CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006724
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peroxisome proliferator-activated receptor gamma 
Protein Synonyms/Alias
 PPAR-gamma; Nuclear receptor subfamily 1 group C member 3 
Gene Name
 PPARG 
Gene Synonyms/Alias
 NR1C3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
63HSHSFDIKPFTTVDFsumoylation[1]
107QEYQSAIKVEPASPPsumoylation[1, 2, 3, 4, 5, 6]
364MLASLMNKDGVLISEsumoylation[4, 5, 6]
395FGDFMEPKFEFAVKFsumoylation[7]
Reference
 [1] Effect of a peroxisome proliferator-activated receptor gamma sumoylation mutant on neointimal formation after balloon injury in rats.
 Lim S, Ahn BY, Chung SS, Park HS, Cho BJ, Kim M, Choi SH, Lee IK, Lee SW, Choi SJ, Chung CH, Cho YM, Lee HK, Park KS.
 Atherosclerosis. 2009 Oct;206(2):411-7. [PMID: 19339015]
 [2] Control of peroxisome proliferator-activated receptor gamma2 stability and activity by SUMOylation.
 Floyd ZE, Stephens JM.
 Obes Res. 2004 Jun;12(6):921-8. [PMID: 15229330]
 [3] The transactivating function of peroxisome proliferator-activated receptor gamma is negatively regulated by SUMO conjugation in the amino-terminal domain.
 Yamashita D, Yamaguchi T, Shimizu M, Nakata N, Hirose F, Osumi T.
 Genes Cells. 2004 Nov;9(11):1017-29. [PMID: 15507114]
 [4] SUMO modification selectively regulates transcriptional activity of peroxisome-proliferator-activated receptor γ in C2C12 myotubes.
 Chung SS, Ahn BY, Kim M, Kho JH, Jung HS, Park KS.
 Biochem J. 2011 Jan 1;433(1):155-61. [PMID: 20950277]
 [5] The story so far: post-translational regulation of peroxisome proliferator-activated receptors by ubiquitination and SUMOylation.
 Wadosky KM, Willis MS.
 Am J Physiol Heart Circ Physiol. 2012 Feb 1;302(3):H515-26. [PMID: 22037188]
 [6] Controlling a master switch of adipocyte development and insulin sensitivity: covalent modifications of PPARγ.
 Floyd ZE, Stephens JM.
 Biochim Biophys Acta. 2012 Jul;1822(7):1090-5. [PMID: 22504298]
 [7] A SUMOylation-dependent pathway mediates transrepression of inflammatory response genes by PPAR-gamma.
 Pascual G, Fong AL, Ogawa S, Gamliel A, Li AC, Perissi V, Rose DW, Willson TM, Rosenfeld MG, Glass CK.
 Nature. 2005 Sep 29;437(7059):759-63. [PMID: 16127449] 
Functional Description
 Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to a promoter element in the gene for acyl-CoA oxidase and activates its transcription. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B- mediated proinflammatory responses. 
Sequence Annotation
 DNA_BIND 136 210 Nuclear receptor.
 ZN_FING 139 159 NR C4-type.
 ZN_FING 176 198 NR C4-type.
 REGION 205 280 Interaction with FAM120B (By similarity).
 REGION 317 505 Ligand-binding.
 BINDING 317 317 Synthetic agonist.
 BINDING 351 351 Synthetic agonist.
 BINDING 477 477 Synthetic agonist.
 BINDING 501 501 Synthetic agonist.
 MOD_RES 112 112 Phosphoserine; by MAPK (By similarity).
 CARBOHYD 84 84 O-linked (GlcNAc...) (By similarity).  
Keyword
 3D-structure; Activator; Alternative splicing; Complete proteome; Cytoplasm; Diabetes mellitus; Disease mutation; DNA-binding; Glycoprotein; Metal-binding; Nucleus; Obesity; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 505 AA 
Protein Sequence
MGETLGDSPI DPESDSFTDT LSANISQEMT MVDTEMPFWP TNFGISSVDL SVMEDHSHSF 60
DIKPFTTVDF SSISTPHYED IPFTRTDPVV ADYKYDLKLQ EYQSAIKVEP ASPPYYSEKT 120
QLYNKPHEEP SNSLMAIECR VCGDKASGFH YGVHACEGCK GFFRRTIRLK LIYDRCDLNC 180
RIHKKSRNKC QYCRFQKCLA VGMSHNAIRF GRMPQAEKEK LLAEISSDID QLNPESADLR 240
ALAKHLYDSY IKSFPLTKAK ARAILTGKTT DKSPFVIYDM NSLMMGEDKI KFKHITPLQE 300
QSKEVAIRIF QGCQFRSVEA VQEITEYAKS IPGFVNLDLN DQVTLLKYGV HEIIYTMLAS 360
LMNKDGVLIS EGQGFMTREF LKSLRKPFGD FMEPKFEFAV KFNALELDDS DLAIFIAVII 420
LSGDRPGLLN VKPIEDIQDN LLQALELQLK LNHPESSQLF AKLLQKMTDL RQIVTEHVQL 480
LQVIKKTETD MSLHPLLQEI YKDLY 505 
Gene Ontology
 GO:0005829; C:cytosol; ISS:BHF-UCL.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0033613; F:activating transcription factor binding; IDA:BHF-UCL.
