor for bile
acids (BAs) such as chenodeoxycholic acid (CDCA), lithocholic acid,
deoxycholic acid (DCA) and allocholic acid (ACA). Plays a essential
role in BA homeostasis through the regulation of genes involved in BA
synthesis, conjugation and enterohepatic circulation. Also regulates
lipid and glucose homeostasis and is involved innate immune response
(PubMed:10334992, PubMed:10334993, PubMed:21383957, PubMed:22820415).
The FXR-RXR heterodimer binds predominantly to farnesoid X receptor
response elements (FXREs) containing two inverted repeats of the
consensus sequence 5'-AGGTCA-3' in which the monomers are spaced by 1
nucleotide (IR-1) but also to tandem repeat DR1 sites with lower
affinity, and can be activated by either FXR or RXR-specific ligands.
It is proposed that monomeric nuclear receptors such as NR5A2/LRH-1
bound to coregulatory nuclear responsive element (NRE) halfsites
located in close proximity to FXREs modulate transcriptional activity
(By similarity). In the liver activates transcription of the
corepressor NR0B2 thereby indirectly inhibiting CYP7A1 and CYP8B1
(involved in BA synthesis) implicating at least in part histone
demethylase KDM1A resulting in epigenomic repression, and SLC10A1/NTCP
(involved in hepatic uptake of conjugated BAs). Activates transcription
of the repressor MAFG (involved in regulation of BA synthesis) (By
similarity). Activates transcription of SLC27A5/BACS and BAAT (involved
in BA conjugation), ABCB11/BSEP (involved in bile salt export) by
directly recruiting histone methyltransferase CARM1, and ABCC2/MRP2
(involved in secretion of conjugated BAs) and ABCB4 (involved in
secretion of phosphatidylcholine in the small intestine)
(PubMed:12754200, PubMed:15471871, PubMed:17895379). Activates
transcription of SLC27A5/BACS and BAAT (involved in BA conjugation),
ABCB11/BSEP (involved in bile salt export) by directly recruiting
histone methyltransferase CARM1, and ABCC2/MRP2 (involved in secretion
of conjugated BAs) and ABCB4 (involved in secretion of
phosphatidylcholine in the small intestine) (PubMed:10514450,
PubMed:15239098, PubMed:16269519). In the intestine activates FGF19
expression and secretion leading to hepatic CYP7A1 repression
(PubMed:12815072, PubMed:19085950). The function also involves the
coordinated induction of hepatic KLB/beta-klotho expression (By
similarity). Regulates transcription of liver UGT2B4 and SULT2A1
involved in BA detoxification; binding to the UGT2B4 promoter seems to
imply a monomeric transactivation independent of RXRA (PubMed:12806625,
PubMed:16946559). Modulates lipid homeostasis by activating liver
NR0B2/SHP-mediated repression of SREBF1 (involved in de novo
lipogenesis), expression of PLTP (involved in HDL formation), SCARB1
(involved in HDL hepatic uptake), APOE, APOC1, APOC4, PPARA (involved
in beta-oxidation of fatty acids), VLDLR and SDC1 (involved in the
hepatic uptake of LDL and IDL remnants), and inhibiting expression of
MTTP (involved in VLDL assembly (PubMed:12660231, PubMed:12554753,
PubMed:15337761). Increases expression of APOC2 (promoting lipoprotein
lipase activity implicated in triglyceride clearance)
(PubMed:11579204). Transrepresses APOA1 involving a monomeric
competition with NR2A1 for binding to a DR1 element (PubMed:11927623,
PubMed:21804189). Also reduces triglyceride clearance by inhibiting
expression of ANGPTL3 and APOC3 (both involved in inhibition of
lipoprotein lipase) (PubMed:12891557). Involved in glucose homeostasis
by modulating hepatic gluconeogenesis through activation of NR0B2/SHP-
mediated repression of respective genes. Modulates glycogen synthesis
(inducing phosphorylation of glycogen synthase kinase-3) (By
similarity). Modulates glucose-stimulated insulin secretion and is
involved in insulin resistance (PubMed:20447400). Involved in
intestinal innate immunity. Plays a role in protecting the distal small
intestine against bacterial overgrowth and preservation of the
epithelial barrier (By similarity). Down-regulates inflammatory
cytokine expression in several types of immune cells including
macrophages and mononuclear cells (PubMed:21242261). Mediates trans-
repression of TLR4-induced cytokine expression; the function seems to
require its sumoylation and prevents N-CoR nuclear receptor corepressor
clearance from target genes such as IL1B and NOS2 (PubMed:19864602).
Involved in the TLR9-mediated protective mechanism in intestinal
inflammation. Plays an anti-inflammatory role in liver inflammation;
proposed to inhibit proinflammatory (but not antiapoptotic) NF-kappa-B
signaling) (By similarity). {ECO:0000250|UniProtKB:Q60641,
ECO:0000250|UniProtKB:Q62735, ECO:0000269|PubMed:10334992,
ECO:0000269|PubMed:10334993, ECO:0000269|PubMed:10514450,
ECO:0000269|PubMed:11579204, ECO:0000269|PubMed:11927623,
ECO:0000269|PubMed:12554753, ECO:0000269|PubMed:12660231,
ECO:0000269|PubMed:12718892, ECO:0000269|PubMed:12754200,
ECO:0000269|PubMed:12806625, ECO:0000269|PubMed:12815072,
ECO:0000269|PubMed:12891557, ECO:0000269|PubMed:14684751,
ECO:0000269|PubMed:15239098, ECO:0000269|PubMed:15337761,
ECO:0000269|PubMed:15471871, ECO:0000269|PubMed:16269519,
ECO:0000269|PubMed:16946559, ECO:0000269|PubMed:17895379,
ECO:0000269|PubMed:18621523, ECO:0000269|PubMed:19085950,
ECO:0000269|PubMed:19410460, ECO:0000269|PubMed:19586769,
ECO:0000269|PubMed:19864602, ECO:0000269|PubMed:20447400,
ECO:0000269|PubMed:21242261, ECO:0000269|PubMed:21804189,
ECO:0000269|PubMed:23928191, ECO:0000305|PubMed:21383957,
ECO:0000305|PubMed:22820415}.
