P37231 (PPARG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxisome proliferator-activated receptor gamma
Short name=PPAR-gamma

Alternative name(s):
Nuclear receptor subfamily 1 group C member 3

Gene names

Name:	PPARG
Synonyms:	NR1C3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	505 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to a promoter element in the gene for acyl-CoA oxidase and activates its transcription. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated proinflammatory responses. Ref.1 Ref.23 Ref.25
Enzyme regulation	PDPK1 activates its transcriptional activity independently of its kinase activity. Ref.23
Subunit structure	Forms a heterodimer with the retinoic acid receptor RXRA 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 FAM120B and PRDM16 By similarity. Interacts with NOCA7 in a ligand-inducible manner. Interacts with NCOA1 and NCOA2 LXXLL motifs. Interacts with ASXL1, ASXL2, DNTTIP2, MAP2K1/MEK1, PDPK1, PRMT2 and TGFB1I1. Interacts (via DNA-binding domain) with HELZ2; the interaction stimulates the transcriptional activity of PPARG. Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.28
Subcellular location	Nucleus. Cytoplasm. Note: Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. Ref.24
Tissue specificity	Highest expression in adipose tissue. Lower in skeletal muscle, spleen, heart and liver. Also detectable in placenta, lung and ovary. Ref.1
Post-translational modification	O-GlcNAcylation at Thr-84 reduces transcriptional activity in adipocytes By similarity.
Polymorphism	Genetic variation in PPARG may influence body mass index (BMI) [MIM:606641]. BMI reflects the amount of fat, lean mass, and body build. 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.
Involvement in disease	Defects in PPARG can lead to type 2 insulin-resistant diabetes and hyptertension. PPARG mutations may be associated with colon cancer. 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. Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry. Ref.41 Familial partial lipodystrophy 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.47 Ref.48 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. 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.
Sequence similarities	Belongs to the nuclear hormone receptor family. NR1 subfamily. Contains 1 nuclear receptor DNA-binding domain.
Sequence caution	The sequence AAN38992.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAA23354.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAF83270.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAA62153.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Diabetes mellitus Disease mutation Obesity
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Receptor
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay PubMed 18293083. Source: BHF-UCL brown fat cell differentiation Inferred from electronic annotation. Source: Compara cell fate commitment Inferred from sequence or structural similarity. Source: BHF-UCL cell maturation Inferred from direct assay PubMed 9568716. Source: BHF-UCL cellular response to insulin stimulus Inferred from mutant phenotype Ref.46. Source: BHF-UCL cellular response to lithium ion Inferred from electronic annotation. Source: Compara epithelial cell differentiation Inferred from sequence or structural similarity. Source: BHF-UCL fatty acid oxidation Inferred from electronic annotation. Source: Compara glucose homeostasis Inferred from mutant phenotype Ref.46. Source: BHF-UCL heart development Inferred from electronic annotation. Source: Compara induction of apoptosis Inferred from direct assay PubMed 18293083. Source: BHF-UCL innate immune response Traceable author statement PubMed 17145956. Source: BHF-UCL lipid homeostasis Traceable author statement PubMed 9113987. Source: BHF-UCL lipid metabolic process Traceable author statement PubMed 9568716. Source: ProtInc lipoprotein transport Inferred from direct assay PubMed 9568716. Source: BHF-UCL long-chain fatty acid transport Inferred from sequence or structural similarity. Source: BHF-UCL low-density lipoprotein particle receptor biosynthetic process Inferred from direct assay PubMed 9568716. Source: BHF-UCL monocyte differentiation Inferred from direct assay PubMed 9568716. Source: BHF-UCL negative regulation of acute inflammatory response Inferred from electronic annotation. Source: Compara negative regulation of cell growth Inferred from electronic annotation. Source: Compara negative regulation of cholesterol storage Inferred from direct assay PubMed 19114110. Source: BHF-UCL negative regulation of interferon-gamma-mediated signaling pathway Inferred from mutant phenotype PubMed 21268089. Source: BHF-UCL negative regulation of macrophage derived foam cell differentiation Inferred from direct assay PubMed 19114110. Source: BHF-UCL negative regulation of receptor biosynthetic process Inferred from direct assay PubMed 12700342. Source: BHF-UCL negative regulation of sequestering of triglyceride Inferred from direct assay PubMed 12700342. Source: BHF-UCL negative regulation of smooth muscle cell proliferation Inferred from direct assay PubMed 20622039. Source: BHF-UCL negative regulation of telomerase activity Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 12700342. Source: BHF-UCL organ regeneration Inferred from electronic annotation. Source: Compara peroxisome proliferator activated receptor signaling pathway Inferred from mutant phenotype PubMed 20622039. Source: BHF-UCL placenta development Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of fat cell differentiation Inferred from sequence or structural similarity. Source: HGNC positive regulation of fatty acid oxidation Inferred from electronic annotation. Source: Compara positive regulation of oligodendrocyte differentiation Inferred from electronic annotation. Source: Compara positive regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 18293083. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.22. Source: UniProtKB regulation of blood pressure Inferred from mutant phenotype Ref.46. Source: BHF-UCL regulation of cholesterol transporter activity Inferred by curator PubMed 17611579. Source: BHF-UCL response to caffeine Inferred from electronic annotation. Source: Compara response to cold Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to low-density lipoprotein particle stimulus Inferred from direct assay PubMed 9568716. Source: BHF-UCL response to nutrient Traceable author statement PubMed 10973253. Source: ProtInc response to retinoic acid Inferred from direct assay Ref.22. Source: UniProtKB response to vitamin A Inferred from electronic annotation. Source: Compara transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome white fat cell differentiation Traceable author statement PubMed 12588810. Source: UniProtKB
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: BHF-UCL nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	RNA polymerase II regulatory region DNA binding Inferred from electronic annotation. Source: Compara activating transcription factor binding Inferred from direct assay Ref.46. Source: BHF-UCL arachidonic acid binding Inferred from sequence or structural similarity PubMed 9568715. Source: BHF-UCL chromatin binding Inferred from electronic annotation. Source: Compara drug binding Inferred from direct assay Ref.46PubMed 9113987. Source: BHF-UCL ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Inferred from direct assay Ref.46. Source: BHF-UCL ligand-dependent nuclear receptor transcription coactivator activity Inferred from direct assay Ref.22. Source: UniProtKB prostaglandin receptor activity Traceable author statement PubMed 9568715. Source: BHF-UCL retinoid X receptor binding Inferred from direct assay PubMed 9568715. Source: BHF-UCL sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro transcription regulatory region DNA binding Inferred from direct assay PubMed 18293083. Source: BHF-UCL zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDK5	Q00535	2	EBI-781416,EBI-1041567
CLU	P10909	3	EBI-781384,EBI-1104674
EDF1	O60869	4	EBI-781384,EBI-781301
SMARCD3	Q6STE5-1	3	EBI-781384,EBI-488506
SMARCD3	Q6STE5-2	3	EBI-781384,EBI-488511

