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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.
30-AUG-2017, entry version 234.
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 ENZYME 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]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
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).
[39]
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).
[40]
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).
[41]
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).
[42]
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).
[43]
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).
[44]
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).
[45]
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).
[46]
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).
[47]
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).
[48]
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).
[49]
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).
[50]
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).
[51]
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).
[52]
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).
[53]
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).
[54]
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).
[55]
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}.
-!- ENZYME 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. {ECO:0000250,
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: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;
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;
Note=Exhibits dominant negative activity over isoform 1.;
-!- 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}.
-!- PTM: O-GlcNAcylation at Thr-84 reduces transcriptional activity in
adipocytes. {ECO:0000250}.
-!- 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.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAN38992.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA23354.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAF83270.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA62153.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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. [P37231-2]
UniGene; Hs.162646; -.
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; 5HZC; X-ray; 2.00 A; A/B=223-505.
PDB; 5JI0; X-ray; 1.98 A; D=234-505.
PDB; 5TTO; X-ray; 2.25 A; A/B=233-505.
PDB; 5TWO; X-ray; 1.93 A; A=234-505.
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; 5HZC; -.
PDBsum; 5JI0; -.
PDBsum; 5TTO; -.
PDBsum; 5TWO; -.
DisProt; DP00718; -.
ProteinModelPortal; P37231; -.
SMR; P37231; -.
BioGrid; 111464; 138.
DIP; DIP-35528N; -.
ELM; P37231; -.
IntAct; P37231; 32.
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; DB04270; (S)-3-(4-(2-Carbazol-9-Yl-Ethoxy)-Phenyl)-2-Ethoxy-Propionic 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; DB07724; 3-{5-methoxy-1-[(4-methoxyphenyl)sulfonyl]-1H-indol-3-yl}propanoic acid.
DrugBank; DB08915; Aleglitazar.
DrugBank; DB01014; Balsalazide.
DrugBank; DB01393; Bezafibrate.
DrugBank; DB05854; CLX-0921.
DrugBank; DB07509; difluoro(5-{2-[(5-octyl-1H-pyrrol-2-yl-kappaN)methylidene]-2H-pyrrol-5-yl-kappaN}pentanoato)boron.
DrugBank; DB05187; GFT505.
DrugBank; DB01067; Glipizide.
DrugBank; DB01050; Ibuprofen.
DrugBank; DB00159; Icosapent.
DrugBank; DB00328; Indomethacin.
DrugBank; DB00244; Mesalazine.
DrugBank; DB01252; Mitiglinide.
DrugBank; DB00731; Nateglinide.
DrugBank; DB01132; Pioglitazone.
DrugBank; DB04971; Reglixane.
DrugBank; DB00912; Repaglinide.
DrugBank; DB00412; Rosiglitazone.
DrugBank; DB00795; Sulfasalazine.
DrugBank; DB05490; T131.
DrugBank; DB00966; Telmisartan.
DrugBank; DB00197; Troglitazone.
GuidetoPHARMACOLOGY; 595; -.
SwissLipids; SLP:000000396; -.
iPTMnet; P37231; -.
PhosphoSitePlus; P37231; -.
BioMuta; PPARG; -.
DMDM; 13432234; -.
EPD; P37231; -.
MaxQB; P37231; -.
PaxDb; P37231; -.
PeptideAtlas; P37231; -.
PRIDE; P37231; -.
DNASU; 5468; -.
Ensembl; ENST00000287820; ENSP00000287820; ENSG00000132170. [P37231-1]
Ensembl; ENST00000309576; ENSP00000312472; ENSG00000132170. [P37231-2]
Ensembl; ENST00000396999; ENSP00000380195; ENSG00000132170. [P37231-3]
Ensembl; ENST00000397010; ENSP00000380205; ENSG00000132170. [P37231-2]
Ensembl; ENST00000397012; ENSP00000380207; ENSG00000132170. [P37231-2]
Ensembl; ENST00000397015; ENSP00000380210; ENSG00000132170. [P37231-2]
GeneID; 5468; -.
