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P37231 (PPARG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 199. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated proinflammatory responses. Ref.1 Ref.23 Ref.25 Ref.27

Enzyme regulation

PDPK1 activates its transcriptional activity independently of its kinase activity. Ref.23

Subunit structure

Heterodimer with other nuclear receptors, such as RXRA. The heterodimer with the retinoic acid receptor RXRA is called adipocyte-specific transcription factor ARF6. Interacts with NCOA6 coactivator, leading to a strong increase in transcription of target genes. Interacts with coactivator PPARBP, leading to a mild increase in transcription of target genes. Interacts with NOCA7 in a ligand-inducible manner. Interacts with NCOA1 and NCOA2 LXXLL motifs. Interacts with ASXL1, ASXL2, DNTTIP2, FAM120B, MAP2K1/MEK1, NR0B2, PDPK1, PRDM16, PRMT2 and TGFB1I1. Interacts (when activated by agonist) with PPP5C. Interacts with HELZ2 and THRAP3; the interaction stimulates the transcriptional activity of PPARG. Interacts with PER2, the interaction is ligand dependent and blocks PPARG recruitment to target promoters. Interacts with CCRN4L/NOC. Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.27 Ref.29

Subcellular location

Nucleus. Cytoplasm. Note: Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. CCRN4L/NOC enhances its nuclear translocation. Ref.24 Ref.27

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.

Phosphorylated in basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated form may be inactive and dephosphorylation at Ser-112 induces adipogenic activity By similarity.

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.42

Lipodystrophy, familial partial, 3 (FPLD3) [MIM:604367]: A form of lipodystrophy characterized by marked loss of subcutaneous fat from the extremities. Facial adipose tissue may be increased, decreased or normal. Affected individuals show an increased preponderance of insulin resistance, diabetes mellitus and dyslipidemia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.48 Ref.49

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 processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDiabetes mellitus
Disease mutation
Obesity
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Receptor
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement PubMed 9568715. Source: GOC

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: Ensembl

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.47. Source: BHF-UCL

cellular response to lithium ion

Inferred from electronic annotation. Source: Ensembl

epithelial cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

fatty acid oxidation

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

glucose homeostasis

Inferred from mutant phenotype Ref.47. Source: BHF-UCL

heart development

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12700342. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: BHF-UCL

organ regeneration

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

positive regulation of oligodendrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

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

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of blood pressure

Inferred from mutant phenotype Ref.47. Source: BHF-UCL

regulation of cholesterol transporter activity

Inferred by curator PubMed 17611579. Source: BHF-UCL

regulation of transcription involved in cell fate commitment

Inferred from sequence or structural similarity. Source: UniProtKB

response to caffeine

Inferred from electronic annotation. Source: Ensembl

response to cold

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to lipid

Inferred from sequence or structural similarity PubMed 9568715. Source: BHF-UCL

response to low-density lipoprotein particle

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: Ensembl

signal transduction

Inferred from direct assay PubMed 9568716. Source: BHF-UCL

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

white fat cell differentiation

Traceable author statement PubMed 12588810. Source: UniProtKB

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 9568716. Source: BHF-UCL

   Molecular_functionDNA binding

Inferred from direct assay Ref.22. Source: UniProtKB

RNA polymerase II regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

activating transcription factor binding

Inferred from direct assay Ref.47. Source: BHF-UCL

arachidonic acid binding

Inferred from sequence or structural similarity PubMed 9568715. Source: BHF-UCL

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

drug binding

Inferred from direct assay Ref.47PubMed 9113987. Source: BHF-UCL

enzyme binding

Inferred from physical interaction Ref.18. Source: UniProtKB

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay Ref.47. 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

protein binding

Inferred from physical interaction PubMed 22078880. Source: IntAct

retinoid X receptor binding

Inferred from direct assay PubMed 9568715. Source: BHF-UCL

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 9568715. Source: BHF-UCL

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...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 505505Peroxisome proliferator-activated receptor gamma
PRO_0000053492

Regions

DNA binding136 – 21075Nuclear receptor
Zinc finger139 – 15921NR C4-type
Zinc finger176 – 19823NR C4-type
Region205 – 28076Interaction with FAM120B By similarity
Region317 – 505189Ligand-binding

Sites

Binding site3171Synthetic agonist
Binding site3511Synthetic agonist
Binding site4771Synthetic agonist
Binding site5011Synthetic agonist