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 2 (identifier: P37231-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 1 (identifier: P37231-2)

Also known as: PPARgamma1(wt);

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Isoform 3 (identifier: P37231-3)

Also known as: PPARgamma1(tr);

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.
     207-213: AIRFGRM → EELQKDS
     214-504: Missing.

Note: Exhibits dominant negative activity over isoform 1.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 505

505

Peroxisome proliferator-activated receptor gamma

PRO_0000053492

Regions

DNA binding

136 – 210

75

Nuclear receptor

Zinc finger

139 – 159

21

NR C4-type

Zinc finger

176 – 198

23

NR C4-type

Region

205 – 280

76

Interaction with FAM120B By similarity

Region

317 – 505

189

Ligand-binding

Sites

Binding site

317

1

Synthetic agonist

Binding site

351

1

Synthetic agonist

Binding site

477

1

Synthetic agonist

Binding site

501

1

Synthetic agonist

Amino acid modifications

Modified residue

112

1

Phosphoserine; by MAPK By similarity

Glycosylation

84

1

O-linked (GlcNAc...) By similarity

Natural variations

Alternative sequence

1 – 28

28

Missing in isoform 1 and isoform 3.

VSP_003645

Alternative sequence

207 – 213

7

AIRFGRM → EELQKDS in isoform 3.

VSP_043906

Alternative sequence

214 – 504

291

Missing in isoform 3.

VSP_043907

Natural variant

12

1

P → A Significant independent determinant of CIMT; may protect from early atherosclerosis in subject at risk for diabetes; associated with BMI. Ref.12 Ref.40 Ref.42 Ref.43 Ref.44 Ref.45 Ref.49 Ref.50 Ref.51
Corresponds to variant rs1801282 [ dbSNP | Ensembl ].

VAR_010723

Natural variant

40

1

P → A.
Corresponds to variant rs1805192 [ dbSNP | Ensembl ].

VAR_016116

Natural variant

113

1

P → Q in obesity. Ref.41
Corresponds to variant rs1800571 [ dbSNP | Ensembl ].

VAR_010724

Natural variant

314

1

Q → P in colon cancer; sporadic; somatic mutation; loss of ligand-binding. Ref.45
Corresponds to variant rs28936407 [ dbSNP | Ensembl ].

VAR_010725

Natural variant

316

1

R → H in colon cancer; sporadic; somatic mutation; partial loss of ligand-binding. Ref.45
Corresponds to variant rs28936407 [ dbSNP | Ensembl ].

VAR_010726

Natural variant

318

1

V → M in diabetes. Ref.46

VAR_010727

Natural variant

388

1

F → L in FPLD3. Ref.47

VAR_022700

Natural variant

425

1

R → C in FPLD3. Ref.48

VAR_022701

Natural variant

495

1

P → L in diabetes. Ref.46

VAR_010728

Experimental info

Sequence conflict

36 – 37

2

MP → IA in BAA18949. Ref.3

Sequence conflict

213 – 214

2

MP → IA in BAA18949. Ref.3

Sequence conflict

240

1

R → RQ in BAA18949. Ref.3

Secondary structure

1

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505

Helix Strand Turn

Details...