KEGG; hsa:5468; -.
UCSC; uc003bwr.4; human. [P37231-1]
CTD; 5468; -.
DisGeNET; 5468; -.
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; 79083; Familial partial lipodystrophy associated with PPARG mutations.
Orphanet; 251579; Giant cell glioblastoma.
Orphanet; 251576; Gliosarcoma.
PharmGKB; PA281; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00870000136388; -.
HOGENOM; HOG000119407; -.
HOVERGEN; HBG106004; -.
InParanoid; P37231; -.
KO; K08530; -.
OMA; PLQEQSK; -.
OrthoDB; EOG091G05U8; -.
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.
SignaLink; P37231; -.
SIGNOR; P37231; -.
ChiTaRS; PPARG; human.
EvolutionaryTrace; P37231; -.
GeneWiki; Peroxisome_proliferator-activated_receptor_gamma; -.
GenomeRNAi; 5468; -.
PRO; PR:P37231; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000132170; -.
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:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0043234; C:protein 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:0001046; F:core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0050692; F:DBD domain binding; IDA:CAFA.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IMP:CAFA.
GO; GO:0008144; F:drug binding; IDA:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0050693; F:LBD domain binding; IDA:CAFA.
GO; GO:0030374; F:ligand-dependent 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:0004879; F:RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
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: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: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: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: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:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl.
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: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 from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS: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:0045600; P:positive regulation of fat cell differentiation; ISS:HGNC.
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:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CAFA.
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: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:0042493; P:response to drug; 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:0055098; P:response to low-density lipoprotein particle; IDA: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.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR003074; 1Cnucl_rcpt.
InterPro; IPR003077; 1Cnucl_rcpt_G.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
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; 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;
Complete proteome; 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 Peroxisome proliferator-activated
receptor gamma.
/FTId=PRO_0000053492.
DNA_BIND 136 210 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 139 159 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 176 198 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 205 280 Interaction with FAM120B. {ECO:0000250}.
REGION 317 505 Ligand-binding.
BINDING 317 317 Synthetic agonist.
{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 351 351 Synthetic agonist.
{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 477 477 Synthetic agonist.
{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 501 501 Synthetic agonist.
{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 112 112 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 84 84 O-linked (GlcNAc) threonine.
{ECO:0000250}.
VAR_SEQ 1 28 Missing (in isoform 1 and isoform 3).
{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}.
/FTId=VSP_003645.
VAR_SEQ 207 213 AIRFGRM -> EELQKDS (in isoform 3).
{ECO:0000303|PubMed:16842753}.
/FTId=VSP_043906.
VAR_SEQ 214 504 Missing (in isoform 3).
{ECO:0000303|PubMed:16842753}.
/FTId=VSP_043907.
VARIANT 12 12 P -> A (polymorphism; significant
independent determinant of CIMT; may
protect from early atherosclerosis in
subject at risk for diabetes; associated
with BMI; dbSNP:rs1801282).
{ECO:0000269|PubMed:10394368,
ECO:0000269|PubMed:10407229,
ECO:0000269|PubMed:15562396,
ECO:0000269|PubMed:9425261,
ECO:0000269|Ref.12}.
/FTId=VAR_010723.
VARIANT 40 40 P -> A (in dbSNP:rs1805192).
/FTId=VAR_016116.
VARIANT 113 113 P -> Q (in obesity; dbSNP:rs1800571).
{ECO:0000269|PubMed:9753710}.
/FTId=VAR_010724.
VARIANT 314 314 Q -> P (in colon cancer; sporadic;
somatic mutation; loss of ligand-binding;
dbSNP:rs28936407).
{ECO:0000269|PubMed:10394368}.
/FTId=VAR_010725.
VARIANT 316 316 R -> H (in colon cancer; sporadic;
somatic mutation; partial loss of ligand-
binding; dbSNP:rs28936407).
{ECO:0000269|PubMed:10394368}.
/FTId=VAR_010726.
VARIANT 318 318 V -> M (in diabetes; dbSNP:rs72551362).
