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Protein Page:
PPAR-alpha (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
PPAR-alpha 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. 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. Belongs to the nuclear hormone receptor family. NR1 subfamily. Note: This description may include information from UniProtKB.
Protein type: DNA binding protein; Nuclear receptor
Cellular Component: nucleoplasm; nucleus
Molecular Function: protein domain specific binding; ligand-dependent nuclear receptor activity; NFAT protein binding; zinc ion binding; drug binding; phosphatase binding; protein binding; DNA binding; ubiquitin conjugating enzyme binding; sequence-specific DNA binding; protein complex binding; steroid hormone receptor activity; lipid binding; transcription factor activity
Biological Process: transcription initiation from RNA polymerase II promoter; epidermis development; intracellular receptor-mediated signaling pathway; wound healing; positive regulation of transcription, DNA-dependent; heart development; behavioral response to nicotine; lipoprotein metabolic process; cellular lipid metabolic process; negative regulation of transcription from RNA polymerase II promoter; fatty acid metabolic process; negative regulation of appetite; response to insulin stimulus; positive regulation of fatty acid beta-oxidation; positive regulation of fatty acid oxidation; response to hypoxia; positive regulation of transcription from RNA polymerase II promoter; gene expression; lipid metabolic process; negative regulation of blood pressure; negative regulation of protein binding; negative regulation of glycolysis; fatty acid transport
Reference #:  Q07869 (UniProtKB)
Alt. Names/Synonyms: hPPAR; MGC2237; MGC2452; NR1C1; Nuclear receptor subfamily 1 group C member 1; peroxisome proliferative activated receptor, alpha; Peroxisome proliferator-activated receptor alpha; PPAR; PPAR-alpha; PPARA; PPARalpha
Gene Symbols: PPARA
Molecular weight: 52,225 Da
Basal Isoelectric point: 5.86  Predict pI for various phosphorylation states
Select Structure to View Below

PPAR-alpha

Protein Structure Not Found.


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Sites Implicated In
transcription, altered: S179‑p, S230‑p
transcription, inhibited: S6‑p, S12‑p, S21‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
2 0 S6-p __MVDTEsPLCPLsP
2 0 S12-p EsPLCPLsPLEAGDL
3 0 S21-p LEAGDLEsPLSEEFL
1 0 S110 RICGDKASGYHYGVH
2 0 T129 CKGFFRRTIRLKLVY
1 0 S142 VYDKCDRSCKIQKKN
1 0 S163 CRFHKCLSVGMSHNA
2 0 S179-p RFGRMPRsEKAKLkA
1 0 K185-s RsEKAKLkAEILTCE
0 1 E196 LTCEHDIEDSETADL
0 1 K204 DSETADLKSLAKRIY
1 0 S230-p VKARVILsGKASNNP
0 1 K425 DDIFLFPKLLQKMAD
0 1 K429 LFPKLLQKMADLRQL
0 1 K449 QLVQIIKKTESDAAL
1 0 S452 QIIKKTESDAALHPL
  mouse

 
S6 __MVDTESPICPLSP
S12 ESPICPLSPLEADDL
S21 LEADDLESPLSEEFL
S110 RICGDKASGYHYGVH
T129 CKGFFRRTIRLKLVY
S142 VYDKCDRSCKIQKKN
S163 CRFHKCLSVGMSHNA
S179 RFGRMPRSEKAKLKA
K185 RSEKAKLKAEILTCE
K196-u LTCEHDLkDSETADL
K204-u DSETADLkSLGKRIH
A230 VKARVILAGKTSNNP
K425-u DDTFLFPkLLQkMVD
K429-u LFPkLLQkMVDLRQL
K449-u QLVQVIKkTEsDAAL
S452-p QVIKkTEsDAALHPL
  rat

 
S6 __MVDTESPICPLSP
S12 ESPICPLSPLEADDL
S21 LEADDLESPLSEEFL
S110-p RICGDKAsGYHYGVH
T129-p CKGFFRRtIRLKLAY
S142-p AYDKCDRsCKIQKKN
S163-p CRFHKCLsVGMSHNA
S179-p RFGRMPRsEKAKLKA
K185 RsEKAKLKAEILTCE
K196 LTCEHDLKDSETADL
K204 DSETADLKSLAKRIH
A230 VKARVILAGKTSNNP
K425 DDTFLFPKLLQKMVD
K429 LFPKLLQKMVDLRQL
K449 QLVQVIKKTESDAAL
S452 QVIKKTESDAALHPL
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