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Peroxisome proliferator-activated receptor gamma (PPAR-gamma) (Nuclear receptor subfamily 1 group C member 3)

 PPARG_HUMAN             Reviewed;         505 AA.
P37231; A8K3G6; B5BUA1; O00684; O00710; O14515; Q0QJH8; Q15178; Q15179;
Q15180; Q15832; Q86U60; Q96J12;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 3.
11-DEC-2019, entry version 260.
RecName: Full=Peroxisome proliferator-activated receptor gamma;
Short=PPAR-gamma;
AltName: Full=Nuclear receptor subfamily 1 group C member 3;
Name=PPARG; Synonyms=NR1C3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Heart;
PubMed=9065481; DOI=10.1074/jbc.272.12.8071;
Mukherjee R., Jow L., Croston G.E., Paterniti J.R. Jr.;
"Identification, characterization, and tissue distribution of human
peroxisome proliferator-activated receptor (PPAR) isoforms PPARgamma2
versus PPARgamma1 and activation with retinoid X receptor agonists and
antagonists.";
J. Biol. Chem. 272:8071-8076(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Adipose tissue;
PubMed=8702406; DOI=10.1006/bbrc.1996.1044;
Elbrecht A., Chen Y., Cullinan C.A., Hayes N., Leibowitz M.D., Moller D.E.,
Berger J.;
"Molecular cloning, expression and characterization of human peroxisome
proliferator activated receptors gamma 1 and gamma 2.";
Biochem. Biophys. Res. Commun. 224:431-437(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Adipose tissue;
PubMed=9144532; DOI=10.1006/bbrc.1997.6446;
Yanase T., Yashiro T., Takitani K., Kato S., Taniguchi S., Takayanagi R.,
Nawata H.;
"Differential expression of PPAR gamma1 and gamma2 isoforms in human
adipose tissue.";
Biochem. Biophys. Res. Commun. 233:320-324(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=7787419;
Greene M.E., Blumberg B., McBride O.W., Yi H.F., Kronquist K., Kwan K.,
Hsieh L., Greene G., Nimer S.D.;
"Isolation of the human peroxisome proliferator activated receptor gamma
cDNA: expression in hematopoietic cells and chromosomal mapping.";
Gene Expr. 4:281-299(1995).
[5]
SEQUENCE REVISION TO 36; 37; 213; 214 AND 240.
Greene M.E.;
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=9356045; DOI=10.2337/diab.46.11.1904;
Okazawa H., Mori H., Tamori Y., Araki S., Niki T., Masugi J., Kawanishi M.,
Kubota T., Shinoda H., Kasuga M.;
"No coding mutations are detected in the peroxisome proliferator-activated
receptor-gamma gene in Japanese patients with lipoatrophic diabetes.";
Diabetes 46:1904-1906(1997).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=8706692; DOI=10.1111/j.1432-1033.1996.0001u.x;
Lambe K.G., Tugwood J.D.;
"A human peroxisome-proliferator-activated receptor-gamma is activated by
inducers of adipogenesis, including thiazolidinedione drugs.";
Eur. J. Biochem. 239:1-7(1996).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=16842753; DOI=10.1016/j.bbrc.2006.06.147;
Kim H.J., Woo I.S., Kang E.S., Eun S.Y., Kim H.J., Lee J.H., Chang K.C.,
Kim J.H., Seo H.G.;
"Identification of a truncated alternative splicing variant of human
PPARgamma1 that exhibits dominant negative activity.";
Biochem. Biophys. Res. Commun. 347:698-706(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
Nomura N.;
"Human Protein Factory: an infrastructure to convert the human
transcriptome into the in vitro-expressed human proteome of versatile
utility.";
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-12.
SeattleSNPs variation discovery resource;
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[14]
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.
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[16]
INTERACTION WITH NCOA6.
PubMed=10681503; DOI=10.1074/jbc.275.8.5308;
Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.;
"Cloning and characterization of RAP250, a nuclear receptor coactivator.";
J. Biol. Chem. 275:5308-5317(2000).
[17]
POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO GLIOMA.
PubMed=10851250; DOI=10.1136/jmg.37.6.410;
Zhou X.P., Smith W.M., Gimm O., Mueller E., Gao X., Sarraf P., Prior T.W.,
Plass C., von Deimling A., Black P.M., Yates A.J., Eng C.;
"Over-representation of PPARgamma sequence variants in sporadic cases of
glioblastoma multiforme: preliminary evidence for common low penetrance
modifiers for brain tumour risk in the general population.";
J. Med. Genet. 37:410-414(2000).
[18]
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).
[19]
INTERACTION WITH NOCA7.
PubMed=11971969; DOI=10.1128/mcb.22.10.3358-3372.2002;
Shao W., Halachmi S., Brown M.;
"ERAP140, a conserved tissue-specific nuclear receptor coactivator.";
Mol. Cell. Biol. 22:3358-3372(2002).
[20]
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).
[21]
INTERACTION WITH TGFB1I1.
PubMed=15687259; DOI=10.1101/gad.1240705;
Drori S., Girnun G.D., Tou L., Szwaya J.D., Mueller E., Xia K.,
Shivdasani R.A., Spiegelman B.M.;
"Hic-5 regulates an epithelial program mediated by PPARgamma.";
Genes Dev. 19:362-375(2005).
[22]
INTERACTION WITH HELZ2.
PubMed=16239304; DOI=10.1210/en.2005-0450;
Tomaru T., Satoh T., Yoshino S., Ishizuka T., Hashimoto K., Monden T.,
Yamada M., Mori M.;
"Isolation and characterization of a transcriptional cofactor and its novel
isoform that bind the DNA-binding domain of peroxisome proliferator-
activated receptor gamma.";
Endocrinology 147:377-388(2006).
[23]
FUNCTION, INTERACTION WITH PDPK1, AND ACTIVITY REGULATION.
PubMed=16150867; DOI=10.1210/me.2005-0197;
Yin Y., Yuan H., Wang C., Pattabiraman N., Rao M., Pestell R.G.,
Glazer R.I.;
"3-phosphoinositide-dependent protein kinase-1 activates the peroxisome
proliferator-activated receptor-gamma and promotes adipocyte
differentiation.";
Mol. Endocrinol. 20:268-278(2006).
[24]
INTERACTION WITH MAP2K1/MEK1, AND SUBCELLULAR LOCATION.
PubMed=17101779; DOI=10.1128/mcb.00601-06;
Burgermeister E., Chuderland D., Hanoch T., Meyer M., Liscovitch M.,
Seger R.;
"Interaction with MEK causes nuclear export and downregulation of
peroxisome proliferator-activated receptor gamma.";
Mol. Cell. Biol. 27:803-817(2007).
[25]
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).
[26]
FUNCTION.
PubMed=20829347; DOI=10.1074/jbc.m110.136259;
Park S.H., Choi H.J., Yang H., Do K.H., Kim J., Lee D.W., Moon Y.;
"Endoplasmic reticulum stress-activated C/EBP homologous protein enhances
nuclear factor-kappaB signals via repression of peroxisome proliferator-
activated receptor gamma.";
J. Biol. Chem. 285:35330-35339(2010).
[27]
INTERACTION WITH ASXL1 AND ASXL2.
PubMed=21047783; DOI=10.1074/jbc.m110.177816;
Park U.H., Yoon S.K., Park T., Kim E.J., Um S.J.;
"Additional sex comb-like (ASXL) proteins 1 and 2 play opposite roles in
adipogenesis via reciprocal regulation of peroxisome proliferator-activated
receptor {gamma}.";
J. Biol. Chem. 286:1354-1363(2011).
[28]
INTERACTION WITH ACTN4.
PubMed=22351778; DOI=10.1074/jbc.m112.345421;
Khurana S., Chakraborty S., Lam M., Liu Y., Su Y.T., Zhao X., Saleem M.A.,
Mathieson P.W., Bruggeman L.A., Kao H.Y.;
"Familial focal segmental glomerulosclerosis (FSGS)-linked alpha-actinin 4
(ACTN4) protein mutants lose ability to activate transcription by nuclear
hormone receptors.";
J. Biol. Chem. 287:12027-12035(2012).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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]
FUNCTION, INTERACTION WITH HELZ2 AND THRAP3, AND SUBCELLULAR LOCATION.
PubMed=23525231; DOI=10.1210/me.2012-1332;
Katano-Toki A., Satoh T., Tomaru T., Yoshino S., Ishizuka T., Ishii S.,
Ozawa A., Shibusawa N., Tsuchiya T., Saito T., Shimizu H., Hashimoto K.,
Okada S., Yamada M., Mori M.;
"THRAP3 interacts with HELZ2 and plays a novel role in adipocyte
differentiation.";
Mol. Endocrinol. 27:769-780(2013).
[31]
FUNCTION (MICROBIAL INFECTION), AND INDUCTION (MICROBIAL INFECTION).
TISSUE=Macrophage;
PubMed=25504154; DOI=10.3892/mmr.2014.3070;
Liu L., Liu J., Niu G., Xu Q., Chen Q.;
"Mycobacterium tuberculosis 19-kDa lipoprotein induces Toll-like receptor
2-dependent peroxisome proliferator-activated receptor gamma expression and
promotes inflammatory responses in human macrophages.";
Mol. Med. Report. 11:2921-2926(2015).
[32]
9AATAD MOTIF.
PubMed=30468856; DOI=10.1016/j.jsbmb.2018.11.008;
Piskacek M., Havelka M., Jendruchova K., Knight A.;
"Nuclear hormone receptors: Ancient 9aaTAD and evolutionally gained NCoA
activation pathways.";
J. Steroid Biochem. Mol. Biol. 187:118-123(2019).
[33]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 232-505.
PubMed=9813012; DOI=10.1074/jbc.273.47.31108;
Uppenberg J., Svensson C., Jaki M., Bertilsson G., Jendeberg L.,
Berkenstam A.;
"Crystal structure of the ligand binding domain of the human nuclear
receptor PPARgamma.";
J. Biol. Chem. 273:31108-31112(1998).
[34]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 235-504 IN COMPLEXES WITH THE
SYNTHETIC AGONIST ROSIGLITAZONE AND NCOA1, AND SUBUNIT.
PubMed=9744270; DOI=10.1038/25931;
Nolte R.T., Wisely G.B., Westin S., Cobb J.E., Lambert M.H., Kurokawa R.,
Rosenfeld M.G., Willson T.M., Glass C.K., Milburn M.V.;
"Ligand binding and co-activator assembly of the peroxisome proliferator-
activated receptor-gamma.";
Nature 395:137-143(1998).
[35]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH RXRA AND SYNTHETIC
AGONISTS.
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).
[36]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 234-505 IN COMPLEXES WITH
SYNTHETIC AGONIST AND NCOA1.
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).
[37]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 225-505 IN COMPLEX WITH SYNTHETIC
AGONIST.