Beta strand

140 – 142

3

Beta strand

148 – 150

3

Beta strand

151 – 154

4

Helix

157 – 167

11

Turn

168 – 170

3

Helix

186 – 188

3

Helix

191 – 200

10

Helix

205 – 207

3

Turn

214 – 217

4

Helix

218 – 220

3

Turn

222 – 226

5

Turn

228 – 231

4

Helix

237 – 253

17

Helix

258 – 265

8

Turn

266 – 268

3

Beta strand

269 – 271

3

Beta strand

275 – 277

3

Helix

280 – 286

7

Turn

287 – 289

3

Beta strand

290 – 292

3

Beta strand

294 – 296

3

Beta strand

297 – 299

3

Beta strand

301 – 303

3

Helix

305 – 329

25

Helix

334 – 336

3

Helix

339 – 360

22

Beta strand

361 – 363

3

Beta strand

366 – 369

4

Turn

370 – 373

4

Beta strand

374 – 377

4

Helix

378 – 383

6

Turn

385 – 387

3

Helix

388 – 390

3

Helix

393 – 403

11

Helix

409 – 420

12

Beta strand

423 – 425

3

Helix

431 – 452

22

Beta strand

454 – 456

3

Helix

459 – 486

28

Beta strand

488 – 490

3

Helix

495 – 501

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified April 27, 2001. Version 3. Checksum: 3933EFF36A0E4CAF	FASTA	505	57,620
	10 20 30 40 50 60 MGETLGDSPI DPESDSFTDT LSANISQEMT MVDTEMPFWP TNFGISSVDL SVMEDHSHSF 70 80 90 100 110 120 DIKPFTTVDF SSISTPHYED IPFTRTDPVV ADYKYDLKLQ EYQSAIKVEP ASPPYYSEKT 130 140 150 160 170 180 QLYNKPHEEP SNSLMAIECR VCGDKASGFH YGVHACEGCK GFFRRTIRLK LIYDRCDLNC 190 200 210 220 230 240 RIHKKSRNKC QYCRFQKCLA VGMSHNAIRF GRMPQAEKEK LLAEISSDID QLNPESADLR 250 260 270 280 290 300 ALAKHLYDSY IKSFPLTKAK ARAILTGKTT DKSPFVIYDM NSLMMGEDKI KFKHITPLQE 310 320 330 340 350 360 QSKEVAIRIF QGCQFRSVEA VQEITEYAKS IPGFVNLDLN DQVTLLKYGV HEIIYTMLAS 370 380 390 400 410 420 LMNKDGVLIS EGQGFMTREF LKSLRKPFGD FMEPKFEFAV KFNALELDDS DLAIFIAVII 430 440 450 460 470 480 LSGDRPGLLN VKPIEDIQDN LLQALELQLK LNHPESSQLF AKLLQKMTDL RQIVTEHVQL 490 500 LQVIKKTETD MSLHPLLQEI YKDLY
	Isoform 1 (PPARgamma1(wt)) [UniParc]. Checksum: 1061C2074B739E0A	FASTA	477	54,681
	10 20 30 40 50 60 MTMVDTEMPF WPTNFGISSV DLSVMEDHSH SFDIKPFTTV DFSSISTPHY EDIPFTRTDP 70 80 90 100 110 120 VVADYKYDLK LQEYQSAIKV EPASPPYYSE KTQLYNKPHE EPSNSLMAIE CRVCGDKASG 130 140 150 160 170 180 FHYGVHACEG CKGFFRRTIR LKLIYDRCDL NCRIHKKSRN KCQYCRFQKC LAVGMSHNAI 190 200 210 220 230 240 RFGRMPQAEK EKLLAEISSD IDQLNPESAD LRALAKHLYD SYIKSFPLTK AKARAILTGK 250 260 270 280 290 300 TTDKSPFVIY DMNSLMMGED KIKFKHITPL QEQSKEVAIR IFQGCQFRSV EAVQEITEYA 310 320 330 340 350 360 KSIPGFVNLD LNDQVTLLKY GVHEIIYTML ASLMNKDGVL ISEGQGFMTR EFLKSLRKPF 370 380 390 400 410 420 GDFMEPKFEF AVKFNALELD DSDLAIFIAV IILSGDRPGL LNVKPIEDIQ DNLLQALELQ 430 440 450 460 470 LKLNHPESSQ LFAKLLQKMT DLRQIVTEHV QLLQVIKKTE TDMSLHPLLQ EIYKDLY
	Isoform 3 (PPARgamma1(tr)) [UniParc]. Checksum: 10E780305F860A5D	FASTA	186	21,580
	10 20 30 40 50 60 MTMVDTEMPF WPTNFGISSV DLSVMEDHSH SFDIKPFTTV DFSSISTPHY EDIPFTRTDP 70 80 90 100 110 120 VVADYKYDLK LQEYQSAIKV EPASPPYYSE KTQLYNKPHE EPSNSLMAIE CRVCGDKASG 130 140 150 160 170 180 FHYGVHACEG CKGFFRRTIR LKLIYDRCDL NCRIHKKSRN KCQYCRFQKC LAVGMSHNEE LQKDSY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Mukherjee R., Jow L., Croston G.E., Paterniti J.R. Jr. J. Biol. Chem. 272:8071-8076(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY. Tissue: Heart.
[2]	"Molecular cloning, expression and characterization of human peroxisome proliferator activated receptors gamma 1 and gamma 2." Elbrecht A., Chen Y., Cullinan C.A., Hayes N., Leibowitz M.D., Moller D.E., Berger J. Biochem. Biophys. Res. Commun. 224:431-437(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Adipose tissue.
[3]	"Differential expression of PPAR gamma1 and gamma2 isoforms in human adipose tissue." Yanase T., Yashiro T., Takitani K., Kato S., Taniguchi S., Takayanagi R., Nawata H. Biochem. Biophys. Res. Commun. 233:320-324(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Adipose tissue.
[4]	"Isolation of the human peroxisome proliferator activated receptor gamma cDNA: expression in hematopoietic cells and chromosomal mapping." Greene M.E., Blumberg B., McBride O.W., Yi H.F., Kronquist K., Kwan K., Hsieh L., Greene G., Nimer S.D. Gene Expr. 4:281-299(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Bone marrow.
[5]	Greene M.E. Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 36; 37; 213; 214 AND 240.
[6]	"No coding mutations are detected in the peroxisome proliferator-activated receptor-gamma gene in Japanese patients with lipoatrophic diabetes." Okazawa H., Mori H., Tamori Y., Araki S., Niki T., Masugi J., Kawanishi M., Kubota T., Shinoda H., Kasuga M. Diabetes 46:1904-1906(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). Tissue: Placenta.
[7]	"A human peroxisome-proliferator-activated receptor-gamma is activated by inducers of adipogenesis, including thiazolidinedione drugs." Lambe K.G., Tugwood J.D. Eur. J. Biochem. 239:1-7(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[8]	"Identification of a truncated alternative splicing variant of human PPARgamma1 that exhibits dominant negative activity." 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. Biochem. Biophys. Res. Commun. 347:698-706(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[9]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[10]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[11]	"Human Protein Factory: an infrastructure to convert the human transcriptome into the in vitro-expressed human proteome of versatile utility." 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. Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[12]	SeattleSNPs variation discovery resource Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-12.