{ECO:0000269|PubMed:10622252}.
/FTId=VAR_010727.
VARIANT 388 388 F -> L (in FPLD3; dbSNP:rs72551363).
{ECO:0000269|PubMed:12453919}.
/FTId=VAR_022700.
VARIANT 425 425 R -> C (in FPLD3; dbSNP:rs72551364).
{ECO:0000269|PubMed:11788685}.
/FTId=VAR_022701.
VARIANT 495 495 P -> L (in diabetes; dbSNP:rs121909244).
{ECO:0000269|PubMed:10622252}.
/FTId=VAR_010728.
CONFLICT 36 37 MP -> IA (in Ref. 3; BAA18949).
{ECO:0000305}.
CONFLICT 213 214 MP -> IA (in Ref. 3; BAA18949).
{ECO:0000305}.
CONFLICT 240 240 R -> RQ (in Ref. 3; BAA18949).
{ECO:0000305}.
STRAND 140 142 {ECO:0000244|PDB:3DZY}.
STRAND 148 150 {ECO:0000244|PDB:3DZU}.
STRAND 151 154 {ECO:0000244|PDB:3DZY}.
HELIX 157 167 {ECO:0000244|PDB:3DZY}.
TURN 168 170 {ECO:0000244|PDB:3DZY}.
HELIX 186 188 {ECO:0000244|PDB:3DZY}.
HELIX 191 200 {ECO:0000244|PDB:3DZY}.
HELIX 205 207 {ECO:0000244|PDB:3DZY}.
TURN 214 217 {ECO:0000244|PDB:3DZY}.
HELIX 218 220 {ECO:0000244|PDB:3DZY}.
TURN 222 226 {ECO:0000244|PDB:3DZY}.
TURN 228 231 {ECO:0000244|PDB:3DZY}.
HELIX 237 253 {ECO:0000244|PDB:3U9Q}.
HELIX 258 265 {ECO:0000244|PDB:3U9Q}.
STRAND 266 268 {ECO:0000244|PDB:5F9B}.
STRAND 269 271 {ECO:0000244|PDB:3U9Q}.
STRAND 275 277 {ECO:0000244|PDB:3U9Q}.
HELIX 280 286 {ECO:0000244|PDB:3U9Q}.
TURN 287 289 {ECO:0000244|PDB:3V9T}.
STRAND 290 292 {ECO:0000244|PDB:1ZGY}.
STRAND 294 296 {ECO:0000244|PDB:1ZGY}.
HELIX 298 300 {ECO:0000244|PDB:5TWO}.
STRAND 301 303 {ECO:0000244|PDB:1FM6}.
HELIX 305 329 {ECO:0000244|PDB:3U9Q}.
HELIX 334 336 {ECO:0000244|PDB:3U9Q}.
HELIX 339 360 {ECO:0000244|PDB:3U9Q}.
STRAND 361 363 {ECO:0000244|PDB:3DZU}.
STRAND 366 369 {ECO:0000244|PDB:3U9Q}.
TURN 370 373 {ECO:0000244|PDB:3U9Q}.
STRAND 374 377 {ECO:0000244|PDB:3U9Q}.
HELIX 378 383 {ECO:0000244|PDB:3U9Q}.
TURN 385 387 {ECO:0000244|PDB:4Y29}.
HELIX 388 390 {ECO:0000244|PDB:3U9Q}.
HELIX 393 403 {ECO:0000244|PDB:3U9Q}.
HELIX 409 420 {ECO:0000244|PDB:3U9Q}.
STRAND 423 425 {ECO:0000244|PDB:3ADT}.
HELIX 431 452 {ECO:0000244|PDB:3U9Q}.
STRAND 454 456 {ECO:0000244|PDB:3SZ1}.
HELIX 459 486 {ECO:0000244|PDB:3U9Q}.
STRAND 488 490 {ECO:0000244|PDB:2HWQ}.
HELIX 491 493 {ECO:0000244|PDB:4L98}.
HELIX 495 501 {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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