PPARG_HUMAN
ID PPARG_HUMAN Reviewed; 505 AA.
AC P37231; A8K3G6; B5BUA1; O00684; O00710; O14515; Q0QJH8; Q15178; Q15179;
AC Q15180; Q15832; Q86U60; Q96J12;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 3.
DT 03-AUG-2022, entry version 273.
DE RecName: Full=Peroxisome proliferator-activated receptor gamma;
DE Short=PPAR-gamma;
DE AltName: Full=Nuclear receptor subfamily 1 group C member 3;
GN Name=PPARG; Synonyms=NR1C3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=9065481; DOI=10.1074/jbc.272.12.8071;
RA Mukherjee R., Jow L., Croston G.E., Paterniti J.R. Jr.;
RT "Identification, characterization, and tissue distribution of human
RT peroxisome proliferator-activated receptor (PPAR) isoforms PPARgamma2
RT versus PPARgamma1 and activation with retinoid X receptor agonists and
RT antagonists.";
RL J. Biol. Chem. 272:8071-8076(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adipose tissue;
RX PubMed=8702406; DOI=10.1006/bbrc.1996.1044;
RA Elbrecht A., Chen Y., Cullinan C.A., Hayes N., Leibowitz M.D., Moller D.E.,
RA Berger J.;
RT "Molecular cloning, expression and characterization of human peroxisome
RT proliferator activated receptors gamma 1 and gamma 2.";
RL Biochem. Biophys. Res. Commun. 224:431-437(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Adipose tissue;
RX PubMed=9144532; DOI=10.1006/bbrc.1997.6446;
RA Yanase T., Yashiro T., Takitani K., Kato S., Taniguchi S., Takayanagi R.,
RA Nawata H.;
RT "Differential expression of PPAR gamma1 and gamma2 isoforms in human
RT adipose tissue.";
RL Biochem. Biophys. Res. Commun. 233:320-324(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7787419;
RA Greene M.E., Blumberg B., McBride O.W., Yi H.F., Kronquist K., Kwan K.,
RA Hsieh L., Greene G., Nimer S.D.;
RT "Isolation of the human peroxisome proliferator activated receptor gamma
RT cDNA: expression in hematopoietic cells and chromosomal mapping.";
RL Gene Expr. 4:281-299(1995).
RN [5]
RP SEQUENCE REVISION TO 36; 37; 213; 214 AND 240.
RA Greene M.E.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=9356045; DOI=10.2337/diab.46.11.1904;
RA Okazawa H., Mori H., Tamori Y., Araki S., Niki T., Masugi J., Kawanishi M.,
RA Kubota T., Shinoda H., Kasuga M.;
RT "No coding mutations are detected in the peroxisome proliferator-activated
RT receptor-gamma gene in Japanese patients with lipoatrophic diabetes.";
RL Diabetes 46:1904-1906(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=8706692; DOI=10.1111/j.1432-1033.1996.0001u.x;
RA Lambe K.G., Tugwood J.D.;
RT "A human peroxisome-proliferator-activated receptor-gamma is activated by
RT inducers of adipogenesis, including thiazolidinedione drugs.";
RL Eur. J. Biochem. 239:1-7(1996).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=16842753; DOI=10.1016/j.bbrc.2006.06.147;
RA Kim H.J., Woo I.S., Kang E.S., Eun S.Y., Kim H.J., Lee J.H., Chang K.C.,
RA Kim J.H., Seo H.G.;
RT "Identification of a truncated alternative splicing variant of human
RT PPARgamma1 that exhibits dominant negative activity.";
RL Biochem. Biophys. Res. Commun. 347:698-706(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human Protein Factory: an infrastructure to convert the human
RT transcriptome into the in vitro-expressed human proteome of versatile
RT utility.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-12.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [16]
RP INTERACTION WITH NCOA6.
RX PubMed=10681503; DOI=10.1074/jbc.275.8.5308;
RA Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.;
RT "Cloning and characterization of RAP250, a nuclear receptor coactivator.";
RL J. Biol. Chem. 275:5308-5317(2000).
RN [17]
RP POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO GLIOMA.
RX PubMed=10851250; DOI=10.1136/jmg.37.6.410;
RA Zhou X.P., Smith W.M., Gimm O., Mueller E., Gao X., Sarraf P., Prior T.W.,
RA Plass C., von Deimling A., Black P.M., Yates A.J., Eng C.;
RT "Over-representation of PPARgamma sequence variants in sporadic cases of
RT glioblastoma multiforme: preliminary evidence for common low penetrance
RT modifiers for brain tumour risk in the general population.";
RL J. Med. Genet. 37:410-414(2000).
RN [18]
RP INTERACTION WITH PRMT2.
RX PubMed=12039952; DOI=10.1074/jbc.m201053200;
RA Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
RT "Identification of protein arginine methyltransferase 2 as a coactivator
RT for estrogen receptor alpha.";
RL J. Biol. Chem. 277:28624-28630(2002).
RN [19]
RP INTERACTION WITH NOCA7.
RX PubMed=11971969; DOI=10.1128/mcb.22.10.3358-3372.2002;
RA Shao W., Halachmi S., Brown M.;
RT "ERAP140, a conserved tissue-specific nuclear receptor coactivator.";
RL Mol. Cell. Biol. 22:3358-3372(2002).
RN [20]
RP INTERACTION WITH DNTTIP2.
RX PubMed=15047147; DOI=10.1016/j.bbrc.2004.02.179;
RA Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M.,
RA Zhu Y.-J.;
RT "ERBP, a novel estrogen receptor binding protein enhancing the activity of
RT estrogen receptor.";
RL Biochem. Biophys. Res. Commun. 317:54-59(2004).
RN [21]
RP INTERACTION WITH TGFB1I1.
RX PubMed=15687259; DOI=10.1101/gad.1240705;
RA Drori S., Girnun G.D., Tou L., Szwaya J.D., Mueller E., Xia K.,
RA Shivdasani R.A., Spiegelman B.M.;
RT "Hic-5 regulates an epithelial program mediated by PPARgamma.";
RL Genes Dev. 19:362-375(2005).
RN [22]
RP INTERACTION WITH HELZ2.
RX PubMed=16239304; DOI=10.1210/en.2005-0450;
RA Tomaru T., Satoh T., Yoshino S., Ishizuka T., Hashimoto K., Monden T.,
RA Yamada M., Mori M.;
RT "Isolation and characterization of a transcriptional cofactor and its novel
RT isoform that bind the DNA-binding domain of peroxisome proliferator-
RT activated receptor gamma.";
RL Endocrinology 147:377-388(2006).
RN [23]
RP FUNCTION, INTERACTION WITH PDPK1, AND ACTIVITY REGULATION.
RX PubMed=16150867; DOI=10.1210/me.2005-0197;
RA Yin Y., Yuan H., Wang C., Pattabiraman N., Rao M., Pestell R.G.,
RA Glazer R.I.;
RT "3-phosphoinositide-dependent protein kinase-1 activates the peroxisome
RT proliferator-activated receptor-gamma and promotes adipocyte
RT differentiation.";
RL Mol. Endocrinol. 20:268-278(2006).
RN [24]
RP INTERACTION WITH MAP2K1/MEK1, AND SUBCELLULAR LOCATION.
RX PubMed=17101779; DOI=10.1128/mcb.00601-06;
RA Burgermeister E., Chuderland D., Hanoch T., Meyer M., Liscovitch M.,
RA Seger R.;
RT "Interaction with MEK causes nuclear export and downregulation of
RT peroxisome proliferator-activated receptor gamma.";
RL Mol. Cell. Biol. 27:803-817(2007).
RN [25]
RP INTERACTION WITH TACC1.
RX PubMed=20078863; DOI=10.1186/1471-2199-11-3;
RA Guyot R., Vincent S., Bertin J., Samarut J., Ravel-Chapuis P.;
RT "The transforming acidic coiled coil (TACC1) protein modulates the
RT transcriptional activity of the nuclear receptors TR and RAR.";
RL BMC Mol. Biol. 11:3-3(2010).
RN [26]
RP FUNCTION.
RX PubMed=20829347; DOI=10.1074/jbc.m110.136259;
RA Park S.H., Choi H.J., Yang H., Do K.H., Kim J., Lee D.W., Moon Y.;
RT "Endoplasmic reticulum stress-activated C/EBP homologous protein enhances
RT nuclear factor-kappaB signals via repression of peroxisome proliferator-
RT activated receptor gamma.";
RL J. Biol. Chem. 285:35330-35339(2010).
RN [27]
RP INTERACTION WITH ASXL1 AND ASXL2.
RX PubMed=21047783; DOI=10.1074/jbc.m110.177816;
RA Park U.H., Yoon S.K., Park T., Kim E.J., Um S.J.;
RT "Additional sex comb-like (ASXL) proteins 1 and 2 play opposite roles in
RT adipogenesis via reciprocal regulation of peroxisome proliferator-activated
RT receptor {gamma}.";
RL J. Biol. Chem. 286:1354-1363(2011).
RN [28]
RP INTERACTION WITH ACTN4.
RX PubMed=22351778; DOI=10.1074/jbc.m112.345421;
RA Khurana S., Chakraborty S., Lam M., Liu Y., Su Y.T., Zhao X., Saleem M.A.,
RA Mathieson P.W., Bruggeman L.A., Kao H.Y.;
RT "Familial focal segmental glomerulosclerosis (FSGS)-linked alpha-actinin 4
RT (ACTN4) protein mutants lose ability to activate transcription by nuclear
RT hormone receptors.";
RL J. Biol. Chem. 287:12027-12035(2012).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [30]
RP FUNCTION, INTERACTION WITH HELZ2 AND THRAP3, AND SUBCELLULAR LOCATION.
RX PubMed=23525231; DOI=10.1210/me.2012-1332;
RA Katano-Toki A., Satoh T., Tomaru T., Yoshino S., Ishizuka T., Ishii S.,
RA Ozawa A., Shibusawa N., Tsuchiya T., Saito T., Shimizu H., Hashimoto K.,
RA Okada S., Yamada M., Mori M.;
RT "THRAP3 interacts with HELZ2 and plays a novel role in adipocyte
RT differentiation.";
RL Mol. Endocrinol. 27:769-780(2013).
RN [31]
RP FUNCTION (MICROBIAL INFECTION), AND INDUCTION (MICROBIAL INFECTION).
RC TISSUE=Macrophage;
RX PubMed=25504154; DOI=10.3892/mmr.2014.3070;
RA Liu L., Liu J., Niu G., Xu Q., Chen Q.;
RT "Mycobacterium tuberculosis 19-kDa lipoprotein induces Toll-like receptor
RT 2-dependent peroxisome proliferator-activated receptor gamma expression and
RT promotes inflammatory responses in human macrophages.";
RL Mol. Med. Report. 11:2921-2926(2015).
RN [32]
RP 9AATAD MOTIF.
