Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Pparg. (This text reflects annotations as of Wednesday, January 23, 2013.)

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a member of the peroxisome proliferator-activated receptor (PPAR) subfamily of nuclear receptors. PPARs form heterodimers with retinoid X receptors (RXRs) and these heterodimers regulate transcription of various genes. Three subtypes of PPARs are known: PPAR-alpha, PPAR-delta, and PPAR-gamma. The protein encoded by this gene is PPAR-gamma and is a regulator of adipocyte differentiation. Additionally, PPAR-gamma has been implicated in the pathology of numerous diseases including obesity, diabetes, atherosclerosis and cancer. Alternatively spliced transcript variants that encode different isoforms have been described. [provided by RefSeq, Jul 2008]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Pparg
  • participates in the following biological processes:
    • brown fat cell differentiation ^[29]
    • cellular response to lithium ion ^[28]
    • cellular response to organic cyclic compound ^[2]
    • fat cell differentiation ^{[8, 26]}
    • negative regulation of transcription from RNA polymerase II promoter ^{[, 18]}
    • negative regulation of transcription, DNA-dependent ^[18]
    • positive regulation of fat cell differentiation ^{[3, 14, 22]}
    • positive regulation of transcription from RNA polymerase II promoter ^{[8, 13, 18, 27]}
    • positive regulation of transcription, DNA-dependent ^{[6, 15]}
    • regulation of fat cell differentiation ^[10]
    • response to lipid ^[16]
    • response to retinoic acid ^[27]
    • white fat cell differentiation ^[29]
  • performs the following molecular functions:
    • arachidonic acid binding ^[16]
    • chromatin binding ^[17]
    • DNA binding ^{[, 8, 11, 27]}
    • ligand-dependent nuclear receptor transcription coactivator activity ^[27]
    • RNA polymerase II regulatory region DNA binding ^[14]
    • sequence-specific DNA binding transcription factor activity ^[8]
    • transcription regulatory region DNA binding ^[18]
  • is located in the following cellular components:
    • cytosol ^{[12, 25]}
    • nucleus ^{[7, 12, 25]}
• The gene product of Pparg has been shown to bind to the gene products of Med1, Pias1, Prdm16, Sirt1. ^{[18, 20, 21, 24, 30]} Researchers have inferred, based on physical interactions, that the gene product of Pparg
  • performs the following molecular functions:
    • DNA binding ^[11]
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Pparg
  • participates in the following biological processes:
    • long-chain fatty acid transport ^[23]
    • negative regulation of cell proliferation ^[9]
    • negative regulation of cytokine production ^[4]
    • negative regulation of transcription, DNA-dependent ^[11]
    • placenta development ^[23]
    • positive regulation of fat cell differentiation ^[17]
• Researchers have inferred, based on genetic interactions, that the gene product of Pparg
  • participates in the following biological processes:
    • cell fate commitment based on interactions with Tgfb1i1 ^[5]
    • epithelial cell differentiation based on interactions with Tgfb1i1 ^[5]
    • fat cell differentiation based on interactions with Wwtr1 ^[13]
    • positive regulation of fat cell differentiation based on interactions with Snai2 ^[19]
    • regulation of fat cell differentiation based on interactions with Ncor2 ^[17]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Pparg:
  • participates in the following biological processes:
    • activation of cysteine-type endopeptidase activity involved in apoptotic process
    • cell maturation
    • cellular response to insulin stimulus
    • fatty acid oxidation
    • glucose homeostasis
    • induction of apoptosis
    • lipoprotein transport
    • low-density lipoprotein particle receptor biosynthetic process
    • monocyte differentiation
    • negative regulation of acute inflammatory response
    • negative regulation of cell growth
    • negative regulation of cell proliferation
    • negative regulation of cholesterol storage
    • negative regulation of interferon-gamma-mediated signaling pathway
    • negative regulation of macrophage derived foam cell differentiation
    • negative regulation of receptor biosynthetic process
    • negative regulation of sequestering of triglyceride
    • negative regulation of smooth muscle cell proliferation
    • negative regulation of telomerase activity
    • negative regulation of transcription from RNA polymerase II promoter
    • peroxisome proliferator activated receptor signaling pathway
    • positive regulation of fatty acid oxidation
    • positive regulation of oligodendrocyte differentiation
    • positive regulation of sequence-specific DNA binding transcription factor activity
    • positive regulation of transcription from RNA polymerase II promoter
    • regulation of blood pressure
    • regulation of fat cell differentiation
    • regulation of lipid metabolic process
    • response to low-density lipoprotein particle stimulus
    • response to retinoic acid
    • signal transduction
  • performs the following molecular functions:
    • activating transcription factor binding
    • DNA binding
    • drug binding
    • enzyme binding
    • ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity
    • ligand-dependent nuclear receptor transcription coactivator activity
    • retinoid X receptor binding
    • sequence-specific DNA binding transcription factor activity
    • transcription regulatory region DNA binding
  • is located in the following cellular components:
    • cytosol
    • nucleus