PubMed=11587644; DOI=10.1016/s0969-2126(01)00634-7;
Cronet P., Petersen J.F.W., Folmer R., Blomberg N., Sjoeblom K.,
Karlsson U., Lindstedt E.-L., Bamberg K.;
"Structure of the PPARalpha and -gamma ligand binding domain in complex
with AZ 242; ligand selectivity and agonist activation in the PPAR
family.";
Structure 9:699-706(2001).
[38]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 230-505 IN COMPLEX WITH SYNTHETIC
AGONIST.
PubMed=12672231; DOI=10.1021/jm021027r;
Ebdrup S., Pettersson I., Rasmussen H.B., Deussen H.-J., Frost Jensen A.,
Mortensen S.B., Fleckner J., Pridal L., Nygaard L., Sauerberg P.;
"Synthesis and biological and structural characterization of the dual-
acting peroxisome proliferator-activated receptor alpha/gamma agonist
ragaglitazar.";
J. Med. Chem. 46:1306-1317(2003).
[39]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 232-505 IN COMPLEX WITH NCOA2 AND
SYNTHETIC AGONIST.
PubMed=15258145; DOI=10.1074/jbc.m401552200;
Oestberg T., Svensson S., Selen G., Uppenberg J., Thor M., Sundbom M.,
Sydow-Baeckman M., Gustavsson A.-L., Jendeberg L.;
"A new class of peroxisome proliferator-activated receptor agonists with a
novel binding epitope shows antidiabetic effects.";
J. Biol. Chem. 279:41124-41130(2004).
[40]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 235-505 IN COMPLEX WITH RXRA;
NCOA1 AND SYNTHETIC AGONIST.
PubMed=15056000; DOI=10.1021/jm030565g;
Haffner C.D., Lenhard J.M., Miller A.B., McDougald D.L., Dwornik K.,
Ittoop O.R., Gampe R.T. Jr., Xu H.E., Blanchard S., Montana V.G.,
Consler T.G., Bledsoe R.K., Ayscue A., Croom D.;
"Structure-based design of potent retinoid X receptor alpha agonists.";
J. Med. Chem. 47:2010-2029(2004).
[41]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 231-505 IN COMPLEX WITH SYNTHETIC
AGONIST.
PubMed=15974597; DOI=10.1021/jm0502135;
Shi G.Q., Dropinski J.F., McKeever B.M., Xu S., Becker J.W., Berger J.P.,
MacNaul K.L., Elbrecht A., Zhou G., Doebber T.W., Wang P., Chao Y.-S.,
Forrest M., Heck J.V., Moller D.E., Jones A.B.;
"Design and synthesis of alpha-aryloxyphenylacetic acid derivatives: a
novel class of PPARalpha/gamma dual agonists with potent antihyperglycemic
and lipid modulating activity.";
J. Med. Chem. 48:4457-4468(2005).
[42]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 234-505 IN COMPLEX WITH SYNTHETIC
AGONIST AND NR0B2.
PubMed=15976031; DOI=10.1073/pnas.0501204102;
Li Y., Choi M., Suino K., Kovach A., Daugherty J., Kliewer S.A., Xu H.E.;
"Structural and biochemical basis for selective repression of the orphan
nuclear receptor liver receptor homolog 1 by small heterodimer partner.";
Proc. Natl. Acad. Sci. U.S.A. 102:9505-9510(2005).
[43]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 234-505 IN COMPLEX WITH SYNTHETIC
AGONIST AND NCOA1.
PubMed=16919947; DOI=10.1016/j.bmcl.2006.08.003;
Hopkins C.R., O'neil S.V., Laufersweiler M.C., Wang Y., Pokross M.,
Mekel M., Evdokimov A., Walter R., Kontoyianni M., Petrey M.E.,
Sabatakos G., Roesgen J.T., Richardson E., Demuth T.P. Jr.;
"Design and synthesis of novel N-sulfonyl-2-indole carboxamides as potent
PPAR-gamma binding agents with potential application to the treatment of
osteoporosis.";
Bioorg. Med. Chem. Lett. 16:5659-5663(2006).
[44]
X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 235-505 IN COMPLEX WITH SYNTHETIC
AGONIST.
PubMed=16451087; DOI=10.1021/jm0510373;
Mahindroo N., Wang C.-C., Liao C.-C., Huang C.-F., Lu I.-L., Lien T.-W.,
Peng Y.-H., Huang W.-J., Lin Y.-T., Hsu M.-C., Lin C.-H., Tsai C.-H.,
Hsu J.-T., Chen X., Lyu P.-C., Chao Y.-S., Wu S.-Y., Hsieh H.-P.;
"Indol-1-yl acetic acids as peroxisome proliferator-activated receptor
agonists: design, synthesis, structural biology, and molecular docking
studies.";
J. Med. Chem. 49:1212-1216(2006).
[45]
X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 235-505 IN COMPLEX WITH SYNTHETIC
AGONIST.
PubMed=16640330; DOI=10.1021/jm051129s;
Lu I.-L., Huang C.-F., Peng Y.-H., Lin Y.-T., Hsieh H.-P., Chen C.-T.,
Lien T.-W., Lee H.-J., Mahindroo N., Prakash E., Yueh A., Chen H.-Y.,
Goparaju C.M.V., Chen X., Liao C.-C., Chao Y.-S., Hsu J.-T., Wu S.-Y.;
"Structure-based drug design of a novel family of PPARgamma partial
agonists: virtual screening, X-ray crystallography, and in vitro/in vivo
biological activities.";
J. Med. Chem. 49:2703-2712(2006).
[46]
VARIANT ALA-12.
PubMed=9425261; DOI=10.1006/bbrc.1997.7798;
Yen C.-J., Beamer B.A., Negri C., Silver K., Brown K.A., Yarnall D.P.,
Burns D.K., Roth J., Shuldiner A.R.;
"Molecular scanning of the human peroxisome proliferator activated receptor
gamma (hPPAR-gamma) gene in diabetic Caucasians: identification of a
pro12ala PPAR-gamma-2 missense mutation.";
Biochem. Biophys. Res. Commun. 241:270-274(1997).
[47]
VARIANT OBESITY GLN-113.
PubMed=9753710; DOI=10.1056/nejm199810013391403;
Ristow M., Muller-Wieland D., Pfeiffer A., Krone W., Kahn C.R.;
"Obesity associated with a mutation in a genetic regulator of adipocyte
differentiation.";
N. Engl. J. Med. 339:953-959(1998).
[48]
INVOLVEMENT IN BMIQ1, AND VARIANT ALA-12.
PubMed=9806549; DOI=10.1038/3099;
Deeb S.S., Fajas L., Nemoto M., Pihlajamaeki J., Mykkaenen L., Kuusisto J.,
Laakso M., Fujimoto W., Auwerx J.;
"A Pro12Ala substitution in PPARgamma2 associated with decreased receptor
activity, lower body mass index and improved insulin sensitivity.";
Nat. Genet. 20:284-287(1998).
[49]
VARIANT ALA-12.
PubMed=10407229; DOI=10.1530/eje.0.1410090;
Hamann A., Munzberg H., Buttron P., Busing B., Hinney A., Mayer H.,
Siegfried W., Hebebrand J., Greten H.;
"Missense variants in the human peroxisome proliferator-activated receptor-
gamma2 gene in lean and obese subjects.";
Eur. J. Endocrinol. 141:90-92(1999).
[50]
INVOLVEMENT IN BMIQ1, AND VARIANT ALA-12.
PubMed=10523018; DOI=10.1210/jcem.84.10.6061;
Valve R., Sivenius K., Miettinen R., Pihlajamaeki J., Rissanen A.,
Deeb S.S., Auwerx J., Uusitupa M., Laakso M.;
"Two polymorphisms in the peroxisome proliferator-activated receptor-gamma
gene are associated with severe overweight among obese women.";
J. Clin. Endocrinol. Metab. 84:3708-3712(1999).
[51]
VARIANTS COLON CANCER PRO-314 AND HIS-316, AND VARIANT ALA-12.
PubMed=10394368; DOI=10.1016/s1097-2765(01)80012-5;
Sarraf P., Mueller E., Smith W.M., Wright H.M., Kum J.B., Aaltonen L.A.,
de la Chapelle A., Spiegelman B.M., Eng C.;
"Loss-of-function mutations in PPAR-gamma associated with human colon
cancer.";
Mol. Cell 3:799-804(1999).
[52]
VARIANTS DIABETES MET-318 AND LEU-495.
PubMed=10622252; DOI=10.1038/47254;
Barroso I., Gurnell M., Crowley V.E.F., Agostini M., Schwabel J.W.,
Soos M.A., Masien G.L., Williams T.D.M., Lewis H., Schafer A.J.,
Chatterjee V.K.K., O'Rahilly S.;
"Dominant negative mutations in human PPAR-gamma associated with severe
insulin resistance, diabetes mellitus and hypertension.";
Nature 402:880-883(1999).
[53]
VARIANT FPLD3 LEU-388.
PubMed=12453919; DOI=10.2337/diabetes.51.12.3586;
Hegele R.A., Cao H., Frankowski C., Mathews S.T., Leff T.;
"PPARG F388L, a transactivation-deficient mutant, in familial partial
lipodystrophy.";
Diabetes 51:3586-3590(2002).
[54]
VARIANT FPLD3 CYS-425.
PubMed=11788685; DOI=10.1210/jcem.87.1.8290;
Agarwal A.K., Garg A.;
"A novel heterozygous mutation in peroxisome proliferator-activated
receptor-gamma gene in a patient with familial partial lipodystrophy.";
J. Clin. Endocrinol. Metab. 87:408-411(2002).
[55]
ASSOCIATION OF VARIANT ALA-12 WITH BMI.
PubMed=14569127; DOI=10.1136/jmg.40.10.773;
Masud S., Ye S.;
"Effect of the peroxisome proliferator activated receptor-gamma gene
Pro12Ala variant on body mass index: a meta-analysis.";
J. Med. Genet. 40:773-780(2003).
[56]
ASSOCIATION OF VARIANT ALA-12 WITH CIMT.
PubMed=15356014; DOI=10.1210/jc.2003-032120;
Temelkova-Kurktschiev T., Hanefeld M., Chinetti G., Zawadzki C., Haulon S.,
Kubaszek A., Koehler C., Leonhardt W., Staels B., Laakso M.;
"Ala12Ala genotype of the peroxisome proliferator-activated receptor gamma2
protects against atherosclerosis.";
J. Clin. Endocrinol. Metab. 89:4238-4242(2004).
[57]
VARIANT ALA-12.
PubMed=15562396; DOI=10.1016/j.metabol.2004.06.019;
Kim K.S., Choi S.M., Shin S.U., Yang H.S., Yoon Y.;
"Effects of peroxisome proliferator-activated receptor-gamma 2 Pro12Ala
polymorphism on body fat distribution in female Korean subjects.";
Metabolism 53:1538-1543(2004).
