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P37231

- PPARG_HUMAN

UniProt

P37231 - PPARG_HUMAN

Protein

Peroxisome proliferator-activated receptor gamma

Gene

PPARG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 201 (01 Oct 2014)
      Sequence version 3 (27 Apr 2001)
      Previous versions | rss
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    Functioni

    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.4 Publications

    Enzyme regulationi

    PDPK1 activates its transcriptional activity independently of its kinase activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei317 – 3171Synthetic agonist9 Publications
    Binding sitei351 – 3511Synthetic agonist9 Publications
    Binding sitei477 – 4771Synthetic agonist9 Publications
    Binding sitei501 – 5011Synthetic agonist9 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi136 – 21075Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri139 – 15921NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri176 – 19823NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. activating transcription factor binding Source: BHF-UCL
    2. arachidonic acid binding Source: BHF-UCL
    3. chromatin binding Source: UniProtKB
    4. DNA binding Source: UniProtKB
    5. drug binding Source: BHF-UCL
    6. enzyme binding Source: UniProtKB
    7. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: BHF-UCL
    8. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    9. prostaglandin receptor activity Source: BHF-UCL
    10. protein binding Source: IntAct
    11. retinoid X receptor binding Source: BHF-UCL
    12. RNA polymerase II regulatory region DNA binding Source: Ensembl
    13. sequence-specific DNA binding Source: InterPro
    14. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    15. steroid hormone receptor activity Source: InterPro
    16. transcription regulatory region DNA binding Source: BHF-UCL
    17. zinc ion binding Source: InterPro

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
    2. brown fat cell differentiation Source: Ensembl
    3. cell fate commitment Source: BHF-UCL
    4. cell maturation Source: BHF-UCL
    5. cellular response to insulin stimulus Source: BHF-UCL
    6. cellular response to lithium ion Source: Ensembl
    7. epithelial cell differentiation Source: BHF-UCL
    8. fatty acid oxidation Source: Ensembl
    9. gene expression Source: Reactome
    10. glucose homeostasis Source: BHF-UCL
    11. G-protein coupled receptor signaling pathway Source: GOC
    12. heart development Source: Ensembl
    13. innate immune response Source: BHF-UCL
    14. lipid homeostasis Source: BHF-UCL
    15. lipid metabolic process Source: ProtInc
    16. lipoprotein transport Source: BHF-UCL
    17. long-chain fatty acid transport Source: BHF-UCL
    18. low-density lipoprotein particle receptor biosynthetic process Source: BHF-UCL
    19. monocyte differentiation Source: BHF-UCL
    20. negative regulation of acute inflammatory response Source: Ensembl
    21. negative regulation of cell growth Source: Ensembl
    22. negative regulation of cholesterol storage Source: BHF-UCL
    23. negative regulation of interferon-gamma-mediated signaling pathway Source: BHF-UCL
    24. negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
    25. negative regulation of receptor biosynthetic process Source: BHF-UCL
    26. negative regulation of sequestering of triglyceride Source: BHF-UCL
    27. negative regulation of smooth muscle cell proliferation Source: BHF-UCL
    28. negative regulation of telomerase activity Source: Ensembl
    29. negative regulation of transcription, DNA-templated Source: BHF-UCL
    30. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    31. organ regeneration Source: Ensembl
    32. peroxisome proliferator activated receptor signaling pathway Source: BHF-UCL
    33. placenta development Source: BHF-UCL
    34. positive regulation of fat cell differentiation Source: HGNC
    35. positive regulation of fatty acid oxidation Source: Ensembl
    36. positive regulation of oligodendrocyte differentiation Source: Ensembl
    37. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    38. positive regulation of transcription, DNA-templated Source: BHF-UCL
    39. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    40. regulation of blood pressure Source: BHF-UCL
    41. regulation of cholesterol transporter activity Source: BHF-UCL
    42. regulation of transcription involved in cell fate commitment Source: UniProtKB
    43. response to caffeine Source: Ensembl
    44. response to cold Source: Ensembl
    45. response to drug Source: Ensembl
    46. response to estrogen Source: Ensembl
    47. response to lipid Source: BHF-UCL
    48. response to low-density lipoprotein particle Source: BHF-UCL
    49. response to nutrient Source: ProtInc
    50. response to retinoic acid Source: UniProtKB
    51. response to vitamin A Source: Ensembl
    52. signal transduction Source: BHF-UCL
    53. transcription initiation from RNA polymerase II promoter Source: Reactome
    54. white fat cell differentiation Source: UniProtKB

    Keywords - Molecular functioni

    Activator, Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_15525. Nuclear Receptor transcription pathway.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinkiP37231.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisome proliferator-activated receptor gamma
    Short name:
    PPAR-gamma
    Alternative name(s):
    Nuclear receptor subfamily 1 group C member 3
    Gene namesi
    Name:PPARG
    Synonyms:NR1C3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9236. PPARG.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytosol Source: BHF-UCL
    2. nucleoplasm Source: Reactome
    3. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry.
    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti388 – 3881F → L in FPLD3. 1 Publication
    VAR_022700
    Natural varianti425 – 4251R → C in FPLD3. 1 Publication
    VAR_022701
    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.