RX PubMed=30468856; DOI=10.1016/j.jsbmb.2018.11.008;
RA Piskacek M., Havelka M., Jendruchova K., Knight A.;
RT "Nuclear hormone receptors: Ancient 9aaTAD and evolutionally gained NCoA
RT activation pathways.";
RL J. Steroid Biochem. Mol. Biol. 187:118-123(2019).
RN [33] {ECO:0007744|PDB:3PRG}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 232-505.
RX PubMed=9813012; DOI=10.1074/jbc.273.47.31108;
RA Uppenberg J., Svensson C., Jaki M., Bertilsson G., Jendeberg L.,
RA Berkenstam A.;
RT "Crystal structure of the ligand binding domain of the human nuclear
RT receptor PPARgamma.";
RL J. Biol. Chem. 273:31108-31112(1998).
RN [34] {ECO:0007744|PDB:2PRG}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 235-504 IN COMPLEXES WITH THE
RP SYNTHETIC AGONIST ROSIGLITAZONE AND NCOA1, AND SUBUNIT.
RX PubMed=9744270; DOI=10.1038/25931;
RA Nolte R.T., Wisely G.B., Westin S., Cobb J.E., Lambert M.H., Kurokawa R.,
RA Rosenfeld M.G., Willson T.M., Glass C.K., Milburn M.V.;
RT "Ligand binding and co-activator assembly of the peroxisome proliferator-
RT activated receptor-gamma.";
RL Nature 395:137-143(1998).
RN [35] {ECO:0007744|PDB:1FM6, ECO:0007744|PDB:1FM9}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH RXRA AND SYNTHETIC
RP AGONISTS.
RX PubMed=10882139; DOI=10.1016/s1097-2765(00)80448-7;
RA Gampe R.T. Jr., Montana V.G., Lambert M.H., Miller A.B., Bledsoe R.K.,
RA Milburn M.V., Kliewer S.A., Willson T.M., Xu H.E.;
RT "Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the
RT molecular basis of heterodimerization among nuclear receptors.";
RL Mol. Cell 5:545-555(2000).
RN [36] {ECO:0007744|PDB:1K74}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 234-505 IN COMPLEXES WITH
RP SYNTHETIC AGONIST AND NCOA1.
RX PubMed=11698662; DOI=10.1073/pnas.241410198;
RA Xu H.E., Lambert M.H., Montana V.G., Plunket K.D., Moore L.B.,
RA Collins J.L., Oplinger J.A., Kliewer S.A., Gampe R.T. Jr., McKee D.D.,
RA Moore J.T., Willson T.M.;
RT "Structural determinants of ligand binding selectivity between the
RT peroxisome proliferator-activated receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13919-13924(2001).
RN [37] {ECO:0007744|PDB:1I7I}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 225-505 IN COMPLEX WITH SYNTHETIC
RP AGONIST.
RX PubMed=11587644; DOI=10.1016/s0969-2126(01)00634-7;
RA Cronet P., Petersen J.F.W., Folmer R., Blomberg N., Sjoeblom K.,
RA Karlsson U., Lindstedt E.-L., Bamberg K.;
RT "Structure of the PPARalpha and -gamma ligand binding domain in complex
RT with AZ 242; ligand selectivity and agonist activation in the PPAR
RT family.";
RL Structure 9:699-706(2001).
RN [38] {ECO:0007744|PDB:1NYX}
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 230-505 IN COMPLEX WITH SYNTHETIC
RP AGONIST.
RX PubMed=12672231; DOI=10.1021/jm021027r;
RA Ebdrup S., Pettersson I., Rasmussen H.B., Deussen H.-J., Frost Jensen A.,
RA Mortensen S.B., Fleckner J., Pridal L., Nygaard L., Sauerberg P.;
RT "Synthesis and biological and structural characterization of the dual-
RT acting peroxisome proliferator-activated receptor alpha/gamma agonist
RT ragaglitazar.";
RL J. Med. Chem. 46:1306-1317(2003).
RN [39] {ECO:0007744|PDB:1WM0}
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 232-505 IN COMPLEX WITH NCOA2 AND
RP SYNTHETIC AGONIST.
RX PubMed=15258145; DOI=10.1074/jbc.m401552200;
RA Oestberg T., Svensson S., Selen G., Uppenberg J., Thor M., Sundbom M.,
RA Sydow-Baeckman M., Gustavsson A.-L., Jendeberg L.;
RT "A new class of peroxisome proliferator-activated receptor agonists with a
RT novel binding epitope shows antidiabetic effects.";
RL J. Biol. Chem. 279:41124-41130(2004).
RN [40] {ECO:0007744|PDB:1RDT}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 235-505 IN COMPLEX WITH RXRA;
RP NCOA1 AND SYNTHETIC AGONIST.
RX PubMed=15056000; DOI=10.1021/jm030565g;
RA Haffner C.D., Lenhard J.M., Miller A.B., McDougald D.L., Dwornik K.,
RA Ittoop O.R., Gampe R.T. Jr., Xu H.E., Blanchard S., Montana V.G.,
RA Consler T.G., Bledsoe R.K., Ayscue A., Croom D.;
RT "Structure-based design of potent retinoid X receptor alpha agonists.";
RL J. Med. Chem. 47:2010-2029(2004).
RN [41] {ECO:0007744|PDB:1ZEO}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 231-505 IN COMPLEX WITH SYNTHETIC
RP AGONIST.
RX PubMed=15974597; DOI=10.1021/jm0502135;
RA Shi G.Q., Dropinski J.F., McKeever B.M., Xu S., Becker J.W., Berger J.P.,
RA MacNaul K.L., Elbrecht A., Zhou G., Doebber T.W., Wang P., Chao Y.-S.,
RA Forrest M., Heck J.V., Moller D.E., Jones A.B.;
RT "Design and synthesis of alpha-aryloxyphenylacetic acid derivatives: a
RT novel class of PPARalpha/gamma dual agonists with potent antihyperglycemic
RT and lipid modulating activity.";
RL J. Med. Chem. 48:4457-4468(2005).
RN [42] {ECO:0007744|PDB:1ZGY}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 234-505 IN COMPLEX WITH SYNTHETIC
RP AGONIST AND NR0B2.
RX PubMed=15976031; DOI=10.1073/pnas.0501204102;
RA Li Y., Choi M., Suino K., Kovach A., Daugherty J., Kliewer S.A., Xu H.E.;
RT "Structural and biochemical basis for selective repression of the orphan
RT nuclear receptor liver receptor homolog 1 by small heterodimer partner.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9505-9510(2005).
RN [43] {ECO:0007744|PDB:2HFP}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 234-505 IN COMPLEX WITH SYNTHETIC
RP AGONIST AND NCOA1.
RX PubMed=16919947; DOI=10.1016/j.bmcl.2006.08.003;
RA Hopkins C.R., O'neil S.V., Laufersweiler M.C., Wang Y., Pokross M.,
RA Mekel M., Evdokimov A., Walter R., Kontoyianni M., Petrey M.E.,
RA Sabatakos G., Roesgen J.T., Richardson E., Demuth T.P. Jr.;
RT "Design and synthesis of novel N-sulfonyl-2-indole carboxamides as potent
RT PPAR-gamma binding agents with potential application to the treatment of
RT osteoporosis.";
RL Bioorg. Med. Chem. Lett. 16:5659-5663(2006).
RN [44] {ECO:0007744|PDB:2F4B}
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 235-505 IN COMPLEX WITH SYNTHETIC
RP AGONIST.
RX PubMed=16451087; DOI=10.1021/jm0510373;
RA Mahindroo N., Wang C.-C., Liao C.-C., Huang C.-F., Lu I.-L., Lien T.-W.,
RA Peng Y.-H., Huang W.-J., Lin Y.-T., Hsu M.-C., Lin C.-H., Tsai C.-H.,
RA Hsu J.-T., Chen X., Lyu P.-C., Chao Y.-S., Wu S.-Y., Hsieh H.-P.;
RT "Indol-1-yl acetic acids as peroxisome proliferator-activated receptor
RT agonists: design, synthesis, structural biology, and molecular docking
RT studies.";
RL J. Med. Chem. 49:1212-1216(2006).
RN [45] {ECO:0007744|PDB:2G0G, ECO:0007744|PDB:2G0H}
RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 235-505 IN COMPLEX WITH SYNTHETIC
RP AGONIST.
RX PubMed=16640330; DOI=10.1021/jm051129s;
RA Lu I.-L., Huang C.-F., Peng Y.-H., Lin Y.-T., Hsieh H.-P., Chen C.-T.,
RA Lien T.-W., Lee H.-J., Mahindroo N., Prakash E., Yueh A., Chen H.-Y.,
RA Goparaju C.M.V., Chen X., Liao C.-C., Chao Y.-S., Hsu J.-T., Wu S.-Y.;
RT "Structure-based drug design of a novel family of PPARgamma partial
RT agonists: virtual screening, X-ray crystallography, and in vitro/in vivo
RT biological activities.";
RL J. Med. Chem. 49:2703-2712(2006).
RN [46]
RP VARIANT ALA-12.
RX PubMed=9425261; DOI=10.1006/bbrc.1997.7798;
RA Yen C.-J., Beamer B.A., Negri C., Silver K., Brown K.A., Yarnall D.P.,
RA Burns D.K., Roth J., Shuldiner A.R.;
RT "Molecular scanning of the human peroxisome proliferator activated receptor
RT gamma (hPPAR-gamma) gene in diabetic Caucasians: identification of a
RT pro12ala PPAR-gamma-2 missense mutation.";
RL Biochem. Biophys. Res. Commun. 241:270-274(1997).
RN [47]
RP VARIANT OBESITY GLN-113.
RX PubMed=9753710; DOI=10.1056/nejm199810013391403;
RA Ristow M., Muller-Wieland D., Pfeiffer A., Krone W., Kahn C.R.;
RT "Obesity associated with a mutation in a genetic regulator of adipocyte
RT differentiation.";
RL N. Engl. J. Med. 339:953-959(1998).
RN [48]
RP INVOLVEMENT IN BMIQ1, AND VARIANT ALA-12.
RX PubMed=9806549; DOI=10.1038/3099;
RA Deeb S.S., Fajas L., Nemoto M., Pihlajamaeki J., Mykkaenen L., Kuusisto J.,
RA Laakso M., Fujimoto W., Auwerx J.;
RT "A Pro12Ala substitution in PPARgamma2 associated with decreased receptor
RT activity, lower body mass index and improved insulin sensitivity.";
RL Nat. Genet. 20:284-287(1998).
RN [49]
RP VARIANT ALA-12.
RX PubMed=10407229; DOI=10.1530/eje.0.1410090;
RA Hamann A., Munzberg H., Buttron P., Busing B., Hinney A., Mayer H.,
RA Siegfried W., Hebebrand J., Greten H.;
RT "Missense variants in the human peroxisome proliferator-activated receptor-
RT gamma2 gene in lean and obese subjects.";
RL Eur. J. Endocrinol. 141:90-92(1999).
RN [50]
RP INVOLVEMENT IN BMIQ1, AND VARIANT ALA-12.