-!- FUNCTION: Nuclear receptor that binds peroxisome proliferators such as
hypolipidemic drugs and fatty acids. Once activated by a ligand, the
nuclear receptor binds to DNA specific PPAR response elements (PPRE)
and modulates the transcription of its target genes, such as acyl-CoA
oxidase. It therefore controls the peroxisomal beta-oxidation pathway
of fatty acids. Key regulator of adipocyte differentiation and glucose
homeostasis. ARF6 acts as a key regulator of the tissue-specific
adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut
homeostasis by suppressing NF-kappa-B-mediated proinflammatory
responses. Plays a role in the regulation of cardiovascular circadian
rhythms by regulating the transcription of ARNTL/BMAL1 in the blood
vessels (By similarity). {ECO:0000250|UniProtKB:P37238,
ECO:0000269|PubMed:16150867, ECO:0000269|PubMed:20829347,
ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:9065481}.
-!- FUNCTION: (Microbial infection) Upon treatment with M.tuberculosis or
its lipoprotein LpqH, phosphorylation of MAPK p38 and IL-6 production
are modulated, probably via this protein.
{ECO:0000269|PubMed:25504154}.
-!- ACTIVITY REGULATION: PDPK1 activates its transcriptional activity
independently of its kinase activity. {ECO:0000269|PubMed:16150867}.
-!- SUBUNIT: Interacts with FOXO1 (acetylated form) (By similarity).
Heterodimer with other nuclear receptors, such as RXRA. The heterodimer
with the retinoic acid receptor RXRA is called adipocyte-specific
transcription factor ARF6. Interacts with NCOA6 coactivator, leading to
a strong increase in transcription of target genes. Interacts with
coactivator PPARBP, leading to a mild increase in transcription of
target genes. Interacts with NOCA7 in a ligand-inducible manner.
Interacts with NCOA1 and NCOA2 LXXLL motifs. Interacts with ASXL1,
ASXL2, DNTTIP2, FAM120B, MAP2K1/MEK1, NR0B2, PDPK1, PRDM16, PRMT2 and
TGFB1I1. Interacts (when activated by agonist) with PPP5C. Interacts
with HELZ2 and THRAP3; the interaction stimulates the transcriptional
activity of PPARG. Interacts with PER2, the interaction is ligand
dependent and blocks PPARG recruitment to target promoters. Interacts
with NOCT. Interacts with ACTN4. Interacts (when in the liganded
conformation) with GPS2 (By similarity). Interacts with CRY1 and CRY2
in a ligand-dependent manner (By similarity). In the absence of
hormonal ligand, interacts with TACC1 (PubMed:20078863).
{ECO:0000250|UniProtKB:P37238, ECO:0000269|PubMed:10681503,
ECO:0000269|PubMed:11587644, ECO:0000269|PubMed:11971969,
ECO:0000269|PubMed:12039952, ECO:0000269|PubMed:12672231,
ECO:0000269|PubMed:15047147, ECO:0000269|PubMed:15056000,
ECO:0000269|PubMed:15258145, ECO:0000269|PubMed:15687259,
ECO:0000269|PubMed:15974597, ECO:0000269|PubMed:15976031,
ECO:0000269|PubMed:16150867, ECO:0000269|PubMed:16239304,
ECO:0000269|PubMed:16451087, ECO:0000269|PubMed:16640330,
ECO:0000269|PubMed:16919947, ECO:0000269|PubMed:17101779,
ECO:0000269|PubMed:20078863, ECO:0000269|PubMed:21047783,
ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:23525231,
ECO:0000269|PubMed:9744270}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-781384, EBI-781384;
Q00535:CDK5; NbExp=2; IntAct=EBI-781416, EBI-1041567;
P10909:CLU; NbExp=3; IntAct=EBI-781384, EBI-1104674;
O60869:EDF1; NbExp=4; IntAct=EBI-781384, EBI-781301;
P42858:HTT; NbExp=4; IntAct=EBI-781384, EBI-466029;
P55055-1:NR1H2; NbExp=2; IntAct=EBI-781384, EBI-21458417;
Q13133:NR1H3; NbExp=2; IntAct=EBI-781384, EBI-781356;
Q9UBK2:PPARGC1A; NbExp=2; IntAct=EBI-781384, EBI-765486;
P19793:RXRA; NbExp=6; IntAct=EBI-15664691, EBI-78598;
Q96EB6:SIRT1; NbExp=5; IntAct=EBI-781384, EBI-1802965;
Q6STE5-1:SMARCD3; NbExp=3; IntAct=EBI-781384, EBI-488506;
Q6STE5-2:SMARCD3; NbExp=3; IntAct=EBI-781384, EBI-488511;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Redistributed from the
nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT
enhances its nuclear translocation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=2;
IsoId=P37231-1; Sequence=Displayed;
Name=1; Synonyms=PPARgamma1(wt);
IsoId=P37231-2; Sequence=VSP_003645;
Name=3; Synonyms=PPARgamma1(tr);
IsoId=P37231-3; Sequence=VSP_003645, VSP_043906, VSP_043907;
-!- TISSUE SPECIFICITY: Highest expression in adipose tissue. Lower in
skeletal muscle, spleen, heart and liver. Also detectable in placenta,
lung and ovary. {ECO:0000269|PubMed:9065481}.
-!- INDUCTION: (Microbial infection) Expression increases when incubated
with M.tuberculosis or its lipoprotein LpqH; induction is TLR2-
dependent (at protein level). {ECO:0000269|PubMed:25504154}.
-!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
number of yeast and animal transcription factors.
{ECO:0000305|PubMed:30468856}.
-!- PTM: O-GlcNAcylation at Thr-84 reduces transcriptional activity in
adipocytes. {ECO:0000250|UniProtKB:P37238}.
-!- PTM: Phosphorylated in basal conditions and dephosphorylated when
treated with the ligand. May be dephosphorylated by PPP5C. The
phosphorylated form may be inactive and dephosphorylation at Ser-112
induces adipogenic activity (By similarity). {ECO:0000250}.
-!- POLYMORPHISM: Genetic variations in PPARG define the body mass index
quantitative trait locus 1 (BMIQ1) [MIM:606641]. The body max index
(BMI) reflects the amount of fat, lean mass, and body build.
{ECO:0000269|PubMed:10523018, ECO:0000269|PubMed:14569127}.
-!- POLYMORPHISM: Genetic variations in PPARG influence the carotid intimal
medial thickness (CIMT) [MIM:609338]. CIMT is a measure of
atherosclerosis that is independently associated with traditional
atherosclerotic cardiovascular disease risk factors and coronary
atherosclerotic burden. 35 to 45% of the variability in multivariable-
adjusted CIMT is explained by genetic factors.
{ECO:0000269|PubMed:15356014}.
-!- DISEASE: Note=Defects in PPARG can lead to type 2 insulin-resistant
diabetes and hyptertension. PPARG mutations may be associated with
colon cancer. {ECO:0000269|PubMed:10394368}.
-!- DISEASE: Obesity (OBESITY) [MIM:601665]: A condition characterized by
an increase of body weight beyond the limitation of skeletal and
physical requirements, as the result of excessive accumulation of body
fat. {ECO:0000269|PubMed:9753710}. Note=Disease susceptibility may be
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Lipodystrophy, familial partial, 3 (FPLD3) [MIM:604367]: A
form of lipodystrophy characterized by marked loss of subcutaneous fat
from the extremities. Facial adipose tissue may be increased, decreased
or normal. Affected individuals show an increased preponderance of
insulin resistance, diabetes mellitus and dyslipidemia.
{ECO:0000269|PubMed:11788685, ECO:0000269|PubMed:12453919}. Note=The
disease is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Glioma 1 (GLM1) [MIM:137800]: Gliomas are benign or malignant
central nervous system neoplasms derived from glial cells. They
comprise astrocytomas and glioblastoma multiforme that are derived from
astrocytes, oligodendrogliomas derived from oligodendrocytes and
ependymomas derived from ependymocytes. {ECO:0000269|PubMed:10851250}.
Note=Disease susceptibility may be associated with variations affecting
the gene represented in this entry. Polymorphic PPARG alleles have been
found to be significantly over-represented among a cohort of American
patients with sporadic glioblastoma multiforme suggesting a possible
contribution to disease susceptibility.
-!- MISCELLANEOUS: [Isoform 3]: Exhibits dominant negative activity over
isoform 1. {ECO:0000305}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAN38992.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=BAA23354.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAF83270.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=CAA62153.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PPARGID383ch3p25.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Peroxisome proliferator-activated
receptor entry;
URL="https://en.wikipedia.org/wiki/Peroxisome_proliferator-activated_receptor";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/pparg/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=PPARG";
---------------------------------------------------------------------------
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EMBL; U79012; AAC51248.1; -; mRNA.
EMBL; U63415; AAB04028.1; -; mRNA.
EMBL; D83233; BAA18949.1; -; mRNA.
EMBL; L40904; AAA80314.2; -; mRNA.
EMBL; AB005526; BAA23354.1; ALT_SEQ; Genomic_DNA.
EMBL; X90563; CAA62152.1; -; mRNA.
EMBL; X90563; CAA62153.1; ALT_INIT; mRNA.
EMBL; DQ356894; ABC97372.1; -; mRNA.
EMBL; BT007281; AAP35945.1; -; mRNA.
EMBL; AK290581; BAF83270.1; ALT_INIT; mRNA.
EMBL; AB451337; BAG70151.1; -; mRNA.
EMBL; AB451486; BAG70300.1; -; mRNA.
EMBL; AY157024; AAN38992.2; ALT_INIT; Genomic_DNA.
EMBL; AC090947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC091492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW64124.1; -; Genomic_DNA.
EMBL; BC006811; AAH06811.1; -; mRNA.
CCDS; CCDS2609.1; -. [P37231-1]
CCDS; CCDS2610.2; -. [P37231-2]
PIR; JC4859; JC4859.
PIR; PC4290; PC4290.
PIR; PC4429; PC4429.
RefSeq; NP_005028.4; NM_005037.5. [P37231-2]
RefSeq; NP_056953.2; NM_015869.4. [P37231-1]
RefSeq; NP_619725.2; NM_138711.3. [P37231-2]
RefSeq; NP_619726.2; NM_138712.3. [P37231-2]
RefSeq; XP_011532143.1; XM_011533841.2.
PDB; 1FM6; X-ray; 2.10 A; D/X=234-505.
PDB; 1FM9; X-ray; 2.10 A; D=234-505.
PDB; 1I7I; X-ray; 2.35 A; A/B=225-505.
PDB; 1K74; X-ray; 2.30 A; D=234-505.
PDB; 1KNU; X-ray; 2.50 A; A/B=232-505.
PDB; 1NYX; X-ray; 2.65 A; A/B=230-505.
PDB; 1PRG; X-ray; 2.20 A; A/B=235-504.
PDB; 1RDT; X-ray; 2.40 A; D=235-505.
PDB; 1WM0; X-ray; 2.90 A; X=232-505.
PDB; 1ZEO; X-ray; 2.50 A; A/B=231-505.
PDB; 1ZGY; X-ray; 1.80 A; A=234-505.
PDB; 2ATH; X-ray; 2.28 A; A/B=235-505.