-!- FUNCTION: [Isoform 1]: Promotes transcriptional activation of target
genes NR0B2/SHP (inducible by unconjugated CDCA), SLC51B/OSTB
(inducible by unconjugated CDCA and DCA) and FABP6/IBAP; low activity
for ABCB11/BSEP (inducible by unconjugated CDCA, DCA and ACA); not
inducible by taurine- and glycine-amidated CDCA.
{ECO:0000269|PubMed:23928191}.
-!- FUNCTION: [Isoform 2]: Promotes transcriptional activation of target
genes ABCB11/BSEP (inducible by unconjugated CDCA, DCA and ACA),
NR0B2/SHP (inducible by unconjugated CDCA DCA and ACA), SLC51B/OSTB
(inducible by unconjugated CDCA and DCA) and FABP6/IBAP; not inducible
by taurine- and glycine-amidated CDCA. {ECO:0000269|PubMed:23928191}.
-!- FUNCTION: [Isoform 3]: Promotes transcriptional activation of target
genes NR0B2/SHP (inducible by unconjugated CDCA), SLC51B/OSTB
(inducible by unconjugated CDCA and DCA) and IBAP; low activity for
ABCB11/BSEP (inducible by unconjugated CDCA, DCA and ACA); not
inducible by taurine- and glycine-amidated CDCA.
{ECO:0000269|PubMed:23928191}.
-!- FUNCTION: [Isoform 4]: Promotes transcriptional activation of target
genes ABCB11/BSEP (inducible by unconjugated CDCA, ACA and DCA),
NR0B2/SHP (inducible by unconjugated CDCA, ACA and DCA), SLC51B/OSTB
(inducible by unconjugated CDCA and DCA) and FABP6/IBAP; most efficient
isoform compared to isoforms 1 to 3; not inducible by taurine- and
glycine-amidated CDCA. {ECO:0000269|PubMed:23928191,
ECO:0000269|PubMed:26888176}.
-!- SUBUNIT: Heterodimer (via C-terminus) with RXRA (via DBD); the
heterodimerization enhances the binding affinity for LXXLL motifs from
coactivators (PubMed:23462506, PubMed:30275017). Binds DNA
predominantly as a heterodimer with RXRA. After activation by agonist
binding interacts with coactivators. Interacts with NCOA1, NCOA2,
PPARGC1A, CARM1, SETD7, PRMT1, GPS2, SMARCA4 and MED1 (PubMed:15202934,
PubMed:14684751, PubMed:15187081, PubMed:15471871, PubMed:15911693,
PubMed:17895379, PubMed:18755856, PubMed:19805516, PubMed:23462506,
PubMed:12718892, PubMed:12718893, PubMed:18621523, PubMed:18391212,
PubMed:19410460, PubMed:19586769). Interacts with EP300 and SMARCD1 (By
similarity). Interacts with XRCC5 and XRCC6; decreasing NR1H4/FXR
transactivation activity towards ABCB11/BSEP (PubMed:19833092).
Interacts with PAGR1 AND NCOA6; indicative for an association with an
MLL2/MLL3 complex (ASCOM) (PubMed:19556342).
{ECO:0000250|UniProtKB:Q60641, ECO:0000250|UniProtKB:Q62735,
ECO:0000269|PubMed:12718892, ECO:0000269|PubMed:12718893,
ECO:0000269|PubMed:14684751, ECO:0000269|PubMed:15187081,
ECO:0000269|PubMed:15202934, ECO:0000269|PubMed:15471871,
ECO:0000269|PubMed:15911693, ECO:0000269|PubMed:17895379,
ECO:0000269|PubMed:18391212, ECO:0000269|PubMed:18621523,
ECO:0000269|PubMed:19159286, ECO:0000269|PubMed:19410460,
ECO:0000269|PubMed:19556342, ECO:0000269|PubMed:19586769,
ECO:0000269|PubMed:19805516, ECO:0000269|PubMed:19833092,
ECO:0000269|PubMed:23462506, ECO:0000269|PubMed:30275017}.
-!- INTERACTION:
Q96RI1-3; P03372: ESR1; NbExp=2; IntAct=EBI-10921781, EBI-78473;
Q96RI1; Q15788: NCOA1; NbExp=4; IntAct=EBI-1250177, EBI-455189;
Q96RI1-2; Q15788: NCOA1; NbExp=5; IntAct=EBI-9640524, EBI-455189;
Q96RI1-2; P78527: PRKDC; NbExp=4; IntAct=EBI-9640524, EBI-352053;
Q96RI1-1; P28702: RXRB; NbExp=7; IntAct=EBI-12417284, EBI-748576;
Q96RI1-1; P28702-3: RXRB; NbExp=3; IntAct=EBI-12417284, EBI-16429492;
Q96RI1-1; P48443: RXRG; NbExp=3; IntAct=EBI-12417284, EBI-712405;
Q96RI1; Q8WTS6: SETD7; NbExp=5; IntAct=EBI-1250177, EBI-1268586;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19864602}.
-!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
{ECO:0000269|PubMed:23928191}.
-!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
{ECO:0000269|PubMed:23928191}.
-!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus
{ECO:0000269|PubMed:23928191}.
-!- SUBCELLULAR LOCATION: [Isoform 4]: Nucleus
{ECO:0000269|PubMed:23928191}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
Name=1; Synonyms=FXRalpha2(+), FXRalpha1, FXRbeta1;
IsoId=Q96RI1-3; Sequence=Displayed;
Name=2; Synonyms=FXRalpha2(-), FXRalpha4, FXRbeta2;
IsoId=Q96RI1-4; Sequence=VSP_003665;
Name=3; Synonyms=FXRalpha1(+), FXRalpha1;
IsoId=Q96RI1-1; Sequence=VSP_010135;
Name=4; Synonyms=FXRalpha1(-), FXRalpha2;
IsoId=Q96RI1-2; Sequence=VSP_010135, VSP_003665;
Name=5;
IsoId=Q96RI1-5; Sequence=VSP_010135, VSP_044547;
-!- TISSUE SPECIFICITY: Liver and hepatocyte-related cells express mainly
FXRalpha1-type isoforms with isoform 3 and isoform 4 in approximately
equal proportions. In intestine and kidney mainly FXRalpha2-type
isoforms are expressed with isoform 1 and isoform 2 in approximately
equal proportions. Expressed in pancreatic beta cells and macrophages.