RX PubMed=10523018; DOI=10.1210/jcem.84.10.6061;
RA Valve R., Sivenius K., Miettinen R., Pihlajamaeki J., Rissanen A.,
RA Deeb S.S., Auwerx J., Uusitupa M., Laakso M.;
RT "Two polymorphisms in the peroxisome proliferator-activated receptor-gamma
RT gene are associated with severe overweight among obese women.";
RL J. Clin. Endocrinol. Metab. 84:3708-3712(1999).
RN [51]
RP VARIANTS COLON CANCER PRO-314 AND HIS-316, AND VARIANT ALA-12.
RX PubMed=10394368; DOI=10.1016/s1097-2765(01)80012-5;
RA Sarraf P., Mueller E., Smith W.M., Wright H.M., Kum J.B., Aaltonen L.A.,
RA de la Chapelle A., Spiegelman B.M., Eng C.;
RT "Loss-of-function mutations in PPAR-gamma associated with human colon
RT cancer.";
RL Mol. Cell 3:799-804(1999).
RN [52]
RP VARIANTS DIABETES MET-318 AND LEU-495.
RX PubMed=10622252; DOI=10.1038/47254;
RA Barroso I., Gurnell M., Crowley V.E.F., Agostini M., Schwabel J.W.,
RA Soos M.A., Masien G.L., Williams T.D.M., Lewis H., Schafer A.J.,
RA Chatterjee V.K.K., O'Rahilly S.;
RT "Dominant negative mutations in human PPAR-gamma associated with severe
RT insulin resistance, diabetes mellitus and hypertension.";
RL Nature 402:880-883(1999).
RN [53]
RP VARIANT FPLD3 LEU-388.
RX PubMed=12453919; DOI=10.2337/diabetes.51.12.3586;
RA Hegele R.A., Cao H., Frankowski C., Mathews S.T., Leff T.;
RT "PPARG F388L, a transactivation-deficient mutant, in familial partial
RT lipodystrophy.";
RL Diabetes 51:3586-3590(2002).
RN [54]
RP VARIANT FPLD3 CYS-425.
RX PubMed=11788685; DOI=10.1210/jcem.87.1.8290;
RA Agarwal A.K., Garg A.;
RT "A novel heterozygous mutation in peroxisome proliferator-activated
RT receptor-gamma gene in a patient with familial partial lipodystrophy.";
RL J. Clin. Endocrinol. Metab. 87:408-411(2002).
RN [55]
RP ASSOCIATION OF VARIANT ALA-12 WITH BMI.
RX PubMed=14569127; DOI=10.1136/jmg.40.10.773;
RA Masud S., Ye S.;
RT "Effect of the peroxisome proliferator activated receptor-gamma gene
RT Pro12Ala variant on body mass index: a meta-analysis.";
RL J. Med. Genet. 40:773-780(2003).
RN [56]
RP ASSOCIATION OF VARIANT ALA-12 WITH CIMT.
RX PubMed=15356014; DOI=10.1210/jc.2003-032120;
RA Temelkova-Kurktschiev T., Hanefeld M., Chinetti G., Zawadzki C., Haulon S.,
RA Kubaszek A., Koehler C., Leonhardt W., Staels B., Laakso M.;
RT "Ala12Ala genotype of the peroxisome proliferator-activated receptor gamma2
RT protects against atherosclerosis.";
RL J. Clin. Endocrinol. Metab. 89:4238-4242(2004).
RN [57]
RP VARIANT ALA-12.
RX PubMed=15562396; DOI=10.1016/j.metabol.2004.06.019;
RA Kim K.S., Choi S.M., Shin S.U., Yang H.S., Yoon Y.;
RT "Effects of peroxisome proliferator-activated receptor-gamma 2 Pro12Ala
RT polymorphism on body fat distribution in female Korean subjects.";
RL Metabolism 53:1538-1543(2004).
CC -!- FUNCTION: Nuclear receptor that binds peroxisome proliferators such as
CC hypolipidemic drugs and fatty acids. Once activated by a ligand, the
CC nuclear receptor binds to DNA specific PPAR response elements (PPRE)
CC and modulates the transcription of its target genes, such as acyl-CoA
CC oxidase. It therefore controls the peroxisomal beta-oxidation pathway
CC of fatty acids. Key regulator of adipocyte differentiation and glucose
CC homeostasis. ARF6 acts as a key regulator of the tissue-specific
CC adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut
CC homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory
CC responses. Plays a role in the regulation of cardiovascular circadian
CC rhythms by regulating the transcription of ARNTL/BMAL1 in the blood
CC vessels (By similarity). {ECO:0000250|UniProtKB:P37238,
CC ECO:0000269|PubMed:16150867, ECO:0000269|PubMed:20829347,
CC ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:9065481}.
CC -!- FUNCTION: (Microbial infection) Upon treatment with M.tuberculosis or
CC its lipoprotein LpqH, phosphorylation of MAPK p38 and IL-6 production
CC are modulated, probably via this protein.
CC {ECO:0000269|PubMed:25504154}.
CC -!- ACTIVITY REGULATION: PDPK1 activates its transcriptional activity
CC independently of its kinase activity. {ECO:0000269|PubMed:16150867}.
CC -!- SUBUNIT: Interacts with FOXO1 (acetylated form) (By similarity).
CC Heterodimer with other nuclear receptors, such as RXRA. The heterodimer
CC with the retinoic acid receptor RXRA is called adipocyte-specific
CC transcription factor ARF6. Interacts with NCOA6 coactivator, leading to
CC a strong increase in transcription of target genes. Interacts with
CC coactivator PPARBP, leading to a mild increase in transcription of
CC target genes. Interacts with NOCA7 in a ligand-inducible manner.
CC Interacts with NCOA1 and NCOA2 LXXLL motifs. Interacts with ASXL1,
CC ASXL2, DNTTIP2, FAM120B, MAP2K1/MEK1, NR0B2, PDPK1, PRDM16, PRMT2 and
CC TGFB1I1. Interacts (when activated by agonist) with PPP5C. Interacts
CC with HELZ2 and THRAP3; the interaction stimulates the transcriptional
CC activity of PPARG. Interacts with PER2, the interaction is ligand
CC dependent and blocks PPARG recruitment to target promoters. Interacts
CC with NOCT. Interacts with ACTN4. Interacts (when in the liganded
CC conformation) with GPS2 (By similarity). Interacts with CRY1 and CRY2
CC in a ligand-dependent manner (By similarity). In the absence of
CC hormonal ligand, interacts with TACC1 (PubMed:20078863).
CC {ECO:0000250|UniProtKB:P37238, ECO:0000269|PubMed:10681503,
CC ECO:0000269|PubMed:11587644, ECO:0000269|PubMed:11971969,
CC ECO:0000269|PubMed:12039952, ECO:0000269|PubMed:12672231,
CC ECO:0000269|PubMed:15047147, ECO:0000269|PubMed:15056000,
CC ECO:0000269|PubMed:15258145, ECO:0000269|PubMed:15687259,
CC ECO:0000269|PubMed:15974597, ECO:0000269|PubMed:15976031,
CC ECO:0000269|PubMed:16150867, ECO:0000269|PubMed:16239304,
CC ECO:0000269|PubMed:16451087, ECO:0000269|PubMed:16640330,
CC ECO:0000269|PubMed:16919947, ECO:0000269|PubMed:17101779,
CC ECO:0000269|PubMed:20078863, ECO:0000269|PubMed:21047783,
CC ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:23525231,
CC ECO:0000269|PubMed:9744270}.
CC -!- INTERACTION:
CC P37231; Q8NFM4: ADCY4; NbExp=3; IntAct=EBI-781384, EBI-2838710;
CC P37231; P10909: CLU; NbExp=3; IntAct=EBI-781384, EBI-1104674;
CC P37231; O60869: EDF1; NbExp=4; IntAct=EBI-781384, EBI-781301;
CC P37231; Q9BWX5: GATA5; NbExp=3; IntAct=EBI-781384, EBI-12132270;
CC P37231; P42858: HTT; NbExp=16; IntAct=EBI-781384, EBI-466029;
CC P37231; P45984: MAPK9; NbExp=3; IntAct=EBI-781384, EBI-713568;
CC P37231; O75376: NCOR1; NbExp=2; IntAct=EBI-781384, EBI-347233;
CC P37231; P55055-1: NR1H2; NbExp=2; IntAct=EBI-781384, EBI-21458417;
CC P37231; Q13133: NR1H3; NbExp=2; IntAct=EBI-781384, EBI-781356;
CC P37231; P37231: PPARG; NbExp=2; IntAct=EBI-781384, EBI-781384;
CC P37231; Q9UBK2: PPARGC1A; NbExp=2; IntAct=EBI-781384, EBI-765486;
CC P37231; P10276: RARA; NbExp=3; IntAct=EBI-781384, EBI-413374;
CC P37231; P19793: RXRA; NbExp=3; IntAct=EBI-781384, EBI-78598;
CC P37231; P28702: RXRB; NbExp=5; IntAct=EBI-781384, EBI-748576;
CC P37231; Q96EB6: SIRT1; NbExp=5; IntAct=EBI-781384, EBI-1802965;
CC P37231; Q6STE5-1: SMARCD3; NbExp=3; IntAct=EBI-781384, EBI-488506;
CC P37231; Q6STE5-2: SMARCD3; NbExp=3; IntAct=EBI-781384, EBI-488511;
CC P37231-1; P37231-1: PPARG; NbExp=2; IntAct=EBI-15664691, EBI-15664691;
CC P37231-1; P19793: RXRA; NbExp=6; IntAct=EBI-15664691, EBI-78598;
CC P37231-2; Q00535: CDK5; NbExp=2; IntAct=EBI-781416, EBI-1041567;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Redistributed from the
CC nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT
CC enhances its nuclear translocation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=2;
CC IsoId=P37231-1; Sequence=Displayed;
CC Name=1; Synonyms=PPARgamma1(wt);
CC IsoId=P37231-2; Sequence=VSP_003645;
CC Name=3; Synonyms=PPARgamma1(tr);
CC IsoId=P37231-3; Sequence=VSP_003645, VSP_043906, VSP_043907;
CC -!- TISSUE SPECIFICITY: Highest expression in adipose tissue. Lower in
CC skeletal muscle, spleen, heart and liver. Also detectable in placenta,
CC lung and ovary. {ECO:0000269|PubMed:9065481}.
CC -!- INDUCTION: (Microbial infection) Expression increases when incubated
CC with M.tuberculosis or its lipoprotein LpqH; induction is TLR2-
CC dependent (at protein level). {ECO:0000269|PubMed:25504154}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000305|PubMed:30468856}.
CC -!- PTM: O-GlcNAcylation at Thr-84 reduces transcriptional activity in
CC adipocytes. {ECO:0000250|UniProtKB:P37238}.
CC -!- PTM: Phosphorylated in basal conditions and dephosphorylated when
CC treated with the ligand. May be dephosphorylated by PPP5C. The
CC phosphorylated form may be inactive and dephosphorylation at Ser-112
CC induces adipogenic activity (By similarity). {ECO:0000250}.