    Keywords - Diseasei

    Diabetes mellitus, Disease mutation, Obesity

    Organism-specific databases

    MIMi137800. phenotype.
    601665. phenotype.
    604367. phenotype.
    606641. phenotype.
    609338. phenotype.
    Orphaneti79083. Familial partial lipodystrophy associated with PPARG mutations.
    251579. Giant cell glioblastoma.
    251576. Gliosarcoma.
    PharmGKBiPA281.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 505505Peroxisome proliferator-activated receptor gammaPRO_0000053492Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi84 – 841O-linked (GlcNAc)By similarity
    Modified residuei112 – 1121Phosphoserine; by MAPKBy similarity

    Post-translational modificationi

    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.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP37231.
    PaxDbiP37231.
    PRIDEiP37231.

    PTM databases

    PhosphoSiteiP37231.

    Expressioni

    Tissue specificityi

    Highest expression in adipose tissue. Lower in skeletal muscle, spleen, heart and liver. Also detectable in placenta, lung and ovary.1 Publication

    Gene expression databases

    ArrayExpressiP37231.
    BgeeiP37231.
    GenevestigatoriP37231.

    Organism-specific databases

    HPAiCAB004282.

    Interactioni

    Subunit structurei

    Interacts with FOXO1 (acetylated form) By similarity. Heterodimer with other nuclear receptors, such as RXRA. The heterodimer with the retinoic acid receptor RXRA is called adipocyte-specific transcription factor ARF6. Interacts with NCOA6 coactivator, leading to a strong increase in transcription of target genes. Interacts with coactivator PPARBP, leading to a mild increase in transcription of target genes. Interacts with NOCA7 in a ligand-inducible manner. Interacts with NCOA1 and NCOA2 LXXLL motifs. Interacts with ASXL1, ASXL2, DNTTIP2, FAM120B, MAP2K1/MEK1, NR0B2, PDPK1, PRDM16, PRMT2 and TGFB1I1. Interacts (when activated by agonist) with PPP5C. Interacts with HELZ2 and THRAP3; the interaction stimulates the transcriptional activity of PPARG. Interacts with PER2, the interaction is ligand dependent and blocks PPARG recruitment to target promoters. Interacts with CCRN4L/NOC.By similarity20 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDK5Q005352EBI-781416,EBI-1041567
    CLUP109093EBI-781384,EBI-1104674
    EDF1O608694EBI-781384,EBI-781301
    HTTP428584EBI-781384,EBI-466029
    SMARCD3Q6STE5-13EBI-781384,EBI-488506
    SMARCD3Q6STE5-23EBI-781384,EBI-488511

    Protein-protein interaction databases

    BioGridi111464. 89 interactions.
    DIPiDIP-35528N.
    IntActiP37231. 27 interactions.

    Structurei

    Secondary structure

    1
    505
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi140 – 1423
    Beta strandi148 – 1503
    Beta strandi151 – 1544
    Helixi157 – 16711
    Turni168 – 1703
    Helixi186 – 1883
    Helixi191 – 20010
    Helixi205 – 2073
    Turni214 – 2174
    Helixi218 – 2203
    Turni222 – 2265
    Turni228 – 2314
    Helixi237 – 25317
    Helixi258 – 2658
    Turni266 – 2683
    Beta strandi269 – 2713
    Beta strandi275 – 2773
    Helixi280 – 2867
    Turni287 – 2893
    Beta strandi290 – 2923
    Beta strandi294 – 2963
    Beta strandi297 – 2993
    Beta strandi301 – 3033
    Helixi305 – 32925
    Helixi334 – 3363
    Helixi339 – 36022
    Beta strandi361 – 3633
    Beta strandi366 – 3694
    Turni370 – 3734
    Beta strandi374 – 3774
    Helixi378 – 3836
    Turni385 – 3873
    Helixi388 – 3903
    Helixi393 – 40311
    Helixi409 – 42012
    Beta strandi423 – 4253
    Helixi431 – 45222
    Beta strandi454 – 4563
    Helixi459 – 48628
    Beta strandi488 – 4903
    Helixi495 – 5017

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    DisProtiDP00718.
    ProteinModelPortaliP37231.
    SMRiP37231. Positions 135-505.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP37231.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni205 – 28076Interaction with FAM120BBy similarityAdd
    BLAST
    Regioni317 – 505189Ligand-bindingAdd
    BLAST

    Sequence similaritiesi

    Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri139 – 15921NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri176 – 19823NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG266867.
    HOVERGENiHBG106004.
    InParanoidiP37231.
    KOiK08530.
    OMAiSTPHYED.
    PhylomeDBiP37231.
    TreeFamiTF316304.

