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Protein

Peroxisome proliferator-activated receptor gamma

Gene

Pparg

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of ARNTL/BMAL1 in the blood vessels (PubMed:19041764).5 Publications

Enzyme regulationi

PDPK1 activates its transcriptional activity independently of its kinase activity.By similarity

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

  • activating transcription factor binding Source: MGI
  • alpha-actinin binding Source: MGI
  • arachidonic acid binding Source: BHF-UCL
  • chromatin binding Source: UniProtKB
  • core promoter sequence-specific DNA binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • drug binding Source: MGI
  • enzyme binding Source: MGI
  • ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: MGI
  • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  • retinoid X receptor binding Source: MGI
  • RNA polymerase II regulatory region DNA binding Source: MGI
  • RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  • sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • steroid hormone receptor activity Source: InterPro
  • transcription regulatory region DNA binding Source: UniProtKB
  • WW domain binding Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  • brown fat cell differentiation Source: MGI
  • cell fate commitment Source: MGI
  • cell maturation Source: MGI
  • cellular response to insulin stimulus Source: MGI
  • cellular response to lithium ion Source: MGI
  • cellular response to organic cyclic compound Source: MGI
  • diet induced thermogenesis Source: MGI
  • epithelial cell differentiation Source: MGI
  • fat cell differentiation Source: MGI
  • glucose homeostasis Source: MGI
  • inflammatory response Source: MGI
  • lipoprotein transport Source: MGI
  • long-chain fatty acid transport Source: MGI
  • low-density lipoprotein particle receptor biosynthetic process Source: MGI
  • monocyte differentiation Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of cellular response to insulin stimulus Source: BHF-UCL
  • negative regulation of cholesterol storage Source: MGI
  • negative regulation of cytokine production Source: BHF-UCL
  • negative regulation of interferon-gamma-mediated signaling pathway Source: MGI
  • negative regulation of macrophage derived foam cell differentiation Source: MGI
  • negative regulation of peptide hormone secretion Source: BHF-UCL
  • negative regulation of receptor biosynthetic process Source: MGI
  • negative regulation of sequestering of triglyceride Source: MGI
  • negative regulation of smooth muscle cell proliferation Source: MGI
  • negative regulation of transcription, DNA-templated Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • peroxisome proliferator activated receptor signaling pathway Source: MGI
  • placenta development Source: MGI
  • positive regulation of fat cell differentiation Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of blood pressure Source: MGI
  • regulation of circadian rhythm Source: UniProtKB
  • regulation of fat cell differentiation Source: MGI
  • regulation of gene expression Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription involved in cell fate commitment Source: UniProtKB
  • response to dietary excess Source: MGI
  • response to food Source: UniProtKB
  • response to light stimulus Source: UniProtKB
  • response to lipid Source: BHF-UCL
  • response to low-density lipoprotein particle Source: MGI
  • response to retinoic acid Source: UniProtKB
  • rhythmic process Source: UniProtKB-KW
  • signal transduction Source: MGI
  • white fat cell differentiation Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
REACT_309805. Transcriptional regulation of white adipocyte differentiation.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:97747. Pparg.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • RNA polymerase II transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice develop abnormalities in circadian variations in blood pressure and heart rate, in parallel with a reduction of diurnal variations in the sympathetic nerve activity, and impaired rhythmicity of ARNTL/BMAL1 in the blood vessels.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1121S → A: Increases basal and ligand-induced adipogenic activity. Abolishes repression by PER2 on transactivation activity. 2 Publications
Mutagenesisi112 – 1121S → D: No effect on repression by PER2 on transactivation activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 505505Peroxisome proliferator-activated receptor gammaPRO_0000053494Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi84 – 841O-linked (GlcNAc)1 Publication
Modified residuei112 – 1121Phosphoserine; by MAPK2 Publications

Post-translational modificationi

O-GlcNAcylation at Thr-84 reduces transcriptional activity in adipocytes.
Phosphorylated in basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated Ser-112 form is recognized by PER2 and repressed, dephosphorylation at Ser-112 induces adipogenic activity. Ser-112 phosphorylation levels are reduced by 65% in brown adipose tissue compared to white adipose tissue.2 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiP37238.