Amino acid modifications

Modified residue1121Phosphoserine; by MAPK By similarity
Glycosylation841O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence1 – 2828Missing in isoform 1 and isoform 3.
VSP_003645
Alternative sequence207 – 2137AIRFGRM → EELQKDS in isoform 3.
VSP_043906
Alternative sequence214 – 504291Missing in isoform 3.
VSP_043907
Natural variant121P → A Significant independent determinant of CIMT; may protect from early atherosclerosis in subject at risk for diabetes; associated with BMI. Ref.12 Ref.41 Ref.43 Ref.44 Ref.45 Ref.46 Ref.50 Ref.51 Ref.52
Corresponds to variant rs1801282 [ dbSNP | Ensembl ].
VAR_010723
Natural variant401P → A.
Corresponds to variant rs1805192 [ dbSNP | Ensembl ].
VAR_016116
Natural variant1131P → Q in obesity. Ref.42
Corresponds to variant rs1800571 [ dbSNP | Ensembl ].
VAR_010724
Natural variant3141Q → P in colon cancer; sporadic; somatic mutation; loss of ligand-binding. Ref.46
Corresponds to variant rs28936407 [ dbSNP | Ensembl ].
VAR_010725
Natural variant3161R → H in colon cancer; sporadic; somatic mutation; partial loss of ligand-binding. Ref.46
Corresponds to variant rs28936407 [ dbSNP | Ensembl ].
VAR_010726
Natural variant3181V → M in diabetes. Ref.47
VAR_010727
Natural variant3881F → L in FPLD3. Ref.48
VAR_022700
Natural variant4251R → C in FPLD3. Ref.49
VAR_022701
Natural variant4951P → L in diabetes. Ref.47
VAR_010728

Experimental info

Sequence conflict36 – 372MP → IA in BAA18949. Ref.3
Sequence conflict213 – 2142MP → IA in BAA18949. Ref.3
Sequence conflict2401R → RQ in BAA18949. Ref.3

Secondary structure

...................................................................... 505
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified April 27, 2001. Version 3.
Checksum: 3933EFF36A0E4CAF

FASTA50557,620
        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 

« Hide

Isoform 1 (PPARgamma1(wt)) [UniParc].

Checksum: 1061C2074B739E0A
Show »

FASTA47754,681
Isoform 3 (PPARgamma1(tr)) [UniParc].

Checksum: 10E780305F860A5D
Show »

FASTA18621,580

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"THRAP3 interacts with HELZ2 and plays a novel role in adipocyte differentiation."
Katano-Toki A., Satoh T., Tomaru T., Yoshino S., Ishizuka T., Ishii S., Ozawa A., Shibusawa N., Tsuchiya T., Saito T., Shimizu H., Hashimoto K., Okada S., Yamada M., Mori M.
Mol. Endocrinol. 27:769-780(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HELZ2 AND THRAP3, SUBCELLULAR LOCATION.
[28]"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.
[29]"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.
[30]"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.
[31]"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.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
[36]"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.
[37]"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.
[38]"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.
[39]"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.
[40]"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.
[41]"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.
[42]"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.
[43]"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.
[44]"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.
[45]"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.
[46]"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.
[47]"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.
[48]"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.
[49]"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.
[50]"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.
[51]"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.
[52]"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