CC -!- POLYMORPHISM: Genetic variations in PPARG define the body mass index
CC quantitative trait locus 1 (BMIQ1) [MIM:606641]. The body max index
CC (BMI) reflects the amount of fat, lean mass, and body build.
CC {ECO:0000269|PubMed:10523018, ECO:0000269|PubMed:14569127}.
CC -!- POLYMORPHISM: Genetic variations in PPARG influence the carotid intimal
CC medial thickness (CIMT) [MIM:609338]. CIMT is a measure of
CC atherosclerosis that is independently associated with traditional
CC atherosclerotic cardiovascular disease risk factors and coronary
CC atherosclerotic burden. 35 to 45% of the variability in multivariable-
CC adjusted CIMT is explained by genetic factors.
CC {ECO:0000269|PubMed:15356014}.
CC -!- DISEASE: Note=Defects in PPARG can lead to type 2 insulin-resistant
CC diabetes and hyptertension. PPARG mutations may be associated with
CC colon cancer. {ECO:0000269|PubMed:10394368}.
CC -!- DISEASE: Obesity (OBESITY) [MIM:601665]: A condition characterized by
CC an increase of body weight beyond the limitation of skeletal and
CC physical requirements, as the result of excessive accumulation of body
CC fat. {ECO:0000269|PubMed:9753710}. Note=Disease susceptibility may be
CC associated with variants affecting the gene represented in this entry.
CC -!- DISEASE: Lipodystrophy, familial partial, 3 (FPLD3) [MIM:604367]: A
CC form of lipodystrophy characterized by marked loss of subcutaneous fat
CC from the extremities. Facial adipose tissue may be increased, decreased
CC or normal. Affected individuals show an increased preponderance of
CC insulin resistance, diabetes mellitus and dyslipidemia.
CC {ECO:0000269|PubMed:11788685, ECO:0000269|PubMed:12453919}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Glioma 1 (GLM1) [MIM:137800]: Gliomas are benign or malignant
CC central nervous system neoplasms derived from glial cells. They
CC comprise astrocytomas and glioblastoma multiforme that are derived from
CC astrocytes, oligodendrogliomas derived from oligodendrocytes and
CC ependymomas derived from ependymocytes. {ECO:0000269|PubMed:10851250}.
CC Note=Disease susceptibility may be associated with variants affecting
CC the gene represented in this entry. Polymorphic PPARG alleles have been
CC found to be significantly over-represented among a cohort of American
CC patients with sporadic glioblastoma multiforme suggesting a possible
CC contribution to disease susceptibility.
CC -!- MISCELLANEOUS: [Isoform 3]: Exhibits dominant negative activity over
CC isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN38992.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA23354.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF83270.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA62153.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PPARGID383ch3p25.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Peroxisome proliferator-activated
CC receptor entry;
CC URL="https://en.wikipedia.org/wiki/Peroxisome_proliferator-activated_receptor";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/pparg/";
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DR EMBL; U79012; AAC51248.1; -; mRNA.
DR EMBL; U63415; AAB04028.1; -; mRNA.
DR EMBL; D83233; BAA18949.1; -; mRNA.
DR EMBL; L40904; AAA80314.2; -; mRNA.
DR EMBL; AB005526; BAA23354.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X90563; CAA62152.1; -; mRNA.
DR EMBL; X90563; CAA62153.1; ALT_INIT; mRNA.
DR EMBL; DQ356894; ABC97372.1; -; mRNA.
DR EMBL; BT007281; AAP35945.1; -; mRNA.
DR EMBL; AK290581; BAF83270.1; ALT_INIT; mRNA.
DR EMBL; AB451337; BAG70151.1; -; mRNA.
DR EMBL; AB451486; BAG70300.1; -; mRNA.
DR EMBL; AY157024; AAN38992.2; ALT_INIT; Genomic_DNA.
DR EMBL; AC090947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64124.1; -; Genomic_DNA.
DR EMBL; BC006811; AAH06811.1; -; mRNA.
DR CCDS; CCDS2609.1; -. [P37231-1]
DR PIR; JC4859; JC4859.
DR PIR; PC4290; PC4290.
DR PIR; PC4429; PC4429.
DR RefSeq; NP_005028.4; NM_005037.5.
DR RefSeq; NP_056953.2; NM_015869.4. [P37231-1]
DR RefSeq; NP_619725.2; NM_138711.3.
DR RefSeq; NP_619726.2; NM_138712.3.
DR RefSeq; XP_011532143.1; XM_011533841.2.
DR PDB; 1FM6; X-ray; 2.10 A; D/X=234-505.
DR PDB; 1FM9; X-ray; 2.10 A; D=234-505.
DR PDB; 1I7I; X-ray; 2.35 A; A/B=225-505.
DR PDB; 1K74; X-ray; 2.30 A; D=234-505.
DR PDB; 1KNU; X-ray; 2.50 A; A/B=232-505.
DR PDB; 1NYX; X-ray; 2.65 A; A/B=230-505.
DR PDB; 1PRG; X-ray; 2.20 A; A/B=235-504.
DR PDB; 1RDT; X-ray; 2.40 A; D=235-505.
DR PDB; 1WM0; X-ray; 2.90 A; X=232-505.
DR PDB; 1ZEO; X-ray; 2.50 A; A/B=231-505.
DR PDB; 1ZGY; X-ray; 1.80 A; A=234-505.
DR PDB; 2ATH; X-ray; 2.28 A; A/B=235-505.
DR PDB; 2F4B; X-ray; 2.07 A; A/B=235-505.
DR PDB; 2FVJ; X-ray; 1.99 A; A=235-505.
DR PDB; 2G0G; X-ray; 2.54 A; A/B=235-505.
DR PDB; 2G0H; X-ray; 2.30 A; A/B=235-505.
DR PDB; 2GTK; X-ray; 2.10 A; A=235-505.
DR PDB; 2HFP; X-ray; 2.00 A; A=234-505.
DR PDB; 2HWQ; X-ray; 1.97 A; A/B=235-505.
DR PDB; 2HWR; X-ray; 2.34 A; A/B=235-505.
DR PDB; 2I4J; X-ray; 2.10 A; A/B=223-504.
DR PDB; 2I4P; X-ray; 2.10 A; A/B=223-504.
DR PDB; 2I4Z; X-ray; 2.25 A; A/B=223-504.
DR PDB; 2OM9; X-ray; 2.80 A; A/B/C/D=232-505.
DR PDB; 2P4Y; X-ray; 2.25 A; A/B=231-505.
DR PDB; 2POB; X-ray; 2.30 A; A/B=234-505.
DR PDB; 2PRG; X-ray; 2.30 A; A/B=235-505.
DR PDB; 2Q59; X-ray; 2.20 A; A/B=233-505.
DR PDB; 2Q5P; X-ray; 2.30 A; A/B=233-505.
DR PDB; 2Q5S; X-ray; 2.05 A; A/B=233-505.
DR PDB; 2Q61; X-ray; 2.20 A; A/B=233-505.
DR PDB; 2Q6R; X-ray; 2.41 A; A/B=233-505.
DR PDB; 2Q6S; X-ray; 2.40 A; A/B=233-505.
DR PDB; 2Q8S; X-ray; 2.30 A; A/B=235-505.
DR PDB; 2QMV; NMR; -; A=235-504.
DR PDB; 2VSR; X-ray; 2.05 A; A/B=232-505.
DR PDB; 2VST; X-ray; 2.35 A; A/B=232-505.
DR PDB; 2VV0; X-ray; 2.55 A; A/B=232-505.
DR PDB; 2VV1; X-ray; 2.20 A; A/B=232-505.
DR PDB; 2VV2; X-ray; 2.75 A; A/B=232-505.
DR PDB; 2VV3; X-ray; 2.85 A; A/B=232-505.
DR PDB; 2VV4; X-ray; 2.35 A; A/B=232-505.
DR PDB; 2XKW; X-ray; 2.02 A; A/B=232-505.
DR PDB; 2YFE; X-ray; 2.00 A; A/B=223-505.
DR PDB; 2ZK0; X-ray; 2.36 A; A/B=223-504.
DR PDB; 2ZK1; X-ray; 2.61 A; A/B=223-504.
DR PDB; 2ZK2; X-ray; 2.26 A; A/B=223-504.
DR PDB; 2ZK3; X-ray; 2.58 A; A/B=223-504.
DR PDB; 2ZK4; X-ray; 2.57 A; A/B=223-504.
DR PDB; 2ZK5; X-ray; 2.45 A; A/B=223-504.
DR PDB; 2ZK6; X-ray; 2.41 A; A/B=223-504.
DR PDB; 2ZNO; X-ray; 2.40 A; A/B=223-504.
DR PDB; 2ZVT; X-ray; 1.90 A; A/B=223-504.
DR PDB; 3ADS; X-ray; 2.25 A; A/B=223-505.
DR PDB; 3ADT; X-ray; 2.70 A; A/B=223-505.
DR PDB; 3ADU; X-ray; 2.77 A; A/B=223-505.
DR PDB; 3ADV; X-ray; 2.27 A; A/B=223-505.
DR PDB; 3ADW; X-ray; 2.07 A; A/B=223-505.
DR PDB; 3ADX; X-ray; 1.95 A; A/B=223-505.
DR PDB; 3AN3; X-ray; 2.30 A; A/B=223-504.
DR PDB; 3AN4; X-ray; 2.30 A; A/B=223-504.
DR PDB; 3B0Q; X-ray; 2.10 A; A/B=231-504.
DR PDB; 3B0R; X-ray; 2.15 A; A/B=231-504.
DR PDB; 3B1M; X-ray; 1.60 A; A=234-505.
DR PDB; 3B3K; X-ray; 2.60 A; A/B=223-504.
DR PDB; 3BC5; X-ray; 2.27 A; A=231-505.
DR PDB; 3CDP; X-ray; 2.80 A; A/B=223-504.
DR PDB; 3CDS; X-ray; 2.65 A; A/B=223-504.
DR PDB; 3CS8; X-ray; 2.30 A; A=234-504.
DR PDB; 3CWD; X-ray; 2.40 A; A/B=236-505.
DR PDB; 3D6D; X-ray; 2.40 A; A/B=223-504.
DR PDB; 3DZU; X-ray; 3.20 A; D=102-505.
DR PDB; 3DZY; X-ray; 3.10 A; D=102-505.
DR PDB; 3E00; X-ray; 3.10 A; D=102-505.
DR PDB; 3ET0; X-ray; 2.40 A; A/B=235-505.
DR PDB; 3ET3; X-ray; 1.95 A; A=235-505.
DR PDB; 3FEJ; X-ray; 2.01 A; A=235-505.
DR PDB; 3FUR; X-ray; 2.30 A; A=234-505.
DR PDB; 3G9E; X-ray; 2.30 A; A=235-505.
DR PDB; 3GBK; X-ray; 2.30 A; A/B=235-505.
DR PDB; 3H0A; X-ray; 2.10 A; D=234-505.
DR PDB; 3HO0; X-ray; 2.60 A; A/B=223-504.