PTM databases

PhosphoSiteiP37238.

Expressioni

Tissue specificityi

Highest expression in white and brown adipose tissue. Also found in liver, skeletal muscle, heart, adrenal gland, spleen, kidney and intestine. Isoform 2 is more abundant than isoform 1 in adipose tissue.2 Publications

Developmental stagei

It appears first at 13.5 dpc and increases until birth.

Inductioni

Expressed in a circadian manner in the aorta.1 Publication

Gene expression databases

BgeeiP37238.
CleanExiMM_PPARG.
GenevisibleiP37238. MM.

Interactioni

Subunit structurei

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. Interacts with FOXO1 (acetylated form). Interacts with ACTN4 (By similarity).By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SIRT1Q96EB63EBI-5260705,EBI-1802965From a different organism.
Sirt1Q923E42EBI-5260705,EBI-1802585

Protein-protein interaction databases

BioGridi202320. 35 interactions.
DIPiDIP-60435N.
IntActiP37238. 4 interactions.
STRINGi10090.ENSMUSP00000000450.

Structurei

3D structure databases

ProteinModelPortaliP37238.
SMRiP37238. Positions 135-505.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni205 – 28076Interaction with FAM120BAdd
BLAST
Regioni317 – 505189Ligand-bindingBy similarityAdd
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.
HOGENOMiHOG000261626.
HOVERGENiHBG106004.
InParanoidiP37238.
KOiK08530.
PhylomeDBiP37238.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: P37238-1) [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

        10         20         30         40         50
MGETLGDSPV DPEHGAFADA LPMSTSQEIT MVDTEMPFWP TNFGISSVDL
60 70 80 90 100
SVMEDHSHSF DIKPFTTVDF SSISAPHYED IPFTRADPMV ADYKYDLKLQ
110 120 130 140 150
EYQSAIKVEP ASPPYYSEKT QLYNRPHEEP SNSLMAIECR VCGDKASGFH
160 170 180 190 200
YGVHACEGCK GFFRRTIRLK LIYDRCDLNC RIHKKSRNKC QYCRFQKCLA
210 220 230 240 250
VGMSHNAIRF GRMPQAEKEK LLAEISSDID QLNPESADLR ALAKHLYDSY
260 270 280 290 300
IKSFPLTKAK ARAILTGKTT DKSPFVIYDM NSLMMGEDKI KFKHITPLQE
310 320 330 340 350
QSKEVAIRIF QGCQFRSVEA VQEITEYAKN IPGFINLDLN DQVTLLKYGV
360 370 380 390 400
HEIIYTMLAS LMNKDGVLIS EGQGFMTREF LKNLRKPFGD FMEPKFEFAV
410 420 430 440 450
KFNALELDDS DLAIFIAVII LSGDRPGLLN VKPIEDIQDN LLQALELQLK
460 470 480 490 500
LNHPESSQLF AKVLQKMTDL RQIVTEHVQL LHVIKKTETD MSLHPLLQEI

YKDLY
Length:505
Mass (Da):57,598
Last modified:April 27, 2001 - v3
Checksum:iAB8F3F6086E2A10A
GO
Isoform 1 (identifier: P37238-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.