    Family and domain databases

    Gene3Di1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProiIPR003074. 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]
    PfamiPF00104. Hormone_recep. 1 hit.
    PF12577. PPARgamma_N. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view]
    PRINTSiPR01288. PROXISOMEPAR.
    PR01291. PROXISOMPAGR.
    PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTiSM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view]
    SUPFAMiSSF48508. SSF48508. 1 hit.
    PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 2 (identifier: P37231-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGETLGDSPI DPESDSFTDT LSANISQEMT MVDTEMPFWP TNFGISSVDL    50
    SVMEDHSHSF DIKPFTTVDF SSISTPHYED IPFTRTDPVV ADYKYDLKLQ 100
    EYQSAIKVEP ASPPYYSEKT QLYNKPHEEP SNSLMAIECR VCGDKASGFH 150
    YGVHACEGCK GFFRRTIRLK LIYDRCDLNC RIHKKSRNKC QYCRFQKCLA 200
    VGMSHNAIRF GRMPQAEKEK LLAEISSDID QLNPESADLR ALAKHLYDSY 250
    IKSFPLTKAK ARAILTGKTT DKSPFVIYDM NSLMMGEDKI KFKHITPLQE 300
    QSKEVAIRIF QGCQFRSVEA VQEITEYAKS IPGFVNLDLN DQVTLLKYGV 350
    HEIIYTMLAS LMNKDGVLIS EGQGFMTREF LKSLRKPFGD FMEPKFEFAV 400
    KFNALELDDS DLAIFIAVII LSGDRPGLLN VKPIEDIQDN LLQALELQLK 450
    LNHPESSQLF AKLLQKMTDL RQIVTEHVQL LQVIKKTETD MSLHPLLQEI 500
    YKDLY 505
    Length:505
    Mass (Da):57,620
    Last modified:April 27, 2001 - v3
    Checksum:i3933EFF36A0E4CAF
    GO
    Isoform 1 (identifier: P37231-2) [UniParc]FASTAAdd to Basket

    Also known as: PPARgamma1(wt)

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

    Show »
    Length:477
    Mass (Da):54,681
    Checksum:i1061C2074B739E0A
    GO
    Isoform 3 (identifier: P37231-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:186
    Mass (Da):21,580
    Checksum:i10E780305F860A5D
    GO

    Sequence cautioni

    The sequence AAN38992.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    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.
    The sequence BAA23354.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 372MP → IA in BAA18949. (PubMed:9144532)Curated
    Sequence conflicti213 – 2142MP → IA in BAA18949. (PubMed:9144532)Curated
    Sequence conflicti240 – 2401R → RQ in BAA18949. (PubMed:9144532)Curated

    Polymorphismi

    Genetic variation in PPARG may influence body mass index (BMI) [MIMi:606641]. BMI reflects the amount of fat, lean mass, and body build.
    Genetic variations in PPARG influence the carotid intimal medial thickness (CIMT) [MIMi: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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121P → A Significant independent determinant of CIMT; may protect from early atherosclerosis in subject at risk for diabetes; associated with BMI. 5 Publications
    Corresponds to variant rs1801282 [ dbSNP | Ensembl ].
    VAR_010723
    Natural varianti40 – 401P → A.
    Corresponds to variant rs1805192 [ dbSNP | Ensembl ].
    VAR_016116
    Natural varianti113 – 1131P → Q in obesity. 1 Publication
    Corresponds to variant rs1800571 [ dbSNP | Ensembl ].
    VAR_010724
    Natural varianti314 – 3141Q → P in colon cancer; sporadic; somatic mutation; loss of ligand-binding. 1 Publication
    Corresponds to variant rs28936407 [ dbSNP | Ensembl ].
    VAR_010725
    Natural varianti316 – 3161R → H in colon cancer; sporadic; somatic mutation; partial loss of ligand-binding. 1 Publication
    Corresponds to variant rs28936407 [ dbSNP | Ensembl ].
    VAR_010726
    Natural varianti318 – 3181V → M in diabetes. 1 Publication
    VAR_010727
    Natural varianti388 – 3881F → L in FPLD3. 1 Publication
    VAR_022700
    Natural varianti425 – 4251R → C in FPLD3. 1 Publication
    VAR_022701
    Natural varianti495 – 4951P → L in diabetes. 1 Publication
    VAR_010728