DR PDB; 3HOD; X-ray; 2.10 A; A/B=223-504.
DR PDB; 3IA6; X-ray; 2.31 A; A/B=235-505.
DR PDB; 3K8S; X-ray; 2.55 A; A/B=234-505.
DR PDB; 3KMG; X-ray; 2.10 A; A/D=234-505.
DR PDB; 3LMP; X-ray; 1.90 A; A=234-505.
DR PDB; 3NOA; X-ray; 1.98 A; A/B=235-505.
DR PDB; 3OSI; X-ray; 2.70 A; A/B=224-504.
DR PDB; 3OSW; X-ray; 2.55 A; A/B=224-504.
DR PDB; 3PBA; X-ray; 2.30 A; A/B=224-505.
DR PDB; 3PO9; X-ray; 2.35 A; A/B=224-505.
DR PDB; 3PRG; X-ray; 2.90 A; A=232-505.
DR PDB; 3QT0; X-ray; 2.50 A; A=235-505.
DR PDB; 3R5N; X-ray; 2.00 A; A=232-505.
DR PDB; 3R8A; X-ray; 2.41 A; A/B=235-505.
DR PDB; 3R8I; X-ray; 2.30 A; A/B=223-505.
DR PDB; 3S9S; X-ray; 2.55 A; A=234-505.
DR PDB; 3SZ1; X-ray; 2.30 A; A/B=232-505.
DR PDB; 3T03; X-ray; 2.10 A; A/B=234-505.
DR PDB; 3TY0; X-ray; 2.00 A; A/B=231-505.
DR PDB; 3U9Q; X-ray; 1.52 A; A=236-504.
DR PDB; 3V9T; X-ray; 1.65 A; A=234-505.
DR PDB; 3V9V; X-ray; 1.60 A; A=234-505.
DR PDB; 3V9Y; X-ray; 2.10 A; A=234-505.
DR PDB; 3VJH; X-ray; 2.22 A; A/B=223-504.
DR PDB; 3VJI; X-ray; 2.61 A; A/B=223-504.
DR PDB; 3VN2; X-ray; 2.18 A; A=225-505.
DR PDB; 3VSO; X-ray; 2.00 A; A/B=223-504.
DR PDB; 3VSP; X-ray; 2.40 A; A/B=223-504.
DR PDB; 3WJ4; X-ray; 1.95 A; A/B=235-505.
DR PDB; 3WJ5; X-ray; 1.89 A; A/B=235-505.
DR PDB; 3WMH; X-ray; 2.10 A; A/B=223-504.
DR PDB; 3X1H; X-ray; 2.30 A; A/B=232-505.
DR PDB; 3X1I; X-ray; 2.40 A; A/B=232-505.
DR PDB; 4A4V; X-ray; 2.00 A; A/B=223-505.
DR PDB; 4A4W; X-ray; 2.00 A; A/B=223-505.
DR PDB; 4CI5; X-ray; 1.77 A; A/B=234-505.
DR PDB; 4E4K; X-ray; 2.50 A; A/B=223-505.
DR PDB; 4E4Q; X-ray; 2.50 A; A/B=223-505.
DR PDB; 4EM9; X-ray; 2.10 A; A/B=235-505.
DR PDB; 4EMA; X-ray; 2.54 A; A/B=235-505.
DR PDB; 4F9M; X-ray; 1.90 A; A=234-505.
DR PDB; 4FGY; X-ray; 2.84 A; A=235-504.
DR PDB; 4HEE; X-ray; 2.50 A; X=235-505.
DR PDB; 4JAZ; X-ray; 2.85 A; A/B=223-505.
DR PDB; 4JL4; X-ray; 2.50 A; A/B=223-505.
DR PDB; 4L96; X-ray; 2.38 A; A=235-505.
DR PDB; 4L98; X-ray; 2.28 A; A/B=235-505.
DR PDB; 4O8F; X-ray; 2.60 A; A/B=223-505.
DR PDB; 4OJ4; X-ray; 2.30 A; A=232-505.
DR PDB; 4PRG; X-ray; 2.90 A; A/B/C/D=235-504.
DR PDB; 4PVU; X-ray; 2.60 A; A/B=223-505.
DR PDB; 4PWL; X-ray; 2.60 A; A/B=223-505.
DR PDB; 4R06; X-ray; 2.22 A; A/B=233-505.
DR PDB; 4R2U; X-ray; 2.30 A; A/D=231-505.
DR PDB; 4R6S; X-ray; 2.30 A; A/B=231-505.
DR PDB; 4XLD; X-ray; 2.45 A; A=231-505.
DR PDB; 4XTA; X-ray; 2.50 A; A/B=232-505.
DR PDB; 4XUH; X-ray; 2.22 A; A/B=232-505.
DR PDB; 4XUM; X-ray; 2.40 A; A/B=232-505.
DR PDB; 4Y29; X-ray; 1.98 A; A=236-504.
DR PDB; 4YT1; X-ray; 2.20 A; A/B=223-504.
DR PDB; 5AZV; X-ray; 2.70 A; A/B=232-505.
DR PDB; 5DSH; X-ray; 2.95 A; A=223-505.
DR PDB; 5DV3; X-ray; 2.75 A; A=223-505.
DR PDB; 5DV6; X-ray; 2.80 A; A=223-505.
DR PDB; 5DV8; X-ray; 2.75 A; A=223-505.
DR PDB; 5DVC; X-ray; 2.30 A; A=223-505.
DR PDB; 5DWL; X-ray; 2.20 A; A=223-505.
DR PDB; 5F9B; X-ray; 2.25 A; A/B=223-505.
DR PDB; 5GTN; X-ray; 1.85 A; A=223-505.
DR PDB; 5GTO; X-ray; 2.10 A; A=223-505.
DR PDB; 5GTP; X-ray; 2.35 A; A=223-505.
DR PDB; 5HZC; X-ray; 2.00 A; A/B=223-505.
DR PDB; 5JI0; X-ray; 1.98 A; D=234-505.
DR PDB; 5LSG; X-ray; 2.00 A; A/B=223-505.
DR PDB; 5TTO; X-ray; 2.25 A; A/B=233-505.
DR PDB; 5TWO; X-ray; 1.93 A; A=234-505.
DR PDB; 5U5L; X-ray; 2.55 A; A/B=233-505.
DR PDB; 5UGM; X-ray; 2.10 A; A/B=235-505.
DR PDB; 5WQX; X-ray; 2.29 A; A/B=232-505.
DR PDB; 5WR0; X-ray; 2.85 A; A/B=232-505.
DR PDB; 5WR1; X-ray; 2.34 A; A/B=232-505.
DR PDB; 5Y2O; X-ray; 1.80 A; A/B=235-505.
DR PDB; 5Y2T; X-ray; 1.70 A; A/B=235-505.
DR PDB; 5YCN; X-ray; 2.15 A; A=223-505.
DR PDB; 5YCP; X-ray; 2.00 A; A=223-505.
DR PDB; 5Z5S; X-ray; 1.80 A; A=234-505.
DR PDB; 5Z6S; X-ray; 1.80 A; A=234-505.
DR PDB; 6AD9; X-ray; 2.20 A; A=223-505.
DR PDB; 6AN1; X-ray; 2.69 A; A/B=224-505.
DR PDB; 6AUG; X-ray; 2.73 A; A/B=231-505.
DR PDB; 6AVI; X-ray; 2.29 A; A/B=231-505.
DR PDB; 6C1I; X-ray; 2.26 A; A/B=231-504.
DR PDB; 6C5Q; X-ray; 2.40 A; A=235-505.
DR PDB; 6C5T; X-ray; 2.75 A; A=235-505.
DR PDB; 6D3E; X-ray; 2.40 A; A/B=235-504.
DR PDB; 6D8X; X-ray; 1.90 A; A=231-505.
DR PDB; 6D94; X-ray; 1.90 A; A=231-505.
DR PDB; 6DBH; X-ray; 2.60 A; A/B=231-505.
DR PDB; 6DCU; X-ray; 2.95 A; A/B=231-505.
DR PDB; 6DGL; X-ray; 1.95 A; A/B=231-505.
DR PDB; 6DGO; X-ray; 3.10 A; A/B=231-505.
DR PDB; 6DGP; X-ray; 3.10 A; A/B=231-505.
DR PDB; 6DGQ; X-ray; 2.45 A; A/B=231-505.
DR PDB; 6DGR; X-ray; 2.15 A; A/B=231-505.
DR PDB; 6DH9; X-ray; 2.70 A; A/B=235-505.
DR PDB; 6DHA; X-ray; 1.88 A; A/B=235-505.
DR PDB; 6E5A; X-ray; 2.40 A; A/B=233-505.
DR PDB; 6ENQ; X-ray; 2.20 A; A/B=224-505.
DR PDB; 6F2L; X-ray; 2.10 A; A/B=223-505.
DR PDB; 6FZF; X-ray; 1.95 A; A/B=231-505.
DR PDB; 6FZG; X-ray; 2.10 A; A=231-505.
DR PDB; 6FZJ; X-ray; 2.01 A; A/B=231-505.
DR PDB; 6FZP; X-ray; 2.30 A; A=231-505.
DR PDB; 6FZY; X-ray; 3.10 A; A/B=231-505.
DR PDB; 6ICJ; X-ray; 2.48 A; A=234-505.
DR PDB; 6IJR; X-ray; 2.85 A; A/C=223-505.
DR PDB; 6IJS; X-ray; 2.15 A; A=232-505.
DR PDB; 6ILQ; X-ray; 2.41 A; A=234-505.
DR PDB; 6IZM; X-ray; 1.80 A; A=234-505.
DR PDB; 6IZN; X-ray; 1.75 A; A=234-505.
DR PDB; 6JEY; X-ray; 2.20 A; A/B=232-505.
DR PDB; 6JF0; X-ray; 3.40 A; A/B=232-505.
DR PDB; 6JQ7; X-ray; 2.55 A; A=223-505.
DR PDB; 6K0T; X-ray; 1.84 A; A/C=223-505.
DR PDB; 6KTM; X-ray; 2.70 A; A=223-505.
DR PDB; 6KTN; X-ray; 2.75 A; A=223-505.
DR PDB; 6L89; X-ray; 2.10 A; A/B=223-505.
DR PDB; 6L8B; X-ray; 2.10 A; A/B=223-505.
DR PDB; 6MCZ; X-ray; 2.10 A; A/B=231-505.
DR PDB; 6MD0; X-ray; 1.95 A; A/B=231-505.
DR PDB; 6MD1; X-ray; 2.20 A; A/B=231-505.
DR PDB; 6MD2; X-ray; 2.20 A; A/B=231-505.
DR PDB; 6MD4; X-ray; 2.24 A; A/B=231-505.
DR PDB; 6MS7; X-ray; 1.43 A; A=234-505.
DR PDB; 6O67; X-ray; 2.52 A; A/B=231-505.
DR PDB; 6O68; X-ray; 2.78 A; A/B=231-505.
DR PDB; 6ONI; X-ray; 1.80 A; B=231-505.