Show »
Length:475
Mass (Da):54,512
Checksum:iFD80BD50D9197D3F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 2142MP → DR in AAA62110 (PubMed:8240342).Curated
Sequence conflicti281 – 2833NSL → SSF in AAA62110 (PubMed:8240342).Curated
Sequence conflicti383 – 3831N → S in AAA62110 (PubMed:8240342).Curated
Sequence conflicti383 – 3831N → S in AAA19971 (PubMed:8041794).Curated
Sequence conflicti497 – 4971L → F in AAA62110 (PubMed:8240342).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3030Missing in isoform 1. 3 PublicationsVSP_003647Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09138 mRNA. Translation: AAA62277.1.
U01664 mRNA. Translation: AAA62110.1.
U01841 mRNA. Translation: AAC52134.1.
U10374 mRNA. Translation: AAA19971.1.
CCDSiCCDS20439.1. [P37238-1]
CCDS51876.1. [P37238-2]
PIRiA54101.
RefSeqiNP_001120802.1. NM_001127330.1.
NP_035276.2. NM_011146.3.
XP_006505803.1. XM_006505740.2.
XP_006505806.1. XM_006505743.2.
XP_006505807.1. XM_006505744.1.
UniGeneiMm.3020.

Genome annotation databases

GeneIDi19016.
KEGGimmu:19016.
UCSCiuc012eqj.1. mouse. [P37238-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09138 mRNA. Translation: AAA62277.1.
U01664 mRNA. Translation: AAA62110.1.
U01841 mRNA. Translation: AAC52134.1.
U10374 mRNA. Translation: AAA19971.1.
CCDSiCCDS20439.1. [P37238-1]
CCDS51876.1. [P37238-2]
PIRiA54101.
RefSeqiNP_001120802.1. NM_001127330.1.
NP_035276.2. NM_011146.3.
XP_006505803.1. XM_006505740.2.
XP_006505806.1. XM_006505743.2.
XP_006505807.1. XM_006505744.1.
UniGeneiMm.3020.

3D structure databases

ProteinModelPortaliP37238.
SMRiP37238. Positions 135-505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202320. 35 interactions.
DIPiDIP-60435N.
IntActiP37238. 4 interactions.
STRINGi10090.ENSMUSP00000000450.

Chemistry

BindingDBiP37238.
ChEMBLiCHEMBL2459.

PTM databases

PhosphoSiteiP37238.

Proteomic databases

PRIDEiP37238.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi19016.
KEGGimmu:19016.
UCSCiuc012eqj.1. mouse. [P37238-2]

Organism-specific databases

CTDi5468.
MGIiMGI:97747. Pparg.

Phylogenomic databases

eggNOGiNOG266867.
HOGENOMiHOG000261626.
HOVERGENiHBG106004.
InParanoidiP37238.
KOiK08530.
PhylomeDBiP37238.

Enzyme and pathway databases

ReactomeiREACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
REACT_309805. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

NextBioi295444.
PROiP37238.
SOURCEiSearch...

Gene expression databases

BgeeiP37238.
CleanExiMM_PPARG.
GenevisibleiP37238. MM.

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]
ProtoNetiSearch...