[13]	"The DNA sequence, annotation and analysis of human chromosome 3." 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. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[15]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta.
[16]	"Cloning and characterization of RAP250, a nuclear receptor coactivator." Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A. J. Biol. Chem. 275:5308-5317(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NCOA6.
[17]	"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." 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. J. Med. Genet. 37:410-414(2000) [PubMed] [Europe PMC] [Abstract] Cited for: POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO GLIOMA.
[18]	"Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha." Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J. J. Biol. Chem. 277:28624-28630(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRMT2.
[19]	"ERAP140, a conserved tissue-specific nuclear receptor coactivator." Shao W., Halachmi S., Brown M. Mol. Cell. Biol. 22:3358-3372(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NOCA7.
[20]	"ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor." Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M., Zhu Y.-J. Biochem. Biophys. Res. Commun. 317:54-59(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DNTTIP2.
[21]	"Hic-5 regulates an epithelial program mediated by PPARgamma." Drori S., Girnun G.D., Tou L., Szwaya J.D., Mueller E., Xia K., Shivdasani R.A., Spiegelman B.M. Genes Dev. 19:362-375(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TGFB1I1.
[22]	"Isolation and characterization of a transcriptional cofactor and its novel isoform that bind the DNA-binding domain of peroxisome proliferator-activated receptor gamma." Tomaru T., Satoh T., Yoshino S., Ishizuka T., Hashimoto K., Monden T., Yamada M., Mori M. Endocrinology 147:377-388(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HELZ2.
[23]	"3-phosphoinositide-dependent protein kinase-1 activates the peroxisome proliferator-activated receptor-gamma and promotes adipocyte differentiation." Yin Y., Yuan H., Wang C., Pattabiraman N., Rao M., Pestell R.G., Glazer R.I. Mol. Endocrinol. 20:268-278(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PDPK1, ENZYME REGULATION.
[24]	"Interaction with MEK causes nuclear export and downregulation of peroxisome proliferator-activated receptor gamma." Burgermeister E., Chuderland D., Hanoch T., Meyer M., Liscovitch M., Seger R. Mol. Cell. Biol. 27:803-817(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAP2K1/MEK1, SUBCELLULAR LOCATION.
[25]	"Endoplasmic reticulum stress-activated C/EBP homologous protein enhances nuclear factor-kappaB signals via repression of peroxisome proliferator-activated receptor gamma." Park S.H., Choi H.J., Yang H., Do K.H., Kim J., Lee D.W., Moon Y. J. Biol. Chem. 285:35330-35339(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[26]	"Additional sex comb-like (ASXL) proteins 1 and 2 play opposite roles in adipogenesis via reciprocal regulation of peroxisome proliferator-activated receptor {gamma}." Park U.H., Yoon S.K., Park T., Kim E.J., Um S.J. J. Biol. Chem. 286:1354-1363(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ASXL1 AND ASXL2.
[27]	"Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma." Uppenberg J., Svensson C., Jaki M., Bertilsson G., Jendeberg L., Berkenstam A. J. Biol. Chem. 273:31108-31112(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 232-505.
[28]	"Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma." 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. Nature 395:137-143(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 235-504 IN COMPLEXES WITH THE SYNTHETIC AGONIST ROSIGLITAZONE AND NCOA1, SUBUNIT.
[29]	"Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors." 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. Mol. Cell 5:545-555(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH RXRA AND SYNTHETIC AGONISTS.
[30]	"Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors." 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. Proc. Natl. Acad. Sci. U.S.A. 98:13919-13924(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 234-505 IN COMPLEXES WITH SYNTHETIC AGONIST AND NCOA1.
[31]	"Structure of the PPARalpha and -gamma ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family." Cronet P., Petersen J.F.W., Folmer R., Blomberg N., Sjoeblom K., Karlsson U., Lindstedt E.-L., Bamberg K. Structure 9:699-706(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 225-505 IN COMPLEX WITH SYNTHETIC AGONIST.
[32]	"Synthesis and biological and structural characterization of the dual-acting peroxisome proliferator-activated receptor alpha/gamma agonist ragaglitazar." Ebdrup S., Pettersson I., Rasmussen H.B., Deussen H.-J., Frost Jensen A., Mortensen S.B., Fleckner J., Pridal L., Nygaard L., Sauerberg P. J. Med. Chem. 46:1306-1317(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 230-505 IN COMPLEX WITH SYNTHETIC AGONIST.
[33]	"A new class of peroxisome proliferator-activated receptor agonists with a novel binding epitope shows antidiabetic effects." Oestberg T., Svensson S., Selen G., Uppenberg J., Thor M., Sundbom M., Sydow-Baeckman M., Gustavsson A.-L., Jendeberg L. J. Biol. Chem. 279:41124-41130(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 232-505 IN COMPLEX WITH NCOA2 AND SYNTHETIC AGONIST.
[34]	"Structure-based design of potent retinoid X receptor alpha agonists." 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. J. Med. Chem. 47:2010-2029(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 235-505 IN COMPLEX WITH RXRA; NCOA1 AND SYNTHETIC AGONIST.