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.
CCDSCCDS2609.1. [P37231-1]
CCDS2610.2. [P37231-2]
PIRJC4859.
PC4290.
PC4429.
RefSeqNP_005028.4. NM_005037.5. [P37231-2]
NP_056953.2. NM_015869.4. [P37231-1]
NP_619725.2. NM_138711.3. [P37231-2]
NP_619726.2. NM_138712.3. [P37231-2]
XP_006713271.1. XM_006713208.1. [P37231-2]
UniGeneHs.162646.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FM6X-ray2.10D/X234-505[»]
1FM9X-ray2.10D234-505[»]
1I7IX-ray2.35A/B225-505[»]
1K74X-ray2.30D234-505[»]
1KNUX-ray2.50A/B232-505[»]
1NYXX-ray2.65A/B230-505[»]
1PRGX-ray2.20A/B235-504[»]
1RDTX-ray2.40D235-505[»]
1WM0X-ray2.90X232-505[»]
1ZEOX-ray2.50A/B231-505[»]
1ZGYX-ray1.80A234-505[»]
2ATHX-ray2.28A/B235-505[»]
2F4BX-ray2.07A/B235-505[»]
2FVJX-ray1.99A235-505[»]
2G0GX-ray2.54A/B235-505[»]
2G0HX-ray2.30A/B235-505[»]
2GTKX-ray2.10A235-505[»]
2HFPX-ray2.00A234-505[»]
2HWQX-ray1.97A/B235-505[»]
2HWRX-ray2.34A/B235-505[»]
2I4JX-ray2.10A/B223-504[»]
2I4PX-ray2.10A/B223-504[»]
2I4ZX-ray2.25A/B223-504[»]
2OM9X-ray2.80A/B/C/D232-505[»]
2P4YX-ray2.25A/B231-505[»]
2POBX-ray2.30A/B234-505[»]
2PRGX-ray2.30A/B235-505[»]
2Q59X-ray2.20A/B233-505[»]
2Q5PX-ray2.30A/B233-505[»]
2Q5SX-ray2.05A/B233-505[»]
2Q61X-ray2.20A/B233-505[»]
2Q6RX-ray2.41A/B233-505[»]
2Q6SX-ray2.40A/B233-505[»]
2Q8SX-ray2.30A/B235-505[»]
2QMVNMR-A235-504[»]
2VSRX-ray2.05A/B232-505[»]
2VSTX-ray2.35A/B232-505[»]
2VV0X-ray2.55A/B232-505[»]
2VV1X-ray2.20A/B232-505[»]
2VV2X-ray2.75A/B232-505[»]
2VV3X-ray2.85A/B232-505[»]
2VV4X-ray2.35A/B232-505[»]
2XKWX-ray2.02A/B232-505[»]
2YFEX-ray2.00A/B223-505[»]
2ZK0X-ray2.36A/B223-504[»]
2ZK1X-ray2.61A/B223-504[»]
2ZK2X-ray2.26A/B223-504[»]
2ZK3X-ray2.58A/B223-504[»]
2ZK4X-ray2.57A/B223-504[»]
2ZK5X-ray2.45A/B223-504[»]
2ZK6X-ray2.41A/B223-504[»]
2ZNOX-ray2.40A/B223-504[»]
2ZVTX-ray1.90A/B223-504[»]
3ADSX-ray2.25A/B223-505[»]
3ADTX-ray2.70A/B223-505[»]
3ADUX-ray2.77A/B223-505[»]
3ADVX-ray2.27A/B223-505[»]
3ADWX-ray2.07A/B223-505[»]
3ADXX-ray1.95A/B223-505[»]
3AN3X-ray2.30A/B223-504[»]
3AN4X-ray2.30A/B223-504[»]
3B0QX-ray2.10A/B231-504[»]
3B0RX-ray2.15A/B231-504[»]
3B1MX-ray1.60A234-505[»]
3B3KX-ray2.60A/B223-504[»]
3BC5X-ray2.27A231-505[»]
3CDPX-ray2.80A/B223-504[»]
3CDSX-ray2.65A/B223-504[»]
3CS8X-ray2.30A234-504[»]
3CWDX-ray2.40A/B236-505[»]
3D6DX-ray2.40A/B223-504[»]
3DZUX-ray3.20D102-505[»]
3DZYX-ray3.10D102-505[»]
3E00X-ray3.10D102-505[»]
3ET0X-ray2.40A/B235-505[»]
3ET3X-ray1.95A235-505[»]
3FEJX-ray2.01A235-505[»]
3FURX-ray2.30A234-505[»]
3G9EX-ray2.30A235-505[»]
3GBKX-ray2.30A/B235-505[»]
3H0AX-ray2.10D234-505[»]
3HO0X-ray2.60A/B223-504[»]
3HODX-ray2.10A/B223-504[»]
3IA6X-ray2.31A/B235-505[»]
3K8SX-ray2.55A/B234-505[»]
3KMGX-ray2.10A/D234-505[»]
3LMPX-ray1.90A234-505[»]
3NOAX-ray1.98A/B235-505[»]
3OSIX-ray2.70A/B224-504[»]
3OSWX-ray2.55A/B224-504[»]
3PBAX-ray2.30A/B224-505[»]
3PO9X-ray2.35A/B224-505[»]
3PRGX-ray2.90A232-505[»]
3QT0X-ray2.50A235-505[»]
3R5NX-ray2.00A232-505[»]
3R8AX-ray2.41A/B235-505[»]
3R8IX-ray2.30A/B223-505[»]
3S9SX-ray2.55A234-505[»]
3SZ1X-ray2.30A/B232-505[»]
3T03X-ray2.10A/B234-505[»]
3TY0X-ray2.00A/B231-505[»]
3U9QX-ray1.52A236-504[»]
3V9TX-ray1.65A234-505[»]
3V9VX-ray1.60A234-505[»]
3V9YX-ray2.10A234-505[»]
3VJHX-ray2.22A/B223-504[»]
3VJIX-ray2.61A/B223-504[»]
3VN2X-ray2.18A225-505[»]
3VSOX-ray2.00A/B223-504[»]
3VSPX-ray2.40A/B223-504[»]
4A4VX-ray2.00A/B223-505[»]
4A4WX-ray2.00A/B223-505[»]
4E4KX-ray2.50A/B223-505[»]
4E4QX-ray2.50A/B223-505[»]
4EM9X-ray2.10A/B235-505[»]
4EMAX-ray2.54A/B235-505[»]
4F9MX-ray1.90A234-505[»]
4FGYX-ray2.84A235-504[»]
4HEEX-ray2.50X235-505[»]
4JAZX-ray2.85A/B223-505[»]
4JL4X-ray2.50A/B223-505[»]
4PRGX-ray2.90A/B/C/D235-504[»]
DisProtDP00718.
ProteinModelPortalP37231.
SMRP37231. Positions 135-505.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111464. 89 interactions.
DIPDIP-35528N.
IntActP37231. 27 interactions.