PDB; 2F4B; X-ray; 2.07 A; A/B=235-505.
PDB; 2FVJ; X-ray; 1.99 A; A=235-505.
PDB; 2G0G; X-ray; 2.54 A; A/B=235-505.
PDB; 2G0H; X-ray; 2.30 A; A/B=235-505.
PDB; 2GTK; X-ray; 2.10 A; A=235-505.
PDB; 2HFP; X-ray; 2.00 A; A=234-505.
PDB; 2HWQ; X-ray; 1.97 A; A/B=235-505.
PDB; 2HWR; X-ray; 2.34 A; A/B=235-505.
PDB; 2I4J; X-ray; 2.10 A; A/B=223-504.
PDB; 2I4P; X-ray; 2.10 A; A/B=223-504.
PDB; 2I4Z; X-ray; 2.25 A; A/B=223-504.
PDB; 2OM9; X-ray; 2.80 A; A/B/C/D=232-505.
PDB; 2P4Y; X-ray; 2.25 A; A/B=231-505.
PDB; 2POB; X-ray; 2.30 A; A/B=234-505.
PDB; 2PRG; X-ray; 2.30 A; A/B=235-505.
PDB; 2Q59; X-ray; 2.20 A; A/B=233-505.
PDB; 2Q5P; X-ray; 2.30 A; A/B=233-505.
PDB; 2Q5S; X-ray; 2.05 A; A/B=233-505.
PDB; 2Q61; X-ray; 2.20 A; A/B=233-505.
PDB; 2Q6R; X-ray; 2.41 A; A/B=233-505.
PDB; 2Q6S; X-ray; 2.40 A; A/B=233-505.
PDB; 2Q8S; X-ray; 2.30 A; A/B=235-505.
PDB; 2QMV; NMR; -; A=235-504.
PDB; 2VSR; X-ray; 2.05 A; A/B=232-505.
PDB; 2VST; X-ray; 2.35 A; A/B=232-505.
PDB; 2VV0; X-ray; 2.55 A; A/B=232-505.
PDB; 2VV1; X-ray; 2.20 A; A/B=232-505.
PDB; 2VV2; X-ray; 2.75 A; A/B=232-505.
PDB; 2VV3; X-ray; 2.85 A; A/B=232-505.
PDB; 2VV4; X-ray; 2.35 A; A/B=232-505.
PDB; 2XKW; X-ray; 2.02 A; A/B=232-505.
PDB; 2YFE; X-ray; 2.00 A; A/B=223-505.
PDB; 2ZK0; X-ray; 2.36 A; A/B=223-504.
PDB; 2ZK1; X-ray; 2.61 A; A/B=223-504.
PDB; 2ZK2; X-ray; 2.26 A; A/B=223-504.
PDB; 2ZK3; X-ray; 2.58 A; A/B=223-504.
PDB; 2ZK4; X-ray; 2.57 A; A/B=223-504.
PDB; 2ZK5; X-ray; 2.45 A; A/B=223-504.
PDB; 2ZK6; X-ray; 2.41 A; A/B=223-504.
PDB; 2ZNO; X-ray; 2.40 A; A/B=223-504.
PDB; 2ZVT; X-ray; 1.90 A; A/B=223-504.
PDB; 3ADS; X-ray; 2.25 A; A/B=223-505.
PDB; 3ADT; X-ray; 2.70 A; A/B=223-505.
PDB; 3ADU; X-ray; 2.77 A; A/B=223-505.
PDB; 3ADV; X-ray; 2.27 A; A/B=223-505.
PDB; 3ADW; X-ray; 2.07 A; A/B=223-505.
PDB; 3ADX; X-ray; 1.95 A; A/B=223-505.
PDB; 3AN3; X-ray; 2.30 A; A/B=223-504.
PDB; 3AN4; X-ray; 2.30 A; A/B=223-504.
PDB; 3B0Q; X-ray; 2.10 A; A/B=231-504.
PDB; 3B0R; X-ray; 2.15 A; A/B=231-504.
PDB; 3B1M; X-ray; 1.60 A; A=234-505.
PDB; 3B3K; X-ray; 2.60 A; A/B=223-504.
PDB; 3BC5; X-ray; 2.27 A; A=231-505.
PDB; 3CDP; X-ray; 2.80 A; A/B=223-504.
PDB; 3CDS; X-ray; 2.65 A; A/B=223-504.
PDB; 3CS8; X-ray; 2.30 A; A=234-504.
PDB; 3CWD; X-ray; 2.40 A; A/B=236-505.
PDB; 3D6D; X-ray; 2.40 A; A/B=223-504.
PDB; 3DZU; X-ray; 3.20 A; D=102-505.
PDB; 3DZY; X-ray; 3.10 A; D=102-505.
PDB; 3E00; X-ray; 3.10 A; D=102-505.
PDB; 3ET0; X-ray; 2.40 A; A/B=235-505.
PDB; 3ET3; X-ray; 1.95 A; A=235-505.
PDB; 3FEJ; X-ray; 2.01 A; A=235-505.
PDB; 3FUR; X-ray; 2.30 A; A=234-505.
PDB; 3G9E; X-ray; 2.30 A; A=235-505.
PDB; 3GBK; X-ray; 2.30 A; A/B=235-505.
PDB; 3H0A; X-ray; 2.10 A; D=234-505.
PDB; 3HO0; X-ray; 2.60 A; A/B=223-504.
PDB; 3HOD; X-ray; 2.10 A; A/B=223-504.
PDB; 3IA6; X-ray; 2.31 A; A/B=235-505.
PDB; 3K8S; X-ray; 2.55 A; A/B=234-505.
PDB; 3KMG; X-ray; 2.10 A; A/D=234-505.
PDB; 3LMP; X-ray; 1.90 A; A=234-505.
PDB; 3NOA; X-ray; 1.98 A; A/B=235-505.
PDB; 3OSI; X-ray; 2.70 A; A/B=224-504.
PDB; 3OSW; X-ray; 2.55 A; A/B=224-504.
PDB; 3PBA; X-ray; 2.30 A; A/B=224-505.
PDB; 3PO9; X-ray; 2.35 A; A/B=224-505.
PDB; 3PRG; X-ray; 2.90 A; A=232-505.
PDB; 3QT0; X-ray; 2.50 A; A=235-505.
PDB; 3R5N; X-ray; 2.00 A; A=232-505.
PDB; 3R8A; X-ray; 2.41 A; A/B=235-505.
PDB; 3R8I; X-ray; 2.30 A; A/B=223-505.
PDB; 3S9S; X-ray; 2.55 A; A=234-505.
PDB; 3SZ1; X-ray; 2.30 A; A/B=232-505.
PDB; 3T03; X-ray; 2.10 A; A/B=234-505.
PDB; 3TY0; X-ray; 2.00 A; A/B=231-505.
PDB; 3U9Q; X-ray; 1.52 A; A=236-504.
PDB; 3V9T; X-ray; 1.65 A; A=234-505.
PDB; 3V9V; X-ray; 1.60 A; A=234-505.
PDB; 3V9Y; X-ray; 2.10 A; A=234-505.
PDB; 3VJH; X-ray; 2.22 A; A/B=223-504.
PDB; 3VJI; X-ray; 2.61 A; A/B=223-504.
PDB; 3VN2; X-ray; 2.18 A; A=225-505.
PDB; 3VSO; X-ray; 2.00 A; A/B=223-504.
PDB; 3VSP; X-ray; 2.40 A; A/B=223-504.
PDB; 3WJ4; X-ray; 1.95 A; A/B=235-505.
PDB; 3WJ5; X-ray; 1.89 A; A/B=235-505.
PDB; 3WMH; X-ray; 2.10 A; A/B=223-504.
PDB; 3X1H; X-ray; 2.30 A; A/B=232-505.
PDB; 3X1I; X-ray; 2.40 A; A/B=232-505.
PDB; 4A4V; X-ray; 2.00 A; A/B=223-505.
PDB; 4A4W; X-ray; 2.00 A; A/B=223-505.
PDB; 4CI5; X-ray; 1.77 A; A/B=234-505.
PDB; 4E4K; X-ray; 2.50 A; A/B=223-505.
PDB; 4E4Q; X-ray; 2.50 A; A/B=223-505.
PDB; 4EM9; X-ray; 2.10 A; A/B=235-505.
PDB; 4EMA; X-ray; 2.54 A; A/B=235-505.
PDB; 4F9M; X-ray; 1.90 A; A=234-505.
PDB; 4FGY; X-ray; 2.84 A; A=235-504.
PDB; 4HEE; X-ray; 2.50 A; X=235-505.
PDB; 4JAZ; X-ray; 2.85 A; A/B=223-505.
PDB; 4JL4; X-ray; 2.50 A; A/B=223-505.
PDB; 4L96; X-ray; 2.38 A; A=235-505.
PDB; 4L98; X-ray; 2.28 A; A/B=235-505.
PDB; 4O8F; X-ray; 2.60 A; A/B=223-505.
PDB; 4OJ4; X-ray; 2.30 A; A=232-505.
PDB; 4PRG; X-ray; 2.90 A; A/B/C/D=235-504.
PDB; 4PVU; X-ray; 2.60 A; A/B=223-505.
PDB; 4PWL; X-ray; 2.60 A; A/B=223-505.
PDB; 4R06; X-ray; 2.22 A; A/B=233-505.
PDB; 4R2U; X-ray; 2.30 A; A/D=231-505.
PDB; 4R6S; X-ray; 2.30 A; A/B=231-505.
PDB; 4XLD; X-ray; 2.45 A; A=231-505.
PDB; 4XTA; X-ray; 2.50 A; A/B=232-505.
PDB; 4XUH; X-ray; 2.22 A; A/B=232-505.
PDB; 4XUM; X-ray; 2.40 A; A/B=232-505.
PDB; 4Y29; X-ray; 1.98 A; A=236-504.
PDB; 4YT1; X-ray; 2.20 A; A/B=223-504.
PDB; 5AZV; X-ray; 2.70 A; A/B=232-505.
PDB; 5DSH; X-ray; 2.95 A; A=223-505.
PDB; 5DV3; X-ray; 2.75 A; A=223-505.
PDB; 5DV6; X-ray; 2.80 A; A=223-505.
PDB; 5DV8; X-ray; 2.75 A; A=223-505.
PDB; 5DVC; X-ray; 2.30 A; A=223-505.
PDB; 5DWL; X-ray; 2.20 A; A=223-505.
PDB; 5F9B; X-ray; 2.25 A; A/B=223-505.
PDB; 5GTN; X-ray; 1.85 A; A=223-505.
PDB; 5GTO; X-ray; 2.10 A; A=223-505.
PDB; 5GTP; X-ray; 2.35 A; A=223-505.
PDB; 5HZC; X-ray; 2.00 A; A/B=223-505.
PDB; 5JI0; X-ray; 1.98 A; D=234-505.
PDB; 5LSG; X-ray; 2.00 A; A/B=223-505.
PDB; 5TTO; X-ray; 2.25 A; A/B=233-505.