{ECO:0000269|PubMed:19393742, ECO:0000269|PubMed:19864602,
ECO:0000269|PubMed:20447400, ECO:0000269|PubMed:23928191}.
-!- PTM: Acetylated by EP300. Lys-227 as is the major acetylation site for
EP300; the dynamicly regulated acetylation inhibits heterodimerization
with RXRA and transactivation activity. Deacetylated by SIRT1.
{ECO:0000269|PubMed:18755856}.
-!- PTM: Methylation may increase transactivation of target genes.
{ECO:0000269|PubMed:22345554}.
-!- PTM: Phosphorylation by PKC/PRKCA increases transactivation activity by
promoting association with PPARGC1A. {ECO:0000269|PubMed:18755856}.
-!- PTM: Sumoylated upon ligand binding. {ECO:0000269|PubMed:19864602,
ECO:0000269|PubMed:23546875}.
-!- DISEASE: Note=May be involved in intrahepatic cholestasis of pregnancy.
{ECO:0000305|PubMed:17681172}.
-!- DISEASE: Note=May be involved in cholesterol cholelithiasis.
{ECO:0000305|PubMed:17931734}.
-!- DISEASE: Cholestasis, progressive familial intrahepatic, 5 (PFIC5)
[MIM:617049]: A disorder characterized by early onset of cholestasis
that progresses to hepatic fibrosis, cirrhosis, and end-stage liver
disease before adulthood. PFIC5 is an autosomal recessive, severe form
characterized by onset of intralobular cholestasis in the neonatal
period. {ECO:0000269|PubMed:26888176}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Ursodeoxycholic (UDCA), a natural agonist of FXR, is
approved to treat primary biliary cirrhosis. However, effects are
discussed controversial. UDCA is also used to dissolve (cholesterol)
gallstones as alternative to surgery. {ECO:0000305|PubMed:23235576}.
-!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
-!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform
1. {ECO:0000305}.
-!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
{ECO:0000305}.
-!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform
3. {ECO:0000305}.
-!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing of isoform
3. {ECO:0000305}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BC144183; Type=Frameshift; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Farnesoid X receptor entry;
URL="https://en.wikipedia.org/wiki/Farnesoid_X_receptor";
---------------------------------------------------------------------------
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EMBL; U68233; AAB08107.1; -; mRNA.
EMBL; AF384555; AAK60271.1; -; mRNA.
EMBL; AF478445; AAM53550.1; -; mRNA.
EMBL; AF478446; AAM53551.1; -; mRNA.
EMBL; AK296612; BAH12398.1; -; mRNA.
EMBL; AC010200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW97639.1; -; Genomic_DNA.
EMBL; BC144183; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC144184; AAI44185.1; -; mRNA.
EMBL; BC130573; AAI30574.1; -; mRNA.
CCDS; CCDS55873.1; -. [Q96RI1-1]
CCDS; CCDS55874.1; -. [Q96RI1-5]
CCDS; CCDS55875.1; -. [Q96RI1-4]
CCDS; CCDS55876.1; -. [Q96RI1-3]
CCDS; CCDS9078.1; -. [Q96RI1-2]
RefSeq; NP_001193906.1; NM_001206977.1. [Q96RI1-1]
RefSeq; NP_001193907.1; NM_001206978.1. [Q96RI1-5]
RefSeq; NP_001193908.1; NM_001206979.1. [Q96RI1-1]
RefSeq; NP_001193921.1; NM_001206992.1. [Q96RI1-4]
RefSeq; NP_001193922.1; NM_001206993.1. [Q96RI1-3]
RefSeq; NP_005114.1; NM_005123.3. [Q96RI1-2]
RefSeq; XP_011537342.1; XM_011539040.2. [Q96RI1-1]
PDB; 1OSH; X-ray; 1.80 A; A=258-486.
PDB; 1OSK; Model; -; A=258-486.
PDB; 3BEJ; X-ray; 1.90 A; A/B=249-486.
PDB; 3DCT; X-ray; 2.50 A; A=252-486.
PDB; 3DCU; X-ray; 2.95 A; A=252-486.
PDB; 3FLI; X-ray; 2.00 A; A=258-486.
PDB; 3FXV; X-ray; 2.26 A; A=258-486.
PDB; 3GD2; X-ray; 3.20 A; A=260-486.
PDB; 3HC5; X-ray; 2.60 A; A=257-486.
PDB; 3HC6; X-ray; 3.20 A; A=257-486.
PDB; 3L1B; X-ray; 1.90 A; A=258-486.
PDB; 3OKH; X-ray; 2.50 A; A=258-486.
PDB; 3OKI; X-ray; 2.00 A; A/C=258-486.
PDB; 3OLF; X-ray; 1.90 A; A/C=258-486.
PDB; 3OMK; X-ray; 1.90 A; A/C=258-486.
PDB; 3OMM; X-ray; 2.10 A; A/C=258-486.
PDB; 3OOF; X-ray; 2.29 A; A/C=258-486.
PDB; 3OOK; X-ray; 2.29 A; A/C=258-486.
PDB; 3P88; X-ray; 2.95 A; A=258-486.
PDB; 3P89; X-ray; 2.30 A; A=258-486.
PDB; 3RUT; X-ray; 3.00 A; A=258-486.
PDB; 3RUU; X-ray; 2.50 A; A=258-486.
PDB; 3RVF; X-ray; 3.10 A; A=257-486.
PDB; 4OIV; X-ray; 1.70 A; A/B=258-483.