 GO:0050544; F:arachidonic acid binding; ISS:BHF-UCL.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0008144; F:drug binding; IDA:BHF-UCL.
 GO:0004879; F:ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity; IDA:BHF-UCL.
 GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:UniProtKB.
 GO:0004955; F:prostaglandin receptor activity; TAS:BHF-UCL.
 GO:0046965; F:retinoid X receptor binding; IDA:BHF-UCL.
 GO:0001012; F:RNA polymerase II regulatory region DNA binding; IEA:Compara.
 GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
 GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
 GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
 GO:0050873; P:brown fat cell differentiation; IEA:Compara.
 GO:0045165; P:cell fate commitment; ISS:BHF-UCL.
 GO:0048469; P:cell maturation; IDA:BHF-UCL.
 GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
 GO:0071285; P:cellular response to lithium ion; IEA:Compara.
 GO:0030855; P:epithelial cell differentiation; ISS:BHF-UCL.
 GO:0019395; P:fatty acid oxidation; IEA:Compara.
 GO:0042593; P:glucose homeostasis; IMP:BHF-UCL.
 GO:0007507; P:heart development; IEA:Compara.
 GO:0045087; P:innate immune response; TAS:BHF-UCL.
 GO:0055088; P:lipid homeostasis; TAS:BHF-UCL.
 GO:0006629; P:lipid metabolic process; TAS:ProtInc.
 GO:0042953; P:lipoprotein transport; IDA:BHF-UCL.
 GO:0015909; P:long-chain fatty acid transport; ISS:BHF-UCL.
 GO:0045713; P:low-density lipoprotein particle receptor biosynthetic process; IDA:BHF-UCL.
 GO:0030224; P:monocyte differentiation; IDA:BHF-UCL.
 GO:0002674; P:negative regulation of acute inflammatory response; IEA:Compara.
 GO:0030308; P:negative regulation of cell growth; IEA:Compara.
 GO:0010887; P:negative regulation of cholesterol storage; IDA:BHF-UCL.
 GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; IMP:BHF-UCL.
 GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
 GO:0010871; P:negative regulation of receptor biosynthetic process; IDA:BHF-UCL.
 GO:0010891; P:negative regulation of sequestering of triglyceride; IDA:BHF-UCL.
 GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
 GO:0051974; P:negative regulation of telomerase activity; IEA:Compara.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:0031100; P:organ regeneration; IEA:Compara.
 GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IMP:BHF-UCL.
 GO:0001890; P:placenta development; ISS:BHF-UCL.
 GO:0045600; P:positive regulation of fat cell differentiation; ISS:HGNC.
 GO:0046321; P:positive regulation of fatty acid oxidation; IEA:Compara.
 GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Compara.
 GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0008217; P:regulation of blood pressure; IMP:BHF-UCL.
 GO:0060694; P:regulation of cholesterol transporter activity; IC:BHF-UCL.
 GO:0031000; P:response to caffeine; IEA:Compara.
 GO:0009409; P:response to cold; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0043627; P:response to estrogen stimulus; IEA:Compara.
 GO:0055098; P:response to low-density lipoprotein particle stimulus; IDA:BHF-UCL.
 GO:0007584; P:response to nutrient; TAS:ProtInc.
 GO:0032526; P:response to retinoic acid; IDA:UniProtKB.
 GO:0033189; P:response to vitamin A; IEA:Compara.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0050872; P:white fat cell differentiation; TAS:UniProtKB. 
Interpro
 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. 
Pfam
 PF00104; Hormone_recep
 PF12577; PPARgamma_N
 PF00105; zf-C4 
SMART
 SM00430; HOLI
 SM00399; ZnF_C4 
PROSITE
 PS00031; NUCLEAR_REC_DBD_1
 PS51030; NUCLEAR_REC_DBD_2 
PRINTS
 PR01288; PROXISOMEPAR.
 PR01291; PROXISOMPAGR.
 PR00398; STRDHORMONER.
 PR00047; STROIDFINGER.