PDB; 5TWO; X-ray; 1.93 A; A=234-505.
PDB; 5U5L; X-ray; 2.55 A; A/B=233-505.
PDB; 5UGM; X-ray; 2.10 A; A/B=235-505.
PDB; 5WQX; X-ray; 2.29 A; A/B=232-505.
PDB; 5WR0; X-ray; 2.85 A; A/B=232-505.
PDB; 5WR1; X-ray; 2.34 A; A/B=232-505.
PDB; 5Y2O; X-ray; 1.80 A; A/B=235-505.
PDB; 5Y2T; X-ray; 1.70 A; A/B=235-505.
PDB; 5YCN; X-ray; 2.15 A; A=223-505.
PDB; 5YCP; X-ray; 2.00 A; A=223-505.
PDB; 5Z5S; X-ray; 1.80 A; A=234-505.
PDB; 5Z6S; X-ray; 1.80 A; A=234-505.
PDB; 6AD9; X-ray; 2.20 A; A=223-505.
PDB; 6AN1; X-ray; 2.69 A; A/B=224-505.
PDB; 6AUG; X-ray; 2.73 A; A/B=231-505.
PDB; 6AVI; X-ray; 2.29 A; A/B=231-505.
PDB; 6C1I; X-ray; 2.26 A; A/B=231-504.
PDB; 6C5Q; X-ray; 2.40 A; A=235-505.
PDB; 6C5T; X-ray; 2.75 A; A=235-505.
PDB; 6D3E; X-ray; 2.40 A; A/B=235-504.
PDB; 6D8X; X-ray; 1.90 A; A=231-505.
PDB; 6D94; X-ray; 1.90 A; A=231-505.
PDB; 6DBH; X-ray; 2.60 A; A/B=231-505.
PDB; 6DCU; X-ray; 2.95 A; A/B=231-505.
PDB; 6DGL; X-ray; 1.95 A; A/B=231-505.
PDB; 6DGO; X-ray; 3.10 A; A/B=231-505.
PDB; 6DGP; X-ray; 3.10 A; A/B=231-505.
PDB; 6DGQ; X-ray; 2.45 A; A/B=231-505.
PDB; 6DGR; X-ray; 2.15 A; A/B=231-505.
PDB; 6DH9; X-ray; 2.70 A; A/B=235-505.
PDB; 6DHA; X-ray; 1.88 A; A/B=235-505.
PDB; 6E5A; X-ray; 2.40 A; A/B=233-505.
PDB; 6ENQ; X-ray; 2.20 A; A/B=224-505.
PDB; 6F2L; X-ray; 2.10 A; A/B=223-505.
PDB; 6FZF; X-ray; 1.95 A; A/B=231-505.
PDB; 6FZG; X-ray; 2.10 A; A=231-505.
PDB; 6FZJ; X-ray; 2.01 A; A/B=231-505.
PDB; 6FZP; X-ray; 2.30 A; A=231-505.
PDB; 6FZY; X-ray; 3.10 A; A/B=231-505.
PDB; 6ICJ; X-ray; 2.48 A; A=234-505.
PDB; 6ILQ; X-ray; 2.41 A; A=234-505.
PDB; 6IZM; X-ray; 1.80 A; A=234-505.
PDB; 6IZN; X-ray; 1.75 A; A=234-505.
PDB; 6MCZ; X-ray; 2.10 A; A/B=231-505.
PDB; 6MD0; X-ray; 1.95 A; A/B=231-505.
PDB; 6MD1; X-ray; 2.20 A; A/B=231-505.
PDB; 6MD2; X-ray; 2.20 A; A/B=231-505.
PDB; 6MD4; X-ray; 2.24 A; A/B=231-505.
PDBsum; 1FM6; -.
PDBsum; 1FM9; -.
PDBsum; 1I7I; -.
PDBsum; 1K74; -.
PDBsum; 1KNU; -.
PDBsum; 1NYX; -.
PDBsum; 1PRG; -.
PDBsum; 1RDT; -.
PDBsum; 1WM0; -.
PDBsum; 1ZEO; -.
PDBsum; 1ZGY; -.
PDBsum; 2ATH; -.
PDBsum; 2F4B; -.
PDBsum; 2FVJ; -.
PDBsum; 2G0G; -.
PDBsum; 2G0H; -.
PDBsum; 2GTK; -.
PDBsum; 2HFP; -.
PDBsum; 2HWQ; -.
PDBsum; 2HWR; -.
PDBsum; 2I4J; -.
PDBsum; 2I4P; -.
PDBsum; 2I4Z; -.
PDBsum; 2OM9; -.
PDBsum; 2P4Y; -.
PDBsum; 2POB; -.
PDBsum; 2PRG; -.
PDBsum; 2Q59; -.
PDBsum; 2Q5P; -.
PDBsum; 2Q5S; -.
PDBsum; 2Q61; -.
PDBsum; 2Q6R; -.
PDBsum; 2Q6S; -.
PDBsum; 2Q8S; -.
PDBsum; 2QMV; -.
PDBsum; 2VSR; -.
PDBsum; 2VST; -.
PDBsum; 2VV0; -.
PDBsum; 2VV1; -.
PDBsum; 2VV2; -.
PDBsum; 2VV3; -.
PDBsum; 2VV4; -.
PDBsum; 2XKW; -.
PDBsum; 2YFE; -.
PDBsum; 2ZK0; -.
PDBsum; 2ZK1; -.
PDBsum; 2ZK2; -.
PDBsum; 2ZK3; -.
PDBsum; 2ZK4; -.
PDBsum; 2ZK5; -.
PDBsum; 2ZK6; -.
PDBsum; 2ZNO; -.
PDBsum; 2ZVT; -.
PDBsum; 3ADS; -.
PDBsum; 3ADT; -.
PDBsum; 3ADU; -.
PDBsum; 3ADV; -.
PDBsum; 3ADW; -.
PDBsum; 3ADX; -.
PDBsum; 3AN3; -.
PDBsum; 3AN4; -.
PDBsum; 3B0Q; -.
PDBsum; 3B0R; -.
PDBsum; 3B1M; -.
PDBsum; 3B3K; -.
PDBsum; 3BC5; -.
PDBsum; 3CDP; -.
PDBsum; 3CDS; -.
PDBsum; 3CS8; -.
PDBsum; 3CWD; -.
PDBsum; 3D6D; -.
PDBsum; 3DZU; -.
PDBsum; 3DZY; -.
PDBsum; 3E00; -.
PDBsum; 3ET0; -.
PDBsum; 3ET3; -.
PDBsum; 3FEJ; -.
PDBsum; 3FUR; -.
PDBsum; 3G9E; -.
PDBsum; 3GBK; -.
PDBsum; 3H0A; -.
PDBsum; 3HO0; -.
PDBsum; 3HOD; -.
PDBsum; 3IA6; -.
PDBsum; 3K8S; -.
PDBsum; 3KMG; -.
PDBsum; 3LMP; -.
PDBsum; 3NOA; -.
PDBsum; 3OSI; -.
PDBsum; 3OSW; -.
PDBsum; 3PBA; -.
PDBsum; 3PO9; -.
PDBsum; 3PRG; -.
PDBsum; 3QT0; -.
PDBsum; 3R5N; -.
PDBsum; 3R8A; -.
PDBsum; 3R8I; -.
PDBsum; 3S9S; -.
PDBsum; 3SZ1; -.
PDBsum; 3T03; -.
PDBsum; 3TY0; -.
PDBsum; 3U9Q; -.
PDBsum; 3V9T; -.
PDBsum; 3V9V; -.
PDBsum; 3V9Y; -.
PDBsum; 3VJH; -.
PDBsum; 3VJI; -.
PDBsum; 3VN2; -.
PDBsum; 3VSO; -.
PDBsum; 3VSP; -.
PDBsum; 3WJ4; -.
PDBsum; 3WJ5; -.
PDBsum; 3WMH; -.
PDBsum; 3X1H; -.
PDBsum; 3X1I; -.
PDBsum; 4A4V; -.
PDBsum; 4A4W; -.
PDBsum; 4CI5; -.
PDBsum; 4E4K; -.
PDBsum; 4E4Q; -.
PDBsum; 4EM9; -.
PDBsum; 4EMA; -.
PDBsum; 4F9M; -.
PDBsum; 4FGY; -.
PDBsum; 4HEE; -.
PDBsum; 4JAZ; -.
PDBsum; 4JL4; -.
PDBsum; 4L96; -.
PDBsum; 4L98; -.
PDBsum; 4O8F; -.
PDBsum; 4OJ4; -.
PDBsum; 4PRG; -.
PDBsum; 4PVU; -.
PDBsum; 4PWL; -.
PDBsum; 4R06; -.
PDBsum; 4R2U; -.
PDBsum; 4R6S; -.
PDBsum; 4XLD; -.
PDBsum; 4XTA; -.
PDBsum; 4XUH; -.
PDBsum; 4XUM; -.
PDBsum; 4Y29; -.
PDBsum; 4YT1; -.
PDBsum; 5AZV; -.
PDBsum; 5DSH; -.
PDBsum; 5DV3; -.
PDBsum; 5DV6; -.
PDBsum; 5DV8; -.
PDBsum; 5DVC; -.
PDBsum; 5DWL; -.
PDBsum; 5F9B; -.
PDBsum; 5GTN; -.
PDBsum; 5GTO; -.
PDBsum; 5GTP; -.
PDBsum; 5HZC; -.
PDBsum; 5JI0; -.
PDBsum; 5LSG; -.
PDBsum; 5TTO; -.
PDBsum; 5TWO; -.
PDBsum; 5U5L; -.
PDBsum; 5UGM; -.
PDBsum; 5WQX; -.
PDBsum; 5WR0; -.
PDBsum; 5WR1; -.
PDBsum; 5Y2O; -.
PDBsum; 5Y2T; -.
PDBsum; 5YCN; -.
PDBsum; 5YCP; -.
PDBsum; 5Z5S; -.
PDBsum; 5Z6S; -.
PDBsum; 6AD9; -.
PDBsum; 6AN1; -.
PDBsum; 6AUG; -.
PDBsum; 6AVI; -.
PDBsum; 6C1I; -.
PDBsum; 6C5Q; -.
PDBsum; 6C5T; -.
PDBsum; 6D3E; -.
PDBsum; 6D8X; -.
PDBsum; 6D94; -.
PDBsum; 6DBH; -.
PDBsum; 6DCU; -.
PDBsum; 6DGL; -.
PDBsum; 6DGO; -.
PDBsum; 6DGP; -.
PDBsum; 6DGQ; -.
PDBsum; 6DGR; -.
PDBsum; 6DH9; -.
PDBsum; 6DHA; -.
PDBsum; 6E5A; -.
PDBsum; 6ENQ; -.
PDBsum; 6F2L; -.
PDBsum; 6FZF; -.
PDBsum; 6FZG; -.
PDBsum; 6FZJ; -.
PDBsum; 6FZP; -.
PDBsum; 6FZY; -.