PDB; 4QE6; X-ray; 1.65 A; A=258-486.
PDB; 4QE8; X-ray; 2.62 A; A/B=258-486.
PDB; 4WVD; X-ray; 2.90 A; A/B=258-468.
PDB; 5IAW; X-ray; 2.58 A; A/B=259-486.
PDB; 5ICK; X-ray; 2.47 A; A/B=258-486.
PDB; 5Q0I; X-ray; 1.70 A; A=258-486.
PDB; 5Q0J; X-ray; 2.00 A; A/C=258-486.
PDB; 5Q0K; X-ray; 1.80 A; A=258-486.
PDB; 5Q0L; X-ray; 2.50 A; A/C=258-486.
PDB; 5Q0M; X-ray; 2.20 A; A=258-486.
PDB; 5Q0N; X-ray; 2.40 A; A/C=258-486.
PDB; 5Q0O; X-ray; 1.90 A; A/C=258-486.
PDB; 5Q0P; X-ray; 1.80 A; A/C=258-486.
PDB; 5Q0Q; X-ray; 2.60 A; A/C=258-486.
PDB; 5Q0R; X-ray; 1.91 A; A=258-486.
PDB; 5Q0S; X-ray; 2.50 A; A/C=258-486.
PDB; 5Q0T; X-ray; 2.14 A; A=258-486.
PDB; 5Q0U; X-ray; 1.90 A; A/C=258-486.
PDB; 5Q0V; X-ray; 1.87 A; A/C=258-486.
PDB; 5Q0W; X-ray; 1.90 A; A=258-486.
PDB; 5Q0X; X-ray; 2.26 A; A=258-486.
PDB; 5Q0Y; X-ray; 2.20 A; A/C=258-486.
PDB; 5Q0Z; X-ray; 2.26 A; A/C=258-486.
PDB; 5Q10; X-ray; 2.20 A; A=258-486.
PDB; 5Q11; X-ray; 2.20 A; A=258-486.
PDB; 5Q12; X-ray; 2.00 A; A=258-486.
PDB; 5Q13; X-ray; 1.90 A; A/C=258-486.
PDB; 5Q14; X-ray; 1.85 A; A/C=258-486.
PDB; 5Q15; X-ray; 1.90 A; A/C=258-486.
PDB; 5Q16; X-ray; 2.00 A; A/C=258-486.
PDB; 5Q17; X-ray; 2.10 A; A=258-486.
PDB; 5Q18; X-ray; 1.90 A; A/C=258-486.
PDB; 5Q19; X-ray; 1.98 A; A/C=258-486.
PDB; 5Q1A; X-ray; 2.00 A; A/C=258-486.
PDB; 5Q1B; X-ray; 2.30 A; A/C=258-486.
PDB; 5Q1C; X-ray; 2.30 A; A/C=258-486.
PDB; 5Q1D; X-ray; 1.89 A; A/C=258-486.
PDB; 5Q1E; X-ray; 1.85 A; A=258-486.
PDB; 5Q1F; X-ray; 2.30 A; A/C=258-486.
PDB; 5Q1G; X-ray; 2.00 A; A=258-486.
PDB; 5Q1H; X-ray; 2.20 A; A/C/E/G=258-486.
PDB; 5Q1I; X-ray; 1.95 A; A=258-486.
PDB; 5WZX; X-ray; 2.95 A; A/B=258-485.
PDB; 5Y1J; X-ray; 2.00 A; A=258-485.
PDB; 5Y44; X-ray; 2.35 A; A=258-485.
PDB; 5Y49; X-ray; 2.40 A; A/B=259-485.
PDB; 5YXB; X-ray; 2.95 A; A=258-486.
PDB; 5YXD; X-ray; 2.98 A; A=258-486.
PDB; 5YXJ; X-ray; 2.62 A; A/B=258-486.
PDB; 5YXL; X-ray; 2.24 A; A/C=258-486.
PDB; 5Z12; X-ray; 2.75 A; A/D=259-486.
PDB; 6A5W; X-ray; 2.88 A; A/C=258-485.
PDB; 6A5X; X-ray; 2.60 A; A=258-486.
PDB; 6A5Y; X-ray; 2.10 A; A=258-485.
PDB; 6A5Z; X-ray; 2.95 A; A/H=258-486.
PDB; 6A60; X-ray; 3.05 A; A=258-486.
PDB; 6HL0; X-ray; 1.66 A; A=258-486.
PDB; 6HL1; X-ray; 1.60 A; A=258-486.
PDB; 6ITM; X-ray; 2.50 A; A/C=257-486.
PDBsum; 1OSH; -.
PDBsum; 1OSK; -.
PDBsum; 3BEJ; -.
PDBsum; 3DCT; -.
PDBsum; 3DCU; -.
PDBsum; 3FLI; -.
PDBsum; 3FXV; -.
PDBsum; 3GD2; -.
PDBsum; 3HC5; -.
PDBsum; 3HC6; -.
PDBsum; 3L1B; -.
PDBsum; 3OKH; -.
PDBsum; 3OKI; -.
PDBsum; 3OLF; -.
PDBsum; 3OMK; -.
PDBsum; 3OMM; -.
PDBsum; 3OOF; -.
PDBsum; 3OOK; -.
PDBsum; 3P88; -.
PDBsum; 3P89; -.
PDBsum; 3RUT; -.
PDBsum; 3RUU; -.
PDBsum; 3RVF; -.
PDBsum; 4OIV; -.
PDBsum; 4QE6; -.
PDBsum; 4QE8; -.
PDBsum; 4WVD; -.
PDBsum; 5IAW; -.
PDBsum; 5ICK; -.
PDBsum; 5Q0I; -.
PDBsum; 5Q0J; -.
PDBsum; 5Q0K; -.
PDBsum; 5Q0L; -.
PDBsum; 5Q0M; -.
PDBsum; 5Q0N; -.
PDBsum; 5Q0O; -.
PDBsum; 5Q0P; -.
PDBsum; 5Q0Q; -.
PDBsum; 5Q0R; -.