DR PDB; 6ONJ; X-ray; 2.30 A; A=231-505.
DR PDB; 6PDZ; X-ray; 2.10 A; A/B=231-505.
DR PDB; 6QJ5; X-ray; 2.00 A; A/B=223-505.
DR PDB; 6T1S; X-ray; 1.65 A; A=231-505.
DR PDB; 6T1V; X-ray; 2.21 A; A=231-505.
DR PDB; 6T6B; X-ray; 2.80 A; A=231-505.
DR PDB; 6T9C; X-ray; 1.95 A; A/B=223-505.
DR PDB; 6TDC; X-ray; 2.33 A; A=235-505.
DR PDB; 6TSG; X-ray; 2.98 A; A=231-505.
DR PDB; 6VZL; X-ray; 2.07 A; A/B=231-505.
DR PDB; 6VZM; X-ray; 2.40 A; A/B=231-505.
DR PDB; 6VZN; X-ray; 2.30 A; A/B=231-505.
DR PDB; 6VZO; X-ray; 2.27 A; A/B=231-505.
DR PDB; 6Y3U; X-ray; 2.62 A; A=231-505.
DR PDB; 6ZLY; X-ray; 1.79 A; A/B=223-505.
DR PDB; 7A7H; X-ray; 2.40 A; A=231-505.
DR PDB; 7AHJ; X-ray; 2.10 A; A/B=232-505.
DR PDB; 7AWC; X-ray; 1.74 A; A=231-505.
DR PDB; 7AWD; X-ray; 1.93 A; A=231-505.
DR PDB; 7CXE; X-ray; 2.50 A; A/B=223-505.
DR PDB; 7CXF; X-ray; 2.35 A; A=223-505.
DR PDB; 7CXG; X-ray; 1.88 A; A/B=223-505.
DR PDB; 7CXH; X-ray; 2.30 A; A=223-505.
DR PDB; 7CXI; X-ray; 2.30 A; A=223-505.
DR PDB; 7CXJ; X-ray; 2.65 A; A=223-505.
DR PDB; 7CXK; X-ray; 2.20 A; A=223-505.
DR PDB; 7CXL; X-ray; 2.70 A; A=223-505.
DR PDB; 7E0A; X-ray; 1.77 A; A=230-505.
DR PDB; 7E2O; X-ray; 3.20 A; A/B=232-505.
DR PDB; 7EFQ; X-ray; 2.30 A; A/B=232-505.
DR PDB; 7JQG; X-ray; 2.15 A; A/B=231-505.
DR PDB; 7LOT; X-ray; 2.29 A; A/B=232-505.
DR PDB; 7WOX; X-ray; 3.20 A; A/B=232-505.
DR PDBsum; 1FM6; -.
DR PDBsum; 1FM9; -.
DR PDBsum; 1I7I; -.
DR PDBsum; 1K74; -.
DR PDBsum; 1KNU; -.
DR PDBsum; 1NYX; -.
DR PDBsum; 1PRG; -.
DR PDBsum; 1RDT; -.
DR PDBsum; 1WM0; -.
DR PDBsum; 1ZEO; -.
DR PDBsum; 1ZGY; -.
DR PDBsum; 2ATH; -.
DR PDBsum; 2F4B; -.
DR PDBsum; 2FVJ; -.
DR PDBsum; 2G0G; -.
DR PDBsum; 2G0H; -.
DR PDBsum; 2GTK; -.
DR PDBsum; 2HFP; -.
DR PDBsum; 2HWQ; -.
DR PDBsum; 2HWR; -.
DR PDBsum; 2I4J; -.
DR PDBsum; 2I4P; -.
DR PDBsum; 2I4Z; -.
DR PDBsum; 2OM9; -.
DR PDBsum; 2P4Y; -.
DR PDBsum; 2POB; -.
DR PDBsum; 2PRG; -.
DR PDBsum; 2Q59; -.
DR PDBsum; 2Q5P; -.
DR PDBsum; 2Q5S; -.
DR PDBsum; 2Q61; -.
DR PDBsum; 2Q6R; -.
DR PDBsum; 2Q6S; -.
DR PDBsum; 2Q8S; -.
DR PDBsum; 2QMV; -.
DR PDBsum; 2VSR; -.
DR PDBsum; 2VST; -.
DR PDBsum; 2VV0; -.
DR PDBsum; 2VV1; -.
DR PDBsum; 2VV2; -.
DR PDBsum; 2VV3; -.
DR PDBsum; 2VV4; -.
DR PDBsum; 2XKW; -.
DR PDBsum; 2YFE; -.
DR PDBsum; 2ZK0; -.
DR PDBsum; 2ZK1; -.
DR PDBsum; 2ZK2; -.
DR PDBsum; 2ZK3; -.
DR PDBsum; 2ZK4; -.
DR PDBsum; 2ZK5; -.
DR PDBsum; 2ZK6; -.
DR PDBsum; 2ZNO; -.
DR PDBsum; 2ZVT; -.
DR PDBsum; 3ADS; -.
DR PDBsum; 3ADT; -.
DR PDBsum; 3ADU; -.
DR PDBsum; 3ADV; -.
DR PDBsum; 3ADW; -.
DR PDBsum; 3ADX; -.
DR PDBsum; 3AN3; -.
DR PDBsum; 3AN4; -.
DR PDBsum; 3B0Q; -.
DR PDBsum; 3B0R; -.
DR PDBsum; 3B1M; -.
DR PDBsum; 3B3K; -.
DR PDBsum; 3BC5; -.
DR PDBsum; 3CDP; -.
DR PDBsum; 3CDS; -.
DR PDBsum; 3CS8; -.
DR PDBsum; 3CWD; -.
DR PDBsum; 3D6D; -.
DR PDBsum; 3DZU; -.
DR PDBsum; 3DZY; -.
DR PDBsum; 3E00; -.
DR PDBsum; 3ET0; -.
DR PDBsum; 3ET3; -.
DR PDBsum; 3FEJ; -.
DR PDBsum; 3FUR; -.
DR PDBsum; 3G9E; -.
DR PDBsum; 3GBK; -.
DR PDBsum; 3H0A; -.
DR PDBsum; 3HO0; -.
DR PDBsum; 3HOD; -.
DR PDBsum; 3IA6; -.
DR PDBsum; 3K8S; -.
DR PDBsum; 3KMG; -.
DR PDBsum; 3LMP; -.
DR PDBsum; 3NOA; -.
DR PDBsum; 3OSI; -.
DR PDBsum; 3OSW; -.
DR PDBsum; 3PBA; -.
DR PDBsum; 3PO9; -.
DR PDBsum; 3PRG; -.
DR PDBsum; 3QT0; -.
DR PDBsum; 3R5N; -.
DR PDBsum; 3R8A; -.
DR PDBsum; 3R8I; -.
DR PDBsum; 3S9S; -.
DR PDBsum; 3SZ1; -.
DR PDBsum; 3T03; -.
DR PDBsum; 3TY0; -.
DR PDBsum; 3U9Q; -.
DR PDBsum; 3V9T; -.
DR PDBsum; 3V9V; -.
DR PDBsum; 3V9Y; -.
DR PDBsum; 3VJH; -.
DR PDBsum; 3VJI; -.
DR PDBsum; 3VN2; -.
DR PDBsum; 3VSO; -.
DR PDBsum; 3VSP; -.
DR PDBsum; 3WJ4; -.
DR PDBsum; 3WJ5; -.
DR PDBsum; 3WMH; -.
DR PDBsum; 3X1H; -.
DR PDBsum; 3X1I; -.
DR PDBsum; 4A4V; -.
DR PDBsum; 4A4W; -.
DR PDBsum; 4CI5; -.
DR PDBsum; 4E4K; -.
DR PDBsum; 4E4Q; -.
DR PDBsum; 4EM9; -.
DR PDBsum; 4EMA; -.
DR PDBsum; 4F9M; -.
DR PDBsum; 4FGY; -.
DR PDBsum; 4HEE; -.
DR PDBsum; 4JAZ; -.
DR PDBsum; 4JL4; -.
DR PDBsum; 4L96; -.
DR PDBsum; 4L98; -.
DR PDBsum; 4O8F; -.
DR PDBsum; 4OJ4; -.
DR PDBsum; 4PRG; -.
DR PDBsum; 4PVU; -.
DR PDBsum; 4PWL; -.
DR PDBsum; 4R06; -.
DR PDBsum; 4R2U; -.
DR PDBsum; 4R6S; -.
DR PDBsum; 4XLD; -.
DR PDBsum; 4XTA; -.
DR PDBsum; 4XUH; -.
DR PDBsum; 4XUM; -.
DR PDBsum; 4Y29; -.
DR PDBsum; 4YT1; -.
DR PDBsum; 5AZV; -.
DR PDBsum; 5DSH; -.
DR PDBsum; 5DV3; -.
DR PDBsum; 5DV6; -.
DR PDBsum; 5DV8; -.
DR PDBsum; 5DVC; -.
DR PDBsum; 5DWL; -.
DR PDBsum; 5F9B; -.
DR PDBsum; 5GTN; -.
DR PDBsum; 5GTO; -.
DR PDBsum; 5GTP; -.
DR PDBsum; 5HZC; -.
DR PDBsum; 5JI0; -.
DR PDBsum; 5LSG; -.
DR PDBsum; 5TTO; -.
DR PDBsum; 5TWO; -.
DR PDBsum; 5U5L; -.
DR PDBsum; 5UGM; -.
DR PDBsum; 5WQX; -.
DR PDBsum; 5WR0; -.
DR PDBsum; 5WR1; -.
DR PDBsum; 5Y2O; -.
DR PDBsum; 5Y2T; -.
DR PDBsum; 5YCN; -.
DR PDBsum; 5YCP; -.
DR PDBsum; 5Z5S; -.
DR PDBsum; 5Z6S; -.
DR PDBsum; 6AD9; -.
DR PDBsum; 6AN1; -.
DR PDBsum; 6AUG; -.
DR PDBsum; 6AVI; -.
DR PDBsum; 6C1I; -.
DR PDBsum; 6C5Q; -.
DR PDBsum; 6C5T; -.
DR PDBsum; 6D3E; -.
DR PDBsum; 6D8X; -.
DR PDBsum; 6D94; -.
DR PDBsum; 6DBH; -.
DR PDBsum; 6DCU; -.
DR PDBsum; 6DGL; -.
DR PDBsum; 6DGO; -.
DR PDBsum; 6DGP; -.
DR PDBsum; 6DGQ; -.
DR PDBsum; 6DGR; -.
DR PDBsum; 6DH9; -.
DR PDBsum; 6DHA; -.
DR PDBsum; 6E5A; -.
DR PDBsum; 6ENQ; -.
DR PDBsum; 6F2L; -.
DR PDBsum; 6FZF; -.
DR PDBsum; 6FZG; -.
DR PDBsum; 6FZJ; -.
DR PDBsum; 6FZP; -.
DR PDBsum; 6FZY; -.
DR PDBsum; 6ICJ; -.