Publicationsi

  1. "mPPAR gamma 2: tissue-specific regulator of an adipocyte enhancer."
    Tontonoz P., Hu E., Graves R.A., Budavari A.I., Spiegelman B.M.
    Genes Dev. 8:1224-1234(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBUNIT.
    Tissue: Adipose tissue.
  2. "Identification of two mPPAR related receptors and evidence for the existence of five subfamily members."
    Chen F., Law S.W., O'Malley B.W.
    Biochem. Biophys. Res. Commun. 196:671-677(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/c.
    Tissue: Heart.
  3. "Cloning of a new member of the peroxisome proliferator-activated receptor gene family from mouse liver."
    Zhu Y., Alvares K., Huang Q., Rao M.S., Reddy J.K.
    J. Biol. Chem. 268:26817-26820(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6 X CBA.
    Tissue: Liver.
  4. "Differential expression and activation of a family of murine peroxisome proliferator-activated receptors."
    Kliewer S.A., Forman B.M., Blumberg B., Ong E.S., Borgmeyer U., Mangelsdorf D.J., Umesono K., Evans R.M.
    Proc. Natl. Acad. Sci. U.S.A. 91:7355-7359(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  5. "Regulation of PPAR gamma gene expression by nutrition and obesity in rodents."
    Vidal-Puig A., Jimenez-Linan M., Lowell B.B., Hamann A., Hu E., Spiegelman B., Flier J.S., Moller D.E.
    J. Clin. Invest. 97:2553-2561(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "Adipocyte-specific transcription factor ARF6 is a heterodimeric complex of two nuclear hormone receptors, PPAR gamma and RXR alpha."
    Tontonoz P., Graves R.A., Budavari A.I., Erdjument-Bromage H., Lui M., Hu E., Tempst P., Spiegelman B.M.
    Nucleic Acids Res. 22:5628-5634(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 66-85 AND 146-160, SUBUNIT, TISSUE SPECIFICITY.
    Tissue: Adipose tissue.
  7. "Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor."
    Zhu Y., Qi C., Jain S., Rao M.S., Reddy J.K.
    J. Biol. Chem. 272:25500-25506(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPARBP.
  8. "Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR."
    Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S., Reddy J.K.
    J. Biol. Chem. 275:13510-13516(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCOA6.
  9. Cited for: INTERACTION WITH TGFB1I1.
  10. "Constitutive coactivator of peroxisome proliferator-activated receptor (PPARgamma), a novel coactivator of PPARgamma that promotes adipogenesis."
    Li D., Kang Q., Wang D.-M.
    Mol. Endocrinol. 21:2320-2333(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM120B.
  11. "Vascular PPARgamma controls circadian variation in blood pressure and heart rate through Bmal1."
    Wang N., Yang G., Jia Z., Zhang H., Aoyagi T., Soodvilai S., Symons J.D., Schnermann J.B., Gonzalez F.J., Litwin S.E., Yang T.
    Cell Metab. 8:482-491(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION.
  12. Cited for: FUNCTION, INTERACTION WITH PRDM16.
  13. "SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive interaction with PPARgamma."
    Wang F., Tong Q.
    Mol. Biol. Cell 20:801-808(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FOXO1.
  14. Cited for: FUNCTION IN ADIPOGENESIS, INTERACTION WITH PER2, PHOSPHORYLATION AT SER-112, MUTAGENESIS OF SER-112, TISSUE SPECIFICITY.
  15. "A circadian-regulated gene, Nocturnin, promotes adipogenesis by stimulating PPAR-gamma nuclear translocation."
    Kawai M., Green C.B., Lecka-Czernik B., Douris N., Gilbert M.R., Kojima S., Ackert-Bicknell C., Garg N., Horowitz M.C., Adamo M.L., Clemmons D.R., Rosen C.J.
    Proc. Natl. Acad. Sci. U.S.A. 107:10508-10513(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CCRN4L.
  16. "Protein phosphatase 5 mediates lipid metabolism through reciprocal control of glucocorticoid receptor and peroxisome proliferator-activated receptor-? (PPAR?)."
    Hinds T.D. Jr., Stechschulte L.A., Cash H.A., Whisler D., Banerjee A., Yong W., Khuder S.S., Kaw M.K., Shou W., Najjar S.M., Sanchez E.R.
    J. Biol. Chem. 286:42911-42922(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ADIPOGENESIS, INTERACTION WITH PPP5C, PHOSPHORYLATION AT SER-112, DEPHOSPHORYLATION AT SER-112, MUTAGENESIS OF SER-112.
  17. "O-GlcNAc modification of PPARgamma reduces its transcriptional activity."
    Ji S., Park S.Y., Roth J., Kim H.S., Cho J.W.
    Biochem. Biophys. Res. Commun. 417:1158-1163(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-84.
  18. Cited for: FUNCTION, INTERACTION WITH HELZ2 AND THRAP3, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPPARG_MOUSE
AccessioniPrimary (citable) accession number: P37238
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: April 27, 2001
Last modified: June 24, 2015
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.