PDBsum; 5Q0S; -.
PDBsum; 5Q0T; -.
PDBsum; 5Q0U; -.
PDBsum; 5Q0V; -.
PDBsum; 5Q0W; -.
PDBsum; 5Q0X; -.
PDBsum; 5Q0Y; -.
PDBsum; 5Q0Z; -.
PDBsum; 5Q10; -.
PDBsum; 5Q11; -.
PDBsum; 5Q12; -.
PDBsum; 5Q13; -.
PDBsum; 5Q14; -.
PDBsum; 5Q15; -.
PDBsum; 5Q16; -.
PDBsum; 5Q17; -.
PDBsum; 5Q18; -.
PDBsum; 5Q19; -.
PDBsum; 5Q1A; -.
PDBsum; 5Q1B; -.
PDBsum; 5Q1C; -.
PDBsum; 5Q1D; -.
PDBsum; 5Q1E; -.
PDBsum; 5Q1F; -.
PDBsum; 5Q1G; -.
PDBsum; 5Q1H; -.
PDBsum; 5Q1I; -.
PDBsum; 5WZX; -.
PDBsum; 5Y1J; -.
PDBsum; 5Y44; -.
PDBsum; 5Y49; -.
PDBsum; 5YXB; -.
PDBsum; 5YXD; -.
PDBsum; 5YXJ; -.
PDBsum; 5YXL; -.
PDBsum; 5Z12; -.
PDBsum; 6A5W; -.
PDBsum; 6A5X; -.
PDBsum; 6A5Y; -.
PDBsum; 6A5Z; -.
PDBsum; 6A60; -.
PDBsum; 6HL0; -.
PDBsum; 6HL1; -.
PDBsum; 6ITM; -.
SMR; Q96RI1; -.
BioGrid; 115296; 25.
DIP; DIP-39370N; -.
IntAct; Q96RI1; 14.
STRING; 9606.ENSP00000447149; -.
BindingDB; Q96RI1; -.
ChEMBL; CHEMBL2047; -.
DrugBank; DB08220; (8alpha,10alpha,13alpha,17beta)-17-[(4-hydroxyphenyl)carbonyl]androsta-3,5-diene-3-carboxylic acid.
DrugBank; DB00132; alpha-Linolenic acid.
DrugBank; DB04557; Arachidonic Acid.
DrugBank; DB06777; Chenodeoxycholic acid.
DrugBank; DB02659; Cholic Acid.
DrugBank; DB03619; Deoxycholic acid.
DrugBank; DB02509; Farnesol.
DrugBank; DB02545; Fexaramine.
DrugBank; DB11605; Myrrh.
DrugBank; DB05990; Obeticholic acid.
DrugBank; DB04348; Taurocholic acid.
DrugBank; DB01586; Ursodeoxycholic acid.
DrugCentral; Q96RI1; -.
GuidetoPHARMACOLOGY; 603; -.
SwissLipids; SLP:000001581; -.
iPTMnet; Q96RI1; -.
PhosphoSitePlus; Q96RI1; -.
BioMuta; NR1H4; -.
DMDM; 46577705; -.
jPOST; Q96RI1; -.
MassIVE; Q96RI1; -.
PaxDb; Q96RI1; -.
PeptideAtlas; Q96RI1; -.
PRIDE; Q96RI1; -.
ProteomicsDB; 29204; -.
ProteomicsDB; 77963; -. [Q96RI1-3]
ProteomicsDB; 77964; -. [Q96RI1-1]
ProteomicsDB; 77965; -. [Q96RI1-2]
ProteomicsDB; 77966; -. [Q96RI1-4]
Antibodypedia; 17868; 424 antibodies.
DNASU; 9971; -.
Ensembl; ENST00000188403; ENSP00000188403; ENSG00000012504. [Q96RI1-4]
Ensembl; ENST00000392986; ENSP00000376712; ENSG00000012504. [Q96RI1-1]
Ensembl; ENST00000548884; ENSP00000448506; ENSG00000012504. [Q96RI1-2]
Ensembl; ENST00000549996; ENSP00000448978; ENSG00000012504. [Q96RI1-5]
Ensembl; ENST00000551379; ENSP00000447149; ENSG00000012504. [Q96RI1-3]
Ensembl; ENST00000648861; ENSP00000496908; ENSG00000012504. [Q96RI1-1]
GeneID; 9971; -.
KEGG; hsa:9971; -.
UCSC; uc001thp.3; human. [Q96RI1-3]
CTD; 9971; -.
DisGeNET; 9971; -.
GeneCards; NR1H4; -.
HGNC; HGNC:7967; NR1H4.
HPA; ENSG00000012504; Tissue enriched (liver).
MalaCards; NR1H4; -.
MIM; 603826; gene.
MIM; 617049; phenotype.
neXtProt; NX_Q96RI1; -.
OpenTargets; ENSG00000012504; -.
Orphanet; 69665; Intrahepatic cholestasis of pregnancy.
Orphanet; 480476; Progressive familial intrahepatic cholestasis type 5.
PharmGKB; PA31752; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00940000158037; -.
HOGENOM; CLU_007368_12_3_1; -.
InParanoid; Q96RI1; -.
KO; K08537; -.
OMA; HPDNPQH; -.
OrthoDB; 1137281at2759; -.
PhylomeDB; Q96RI1; -.
TreeFam; TF316304; -.
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-211976; Endogenous sterols.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-4090294; SUMOylation of intracellular receptors. [Q96RI1-2]
SignaLink; Q96RI1; -.
SIGNOR; Q96RI1; -.
ChiTaRS; NR1H4; human.
EvolutionaryTrace; Q96RI1; -.
GeneWiki; Farnesoid_X_receptor; -.
GenomeRNAi; 9971; -.
Pharos; Q96RI1; Tclin.
PRO; PR:Q96RI1; -.
Proteomes; UP000005640; Chromosome 12.
RNAct; Q96RI1; protein.
Bgee; ENSG00000012504; Expressed in right lobe of liver and 89 other tissues.