[35]	"Design and synthesis of alpha-aryloxyphenylacetic acid derivatives: a novel class of PPARalpha/gamma dual agonists with potent antihyperglycemic and lipid modulating activity." 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. J. Med. Chem. 48:4457-4468(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 231-505 IN COMPLEX WITH SYNTHETIC AGONIST.
[36]	"Structural and biochemical basis for selective repression of the orphan nuclear receptor liver receptor homolog 1 by small heterodimer partner." Li Y., Choi M., Suino K., Kovach A., Daugherty J., Kliewer S.A., Xu H.E. Proc. Natl. Acad. Sci. U.S.A. 102:9505-9510(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 234-505 IN COMPLEX WITH SYNTHETIC AGONIST AND NR0B2.
[37]	"Design and synthesis of novel N-sulfonyl-2-indole carboxamides as potent PPAR-gamma binding agents with potential application to the treatment of osteoporosis." 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. Bioorg. Med. Chem. Lett. 16:5659-5663(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 234-505 IN COMPLEX WITH SYNTHETIC AGONIST AND NCOA1.
[38]	"Indol-1-yl acetic acids as peroxisome proliferator-activated receptor agonists: design, synthesis, structural biology, and molecular docking studies." 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. J. Med. Chem. 49:1212-1216(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 235-505 IN COMPLEX WITH SYNTHETIC AGONIST.
[39]	"Structure-based drug design of a novel family of PPARgamma partial agonists: virtual screening, X-ray crystallography, and in vitro/in vivo biological activities." 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. J. Med. Chem. 49:2703-2712(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 235-505 IN COMPLEX WITH SYNTHETIC AGONIST.
[40]	"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." Yen C.-J., Beamer B.A., Negri C., Silver K., Brown K.A., Yarnall D.P., Burns D.K., Roth J., Shuldiner A.R. Biochem. Biophys. Res. Commun. 241:270-274(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALA-12.
[41]	"Obesity associated with a mutation in a genetic regulator of adipocyte differentiation." Ristow M., Muller-Wieland D., Pfeiffer A., Krone W., Kahn C.R. N. Engl. J. Med. 339:953-959(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OBESITY GLN-113.
[42]	"A Pro12Ala substitution in PPARgamma2 associated with decreased receptor activity, lower body mass index and improved insulin sensitivity." Deeb S.S., Fajas L., Nemoto M., Pihlajamaeki J., Mykkaenen L., Kuusisto J., Laakso M., Fujimoto W., Auwerx J. Nat. Genet. 20:284-287(1998) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION OF VARIANT ALA-12 WITH BMI.
[43]	"Missense variants in the human peroxisome proliferator-activated receptor-gamma2 gene in lean and obese subjects." Hamann A., Munzberg H., Buttron P., Busing B., Hinney A., Mayer H., Siegfried W., Hebebrand J., Greten H. Eur. J. Endocrinol. 141:90-92(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALA-12.
[44]	"Two polymorphisms in the peroxisome proliferator-activated receptor-gamma gene are associated with severe overweight among obese women." Valve R., Sivenius K., Miettinen R., Pihlajamaeki J., Rissanen A., Deeb S.S., Auwerx J., Uusitupa M., Laakso M. J. Clin. Endocrinol. Metab. 84:3708-3712(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION OF VARIANT ALA-12 WITH BMI.
[45]	"Loss-of-function mutations in PPAR-gamma associated with human colon cancer." 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. Mol. Cell 3:799-804(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS COLON CANCER PRO-314 AND HIS-316, VARIANT ALA-12.
[46]	"Dominant negative mutations in human PPAR-gamma associated with severe insulin resistance, diabetes mellitus and hypertension." 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. Nature 402:880-883(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DIABETES MET-318 AND LEU-495.
[47]	"PPARG F388L, a transactivation-deficient mutant, in familial partial lipodystrophy." Hegele R.A., Cao H., Frankowski C., Mathews S.T., Leff T. Diabetes 51:3586-3590(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FPLD3 LEU-388.
[48]	"A novel heterozygous mutation in peroxisome proliferator-activated receptor-gamma gene in a patient with familial partial lipodystrophy." Agarwal A.K., Garg A. J. Clin. Endocrinol. Metab. 87:408-411(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FPLD3 CYS-425.
[49]	"Effect of the peroxisome proliferator activated receptor-gamma gene Pro12Ala variant on body mass index: a meta-analysis." Masud S., Ye S. J. Med. Genet. 40:773-780(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION OF VARIANT ALA-12 WITH BMI.
[50]	"Ala12Ala genotype of the peroxisome proliferator-activated receptor gamma2 protects against atherosclerosis." Temelkova-Kurktschiev T., Hanefeld M., Chinetti G., Zawadzki C., Haulon S., Kubaszek A., Koehler C., Leonhardt W., Staels B., Laakso M. J. Clin. Endocrinol. Metab. 89:4238-4242(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION OF VARIANT ALA-12 WITH CIMT.
[51]	"Effects of peroxisome proliferator-activated receptor-gamma 2 Pro12Ala polymorphism on body fat distribution in female Korean subjects." Kim K.S., Choi S.M., Shin S.U., Yang H.S., Yoon Y. Metabolism 53:1538-1543(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALA-12.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Wikipedia