DR PDBsum; 6IJR; -.
DR PDBsum; 6IJS; -.
DR PDBsum; 6ILQ; -.
DR PDBsum; 6IZM; -.
DR PDBsum; 6IZN; -.
DR PDBsum; 6JEY; -.
DR PDBsum; 6JF0; -.
DR PDBsum; 6JQ7; -.
DR PDBsum; 6K0T; -.
DR PDBsum; 6KTM; -.
DR PDBsum; 6KTN; -.
DR PDBsum; 6L89; -.
DR PDBsum; 6L8B; -.
DR PDBsum; 6MCZ; -.
DR PDBsum; 6MD0; -.
DR PDBsum; 6MD1; -.
DR PDBsum; 6MD2; -.
DR PDBsum; 6MD4; -.
DR PDBsum; 6MS7; -.
DR PDBsum; 6O67; -.
DR PDBsum; 6O68; -.
DR PDBsum; 6ONI; -.
DR PDBsum; 6ONJ; -.
DR PDBsum; 6PDZ; -.
DR PDBsum; 6QJ5; -.
DR PDBsum; 6T1S; -.
DR PDBsum; 6T1V; -.
DR PDBsum; 6T6B; -.
DR PDBsum; 6T9C; -.
DR PDBsum; 6TDC; -.
DR PDBsum; 6TSG; -.
DR PDBsum; 6VZL; -.
DR PDBsum; 6VZM; -.
DR PDBsum; 6VZN; -.
DR PDBsum; 6VZO; -.
DR PDBsum; 6Y3U; -.
DR PDBsum; 6ZLY; -.
DR PDBsum; 7A7H; -.
DR PDBsum; 7AHJ; -.
DR PDBsum; 7AWC; -.
DR PDBsum; 7AWD; -.
DR PDBsum; 7CXE; -.
DR PDBsum; 7CXF; -.
DR PDBsum; 7CXG; -.
DR PDBsum; 7CXH; -.
DR PDBsum; 7CXI; -.
DR PDBsum; 7CXJ; -.
DR PDBsum; 7CXK; -.
DR PDBsum; 7CXL; -.
DR PDBsum; 7E0A; -.
DR PDBsum; 7E2O; -.
DR PDBsum; 7EFQ; -.
DR PDBsum; 7JQG; -.
DR PDBsum; 7LOT; -.
DR PDBsum; 7WOX; -.
DR AlphaFoldDB; P37231; -.
DR SMR; P37231; -.
DR BioGRID; 111464; 279.
DR ComplexPortal; CPX-702; PPARgamma-NCOA2 activated nuclear receptor complex.
DR ComplexPortal; CPX-711; PPARgamma-NCOA1 activated nuclear receptor complex.
DR DIP; DIP-35528N; -.
DR ELM; P37231; -.
DR IntAct; P37231; 91.
DR MINT; P37231; -.
DR STRING; 9606.ENSP00000287820; -.
DR BindingDB; P37231; -.
DR ChEMBL; CHEMBL235; -.
DR DrugBank; DB08760; (2S)-2-(4-chlorophenoxy)-3-phenylpropanoic acid.
DR DrugBank; DB07842; (2S)-2-(4-ethylphenoxy)-3-phenylpropanoic acid.
DR DrugBank; DB08121; (2S)-2-(biphenyl-4-yloxy)-3-phenylpropanoic acid.
DR DrugBank; DB07675; (2S)-2-ETHOXY-3-{4-[2-(10H-PHENOXAZIN-10-YL)ETHOXY]PHENYL}PROPANOIC ACID.
DR DrugBank; DB06908; (2S)-3-(1-{[2-(2-CHLOROPHENYL)-5-METHYL-1,3-OXAZOL-4-YL]METHYL}-1H-INDOL-5-YL)-2-ETHOXYPROPANOIC ACID.
DR DrugBank; DB07111; (4S,5E,7Z,10Z,13Z,16Z,19Z)-4-hydroxydocosa-5,7,10,13,16,19-hexaenoic acid.
DR DrugBank; DB08435; (5E,14E)-11-oxoprosta-5,9,12,14-tetraen-1-oic acid.
DR DrugBank; DB07172; (5R,6E,8Z,11Z,14Z,17Z)-5-hydroxyicosa-6,8,11,14,17-pentaenoic acid.
DR DrugBank; DB07208; (8E,10S,12Z)-10-hydroxy-6-oxooctadeca-8,12-dienoic acid.
DR DrugBank; DB07209; (8R,9Z,12Z)-8-hydroxy-6-oxooctadeca-9,12-dienoic acid.
DR DrugBank; DB06926; (9Z,11E,13S)-13-hydroxyoctadeca-9,11-dienoic acid.
DR DrugBank; DB04270; (S)-3-(4-(2-Carbazol-9-Yl-Ethoxy)-Phenyl)-2-Ethoxy-Propionic Acid.
DR DrugBank; DB08402; 2-[(2,4-DICHLOROBENZOYL)AMINO]-5-(PYRIMIDIN-2-YLOXY)BENZOIC ACID.
DR DrugBank; DB07863; 2-chloro-5-nitro-N-phenylbenzamide.
DR DrugBank; DB04689; 2-{5-[3-(6-BENZOYL-1-PROPYLNAPHTHALEN-2-YLOXY)PROPOXY]INDOL-1-YL}ETHANOIC ACID.
DR DrugBank; DB07053; 2-{5-[3-(7-PROPYL-3-TRIFLUOROMETHYLBENZO[D]ISOXAZOL-6-YLOXY)PROPOXY]INDOL-1-YL}ETHANOIC ACID.
DR DrugBank; DB07723; 3-(5-methoxy-1H-indol-3-yl)propanoic acid.
DR DrugBank; DB08302; 3-[5-(2-nitropent-1-en-1-yl)furan-2-yl]benzoic acid.
DR DrugBank; DB08560; 3-FLUORO-N-[1-(4-FLUOROPHENYL)-3-(2-THIENYL)-1H-PYRAZOL-5-YL]BENZENESULFONAMIDE.
DR DrugBank; DB07302; 9(S)-HODE.
DR DrugBank; DB08915; Aleglitazar.
DR DrugBank; DB00132; alpha-Linolenic acid.
DR DrugBank; DB05490; AMG-131.
DR DrugBank; DB01118; Amiodarone.
DR DrugBank; DB11811; Arhalofenate.
DR DrugBank; DB01014; Balsalazide.
DR DrugBank; DB01393; Bezafibrate.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB03600; Capric acid.
DR DrugBank; DB09201; Ciglitazone.
DR DrugBank; DB09006; Clinofibrate.
DR DrugBank; DB00845; Clofazimine.
DR DrugBank; DB05854; CLX-0921.
DR DrugBank; DB11672; Curcumin.
DR DrugBank; DB14635; Curcumin sulfate.
DR DrugBank; DB14034; Darglitazone.
DR DrugBank; DB09213; Dexibuprofen.
DR DrugBank; DB07509; difluoro(5-{2-[(5-octyl-1H-pyrrol-2-yl-kappaN)methylidene]-2H-pyrrol-5-yl-kappaN}pentanoato)boron.
DR DrugBank; DB03756; Doconexent.
DR DrugBank; DB05187; Elafibranor.
DR DrugBank; DB06521; Ertiprotafib.
DR DrugBank; DB13873; Fenofibric acid.
DR DrugBank; DB00573; Fenoprofen.
DR DrugBank; DB13961; Fish oil.
DR DrugBank; DB02266; Flufenamic acid.
DR DrugBank; DB01067; Glipizide.
DR DrugBank; DB01050; Ibuprofen.
DR DrugBank; DB00159; Icosapent.
DR DrugBank; DB07724; Indeglitazar.
DR DrugBank; DB00328; Indomethacin.
DR DrugBank; DB12007; Isoflavone.
DR DrugBank; DB09198; Lobeglitazone.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB00244; Mesalazine.
DR DrugBank; DB01252; Mitiglinide.
DR DrugBank; DB06510; Muraglitazar.
DR DrugBank; DB14011; Nabiximols.
DR DrugBank; DB00731; Nateglinide.
DR DrugBank; DB12662; Naveglitazar.
DR DrugBank; DB04224; Oleic Acid.
DR DrugBank; DB11133; Omega-3 fatty acids.
DR DrugBank; DB02746; Phthalic Acid.
DR DrugBank; DB01132; Pioglitazone.
DR DrugBank; DB06533; Ragaglitazar.
DR DrugBank; DB04971; Reglitazar.
DR DrugBank; DB00912; Repaglinide.
DR DrugBank; DB02709; Resveratrol.
DR DrugBank; DB00412; Rosiglitazone.
DR DrugBank; DB00795; Sulfasalazine.
DR DrugBank; DB00966; Telmisartan.
DR DrugBank; DB06536; Tesaglitazar.
DR DrugBank; DB08604; Triclosan.
DR DrugBank; DB00197; Troglitazone.
DR DrugBank; DB00313; Valproic acid.
DR DrugCentral; P37231; -.
DR GuidetoPHARMACOLOGY; 595; -.
DR SwissLipids; SLP:000000396; -.
DR MoonDB; P37231; Predicted.
DR GlyGen; P37231; 1 site.
DR iPTMnet; P37231; -.
DR PhosphoSitePlus; P37231; -.
DR BioMuta; PPARG; -.
DR DMDM; 13432234; -.
DR EPD; P37231; -.
DR jPOST; P37231; -.
DR MassIVE; P37231; -.
DR MaxQB; P37231; -.
DR PaxDb; P37231; -.
DR PeptideAtlas; P37231; -.
DR PRIDE; P37231; -.
DR ProteomicsDB; 55267; -. [P37231-1]
DR ProteomicsDB; 55268; -. [P37231-2]
DR ProteomicsDB; 55269; -. [P37231-3]
DR Antibodypedia; 3799; 1115 antibodies from 46 providers.
DR DNASU; 5468; -.
DR Ensembl; ENST00000287820.10; ENSP00000287820.6; ENSG00000132170.24. [P37231-1]
DR GeneID; 5468; -.
DR KEGG; hsa:5468; -.
DR UCSC; uc003bwr.4; human. [P37231-1]
DR CTD; 5468; -.
DR DisGeNET; 5468; -.
DR GeneCards; PPARG; -.
DR HGNC; HGNC:9236; PPARG.
DR HPA; ENSG00000132170; Tissue enhanced (adipose).
DR MalaCards; PPARG; -.
DR MIM; 137800; phenotype.
DR MIM; 601487; gene.
DR MIM; 601665; phenotype.
DR MIM; 604367; phenotype.
DR MIM; 606641; phenotype.
DR MIM; 609338; phenotype.
DR neXtProt; NX_P37231; -.
DR OpenTargets; ENSG00000132170; -.
DR Orphanet; 528; Congenital generalized lipodystrophy.
DR Orphanet; 146; Differentiated thyroid carcinoma.
DR Orphanet; 251579; Giant cell glioblastoma.
DR Orphanet; 251576; Gliosarcoma.
DR Orphanet; 79083; PPARG-related familial partial lipodystrophy.