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Summary text based on GO annotations supported by structural data

• Pparg encodes a protein or proteins that contain the following InterPro domains: Nuclear hormone receptor, ligand-binding, Nuclear hormone receptor, ligand-binding, core, Peroxisome proliferator-activated receptor, Peroxisome proliferator-activated receptor gamma, N-terminal, Peroxisome proliferator-activated receptor, gamma, Steroid hormone receptor, Zinc finger, NHR/GATA-type, Zinc finger, nuclear hormone receptor-type, indicating that the gene product:
  • participates in the following biological processes:
    • regulation of transcription, DNA-dependent
    • steroid hormone mediated signaling pathway
  • performs the following molecular functions:
    • sequence-specific DNA binding
    • steroid hormone receptor activity
    • zinc ion binding

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Pparg indicates that it:
  • participates in the following biological processes:
    • regulation of transcription, DNA-dependent
    • transcription, DNA-dependent
  • performs the following molecular functions:
    • metal ion binding
  • is located in the following cellular components:
    • cytoplasm

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References

1. . () , :. (PubMed:)
2. Bennett CN et al. (2002) Regulation of Wnt signaling during adipogenesis. J Biol Chem, 277:30998-1004. (PubMed:12055200)
3. Bennett CN et al. (2005) Regulation of osteoblastogenesis and bone mass by Wnt10b. Proc Natl Acad Sci U S A, 102:3324-9. (PubMed:15728361)
4. Bonfield TL et al. (2008) Peroxisome proliferator-activated receptor-gamma regulates the expression of alveolar macrophage macrophage colony-stimulating factor. J Immunol, 181:235-42. (PubMed:18566389)
5. Drori S et al. (2005) Hic-5 regulates an epithelial program mediated by PPARgamma. Genes Dev, 19:362-75. (PubMed:15687259)
6. Fan M et al. (2004) Suppression of mitochondrial respiration through recruitment of p160 myb binding protein to PGC-1alpha: modulation by p38 MAPK. Genes Dev, 18:278-89. (PubMed:14744933)
7. Fei Z et al. (2011) Ankrd26 gene disruption enhances adipogenesis of mouse embryonic fibroblasts. J Biol Chem, 286:27761-8. (PubMed:21669876)
8. Ge K et al. (2002) Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated adipogenesis. Nature, 417:563-7. (PubMed:12037571)
9. Girnun GD et al. (2002) APC-dependent suppression of colon carcinogenesis by PPARgamma. Proc Natl Acad Sci U S A, 99:13771-6. (PubMed:12370429)
10. Gray S et al. (2002) The Kruppel-like factor KLF15 regulates the insulin-sensitive glucose transporter GLUT4. J Biol Chem, 277:34322-8. (PubMed:12097321)
11. Guan HP et al. (2005) Corepressors selectively control the transcriptional activity of PPARgamma in adipocytes. Genes Dev, 19:453-61. (PubMed:15681609)
12. Guthmann F et al. (2004) Phenotype of palmitic acid transport and of signalling in alveolar type II cells from E/H-FABP double-knockout mice: contribution of caveolin-1 and PPARgamma. Biochim Biophys Acta, 1636:196-204. (PubMed:15164767)