Peroxisome proliferator-activated receptor entry

GeneReviews

SeattleSNPs

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U79012 mRNA. Translation: AAC51248.1.
U63415 mRNA. Translation: AAB04028.1.
D83233 mRNA. Translation: BAA18949.1.
L40904 mRNA. Translation: AAA80314.2.
AB005526 Genomic DNA. Translation: BAA23354.1. Sequence problems.
X90563 mRNA. Translation: CAA62152.1.
X90563 mRNA. Translation: CAA62153.1. Different initiation.
DQ356894 mRNA. Translation: ABC97372.1.
BT007281 mRNA. Translation: AAP35945.1.
AK290581 mRNA. Translation: BAF83270.1. Different initiation.
AB451337 mRNA. Translation: BAG70151.1.
AB451486 mRNA. Translation: BAG70300.1.
AY157024 Genomic DNA. Translation: AAN38992.2. Different initiation.
AC090947 Genomic DNA. No translation available.
AC091492 Genomic DNA. No translation available.
AC093174 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64124.1.
BC006811 mRNA. Translation: AAH06811.1.

IPI

IPI00020897.
IPI00853091.
IPI00926009.

PIR

JC4859.
PC4290.
PC4429.

RefSeq

NP_005028.4. NM_005037.5.
NP_056953.2. NM_015869.4.
NP_619725.2. NM_138711.3.
NP_619726.2. NM_138712.3.