ExpressionAtlas; Q96RI1; baseline and differential.
Genevisible; Q96RI1; HS.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
GO; GO:0005719; C:nuclear euchromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IBA:GO_Central.
GO; GO:0032052; F:bile acid binding; ISS:BHF-UCL.
GO; GO:0038181; F:bile acid receptor activity; IDA:UniProtKB.
GO; GO:1902122; F:chenodeoxycholic acid binding; IDA:UniProtKB.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
GO; GO:0098531; F:ligand-activated transcription factor activity; IBA:GO_Central.
GO; GO:0004879; F:nuclear receptor activity; IDA:ParkinsonsUK-UCL.
GO; GO:0016922; F:nuclear receptor binding; TAS:BHF-UCL.
GO; GO:0030374; F:nuclear receptor transcription coactivator activity; IBA:GO_Central.
GO; GO:0046965; F:retinoid X receptor binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IMP:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0015721; P:bile acid and bile salt transport; TAS:Reactome.
GO; GO:0008206; P:bile acid metabolic process; IEA:Ensembl.
GO; GO:0038183; P:bile acid signaling pathway; ISS:BHF-UCL.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0007043; P:cell-cell junction assembly; IEA:Ensembl.
GO; GO:0001678; P:cellular glucose homeostasis; IEA:Ensembl.
GO; GO:1903413; P:cellular response to bile acid; IDA:UniProtKB.
GO; GO:0071398; P:cellular response to fatty acid; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0071417; P:cellular response to organonitrogen compound; ISS:BHF-UCL.
GO; GO:0035356; P:cellular triglyceride homeostasis; IDA:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
GO; GO:0034971; P:histone H3-R17 methylation; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0072615; P:interleukin-17 secretion; IDA:UniProtKB.
GO; GO:0038185; P:intracellular bile acid receptor signaling pathway; IDA:UniProtKB.
GO; GO:0030522; P:intracellular receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; IBA:GO_Central.
GO; GO:1902714; P:negative regulation of interferon-gamma secretion; IDA:UniProtKB.
GO; GO:0032692; P:negative regulation of interleukin-1 production; IEA:Ensembl.
GO; GO:0032703; P:negative regulation of interleukin-2 production; IEA:Ensembl.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IEA:Ensembl.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
GO; GO:1904468; P:negative regulation of tumor necrosis factor secretion; IDA:UniProtKB.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
GO; GO:0001080; P:nitrogen catabolite activation of transcription from RNA polymerase II promoter; IC:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:1904179; P:positive regulation of adipose tissue development; IEA:Ensembl.
GO; GO:2001250; P:positive regulation of ammonia assimilation cycle; IEA:Ensembl.
GO; GO:2000213; P:positive regulation of glutamate metabolic process; ISS:BHF-UCL.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:1905695; P:positive regulation of phosphatidic acid biosynthetic process; IDA:ParkinsonsUK-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
GO; GO:0070857; P:regulation of bile acid biosynthetic process; TAS:BHF-UCL.
GO; GO:0090181; P:regulation of cholesterol metabolic process; TAS:BHF-UCL.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:UniProtKB.
GO; GO:0010988; P:regulation of low-density lipoprotein particle clearance; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0034255; P:regulation of urea metabolic process; ISS:BHF-UCL.
GO; GO:0033993; P:response to lipid; IBA:GO_Central.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IDA:UniProtKB.
GO; GO:0034162; P:toll-like receptor 9 signaling pathway; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DisProt; DP01914; -.
Gene3D; 1.10.565.10; -; 1.
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; Acetylation; Activator; Alternative promoter usage;
Alternative splicing; Disease mutation; DNA-binding; Immunity;
Inflammatory response; Innate immunity; Intrahepatic cholestasis;
Isopeptide bond; Metal-binding; Methylation; Nucleus; Phosphoprotein;
Receptor; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1..486
/note="Bile acid receptor"
/id="PRO_0000053538"
DOMAIN 262..486
/note="NR LBD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
DNA_BIND 134..209
/note="Nuclear receptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 137..157
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 173..197
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
REGION 342..350
/note="Agonist binding"
/evidence="ECO:0000250|UniProtKB:Q62735"
BINDING 375
/note="Agonist"
/evidence="ECO:0000250|UniProtKB:Q62735"
BINDING 383
/note="Agonist"
/evidence="ECO:0000250|UniProtKB:Q62735"
BINDING 461
/note="Agonist"
/evidence="ECO:0000250|UniProtKB:Q62735"
BINDING 483
/note="Agonist"
/evidence="ECO:0000250|UniProtKB:Q62735"
MOD_RES 145
/note="Phosphoserine; by PKC/PRKCA"
/evidence="ECO:0000269|PubMed:18755856"
MOD_RES 164
/note="Phosphoserine; by PKC/PRKCA"
/evidence="ECO:0000269|PubMed:18755856"
MOD_RES 167
/note="N6-acetyllysine; by EP300"
MOD_RES 220
/note="N6-methyllysine; by SETD7"
/evidence="ECO:0000269|PubMed:22345554"
MOD_RES 227
/note="N6-acetyllysine; by EP300"
MOD_RES 456
/note="Phosphothreonine; by PKC/PRKCZ"
/evidence="ECO:0000305|PubMed:18668687"
CROSSLNK 132
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1)"
/evidence="ECO:0000305|PubMed:23546875"
CROSSLNK 289
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO1)"
/evidence="ECO:0000305|PubMed:23546875"
VAR_SEQ 1..36
/note="MVMQFQGLENPIQISPHCSCTPSGFFMEMMSMKPAK -> MGSKMNLIEHSH
LPTTDEFSFSENLF (in isoform 3, isoform 4 and isoform 5)"
/evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
ECO:0000303|Ref.2"
/id="VSP_010135"
VAR_SEQ 159..209
/note="Missing (in isoform 5)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_044547"
VAR_SEQ 207..210
/note="Missing (in isoform 2 and isoform 4)"
/evidence="ECO:0000303|PubMed:12062799, ECO:0000303|Ref.2"
/id="VSP_003665"
VARIANT 149
/note="Y -> YK (in PFIC5; loss of isoform 4 transcription
regulatory region sequence-specific DNA binding activity;
loss of isoform 4 function in regulation of transcription
DNA-templated)"
/evidence="ECO:0000269|PubMed:26888176"
/id="VAR_077017"
MUTAGEN 132
/note="K->R: Abrogates SUMO1-mediated inhibition of ligand-
induced transcactivation at ABCB11/BSEP and NR0B2/SHP
promoters; when associated with R-289 and A-291."