13. Hong JH et al. (2005) TAZ, a transcriptional modulator of mesenchymal stem cell differentiation. Science, 309:1074-8. (PubMed:16099986)
14. Ichida F et al. (2004) Reciprocal roles of MSX2 in regulation of osteoblast and adipocyte differentiation. J Biol Chem, 279:34015-22. (PubMed:15175325)
15. Makowski L et al. (2005) The fatty acid-binding protein, aP2, coordinates macrophage cholesterol trafficking and inflammatory activity. Macrophage expression of aP2 impacts peroxisome proliferator-activated receptor gamma and IkappaB kinase activities. J Biol Chem, 280:12888-95. (PubMed:15684432)
16. Nagy L et al. (1998) Oxidized LDL regulates macrophage gene expression through ligand activation of PPARgamma. Cell, 93:229-40. (PubMed:9568715)
17. Nofsinger RR et al. (2008) SMRT repression of nuclear receptors controls the adipogenic set point and metabolic homeostasis. Proc Natl Acad Sci U S A, 105:20021-6. (PubMed:19066220)
18. Pascual G et al. (2005) A SUMOylation-dependent pathway mediates transrepression of inflammatory response genes by PPAR-gamma. Nature, 437:759-63. (PubMed:16127449)
19. Perez-Mancera PA et al. (2007) Adipose tissue mass is modulated by SLUG (SNAI2). Hum Mol Genet, 16:2972-86. (PubMed:17905753)
20. Picard F et al. (2004) Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma. Nature, 429:771-6. (PubMed:15175761)
21. Qiang L et al. (2012) Brown remodeling of white adipose tissue by SirT1-dependent deacetylation of Ppargamma. Cell, 150:620-32. (PubMed:22863012)
22. Ross SE et al. (2000) Inhibition of adipogenesis by Wnt signaling. Science, 289:950-3. (PubMed:10937998)
23. Schaiff WT et al. (2007) Ligand-activated peroxisome proliferator activated receptor gamma alters placental morphology and placental fatty acid uptake in mice. Endocrinology, 148:3625-34. (PubMed:17463056)
24. Seale P et al. (2008) PRDM16 controls a brown fat/skeletal muscle switch. Nature, 454:961-7. (PubMed:18719582)
25. Shibuya A et al. (2002) Nitration of PPARgamma inhibits ligand-dependent translocation into the nucleus in a macrophage-like cell line, RAW 264. FEBS Lett, 525:43-7. (PubMed:12163159)
26. Tang QQ et al. (2003) Mitotic clonal expansion: A synchronous process required for adipogenesis. Proc Natl Acad Sci U S A, 100:44-9. (PubMed:12502791)
27. Tomaru T et al. (2006) Isolation and characterization of a transcriptional cofactor and its novel isoform that bind the deoxyribonucleic acid-binding domain of peroxisome proliferator-activated receptor-gamma. Endocrinology, 147:377-88. (PubMed:16239304)
28. Vertino AM et al. (2005) Wnt10b deficiency promotes coexpression of myogenic and adipogenic programs in myoblasts. Mol Biol Cell, 16:2039-48. (PubMed:15673614)
29. Wu Y et al. (2008) Wdnm1-like, a new adipokine with a role in MMP-2 activation. Am J Physiol Endocrinol Metab, 295:E205-15. (PubMed:18492766)
30. Zhu Y et al. (1997) Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor. J Biol Chem, 272:25500-6. (PubMed:9325263)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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