UniGene

Hs.162646.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FM6	X-ray	2.10	D/X	234-505	[»]
1FM9	X-ray	2.10	D	234-505	[»]
1I7I	X-ray	2.35	A/B	225-505	[»]
1K74	X-ray	2.30	D	234-505	[»]
1KNU	X-ray	2.50	A/B	232-505	[»]
1NYX	X-ray	2.65	A/B	230-505	[»]
1PRG	X-ray	2.20	A/B	235-504	[»]
1RDT	X-ray	2.40	D	235-505	[»]
1WM0	X-ray	2.90	X	232-505	[»]
1ZEO	X-ray	2.50	A/B	231-505	[»]
1ZGY	X-ray	1.80	A	234-505	[»]
2ATH	X-ray	2.28	A/B	235-505	[»]
2F4B	X-ray	2.07	A/B	235-505	[»]
2FVJ	X-ray	1.99	A	235-505	[»]
2G0G	X-ray	2.54	A/B	235-505	[»]
2G0H	X-ray	2.30	A/B	235-505	[»]
2GTK	X-ray	2.10	A	235-505	[»]
2HFP	X-ray	2.00	A	234-505	[»]
2HWQ	X-ray	1.97	A/B	235-505	[»]
2HWR	X-ray	2.34	A/B	235-505	[»]
2I4J	X-ray	2.10	A/B	223-504	[»]
2I4P	X-ray	2.10	A/B	223-504	[»]
2I4Z	X-ray	2.25	A/B	223-504	[»]
2OM9	X-ray	2.80	A/B/C/D	232-505	[»]
2P4Y	X-ray	2.25	A/B	231-505	[»]
2POB	X-ray	2.30	A/B	234-505	[»]
2PRG	X-ray	2.30	A/B	235-505	[»]
2Q59	X-ray	2.20	A/B	233-505	[»]
2Q5P	X-ray	2.30	A/B	233-505	[»]
2Q5S	X-ray	2.05	A/B	233-505	[»]
2Q61	X-ray	2.20	A/B	233-505	[»]
2Q6R	X-ray	2.41	A/B	233-505	[»]
2Q6S	X-ray	2.40	A/B	233-505	[»]
2Q8S	X-ray	2.30	A/B	235-505	[»]
2QMV	NMR	-	A	235-504	[»]
2VSR	X-ray	2.05	A/B	232-505	[»]
2VST	X-ray	2.35	A/B	232-505	[»]
2VV0	X-ray	2.55	A/B	232-505	[»]
2VV1	X-ray	2.20	A/B	232-505	[»]
2VV2	X-ray	2.75	A/B	232-505	[»]
2VV3	X-ray	2.85	A/B	232-505	[»]
2VV4	X-ray	2.35	A/B	232-505	[»]
2XKW	X-ray	2.02	A/B	232-505	[»]
2YFE	X-ray	2.00	A/B	223-505	[»]
2ZK0	X-ray	2.36	A/B	223-504	[»]
2ZK1	X-ray	2.61	A/B	223-504	[»]
2ZK2	X-ray	2.26	A/B	223-504	[»]
2ZK3	X-ray	2.58	A/B	223-504	[»]
2ZK4	X-ray	2.57	A/B	223-504	[»]
2ZK5	X-ray	2.45	A/B	223-504	[»]
2ZK6	X-ray	2.41	A/B	223-504	[»]
2ZNO	X-ray	2.40	A/B	223-504	[»]
2ZVT	X-ray	1.90	A/B	223-504	[»]
3ADS	X-ray	2.25	A/B	223-505	[»]
3ADT	X-ray	2.70	A/B	223-505	[»]
3ADU	X-ray	2.77	A/B	223-505	[»]
3ADV	X-ray	2.27	A/B	223-505	[»]
3ADW	X-ray	2.07	A/B	223-505	[»]
3ADX	X-ray	1.95	A/B	223-505	[»]
3AN3	X-ray	2.30	A/B	223-504	[»]
3AN4	X-ray	2.30	A/B	223-504	[»]
3B0Q	X-ray	2.10	A/B	231-504	[»]
3B0R	X-ray	2.15	A/B	231-504	[»]
3B1M	X-ray	1.60	A	234-505	[»]
3B3K	X-ray	2.60	A/B	223-504	[»]
3BC5	X-ray	2.27	A	231-505	[»]
3CDP	X-ray	2.80	A/B	223-504	[»]
3CDS	X-ray	2.65	A/B	223-504	[»]
3CS8	X-ray	2.30	A	234-504	[»]
3CWD	X-ray	2.40	A/B	236-505	[»]
3D6D	X-ray	2.40	A/B	223-504	[»]
3DZU	X-ray	3.20	D	102-505	[»]
3DZY	X-ray	3.10	D	102-505	[»]
3E00	X-ray	3.10	D	102-505	[»]
3ET0	X-ray	2.40	A/B	235-505	[»]
3ET3	X-ray	1.95	A	235-505	[»]
3FEJ	X-ray	2.01	A	235-505	[»]
3FUR	X-ray	2.30	A	234-505	[»]
3G9E	X-ray	2.30	A	235-505	[»]
3GBK	X-ray	2.30	A/B	235-505	[»]
3H0A	X-ray	2.10	D	234-505	[»]
3HO0	X-ray	2.60	A/B	223-504	[»]
3HOD	X-ray	2.10	A/B	223-504	[»]
3IA6	X-ray	2.31	A/B	235-505	[»]
3K8S	X-ray	2.55	A/B	234-505	[»]
3KMG	X-ray	2.10	A/D	234-505	[»]
3LMP	X-ray	1.90	A	234-505	[»]
3NOA	X-ray	1.98	A/B	235-505	[»]
3OSI	X-ray	2.70	A/B	224-504	[»]
3OSW	X-ray	2.55	A/B	224-504	[»]
3PBA	X-ray	2.30	A/B	224-505	[»]
3PO9	X-ray	2.35	A/B	224-505	[»]
3PRG	X-ray	2.90	A	232-505	[»]
3QT0	X-ray	2.50	A	235-505	[»]
3R5N	X-ray	2.00	A	232-505	[»]
3R8A	X-ray	2.41	A/B	235-505	[»]
3R8I	X-ray	2.30	A/B	223-505	[»]
3S9S	X-ray	2.55	A	234-505	[»]
3SZ1	X-ray	2.30	A/B	232-505	[»]
3T03	X-ray	2.10	A/B	234-505	[»]
3TY0	X-ray	2.00	A/B	231-505	[»]
3U9Q	X-ray	1.52	A	236-504	[»]
3V9T	X-ray	1.65	A	234-505	[»]
3V9V	X-ray	1.60	A	234-505	[»]
3V9Y	X-ray	2.10	A	234-505	[»]
3VJH	X-ray	2.22	A/B	223-504	[»]
3VJI	X-ray	2.61	A/B	223-504	[»]
3VN2	X-ray	2.18	A	225-505	[»]
4A4V	X-ray	2.00	A/B	223-505	[»]
4A4W	X-ray	2.00	A/B	223-505	[»]
4E4K	X-ray	2.50	A/B	223-505	[»]
4E4Q	X-ray	2.50	A/B	223-505	[»]
4EM9	X-ray	2.10	A/B	235-505	[»]
4EMA	X-ray	2.54	A/B	235-505	[»]
4F9M	X-ray	1.90	A	234-505	[»]
4PRG	X-ray	2.90	A/B/C/D	235-504	[»]

