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P37238

- PPARG_MOUSE

UniProt

P37238 - PPARG_MOUSE

Protein

Peroxisome proliferator-activated receptor gamma

Gene

Pparg

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (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.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

    1. arachidonic acid binding Source: BHF-UCL
    2. chromatin binding Source: UniProtKB
    3. DNA binding Source: UniProtKB
    4. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: MGI
    5. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    6. protein binding Source: IntAct
    7. RNA polymerase II regulatory region DNA binding Source: MGI
    8. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
    9. sequence-specific DNA binding Source: InterPro
    10. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    11. steroid hormone receptor activity Source: InterPro
    12. transcription regulatory region DNA binding Source: UniProtKB
    13. zinc ion binding Source: InterPro

    GO - Biological processi

    1. brown fat cell differentiation Source: MGI
    2. cell fate commitment Source: MGI
    3. cellular response to lithium ion Source: MGI
    4. cellular response to organic cyclic compound Source: MGI
    5. epithelial cell differentiation Source: MGI
    6. fat cell differentiation Source: MGI
    7. inflammatory response Source: MGI
    8. intracellular receptor signaling pathway Source: GOC
    9. long-chain fatty acid transport Source: MGI
    10. negative regulation of cell proliferation Source: MGI
    11. negative regulation of cellular response to insulin stimulus Source: BHF-UCL
    12. negative regulation of cytokine production Source: BHF-UCL
    13. negative regulation of peptide hormone secretion Source: BHF-UCL
    14. negative regulation of transcription, DNA-templated Source: BHF-UCL
    15. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    16. placenta development Source: MGI
    17. positive regulation of fat cell differentiation Source: UniProtKB
    18. positive regulation of transcription, DNA-templated Source: UniProtKB
    19. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    20. regulation of fat cell differentiation Source: MGI
    21. regulation of transcription involved in cell fate commitment Source: UniProtKB
    22. response to lipid Source: BHF-UCL
    23. response to retinoic acid Source: UniProtKB
    24. white fat cell differentiation Source: HGNC

    Keywords - Molecular functioni

    Activator, Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198602. PPARA activates gene expression.
    REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    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: Unplaced

    Organism-specific databases

    MGIiMGI:97747. Pparg.

    Subcellular locationi

    Nucleus 2 PublicationsPROSITE-ProRule annotation. Cytoplasm By similarity
    Note: Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner By similarity. CCRN4L/NOC enhances its nuclear translocation.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: MGI
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    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.

    Gene expression databases

    ArrayExpressiP37238.
    BgeeiP37238.
    CleanExiMM_PPARG.
    GenevestigatoriP37238.

    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).12 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi202320. 27 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. Align

    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

    MGETLGDSPV DPEHGAFADA LPMSTSQEIT MVDTEMPFWP TNFGISSVDL    50
    SVMEDHSHSF DIKPFTTVDF SSISAPHYED IPFTRADPMV ADYKYDLKLQ 100
    EYQSAIKVEP ASPPYYSEKT QLYNRPHEEP SNSLMAIECR VCGDKASGFH 150
    YGVHACEGCK GFFRRTIRLK LIYDRCDLNC RIHKKSRNKC QYCRFQKCLA 200
    VGMSHNAIRF GRMPQAEKEK LLAEISSDID QLNPESADLR ALAKHLYDSY 250
    IKSFPLTKAK ARAILTGKTT DKSPFVIYDM NSLMMGEDKI KFKHITPLQE 300
    QSKEVAIRIF QGCQFRSVEA VQEITEYAKN IPGFINLDLN DQVTLLKYGV 350
    HEIIYTMLAS LMNKDGVLIS EGQGFMTREF LKNLRKPFGD FMEPKFEFAV 400
    KFNALELDDS DLAIFIAVII LSGDRPGLLN VKPIEDIQDN LLQALELQLK 450
    LNHPESSQLF AKVLQKMTDL RQIVTEHVQL LHVIKKTETD MSLHPLLQEI 500
    YKDLY 505
    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:
    EMBL
    GenBank
    DDBJ
    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_006505740.1.
    XP_006505804.1. XM_006505741.1.
    XP_006505805.1. XM_006505742.1.
    XP_006505806.1. XM_006505743.1.
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09138 mRNA. Translation: AAA62277.1 .
    U01664 mRNA. Translation: AAA62110.1 .
    U01841 mRNA. Translation: AAC52134.1 .
    U10374 mRNA. Translation: AAA19971.1 .
    CCDSi CCDS20439.1. [P37238-1 ]
    CCDS51876.1. [P37238-2 ]
    PIRi A54101.
    RefSeqi NP_001120802.1. NM_001127330.1.
    NP_035276.2. NM_011146.3.
    XP_006505803.1. XM_006505740.1.
    XP_006505804.1. XM_006505741.1.
    XP_006505805.1. XM_006505742.1.
    XP_006505806.1. XM_006505743.1.
    XP_006505807.1. XM_006505744.1.
    UniGenei Mm.3020.

    3D structure databases

    ProteinModelPortali P37238.
    SMRi P37238. Positions 135-505.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202320. 27 interactions.
    DIPi DIP-60435N.
    IntActi P37238. 4 interactions.
    STRINGi 10090.ENSMUSP00000000450.

    Chemistry

    BindingDBi P37238.
    ChEMBLi CHEMBL2459.

    PTM databases

    PhosphoSitei P37238.

    Proteomic databases

    PRIDEi P37238.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 19016.
    KEGGi mmu:19016.
    UCSCi uc012eqj.1. mouse. [P37238-2 ]

    Organism-specific databases

    CTDi 5468.
    MGIi MGI:97747. Pparg.

    Phylogenomic databases

    eggNOGi NOG266867.
    HOGENOMi HOG000261626.
    HOVERGENi HBG106004.
    InParanoidi P37238.
    KOi K08530.
    PhylomeDBi P37238.

    Enzyme and pathway databases

    Reactomei REACT_198602. PPARA activates gene expression.
    REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Miscellaneous databases

    NextBioi 295444.
    PROi P37238.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P37238.
    Bgeei P37238.
    CleanExi MM_PPARG.
    Genevestigatori P37238.

    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. "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. Cited for: FUNCTION, INTERACTION WITH PRDM16.
    12. "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.
    13. Cited for: FUNCTION IN ADIPOGENESIS, INTERACTION WITH PER2, PHOSPHORYLATION AT SER-112, MUTAGENESIS OF SER-112, TISSUE SPECIFICITY.
    14. "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.
    15. "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.
    16. "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.
    17. 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: October 1, 2014
    This is version 156 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