DR PharmGKB; PA281; -.
DR VEuPathDB; HostDB:ENSG00000132170; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000158273; -.
DR HOGENOM; CLU_007368_4_2_1; -.
DR InParanoid; P37231; -.
DR OrthoDB; 1240230at2759; -.
DR PhylomeDB; P37231; -.
DR TreeFam; TF316304; -.
DR PathwayCommons; P37231; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9022707; MECP2 regulates transcription factors.
DR SignaLink; P37231; -.
DR SIGNOR; P37231; -.
DR BioGRID-ORCS; 5468; 28 hits in 1098 CRISPR screens.
DR ChiTaRS; PPARG; human.
DR EvolutionaryTrace; P37231; -.
DR GeneWiki; Peroxisome_proliferator-activated_receptor_gamma; -.
DR GenomeRNAi; 5468; -.
DR Pharos; P37231; Tclin.
DR PRO; PR:P37231; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P37231; protein.
DR Bgee; ENSG00000132170; Expressed in omental fat pad and 116 other tissues.
DR ExpressionAtlas; P37231; baseline and differential.
DR Genevisible; P37231; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0051393; F:alpha-actinin binding; IPI:UniProtKB.
DR GO; GO:0050544; F:arachidonic acid binding; ISS:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:BHF-UCL.
DR GO; GO:0050692; F:DNA binding domain binding; IDA:CAFA.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:BHF-UCL.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IMP:CAFA.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0050693; F:LBD domain binding; IDA:CAFA.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:BHF-UCL.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IDA:BHF-UCL.
DR GO; GO:0042277; F:peptide binding; IDA:CAFA.
DR GO; GO:0004955; F:prostaglandin receptor activity; TAS:BHF-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; IDA:CAFA.
DR GO; GO:0043621; F:protein self-association; IDA:CAFA.
DR GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0097677; F:STAT family protein binding; IPI:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
DR GO; GO:0030509; P:BMP signaling pathway; IGI:BHF-UCL.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; ISS:BHF-UCL.
DR GO; GO:0048469; P:cell maturation; IDA:BHF-UCL.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:BHF-UCL.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IDA:BHF-UCL.
DR GO; GO:0030855; P:epithelial cell differentiation; ISS:BHF-UCL.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; IMP:BHF-UCL.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; TAS:BHF-UCL.
DR GO; GO:0055088; P:lipid homeostasis; TAS:BHF-UCL.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0042953; P:lipoprotein transport; IDA:BHF-UCL.
DR GO; GO:0015909; P:long-chain fatty acid transport; ISS:BHF-UCL.
DR GO; GO:0010742; P:macrophage derived foam cell differentiation; IDA:UniProtKB.
DR GO; GO:0030224; P:monocyte differentiation; IDA:BHF-UCL.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:BHF-UCL.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:ARUK-UCL.
DR GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; ISS:BHF-UCL.
DR GO; GO:1903845; P:negative regulation of cellular response to transforming growth factor beta stimulus; IGI:ARUK-UCL.
DR GO; GO:0010887; P:negative regulation of cholesterol storage; IDA:BHF-UCL.
DR GO; GO:1904597; P:negative regulation of connective tissue replacement involved in inflammatory response wound healing; ISS:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:ARUK-UCL.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IBA:GO_Central.
DR GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0010888; P:negative regulation of lipid storage; ISS:BHF-UCL.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:BHF-UCL.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0060965; P:negative regulation of miRNA-mediated gene silencing; IMP:BHF-UCL.
DR GO; GO:0090258; P:negative regulation of mitochondrial fission; IMP:BHF-UCL.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:ARUK-UCL.
DR GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; IGI:ARUK-UCL.
DR GO; GO:1904893; P:negative regulation of receptor signaling pathway via STAT; IDA:ARUK-UCL.
DR GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IDA:BHF-UCL.
DR GO; GO:2000272; P:negative regulation of signaling receptor activity; IDA:BHF-UCL.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IGI:ARUK-UCL.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IDA:BHF-UCL.
DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0001890; P:placenta development; ISS:BHF-UCL.
DR GO; GO:0070165; P:positive regulation of adiponectin secretion; ISS:BHF-UCL.
DR GO; GO:1904179; P:positive regulation of adipose tissue development; IC:ComplexPortal.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:BHF-UCL.
DR GO; GO:0043388; P:positive regulation of DNA binding; IMP:CAFA.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:HGNC-UCL.
DR GO; GO:0045923; P:positive regulation of fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; IDA:BHF-UCL.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IGI:BHF-UCL.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IGI:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CAFA.
DR GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; IMP:BHF-UCL.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:BHF-UCL.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IC:ComplexPortal.
DR GO; GO:0060694; P:regulation of cholesterol transporter activity; IC:BHF-UCL.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0033993; P:response to lipid; ISS:BHF-UCL.
DR GO; GO:0007584; P:response to nutrient; TAS:ProtInc.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IDA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IDA:BHF-UCL.
DR GO; GO:0050872; P:white fat cell differentiation; ISS:HGNC-UCL.
DR DisProt; DP00718; -.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID00041; -.
DR InterPro; IPR003074; 1Cnucl_rcpt.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR003077; PPAR-gamma.
DR InterPro; IPR022590; PPARgamma_N.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF12577; PPARgamma_N; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR01288; PROXISOMEPAR.
DR PRINTS; PR01291; PROXISOMPAGR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Biological rhythms;
KW Cytoplasm; Diabetes mellitus; Disease variant; DNA-binding; Glycoprotein;
KW Metal-binding; Nucleus; Obesity; Phosphoprotein; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..505
FT /note="Peroxisome proliferator-activated receptor gamma"
FT /id="PRO_0000053492"
FT DOMAIN 238..503
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 136..210
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 139..159
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 176..198
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 205..280
FT /note="Interaction with FAM120B"
FT /evidence="ECO:0000250"
FT MOTIF 495..503
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:30468856"
FT BINDING 314..317
FT /ligand="rosiglitazone"
FT /ligand_id="ChEBI:CHEBI:188074"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:9744270,
FT ECO:0007744|PDB:2PRG"
FT BINDING 351
FT /ligand="rosiglitazone"
FT /ligand_id="ChEBI:CHEBI:188074"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:9744270,
FT ECO:0007744|PDB:2PRG"
FT BINDING 477
FT /ligand="rosiglitazone"
FT /ligand_id="ChEBI:CHEBI:188074"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:9744270,
FT ECO:0007744|PDB:2PRG"
FT BINDING 501
FT /ligand="rosiglitazone"
FT /ligand_id="ChEBI:CHEBI:188074"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:9744270,
FT ECO:0007744|PDB:2PRG"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 84
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform 1 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16842753,
FT ECO:0000303|PubMed:7787419, ECO:0000303|PubMed:8702406,
FT ECO:0000303|PubMed:8706692, ECO:0000303|PubMed:9065481"
FT /id="VSP_003645"
FT VAR_SEQ 207..213
FT /note="AIRFGRM -> EELQKDS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16842753"
FT /id="VSP_043906"
FT VAR_SEQ 214..504
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16842753"
FT /id="VSP_043907"
FT VARIANT 12
FT /note="P -> A (significant independent determinant of CIMT;
FT may protect from early atherosclerosis in subject at risk
FT for diabetes; associated with BMI; dbSNP:rs1801282)"
FT /evidence="ECO:0000269|PubMed:10394368,
FT ECO:0000269|PubMed:10407229, ECO:0000269|PubMed:15562396,
FT ECO:0000269|PubMed:9425261, ECO:0000269|Ref.12"
FT /id="VAR_010723"
FT VARIANT 40
FT /note="P -> A (in dbSNP:rs1805192)"
FT /id="VAR_016116"
FT VARIANT 113
FT /note="P -> Q (in obesity; dbSNP:rs1800571)"
FT /evidence="ECO:0000269|PubMed:9753710"
FT /id="VAR_010724"
FT VARIANT 314
FT /note="Q -> P (in colon cancer; sporadic; somatic mutation;
FT loss of ligand-binding; dbSNP:rs121909242)"
FT /evidence="ECO:0000269|PubMed:10394368"
FT /id="VAR_010725"
FT VARIANT 316
FT /note="R -> H (in colon cancer; sporadic; somatic mutation;
FT partial loss of ligand-binding; dbSNP:rs28936407)"
FT /evidence="ECO:0000269|PubMed:10394368"
FT /id="VAR_010726"
FT VARIANT 318
FT /note="V -> M (in diabetes; dbSNP:rs72551362)"
FT /evidence="ECO:0000269|PubMed:10622252"
FT /id="VAR_010727"
FT VARIANT 388
FT /note="F -> L (in FPLD3; dbSNP:rs72551363)"
FT /evidence="ECO:0000269|PubMed:12453919"
FT /id="VAR_022700"
FT VARIANT 425
FT /note="R -> C (in FPLD3; dbSNP:rs72551364)"
FT /evidence="ECO:0000269|PubMed:11788685"
FT /id="VAR_022701"
FT VARIANT 495
FT /note="P -> L (in diabetes; dbSNP:rs121909244)"
FT /evidence="ECO:0000269|PubMed:10622252"
FT /id="VAR_010728"
FT CONFLICT 36..37
FT /note="MP -> IA (in Ref. 3; BAA18949)"
FT /evidence="ECO:0000305"
FT CONFLICT 213..214
FT /note="MP -> IA (in Ref. 3; BAA18949)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="R -> RQ (in Ref. 3; BAA18949)"
FT /evidence="ECO:0000305"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:3DZY"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3DZU"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:3DZY"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:3DZY"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:3DZY"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:3DZY"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:3DZY"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3DZY"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:3DZY"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:3DZY"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:6IJR"
FT HELIX 234..253
FT /evidence="ECO:0007829|PDB:6MS7"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:6MS7"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6ZLY"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3U9Q"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:6MS7"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:6MS7"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:3NOA"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1ZGY"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:6T1S"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:7AWC"
FT HELIX 305..329
FT /evidence="ECO:0007829|PDB:6MS7"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:6MS7"
FT HELIX 339..360
FT /evidence="ECO:0007829|PDB:6MS7"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:3DZU"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:6MS7"
FT TURN 370..373
FT /evidence="ECO:0007829|PDB:6MS7"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:6MS7"
FT HELIX 378..383
FT /evidence="ECO:0007829|PDB:6MS7"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:6MS7"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:6MS7"
FT HELIX 393..403
FT /evidence="ECO:0007829|PDB:6MS7"
FT HELIX 409..420
FT /evidence="ECO:0007829|PDB:6MS7"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:3ADT"
FT HELIX 431..452
FT /evidence="ECO:0007829|PDB:6MS7"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:4R2U"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:7CXK"
FT HELIX 459..487
FT /evidence="ECO:0007829|PDB:6MS7"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:7AWC"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:4L98"
FT HELIX 495..501
FT /evidence="ECO:0007829|PDB:6MS7"
FT TURN 502..504
FT /evidence="ECO:0007829|PDB:6IJS"
SQ 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