Chemistry

BindingDBP37231.
ChEMBLCHEMBL235.
DrugBankDB01076. Atorvastatin.
DB00159. Icosapent.
DB01132. Pioglitazone.
DB00412. Rosiglitazone.
DB00197. Troglitazone.
GuidetoPHARMACOLOGY595.

PTM databases

PhosphoSiteP37231.

Polymorphism databases

DMDM13432234.

Proteomic databases

MaxQBP37231.
PaxDbP37231.
PRIDEP37231.

Protocols and materials databases

DNASU5468.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000287820; ENSP00000287820; ENSG00000132170. [P37231-1]
ENST00000309576; ENSP00000312472; ENSG00000132170. [P37231-2]
ENST00000396999; ENSP00000380195; ENSG00000132170. [P37231-3]
ENST00000397010; ENSP00000380205; ENSG00000132170. [P37231-2]
ENST00000397012; ENSP00000380207; ENSG00000132170. [P37231-2]
ENST00000397015; ENSP00000380210; ENSG00000132170. [P37231-2]
GeneID5468.
KEGGhsa:5468.
UCSCuc003bwr.3. human. [P37231-1]

Organism-specific databases

CTD5468.
GeneCardsGC03P012328.
HGNCHGNC:9236. PPARG.
HPACAB004282.
MIM137800. phenotype.
601487. gene.
601665. phenotype.
604367. phenotype.
606641. phenotype.
609338. phenotype.
neXtProtNX_P37231.
Orphanet79083. Familial partial lipodystrophy associated with PPARG mutations.
251579. Giant cell glioblastoma.
251576. Gliosarcoma.
PharmGKBPA281.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266867.
HOVERGENHBG106004.
InParanoidP37231.
KOK08530.
OMASTPHYED.
PhylomeDBP37231.
TreeFamTF316304.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_71. Gene Expression.
SignaLinkP37231.

Gene expression databases

ArrayExpressP37231.
BgeeP37231.
GenevestigatorP37231.

Family and domain databases

Gene3D1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProIPR003074. 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]
PfamPF00104. Hormone_recep. 1 hit.
PF12577. PPARgamma_N. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR01288. PROXISOMEPAR.
PR01291. PROXISOMPAGR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPARG. human.
EvolutionaryTraceP37231.
GeneWikiPeroxisome_proliferator-activated_receptor_gamma.
GenomeRNAi5468.
NextBio21164.
PROP37231.
SOURCESearch...

Entry information

Entry namePPARG_HUMAN
AccessionPrimary (citable) accession number: P37231
Secondary accession number(s): A8K3G6 expand/collapse secondary AC list , 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: July 9, 2014
This is version 199 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM