CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011535
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peroxisome proliferator-activated receptor alpha 
Protein Synonyms/Alias
 PPAR-alpha; Nuclear receptor subfamily 1 group C member 1 
Gene Name
 PPARA 
Gene Synonyms/Alias
 NR1C1; PPAR 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
185RSEKAKLKAEILTCEsumoylation[1]
358FCDIMEPKFDFAMKFsumoylation[2]
Reference
 [1] SUMOylation of human peroxisome proliferator-activated receptor alpha inhibits its trans-activity through the recruitment of the nuclear corepressor NCoR.
 Pourcet B, Pineda-Torra I, Derudas B, Staels B, Glineur C.
 J Biol Chem. 2010 Feb 26;285(9):5983-92. [PMID: 19955185]
 [2] Sumoylated PPARalpha mediates sex-specific gene repression and protects the liver from estrogen-induced toxicity in mice.
 Leuenberger N, Pradervand S, Wahli W.
 J Clin Invest. 2009 Oct;119(10):3138-48. [PMID: 19729835
Functional Description
 Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl- 2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety (By similarity). Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. 
Sequence Annotation
 DNA_BIND 99 173 Nuclear receptor.
 ZN_FING 102 122 NR C4-type.
 ZN_FING 139 161 NR C4-type.
 REGION 280 468 Ligand-binding.
 REGION 304 433 Required for heterodimerization with
 BINDING 280 280 Synthetic agonist.
 BINDING 314 314 Synthetic agonist.
 BINDING 440 440 Synthetic agonist.
 BINDING 464 464 Synthetic agonist.  
Keyword
 3D-structure; Activator; Alternative splicing; Complete proteome; DNA-binding; Lipid-binding; Metal-binding; Nucleus; Polymorphism; Receptor; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 468 AA 
Protein Sequence
MVDTESPLCP LSPLEAGDLE SPLSEEFLQE MGNIQEISQS IGEDSSGSFG FTEYQYLGSC 60
PGSDGSVITD TLSPASSPSS VTYPVVPGSV DESPSGALNI ECRICGDKAS GYHYGVHACE 120
GCKGFFRRTI RLKLVYDKCD RSCKIQKKNR NKCQYCRFHK CLSVGMSHNA IRFGRMPRSE 180
KAKLKAEILT CEHDIEDSET ADLKSLAKRI YEAYLKNFNM NKVKARVILS GKASNNPPFV 240
IHDMETLCMA EKTLVAKLVA NGIQNKEAEV RIFHCCQCTS VETVTELTEF AKAIPGFANL 300
DLNDQVTLLK YGVYEAIFAM LSSVMNKDGM LVAYGNGFIT REFLKSLRKP FCDIMEPKFD 360
FAMKFNALEL DDSDISLFVA AIICCGDRPG LLNVGHIEKM QEGIVHVLRL HLQSNHPDDI 420
FLFPKLLQKM ADLRQLVTEH AQLVQIIKKT ESDAALHPLL QEIYRDMY 468 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0008144; F:drug binding; IDA:UniProtKB.
 GO:0004879; F:ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity; IDA:UniProtKB.
 GO:0008289; F:lipid binding; IDA:UniProtKB.
 GO:0043565; F:sequence-specific DNA binding; ISS:BHF-UCL.
 GO:0003707; F:steroid hormone receptor activity; IDA:BHF-UCL.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0035095; P:behavioral response to nicotine; IEA:Compara.
 GO:0070166; P:enamel mineralization; IEA:Compara.
 GO:0008544; P:epidermis development; IEA:Compara.
 GO:0006631; P:fatty acid metabolic process; TAS:ProtInc.
 GO:0015908; P:fatty acid transport; TAS:UniProtKB.
 GO:0007507; P:heart development; IEA:Compara.
 GO:0042157; P:lipoprotein metabolic process; IEA:Compara.
 GO:0032099; P:negative regulation of appetite; ISS:UniProtKB.
 GO:0045776; P:negative regulation of blood pressure; IEA:Compara.
 GO:0010887; P:negative regulation of cholesterol storage; IDA:BHF-UCL.
 GO:0045820; P:negative regulation of glycolysis; IC:BHF-UCL.
 GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
 GO:1901215; P:negative regulation of neuron death; IEA:Compara.
 GO:0032091; P:negative regulation of protein binding; IEA:Compara.
 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:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IEA:Compara.
 GO:0032000; P:positive regulation of fatty acid beta-oxidation; TAS:UniProtKB.
 GO:0072366; P:regulation of cellular ketone metabolic process by positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:0072363; P:regulation of glycolysis by positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:0072369; P:regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0032868; P:response to insulin stimulus; IEA:Compara.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0042060; P:wound healing; IEA:Compara. 
Interpro
 IPR003074; 1Cnucl_rcpt.
 IPR003076; 1Cnucl_rcpt_A.
 IPR008946; Nucl_hormone_rcpt_ligand-bd.
 IPR000536; Nucl_hrmn_rcpt_lig-bd_core.
 IPR001723; Str_hrmn_rcpt.
 IPR001628; Znf_hrmn_rcpt.
 IPR013088; Znf_NHR/GATA. 
Pfam
 PF00104; Hormone_recep
 PF00105; zf-C4 
SMART
 SM00430; HOLI
 SM00399; ZnF_C4 
PROSITE
 PS00031; NUCLEAR_REC_DBD_1
 PS51030; NUCLEAR_REC_DBD_2 
PRINTS
 PR01288; PROXISOMEPAR.
 PR01289; PROXISOMPAAR.
 PR00398; STRDHORMONER.
 PR00047; STROIDFINGER.