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828Missing in isoform 1 and isoform 3. 7 PublicationsVSP_003645Add
    BLAST
    Alternative sequencei207 – 2137AIRFGRM → EELQKDS in isoform 3. 1 PublicationVSP_043906
    Alternative sequencei214 – 504291Missing in isoform 3. 1 PublicationVSP_043907Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS2609.1. [P37231-1]
    CCDS2610.2. [P37231-2]
    PIRiJC4859.
    PC4290.
    PC4429.
    RefSeqiNP_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]
    UniGeneiHs.162646.

    Genome annotation databases

    EnsembliENST00000287820; 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]
    GeneIDi5468.
    KEGGihsa:5468.
    UCSCiuc003bwr.3. human. [P37231-1]

    Polymorphism databases

    DMDMi13432234.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Wikipedia

    Peroxisome proliferator-activated receptor entry

    SeattleSNPs
    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS2609.1. [P37231-1 ]
    CCDS2610.2. [P37231-2 ]
    PIRi JC4859.
    PC4290.
    PC4429.
    RefSeqi NP_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 ]
    UniGenei Hs.162646.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    3VSO X-ray 2.00 A/B 223-504 [» ]
    3VSP X-ray 2.40 A/B 223-504 [» ]
    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 [» ]
    4FGY X-ray 2.84 A 235-504 [» ]
    4HEE X-ray 2.50 X 235-505 [» ]
    4JAZ X-ray 2.85 A/B 223-505 [» ]
    4JL4 X-ray 2.50 A/B 223-505 [» ]
    4PRG X-ray 2.90 A/B/C/D 235-504 [» ]
    DisProti DP00718.
    ProteinModelPortali P37231.
    SMRi P37231. Positions 135-505.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111464. 89 interactions.
    DIPi DIP-35528N.
    IntActi P37231. 27 interactions.

    Chemistry

    BindingDBi P37231.
    ChEMBLi CHEMBL235.
    DrugBanki DB01076. Atorvastatin.
    DB00159. Icosapent.
    DB01132. Pioglitazone.
    DB00412. Rosiglitazone.
    DB00197. Troglitazone.
    GuidetoPHARMACOLOGYi 595.

    PTM databases

    PhosphoSitei P37231.

    Polymorphism databases

    DMDMi 13432234.

    Proteomic databases

    MaxQBi P37231.
    PaxDbi P37231.
    PRIDEi P37231.

    Protocols and materials databases

    DNASUi 5468.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000287820 ; 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 ]
    GeneIDi 5468.
    KEGGi hsa:5468.
    UCSCi uc003bwr.3. human. [P37231-1 ]

    Organism-specific databases

    CTDi 5468.
    GeneCardsi GC03P012328.
    HGNCi HGNC:9236. PPARG.
    HPAi CAB004282.
    MIMi 137800. phenotype.
    601487. gene.
    601665. phenotype.
    604367. phenotype.
    606641. phenotype.
    609338. phenotype.
    neXtProti NX_P37231.
    Orphaneti 79083. Familial partial lipodystrophy associated with PPARG mutations.
    251579. Giant cell glioblastoma.
    251576. Gliosarcoma.
    PharmGKBi PA281.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG266867.
    HOVERGENi HBG106004.
    InParanoidi P37231.
    KOi K08530.
    OMAi STPHYED.
    PhylomeDBi P37231.
    TreeFami TF316304.

    Enzyme and pathway databases

    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_15525. Nuclear Receptor transcription pathway.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinki P37231.

    Miscellaneous databases

    ChiTaRSi PPARG. human.
    EvolutionaryTracei P37231.
    GeneWikii Peroxisome_proliferator-activated_receptor_gamma.
    GenomeRNAii 5468.
    NextBioi 21164.
    PROi P37231.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P37231.
    Bgeei P37231.
    Genevestigatori P37231.

    Family and domain databases

    Gene3Di 1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProi 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 ]
    Pfami PF00104. Hormone_recep. 1 hit.
    PF12577. PPARgamma_N. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view ]
    PRINTSi PR01288. PROXISOMEPAR.
    PR01291. PROXISOMPAGR.
    PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTi SM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48508. SSF48508. 1 hit.
    PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiPPARG_HUMAN
    AccessioniPrimary (citable) accession number: P37231
    Secondary accession number(s): A8K3G6
    , B5BUA1, O00684, O00710, O14515, Q0QJH8, Q15178, Q15179, Q15180, Q15832, Q86U60, Q96J12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 201 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3