PDBsum; 6ICJ; -.
PDBsum; 6ILQ; -.
PDBsum; 6IZM; -.
PDBsum; 6IZN; -.
PDBsum; 6MCZ; -.
PDBsum; 6MD0; -.
PDBsum; 6MD1; -.
PDBsum; 6MD2; -.
PDBsum; 6MD4; -.
SMR; P37231; -.
BioGrid; 111464; 144.
ComplexPortal; CPX-702; PPARgamma-NCOA2 activated nuclear receptor complex.
ComplexPortal; CPX-711; PPARgamma-NCOA1 activated nuclear receptor complex.
DIP; DIP-35528N; -.
ELM; P37231; -.
IntAct; P37231; 43.
MINT; P37231; -.
STRING; 9606.ENSP00000287820; -.
BindingDB; P37231; -.
ChEMBL; CHEMBL235; -.
DrugBank; DB08760; (2S)-2-(4-chlorophenoxy)-3-phenylpropanoic acid.
DrugBank; DB07842; (2S)-2-(4-ethylphenoxy)-3-phenylpropanoic acid.
DrugBank; DB08121; (2S)-2-(biphenyl-4-yloxy)-3-phenylpropanoic acid.
DrugBank; DB07675; (2S)-2-ETHOXY-3-{4-[2-(10H-PHENOXAZIN-10-YL)ETHOXY]PHENYL}PROPANOIC ACID.
DrugBank; DB06908; (2S)-3-(1-{[2-(2-CHLOROPHENYL)-5-METHYL-1,3-OXAZOL-4-YL]METHYL}-1H-INDOL-5-YL)-2-ETHOXYPROPANOIC ACID.
DrugBank; DB07111; (4S,5E,7Z,10Z,13Z,16Z,19Z)-4-hydroxydocosa-5,7,10,13,16,19-hexaenoic acid.
DrugBank; DB08435; (5E,14E)-11-oxoprosta-5,9,12,14-tetraen-1-oic acid.
DrugBank; DB07172; (5R,6E,8Z,11Z,14Z,17Z)-5-hydroxyicosa-6,8,11,14,17-pentaenoic acid.
DrugBank; DB07208; (8E,10S,12Z)-10-hydroxy-6-oxooctadeca-8,12-dienoic acid.
DrugBank; DB07209; (8R,9Z,12Z)-8-hydroxy-6-oxooctadeca-9,12-dienoic acid.
DrugBank; DB07302; (9S,10E,12Z)-9-hydroxyoctadeca-10,12-dienoic acid.
DrugBank; DB06926; (9Z,11E,13S)-13-hydroxyoctadeca-9,11-dienoic acid.
DrugBank; DB04270; (S)-3-(4-(2-Carbazol-9-Yl-Ethoxy)-Phenyl)-2-Ethoxy-Propionic Acid.
DrugBank; DB08402; 2-[(2,4-DICHLOROBENZOYL)AMINO]-5-(PYRIMIDIN-2-YLOXY)BENZOIC ACID.
DrugBank; DB07863; 2-chloro-5-nitro-N-phenylbenzamide.
DrugBank; DB04689; 2-{5-[3-(6-BENZOYL-1-PROPYLNAPHTHALEN-2-YLOXY)PROPOXY]INDOL-1-YL}ETHANOIC ACID.
DrugBank; DB07053; 2-{5-[3-(7-PROPYL-3-TRIFLUOROMETHYLBENZO[D]ISOXAZOL-6-YLOXY)PROPOXY]INDOL-1-YL}ETHANOIC ACID.
DrugBank; DB07723; 3-(5-methoxy-1H-indol-3-yl)propanoic acid.
DrugBank; DB08302; 3-[5-(2-nitropent-1-en-1-yl)furan-2-yl]benzoic acid.
DrugBank; DB08560; 3-FLUORO-N-[1-(4-FLUOROPHENYL)-3-(2-THIENYL)-1H-PYRAZOL-5-YL]BENZENESULFONAMIDE.
DrugBank; DB08915; Aleglitazar.
DrugBank; DB00132; Alpha-Linolenic Acid.
DrugBank; DB05490; AMG-131.
DrugBank; DB01118; Amiodarone.
DrugBank; DB11811; Arhalofenate.
DrugBank; DB01014; Balsalazide.
DrugBank; DB01393; Bezafibrate.
DrugBank; DB09061; Cannabidiol.
DrugBank; DB03600; Capric acid.
DrugBank; DB09201; Ciglitazone.
DrugBank; DB09006; Clinofibrate.
DrugBank; DB05854; CLX-0921.
DrugBank; DB11672; Curcumin.
DrugBank; DB14635; Curcumin sulfate.
DrugBank; DB14034; Darglitazone.
DrugBank; DB09213; Dexibuprofen.
DrugBank; DB07509; difluoro(5-{2-[(5-octyl-1H-pyrrol-2-yl-kappaN)methylidene]-2H-pyrrol-5-yl-kappaN}pentanoato)boron.
DrugBank; DB03756; Doconexent.
DrugBank; DB05187; Elafibranor.
DrugBank; DB06521; Ertiprotafib.
DrugBank; DB01039; Fenofibrate.
DrugBank; DB13873; Fenofibric acid.
DrugBank; DB00573; Fenoprofen.
DrugBank; DB13961; Fish oil.
DrugBank; DB02266; Flufenamic Acid.
DrugBank; DB01067; Glipizide.
DrugBank; DB01050; Ibuprofen.
DrugBank; DB00159; Icosapent.
DrugBank; DB07724; Indeglitazar.
DrugBank; DB00328; Indometacin.
DrugBank; DB12007; Isoflavone.
DrugBank; DB09198; Lobeglitazone.
DrugBank; DB14009; Medical Cannabis.
DrugBank; DB00244; Mesalazine.
DrugBank; DB01252; Mitiglinide.
DrugBank; DB06510; Muraglitazar.
DrugBank; DB14011; Nabiximols.
DrugBank; DB00731; Nateglinide.
DrugBank; DB12662; Naveglitazar.
DrugBank; DB04224; Oleic Acid.
DrugBank; DB11133; Omega-3 fatty acids.
DrugBank; DB02746; Phthalic Acid.
DrugBank; DB01132; Pioglitazone.
DrugBank; DB06533; Ragaglitazar.
DrugBank; DB04971; Reglitazar.
DrugBank; DB00912; Repaglinide.
DrugBank; DB02709; Resveratrol.
DrugBank; DB00412; Rosiglitazone.
DrugBank; DB00795; Sulfasalazine.
DrugBank; DB00966; Telmisartan.
DrugBank; DB06536; Tesaglitazar.
DrugBank; DB08604; Triclosan.
DrugBank; DB00197; Troglitazone.
DrugBank; DB00313; Valproic Acid.
DrugCentral; P37231; -.
GuidetoPHARMACOLOGY; 595; -.
SwissLipids; SLP:000000396; -.
MoonDB; P37231; Predicted.
iPTMnet; P37231; -.
PhosphoSitePlus; P37231; -.
BioMuta; PPARG; -.
DMDM; 13432234; -.
EPD; P37231; -.
jPOST; P37231; -.
MassIVE; P37231; -.
MaxQB; P37231; -.
PaxDb; P37231; -.
PeptideAtlas; P37231; -.
PRIDE; P37231; -.
ProteomicsDB; 55267; -. [P37231-1]
ProteomicsDB; 55268; -. [P37231-2]
ProteomicsDB; 55269; -. [P37231-3]
DNASU; 5468; -.
Ensembl; ENST00000287820; ENSP00000287820; ENSG00000132170. [P37231-1]
Ensembl; ENST00000397012; ENSP00000380207; ENSG00000132170. [P37231-2]
Ensembl; ENST00000650650; ENSP00000498420; ENSG00000132170. [P37231-3]
Ensembl; ENST00000650761; ENSP00000498354; ENSG00000132170. [P37231-2]
Ensembl; ENST00000651826; ENSP00000499004; ENSG00000132170. [P37231-2]
GeneID; 5468; -.
KEGG; hsa:5468; -.
UCSC; uc003bwr.4; human. [P37231-1]
CTD; 5468; -.
DisGeNET; 5468; -.
EuPathDB; HostDB:ENSG00000132170.19; -.
GeneCards; PPARG; -.
HGNC; HGNC:9236; PPARG.
HPA; CAB004282; -.
HPA; HPA051239; -.
HPA; HPA063663; -.
MalaCards; PPARG; -.
MIM; 137800; phenotype.
MIM; 601487; gene.
MIM; 601665; phenotype.
MIM; 604367; phenotype.
MIM; 606641; phenotype.
MIM; 609338; phenotype.
neXtProt; NX_P37231; -.
OpenTargets; ENSG00000132170; -.
Orphanet; 528; Berardinelli-Seip congenital lipodystrophy.
Orphanet; 146; Differentiated thyroid carcinoma.
Orphanet; 251579; Giant cell glioblastoma.
Orphanet; 251576; Gliosarcoma.
Orphanet; 79083; PPARG-related familial partial lipodystrophy.
PharmGKB; PA281; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00940000158273; -.
HOGENOM; HOG000119407; -.
InParanoid; P37231; -.
KO; K08530; -.
OMA; QRCQFRS; -.
OrthoDB; 492485at2759; -.
PhylomeDB; P37231; -.
TreeFam; TF316304; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
Reactome; R-HSA-9022707; MECP2 regulates transcription factors.
SignaLink; P37231; -.
SIGNOR; P37231; -.
ChiTaRS; PPARG; human.
EvolutionaryTrace; P37231; -.
GeneWiki; Peroxisome_proliferator-activated_receptor_gamma; -.
GenomeRNAi; 5468; -.
Pharos; P37231; Tclin.
PRO; PR:P37231; -.
Proteomes; UP000005640; Chromosome 3.
RNAct; P37231; protein.
Bgee; ENSG00000132170; Expressed in 136 organ(s), highest expression level in subcutaneous adipose tissue.
ExpressionAtlas; P37231; baseline and differential.
Genevisible; P37231; HS.
GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:BHF-UCL.
GO; GO:0033613; F:activating transcription factor binding; IDA:BHF-UCL.
GO; GO:0051393; F:alpha-actinin binding; IPI:UniProtKB.
GO; GO:0050544; F:arachidonic acid binding; ISS:BHF-UCL.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0050692; F:DBD domain binding; IDA:CAFA.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
GO; GO:0003690; F:double-stranded DNA binding; IMP:CAFA.
GO; GO:0008144; F:drug binding; IDA:BHF-UCL.
GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IEA:Ensembl.
GO; GO:0005504; F:fatty acid binding; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0050693; F:LBD domain binding; IDA:CAFA.
GO; GO:0008289; F:lipid binding; IBA:GO_Central.
GO; GO:0004879; F:nuclear receptor activity; IDA:BHF-UCL.
GO; GO:0030374; F:nuclear receptor transcription coactivator activity; IDA:UniProtKB.
GO; GO:0042277; F:peptide binding; IDA:CAFA.