/evidence="ECO:0000269|PubMed:23546875"
MUTAGEN 132
/note="K->R: Decreases transcriptional activation
SLC51A/OSTA, SLC51B/OSTB and ABCB11/BSEP, no effect on
interaction with RXRA and SETD7."
/evidence="ECO:0000269|PubMed:23462506"
MUTAGEN 145
/note="S->A: Impairs ligand-dependent transactivation
activity, impairs interaction with PPARGC1A; when
associated with A-164."
/evidence="ECO:0000269|PubMed:18755856"
MUTAGEN 164
/note="S->A: Impairs ligand-dependent transactivation
activity, impairs interaction with PPARGC1A; when
associated with A-145."
/evidence="ECO:0000269|PubMed:18755856"
MUTAGEN 167
/note="K->R: Decreases transcriptional activation of
SLC51B/OSTB, no effect on SLC51A/OSTA and ABCB11/BSEP, no
effect on interaction with RXRA and SETD7."
/evidence="ECO:0000269|PubMed:23462506"
MUTAGEN 220
/note="K->R: Decreases transcriptional activation of
SLC51B/OSTB, no effect on SLC51A/OSTA and ABCB11/BSEP,
impairs interaction with RXRA and SETD7."
/evidence="ECO:0000269|PubMed:23462506"
MUTAGEN 227
/note="K->R: Decreases transcriptional activation
SC51A/OSTA, SLC51B/OSTB and ABCB11/BSEP, impairs
interaction with RXRA and enhances interaction with SETD7,
decreases association with ABCB11/BSEP promoter."
/evidence="ECO:0000269|PubMed:23462506"
MUTAGEN 289
/note="K->R: Abrogates SUMO1-mediated inhibition of ligand-
induced transcactivation at ABCB11/BSEP and NR0B2/SHP
promoters; when associated with R-132 and A-291."
/evidence="ECO:0000269|PubMed:23546875"
MUTAGEN 291
/note="E->A: Abrogates SUMO1-mediated inhibition of ligand-
induced transcactivation at ABCB11/BSEP and NR0B2/SHP
promoters; when associated with R-132 and R-289."
/evidence="ECO:0000269|PubMed:23546875"
MUTAGEN 353
/note="K->R: Decreases transcriptional activation
SLC51A/OSTA, SLC51B/OSTB and ABCB11/BSEP, no effect on
interaction with RXRA and SETD7, decreases association with
ABCB11/BSEP promoter."
/evidence="ECO:0000269|PubMed:23462506"
MUTAGEN 455
/note="R->S: As a heterodimer with RXRA, impaired
transcriptional activity."
/evidence="ECO:0000269|PubMed:30275017"
MUTAGEN 456
/note="T->A: Impairs transcriptional activation of
ABCB11/BSEP."
/evidence="ECO:0000269|PubMed:18668687"
MUTAGEN 474
/note="K->R: Decreases transcriptional activation
SLC51A/OSTA, SLC51B/OSTB and ABCB11/BSEP, no effect on
interaction with RXRA and impairs interaction with SETD7."
/evidence="ECO:0000269|PubMed:23462506"
CONFLICT 198
/note="K -> R (in Ref. 7; AAI44185)"
/evidence="ECO:0000305"
CONFLICT 217
/note="C -> V (in Ref. 7; BC144183)"
/evidence="ECO:0000305"
HELIX 261..274
/evidence="ECO:0000244|PDB:6HL1"
HELIX 281..289
/evidence="ECO:0000244|PDB:6HL1"
HELIX 294..317
/evidence="ECO:0000244|PDB:6HL1"
HELIX 322..324
/evidence="ECO:0000244|PDB:6HL1"
HELIX 327..349
/evidence="ECO:0000244|PDB:6HL1"
STRAND 350..353
/evidence="ECO:0000244|PDB:5YXD"
TURN 354..356
/evidence="ECO:0000244|PDB:4OIV"
STRAND 357..359
/evidence="ECO:0000244|PDB:5Y49"
HELIX 360..367
/evidence="ECO:0000244|PDB:6HL1"
STRAND 369..371
/evidence="ECO:0000244|PDB:5Q0I"
HELIX 373..387
/evidence="ECO:0000244|PDB:6HL1"
TURN 388..390
/evidence="ECO:0000244|PDB:4OIV"
HELIX 393..404
/evidence="ECO:0000244|PDB:6HL1"
STRAND 409..411
/evidence="ECO:0000244|PDB:5Q0I"
HELIX 415..436
/evidence="ECO:0000244|PDB:6HL1"
STRAND 438..440
/evidence="ECO:0000244|PDB:6A5X"
HELIX 443..465
/evidence="ECO:0000244|PDB:6HL1"
HELIX 470..472
/evidence="ECO:0000244|PDB:6HL0"
HELIX 477..483
/evidence="ECO:0000244|PDB:6HL1"
SEQUENCE 486 AA; 55914 MW; C23283576A8CF76B CRC64;
MVMQFQGLEN PIQISPHCSC TPSGFFMEMM SMKPAKGVLT EQVAGPLGQN LEVEPYSQYS
NVQFPQVQPQ ISSSSYYSNL GFYPQQPEEW YSPGIYELRR MPAETLYQGE TEVAEMPVTK
KPRMGASAGR IKGDELCVVC GDRASGYHYN ALTCEGCKGF FRRSITKNAV YKCKNGGNCV
MDMYMRRKCQ ECRLRKCKEM GMLAECMYTG LLTEIQCKSK RLRKNVKQHA DQTVNEDSEG
RDLRQVTSTT KSCREKTELT PDQQTLLHFI MDSYNKQRMP QEITNKILKE EFSAEENFLI
LTEMATNHVQ VLVEFTKKLP GFQTLDHEDQ IALLKGSAVE AMFLRSAEIF NKKLPSGHSD
LLEERIRNSG ISDEYITPMF SFYKSIGELK MTQEEYALLT AIVILSPDRQ YIKDREAVEK
LQEPLLDVLQ KLCKIHQPEN PQHFACLLGR LTELRTFNHH HAEMLMSWRV NDHKFTPLLC
EIWDVQ


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Related Genes :