ProteinModelPortal

P37231.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35528N.

IntAct

P37231. 23 interactions.

MINT

MINT-5209723.

PTM databases

PhosphoSite

P37231.

Polymorphism databases

DMDM

13432234.

Proteomic databases

PaxDb

P37231.

PRIDE

P37231.

Protocols and materials databases

DNASU

5468.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000287820; ENSP00000287820; ENSG00000132170.
ENST00000309576; ENSP00000312472; ENSG00000132170.
ENST00000396999; ENSP00000380195; ENSG00000132170.
ENST00000397010; ENSP00000380205; ENSG00000132170.
ENST00000397012; ENSP00000380207; ENSG00000132170.
ENST00000397015; ENSP00000380210; ENSG00000132170.

GeneID

5468.

KEGG

hsa:5468.

UCSC

uc003bwr.3. human.

Organism-specific databases

CTD

5468.

GeneCards

GC03P012328.

HGNC

HGNC:9236. PPARG.

HPA

CAB004282.

MIM

137800. phenotype.
601487. gene.
601665. phenotype.
604367. phenotype.
606641. phenotype.
609338. phenotype.

neXtProt

NX_P37231.

Orphanet

79083. Familial partial lipodystrophy associated with PPARG mutations.
360. Glioblastoma.

PharmGKB

PA281.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG266867.

HOVERGEN

HBG106004.

InParanoid

P37231.

KO

K08530.

OMA

KTTDKSP.

PhylomeDB

P37231.

Enzyme and pathway databases

Pathway_Interaction_DB

nfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
rxr_vdr_pathway. RXR and RAR hetrodimerization with other nuclear receptor.

Reactome

REACT_111045. Developmental Biology.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P37231.

Bgee

P37231.

Genevestigator

P37231.

GermOnline

ENSG00000132170. Homo sapiens.

Family and domain databases

Gene3D

1.10.565.10. 2 hits.
3.30.50.10. 1 hit.

InterPro

IPR003074. 1Cnucl_rcpt.
IPR003077. 1Cnucl_rcpt_G.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR022590. PPARgamma_N.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]

Pfam

PF00104. Hormone_recep. 1 hit.
PF12577. PPARgamma_N. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PRINTS

PR01288. PROXISOMEPAR.
PR01291. PROXISOMPAGR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P37231.

ChEMBL

CHEMBL235.

ChiTaRS

PPARG. human.

DrugBank

DB01076. Atorvastatin.
DB00159. Icosapent.
DB01132. Pioglitazone.
DB00412. Rosiglitazone.
DB00197. Troglitazone.

EvolutionaryTrace

P37231.

GenomeRNAi

5468.

NextBio

21164.

SOURCE

Search...

Entry information

Entry name

PPARG_HUMAN

Accession

Primary (citable) accession number: P37231
Secondary accession number(s): A8K3G6 , B5BUA1, O00684, O00710, O14515, Q0QJH8, Q15178, Q15179, Q15180, Q15832, Q86U60, Q96J12

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	April 27, 2001
Last modified:	May 1, 2013
This is version 185 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.