GO; GO:0004955; F:prostaglandin receptor activity; TAS:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IDA:CAFA.
GO; GO:0046982; F:protein heterodimerization activity; IDA:CAFA.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0043621; F:protein self-association; IDA:CAFA.
GO; GO:0046965; F:retinoid X receptor binding; IDA:BHF-UCL.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IBA:GO_Central.
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; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0045165; P:cell fate commitment; ISS:BHF-UCL.
GO; GO:0048469; P:cell maturation; IDA:BHF-UCL.
GO; GO:0071455; P:cellular response to hyperoxia; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IDA:BHF-UCL.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEA:Ensembl.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0071306; P:cellular response to vitamin E; IEA:Ensembl.
GO; GO:0030855; P:epithelial cell differentiation; ISS:BHF-UCL.
GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
GO; GO:0019395; P:fatty acid oxidation; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; IMP:BHF-UCL.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; TAS:BHF-UCL.
GO; GO:0055088; P:lipid homeostasis; TAS:BHF-UCL.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0042953; P:lipoprotein transport; IDA:BHF-UCL.
GO; GO:0015909; P:long-chain fatty acid transport; ISS:BHF-UCL.
GO; GO:0045713; P:low-density lipoprotein particle receptor biosynthetic process; IDA:BHF-UCL.
GO; GO:0010742; P:macrophage derived foam cell differentiation; IDA:UniProtKB.
GO; GO:0030224; P:monocyte differentiation; IDA:BHF-UCL.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl.
GO; GO:0016525; P:negative regulation of angiogenesis; IDA:BHF-UCL.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
GO; GO:0010887; P:negative regulation of cholesterol storage; IDA:BHF-UCL.
GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IEA:Ensembl.
GO; GO:0060965; P:negative regulation of gene silencing by miRNA; IMP:BHF-UCL.
GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
GO; GO:2000230; P:negative regulation of pancreatic stellate cell proliferation; IEA:Ensembl.
GO; GO:0010871; P:negative regulation of receptor biosynthetic process; IDA:BHF-UCL.
GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IDA:BHF-UCL.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0051974; P:negative regulation of telomerase activity; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:BHF-UCL.
GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; IMP:BHF-UCL.
GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0001890; P:placenta development; ISS:BHF-UCL.
GO; GO:0043388; P:positive regulation of DNA binding; IMP:CAFA.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:HGNC-UCL.
GO; GO:0046321; P:positive regulation of fatty acid oxidation; IEA:Ensembl.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CAFA.
GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; IMP:BHF-UCL.
GO; GO:0061614; P:pri-miRNA transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0008217; P:regulation of blood pressure; IMP:BHF-UCL.
GO; GO:0060694; P:regulation of cholesterol transporter activity; IC:BHF-UCL.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0019216; P:regulation of lipid metabolic process; IBA:GO_Central.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0060850; P:regulation of transcription involved in cell fate commitment; ISS:UniProtKB.
GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
GO; GO:0009409; P:response to cold; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
GO; GO:0033993; P:response to lipid; ISS:BHF-UCL.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:1901558; P:response to metformin; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; TAS:ProtInc.
GO; GO:0032526; P:response to retinoic acid; IDA:UniProtKB.
GO; GO:0042594; P:response to starvation; IEA:Ensembl.
GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; IDA:BHF-UCL.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0050872; P:white fat cell differentiation; ISS:HGNC-UCL.
DisProt; DP00718; -.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR003074; 1Cnucl_rcpt.
InterPro; IPR035500; NHR-like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR003077; PPAR-gamma.
InterPro; IPR022590; PPARgamma_N.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF12577; PPARgamma_N; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR01288; PROXISOMEPAR.
PRINTS; PR01291; PROXISOMPAGR.
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; Activator; Alternative splicing; Biological rhythms;
Cytoplasm; Diabetes mellitus; Disease mutation; DNA-binding; Glycoprotein;
Metal-binding; Nucleus; Obesity; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Transcription; Transcription regulation; Zinc;
Zinc-finger.
CHAIN 1..505
/note="Peroxisome proliferator-activated receptor gamma"
/id="PRO_0000053492"
DOMAIN 238..503
/note="NR LBD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
DNA_BIND 136..210
/note="Nuclear receptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 139..159
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 176..198
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
REGION 205..280
/note="Interaction with FAM120B"
/evidence="ECO:0000250"
MOTIF 495..503
/note="9aaTAD"
/evidence="ECO:0000269|PubMed:30468856"
BINDING 317
/note="Synthetic agonist"
/evidence="ECO:0000269|PubMed:11587644,
ECO:0000269|PubMed:12672231, ECO:0000269|PubMed:15056000,
ECO:0000269|PubMed:15258145, ECO:0000269|PubMed:15974597,
ECO:0000269|PubMed:15976031, ECO:0000269|PubMed:16451087,
ECO:0000269|PubMed:16640330, ECO:0000269|PubMed:16919947"
BINDING 351
/note="Synthetic agonist"
/evidence="ECO:0000269|PubMed:11587644,
ECO:0000269|PubMed:12672231, ECO:0000269|PubMed:15056000,
ECO:0000269|PubMed:15258145, ECO:0000269|PubMed:15974597,
ECO:0000269|PubMed:15976031, ECO:0000269|PubMed:16451087,
ECO:0000269|PubMed:16640330, ECO:0000269|PubMed:16919947"
BINDING 477
/note="Synthetic agonist"
/evidence="ECO:0000269|PubMed:11587644,
ECO:0000269|PubMed:12672231, ECO:0000269|PubMed:15056000,
ECO:0000269|PubMed:15258145, ECO:0000269|PubMed:15974597,
ECO:0000269|PubMed:15976031, ECO:0000269|PubMed:16451087,
ECO:0000269|PubMed:16640330, ECO:0000269|PubMed:16919947"
BINDING 501
/note="Synthetic agonist"
/evidence="ECO:0000269|PubMed:11587644,
ECO:0000269|PubMed:12672231, ECO:0000269|PubMed:15056000,
ECO:0000269|PubMed:15258145, ECO:0000269|PubMed:15974597,
ECO:0000269|PubMed:15976031, ECO:0000269|PubMed:16451087,
ECO:0000269|PubMed:16640330, ECO:0000269|PubMed:16919947"
MOD_RES 112
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
CARBOHYD 84
/note="O-linked (GlcNAc) threonine"
/evidence="ECO:0000250"
VAR_SEQ 1..28
/note="Missing (in isoform 1 and isoform 3)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16842753,
ECO:0000303|PubMed:7787419, ECO:0000303|PubMed:8702406,
ECO:0000303|PubMed:8706692, ECO:0000303|PubMed:9065481"
/id="VSP_003645"
VAR_SEQ 207..213
/note="AIRFGRM -> EELQKDS (in isoform 3)"
/evidence="ECO:0000303|PubMed:16842753"
/id="VSP_043906"
VAR_SEQ 214..504
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:16842753"
/id="VSP_043907"
VARIANT 12
/note="P -> A (polymorphism; significant independent
determinant of CIMT; may protect from early atherosclerosis
in subject at risk for diabetes; associated with BMI;
dbSNP:rs1801282)"
/evidence="ECO:0000269|PubMed:10394368,
ECO:0000269|PubMed:10407229, ECO:0000269|PubMed:15562396,
ECO:0000269|PubMed:9425261, ECO:0000269|Ref.12"
/id="VAR_010723"
VARIANT 40
/note="P -> A (in dbSNP:rs1805192)"
/id="VAR_016116"
VARIANT 113
/note="P -> Q (in obesity; dbSNP:rs1800571)"
/evidence="ECO:0000269|PubMed:9753710"
/id="VAR_010724"
VARIANT 314
/note="Q -> P (in colon cancer; sporadic; somatic mutation;
loss of ligand-binding; dbSNP:rs121909242)"
/evidence="ECO:0000269|PubMed:10394368"
/id="VAR_010725"
VARIANT 316
/note="R -> H (in colon cancer; sporadic; somatic mutation;
partial loss of ligand-binding; dbSNP:rs28936407)"
/evidence="ECO:0000269|PubMed:10394368"
/id="VAR_010726"
VARIANT 318
/note="V -> M (in diabetes; dbSNP:rs72551362)"
/evidence="ECO:0000269|PubMed:10622252"
/id="VAR_010727"
VARIANT 388
/note="F -> L (in FPLD3; dbSNP:rs72551363)"
/evidence="ECO:0000269|PubMed:12453919"
/id="VAR_022700"
VARIANT 425
/note="R -> C (in FPLD3; dbSNP:rs72551364)"
/evidence="ECO:0000269|PubMed:11788685"
/id="VAR_022701"
VARIANT 495
/note="P -> L (in diabetes; dbSNP:rs121909244)"
/evidence="ECO:0000269|PubMed:10622252"
/id="VAR_010728"
CONFLICT 36..37
/note="MP -> IA (in Ref. 3; BAA18949)"
/evidence="ECO:0000305"
CONFLICT 213..214
/note="MP -> IA (in Ref. 3; BAA18949)"
/evidence="ECO:0000305"
CONFLICT 240
/note="R -> RQ (in Ref. 3; BAA18949)"
/evidence="ECO:0000305"
STRAND 140..142
/evidence="ECO:0000244|PDB:3DZY"
STRAND 148..150
/evidence="ECO:0000244|PDB:3DZU"
STRAND 151..154
/evidence="ECO:0000244|PDB:3DZY"
HELIX 157..167
/evidence="ECO:0000244|PDB:3DZY"
TURN 168..170
/evidence="ECO:0000244|PDB:3DZY"
HELIX 186..188
/evidence="ECO:0000244|PDB:3DZY"
HELIX 191..200
/evidence="ECO:0000244|PDB:3DZY"
HELIX 205..207
/evidence="ECO:0000244|PDB:3DZY"
TURN 214..217
/evidence="ECO:0000244|PDB:3DZY"
HELIX 218..220
/evidence="ECO:0000244|PDB:3DZY"
TURN 222..226
/evidence="ECO:0000244|PDB:3DZY"
TURN 228..231
/evidence="ECO:0000244|PDB:3DZY"
HELIX 237..253
/evidence="ECO:0000244|PDB:3U9Q"
HELIX 258..265