[NR1H4 BAR FXR HRR1 RIP14] Bile acid receptor (Farnesoid X-activated receptor) (Farnesol receptor HRR-1) (Nuclear receptor subfamily 1 group H member 4) (Retinoid X receptor-interacting protein 14) (RXR-interacting protein 14)
[Nr1h4 Bar Fxr Rip14] Bile acid receptor (Farnesoid X-activated receptor) (Farnesol receptor HRR-1) (Nuclear receptor subfamily 1 group H member 4) (Retinoid X receptor-interacting protein 14) (RXR-interacting protein 14)
[Nr1h4 Bar Fxr Rip14] Bile acid receptor (Farnesoid X-activated receptor) (Farnesol receptor HRR-1) (Nuclear receptor subfamily 1 group H member 4) (Retinoid X receptor-interacting protein 14) (RXR-interacting protein 14)
[NR1H4] Bile acid receptor (Farnesoid X-activated receptor) (Farnesol receptor HRR-1) (Nuclear receptor subfamily 1 group H member 4)
[RXRA NR2B1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[Rxra Nr2b1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[Rxrb Nr2b2] Retinoic acid receptor RXR-beta (MHC class I regulatory element-binding protein H-2RIIBP) (Nuclear receptor subfamily 2 group B member 2) (Retinoid X receptor beta)
[Rxra Nr2b1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[Rxrb Nr2b2 Rcor-1] Retinoic acid receptor RXR-beta (Nuclear receptor coregulator 1) (Nuclear receptor subfamily 2 group B member 2) (Retinoid X receptor beta) (Fragment)
[rxrga nr2b1 nr2b3a rxr rxra rxrg] Retinoic acid receptor RXR-gamma-A (Nuclear receptor subfamily 2 group B member 3-A) (Retinoic acid receptor RXR-alpha) (Retinoid X receptor alpha) (Retinoid X receptor gamma-A)
[RXRB NR2B2] Retinoic acid receptor RXR-beta (Nuclear receptor subfamily 2 group B member 2) (Retinoid X receptor beta)
[RXRG NR2B3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[rxrbb nr2b2b rxrd] Retinoic acid receptor RXR-beta-B (Nuclear receptor subfamily 2 group B member 2-B) (Retinoic acid receptor RXR-delta) (Retinoid X receptor beta-B) (Retinoid X receptor delta)
[Rxrg Nr2b3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[Rxrg Nr2b3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[rxrba nr2b2a rxrb rxre] Retinoic acid receptor RXR-beta-A (Nuclear receptor subfamily 2 group B member 2-A) (Retinoid X receptor beta-A)
[Nr1h2 Lxrb] Oxysterols receptor LXR-beta (Liver X receptor beta) (Nuclear receptor subfamily 1 group H member 2) (Orphan nuclear receptor OR-1) (Ubiquitously-expressed nuclear receptor) (UR)
[RXRG NR2B3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[rxrab nr2b1b rxra rxrg] Retinoic acid receptor RXR-alpha-B (Nuclear receptor subfamily 2 group B member 1-B) (Retinoid X receptor alpha-B)
[RORA NR1F1 RZRA] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)
[Rora Nr1f1 Rzra] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)
[Nr2c1 Tr2 Tr2-11] Nuclear receptor subfamily 2 group C member 1 (Orphan nuclear receptor TR2) (Testicular receptor 2) (mTR2)
[Rorc Nr1f3 Rorg Thor] Nuclear receptor ROR-gamma (Nuclear receptor RZR-gamma) (Nuclear receptor subfamily 1 group F member 3) (RAR-related orphan receptor C) (Retinoid-related orphan receptor-gamma) (Thymus orphan receptor) (TOR)
[RARB HAP NR1B2] Retinoic acid receptor beta (RAR-beta) (HBV-activated protein) (Nuclear receptor subfamily 1 group B member 2) (RAR-epsilon)
[NR4A1 GFRP1 HMR NAK1] Nuclear receptor subfamily 4 group A member 1 (Early response protein NAK1) (Nuclear hormone receptor NUR/77) (Nur77) (Orphan nuclear receptor HMR) (Orphan nuclear receptor TR3) (ST-59) (Testicular receptor 3)
[RORC NR1F3 RORG RZRG] Nuclear receptor ROR-gamma (Nuclear receptor RZR-gamma) (Nuclear receptor subfamily 1 group F member 3) (RAR-related orphan receptor C) (Retinoid-related orphan receptor-gamma)
[rxraa nr2b1a] Retinoic acid receptor RXR-alpha-A (Nuclear receptor subfamily 2 group B member 1-A) (RXRalpha-B) (Retinoid X receptor alpha-A)
[NR2C2 TAK1 TR4] Nuclear receptor subfamily 2 group C member 2 (Orphan nuclear receptor TAK1) (Orphan nuclear receptor TR4) (Testicular receptor 4)
[Hnf4a Hnf-4 Hnf4 Nr2a1 Tcf14] Hepatocyte nuclear factor 4-alpha (HNF-4-alpha) (Nuclear receptor subfamily 2 group A member 1) (Transcription factor 14) (TCF-14) (Transcription factor HNF-4)
[VDR NR1I1] Vitamin D3 receptor (VDR) (1,25-dihydroxyvitamin D3 receptor) (Nuclear receptor subfamily 1 group I member 1)

Bibliography :