/evidence="ECO:0000244|PDB:3U9Q"
STRAND 266..268
/evidence="ECO:0000244|PDB:5F9B"
STRAND 269..271
/evidence="ECO:0000244|PDB:3U9Q"
STRAND 275..277
/evidence="ECO:0000244|PDB:3U9Q"
HELIX 280..286
/evidence="ECO:0000244|PDB:3U9Q"
TURN 287..289
/evidence="ECO:0000244|PDB:3V9T"
STRAND 290..292
/evidence="ECO:0000244|PDB:1ZGY"
STRAND 294..296
/evidence="ECO:0000244|PDB:1ZGY"
HELIX 298..300
/evidence="ECO:0000244|PDB:6D94"
STRAND 301..303
/evidence="ECO:0000244|PDB:1FM6"
HELIX 305..329
/evidence="ECO:0000244|PDB:3U9Q"
HELIX 334..336
/evidence="ECO:0000244|PDB:3U9Q"
HELIX 339..360
/evidence="ECO:0000244|PDB:3U9Q"
STRAND 361..363
/evidence="ECO:0000244|PDB:3DZU"
STRAND 366..369
/evidence="ECO:0000244|PDB:3U9Q"
TURN 370..373
/evidence="ECO:0000244|PDB:3U9Q"
STRAND 374..377
/evidence="ECO:0000244|PDB:3U9Q"
HELIX 378..383
/evidence="ECO:0000244|PDB:3U9Q"
TURN 385..387
/evidence="ECO:0000244|PDB:6IZN"
HELIX 388..390
/evidence="ECO:0000244|PDB:3U9Q"
HELIX 393..403
/evidence="ECO:0000244|PDB:3U9Q"
HELIX 409..420
/evidence="ECO:0000244|PDB:3U9Q"
STRAND 423..425
/evidence="ECO:0000244|PDB:3ADT"
HELIX 431..452
/evidence="ECO:0000244|PDB:3U9Q"
STRAND 454..456
/evidence="ECO:0000244|PDB:3SZ1"
HELIX 459..486
/evidence="ECO:0000244|PDB:3U9Q"
STRAND 488..490
/evidence="ECO:0000244|PDB:6D94"
HELIX 491..493
/evidence="ECO:0000244|PDB:4L98"
HELIX 495..501
/evidence="ECO:0000244|PDB:3U9Q"
SEQUENCE 505 AA; 57620 MW; 3933EFF36A0E4CAF CRC64;
MGETLGDSPI DPESDSFTDT LSANISQEMT MVDTEMPFWP TNFGISSVDL SVMEDHSHSF
DIKPFTTVDF SSISTPHYED IPFTRTDPVV ADYKYDLKLQ EYQSAIKVEP ASPPYYSEKT
QLYNKPHEEP SNSLMAIECR VCGDKASGFH YGVHACEGCK GFFRRTIRLK LIYDRCDLNC
RIHKKSRNKC QYCRFQKCLA VGMSHNAIRF GRMPQAEKEK LLAEISSDID QLNPESADLR
ALAKHLYDSY IKSFPLTKAK ARAILTGKTT DKSPFVIYDM NSLMMGEDKI KFKHITPLQE
QSKEVAIRIF QGCQFRSVEA VQEITEYAKS IPGFVNLDLN DQVTLLKYGV HEIIYTMLAS
LMNKDGVLIS EGQGFMTREF LKSLRKPFGD FMEPKFEFAV KFNALELDDS DLAIFIAVII
LSGDRPGLLN VKPIEDIQDN LLQALELQLK LNHPESSQLF AKLLQKMTDL RQIVTEHVQL
LQVIKKTETD MSLHPLLQEI YKDLY


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E0886h ELISA Homo sapiens,Human,NR1C3,Nuclear receptor subfamily 1 group C member 3,Peroxisome proliferator-activated receptor gamma,PPARG,PPAR-gamma 96T
U0886h CLIA Homo sapiens,Human,NR1C3,Nuclear receptor subfamily 1 group C member 3,Peroxisome proliferator-activated receptor gamma,PPARG,PPAR-gamma 96T
U0886Rb CLIA NR1C3,Nuclear receptor subfamily 1 group C member 3,Oryctolagus cuniculus,Peroxisome proliferator-activated receptor gamma,PPARG,PPAR-gamma,Rabbit 96T
E0886Rb ELISA kit NR1C3,Nuclear receptor subfamily 1 group C member 3,Oryctolagus cuniculus,Peroxisome proliferator-activated receptor gamma,PPARG,PPAR-gamma,Rabbit 96T
U0886c CLIA Canis familiaris,Canis lupus familiaris,Dog,NR1C3,Nuclear receptor subfamily 1 group C member 3,Peroxisome proliferator-activated receptor gamma,PPARG,PPAR-gamma 96T
E0886c ELISA kit Canis familiaris,Canis lupus familiaris,Dog,NR1C3,Nuclear receptor subfamily 1 group C member 3,Peroxisome proliferator-activated receptor gamma,PPARG,PPAR-gamma 96T
E0886c ELISA Canis familiaris,Canis lupus familiaris,Dog,NR1C3,Nuclear receptor subfamily 1 group C member 3,Peroxisome proliferator-activated receptor gamma,PPARG,PPAR-gamma 96T
32-204 PPAR gamma(PPARG), which encodes a member of the peroxisome proliferator-activated receptor (PPAR) subfamily of nuclear receptors. Three subtypes of PPARs are known PPAR-alpha, PPAR-delta, and PPAR-g 0.1 mL
U2041m CLIA Mouse,Mus musculus,Nr1c2,NUC1,Nuclear hormone receptor 1,Nuclear receptor subfamily 1 group C member 2,Peroxisome proliferator-activated receptor beta,Peroxisome proliferator-activated receptor d 96T
E2041m ELISA Mouse,Mus musculus,Nr1c2,NUC1,Nuclear hormone receptor 1,Nuclear receptor subfamily 1 group C member 2,Peroxisome proliferator-activated receptor beta,Peroxisome proliferator-activated receptor 96T
U2041h CLIA kit Homo sapiens,Human,NR1C2,NUC1,NUCI,Nuclear hormone receptor 1,Nuclear receptor subfamily 1 group C member 2,Peroxisome proliferator-activated receptor beta,Peroxisome proliferator-activated 96T
Pathways :
WP2292: Chemokine signaling pathway
WP1836: Interferon gamma signaling
WP304: Kit receptor signaling pathway
WP809: TGF-beta Receptor Signaling Pathway
WP1004: Kit Receptor Signaling Pathway
WP1354: B Cell Receptor Signaling Pathway
WP581: EPO Receptor Signaling
WP949: Toll-like receptor signaling pathway
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP2272: Pathogenic Escherichia coli infection
WP996: EPO Receptor Signaling
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP1886: Post-translational modification: gamma carboxylation and hypusine formation
WP352: T Cell Receptor Signaling Pathway
WP1025: B Cell Receptor Signaling Pathway
WP1384: Toll-like receptor signaling pathway
WP868: estrogen signalling
WP1067: Toll-like receptor signaling pathway
WP1449: Regulation of toll-like receptor signaling pathway
WP734: Serotonin Receptor 4/6/7 and NR3C Signaling
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP758: EBV LMP1 signaling
WP1284: EPO Receptor Signaling
WP1965: VEGF-receptor Signal Transduction
WP480: T Cell Receptor Signaling Pathway

Related Genes :
[PPARG NR1C3] Peroxisome proliferator-activated receptor gamma (PPAR-gamma) (Nuclear receptor subfamily 1 group C member 3)
[Med1 Crsp210 Drip205 Pbp Pparbp Trap220 Trip2] Mediator of RNA polymerase II transcription subunit 1 (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2)
[Ncoa6 Aib3 Prip Rap250 Trbp] Nuclear receptor coactivator 6 (Activating signal cointegrator 2) (ASC-2) (Amplified in breast cancer protein 3) (Cancer-amplified transcriptional coactivator ASC-2) (Nuclear receptor coactivator RAP250) (NRC) (Nuclear receptor-activating protein, 250 kDa) (Peroxisome proliferator-activated receptor-interacting protein) (PPAR-interacting protein) (Thyroid hormone receptor-binding protein)
[MED1 ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2] Mediator of RNA polymerase II transcription subunit 1 (Activator-recruited cofactor 205 kDa component) (ARC205) (Mediator complex subunit 1) (Peroxisome proliferator-activated receptor-binding protein) (PBP) (PPAR-binding protein) (Thyroid hormone receptor-associated protein complex 220 kDa component) (Trap220) (Thyroid receptor-interacting protein 2) (TR-interacting protein 2) (TRIP-2) (Vitamin D receptor-interacting protein complex component DRIP205) (p53 regulatory protein RB18A)
[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)
[Ncoa6 Aib3 Rap250 Trbp] Nuclear receptor coactivator 6 (Activating signal cointegrator 2) (ASC-2) (Amplified in breast cancer protein 3) (Cancer-amplified transcriptional coactivator ASC-2) (Nuclear receptor coactivator RAP250) (NRC) (Nuclear receptor-activating protein, 250 kDa) (Peroxisome proliferator-activated receptor-interacting protein) (PPAR-interacting protein) (PRIP) (Thyroid hormone receptor-binding protein) (Fragment)
[NCOA6 AIB3 KIAA0181 RAP250 TRBP] Nuclear receptor coactivator 6 (Activating signal cointegrator 2) (ASC-2) (Amplified in breast cancer protein 3) (Cancer-amplified transcriptional coactivator ASC-2) (Nuclear receptor coactivator RAP250) (NRC RAP250) (Nuclear receptor-activating protein, 250 kDa) (Peroxisome proliferator-activated receptor-interacting protein) (PPAR-interacting protein) (PRIP) (Thyroid hormone receptor-binding protein)
[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)
[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 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)
[Esr2 Estrb Nr3a2] Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2)
[Nr3c1 Grl Grl1] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[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)
[Esr1 Esr Estr Estra Nr3a1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[Rxra Nr2b1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[Rarg Nr1b3] Retinoic acid receptor gamma (RAR-gamma) (Nuclear receptor subfamily 1 group B member 3)
[Rara Nr1b1] Retinoic acid receptor alpha (RAR-alpha) (Nuclear receptor subfamily 1 group B member 1)
[ESRRA ERR1 ESRL1 NR3B1] Steroid hormone receptor ERR1 (Estrogen receptor-like 1) (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)
[Rxrg Nr2b3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[Esrrg Err3 Kiaa0832 Nr3b3] Estrogen-related receptor gamma (Estrogen receptor-related protein 3) (Nuclear receptor subfamily 3 group B member 3)
[NR2C2 TAK1 TR4] Nuclear receptor subfamily 2 group C member 2 (Orphan nuclear receptor TAK1) (Orphan nuclear receptor TR4) (Testicular receptor 4)
[RXRA NR2B1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[RARG NR1B3] Retinoic acid receptor gamma (RAR-gamma) (Nuclear receptor subfamily 1 group B member 3)
[rarga nr1b3a rarg rarg2 si:dkey-148f24.2] Retinoic acid receptor gamma-A (RAR-gamma-A) (zRAR gamma) (Nuclear receptor subfamily 1 group B member 3-A) (RAR-gamma-2)
[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)
[Nr2c1 Tr2 Tr2-11] Nuclear receptor subfamily 2 group C member 1 (Orphan nuclear receptor TR2) (Testicular receptor 2) (mTR2)
[RXRG NR2B3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[rargb nr1b3b] Retinoic acid receptor gamma-B (RAR-gamma-B) (Nuclear receptor subfamily 1 group B member 3-B)
[RXRG NR2B3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[ESRRB ERRB2 ESRL2 NR3B2] Steroid hormone receptor ERR2 (ERR beta-2) (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2)

Bibliography :