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Protein Page:
PPAR-alpha (mouse)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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: Nuclear receptor; DNA binding protein
Cellular Component: nucleus
Molecular Function: protein domain specific binding; ligand-dependent nuclear receptor activity; NFAT protein binding; zinc ion binding; metal ion binding; drug binding; receptor activity; phosphatase binding; protein binding; DNA binding; ubiquitin conjugating enzyme binding; sequence-specific DNA binding; protein heterodimerization activity; protein complex binding; steroid hormone receptor activity; lipid binding; transcription factor activity
Biological Process: transcription from RNA polymerase II promoter; epidermis development; wound healing; positive regulation of transcription, DNA-dependent; rhythmic process; behavioral response to nicotine; negative regulation of transcription from RNA polymerase II promoter; fatty acid metabolic process; negative regulation of appetite; response to insulin stimulus; positive regulation of gluconeogenesis; regulation of transcription, DNA-dependent; regulation of fatty acid metabolic process; negative regulation of blood pressure; circadian regulation of gene expression; negative regulation of protein binding; intracellular receptor-mediated signaling pathway; transcription, DNA-dependent; glucose metabolic process; lipoprotein metabolic process; regulation of circadian rhythm; regulation of gene expression; positive regulation of fatty acid oxidation; response to hypoxia; steroid hormone mediated signaling; positive regulation of transcription from RNA polymerase II promoter; lipid metabolic process
Reference #:  P23204 (UniProtKB)
Alt. Names/Synonyms: 4933429D07Rik; AW742785; Nr1c1; Nuclear receptor subfamily 1 group C member 1; OTTMUSP00000027777; OTTMUSP00000027778; OTTMUSP00000027779; peroxisome proliferator activated receptor alpha; Peroxisome proliferator-activated receptor alpha; Ppar; PPAR-alpha; Ppara; PPARalpha
Gene Symbols: Ppara
Molecular weight: 52,347 Da
Basal Isoelectric point: 5.78  Predict pI for various phosphorylation states
Select Structure to View Below

PPAR-alpha

Protein Structure Not Found.


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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.


       mouse

 
2 0 S6 __MVDTESPICPLSP
2 0 S12 ESPICPLSPLEADDL
3 0 S21 LEADDLESPLSEEFL
0 1 S45 SQSIGEESSGSFGFA
1 0 S110 RICGDKASGYHYGVH
2 0 T129 CKGFFRRTIRLKLVY
1 0 S142 VYDKCDRSCKIQKKN
1 0 S163 CRFHKCLSVGMSHNA
2 0 S179 RFGRMPRSEKAKLKA
1 0 K185 RSEKAKLKAEILTCE
0 1 K196-ub LTCEHDLkDSETADL
0 1 K204-ub DSETADLkSLGKRIH
1 0 A230 VKARVILAGKTSNNP
0 1 Y311-p DQVTLLKyGVyEAIF
0 1 Y314-p TLLKyGVyEAIFtML
0 1 T319-p GVyEAIFtMLSSLMN
0 1 K425-ub DDTFLFPkLLQkMVD
0 1 K429-ub LFPkLLQkMVDLRQL
0 1 K449-ub QLVQVIKkTEsDAAL
1 0 S452-p QVIKkTEsDAALHPL
  human

 
S6-p __MVDTEsPLCPLsP
S12-p EsPLCPLsPLEAGDL
S21-p LEAGDLEsPLSEEFL
S45-p SQSIGEDsSGSFGFT
S110 RICGDKASGYHYGVH
T129 CKGFFRRTIRLKLVY
S142 VYDKCDRSCKIQKKN
S163 CRFHKCLSVGMSHNA
S179-p RFGRMPRsEKAKLkA
K185-sm RsEKAKLkAEILTCE
E196 LTCEHDIEDSETADL
K204 DSETADLKSLAKRIY
S230-p VKARVILsGKASNNP
Y311 DQVTLLKYGVYEAIF
Y314 TLLKYGVYEAIFAML
A319 GVYEAIFAMLSSVMN
K425 DDIFLFPKLLQKMAD
K429 LFPKLLQKMADLRQL
K449 QLVQIIKKTESDAAL
S452 QIIKKTESDAALHPL
  rat

 
S6 __MVDTESPICPLSP
S12 ESPICPLSPLEADDL
S21 LEADDLESPLSEEFL
S45 SQSLGEESSGSFSFA
S110-p RICGDKAsGYHYGVH
T129-p CKGFFRRtIRLKLAY
S142-p AYDKCDRsCKIQKKN
S163-p CRFHKCLsVGMSHNA
S179-p RFGRMPRsEKAKLKA
K185 RsEKAKLKAEILTCE
K196 LTCEHDLKDSETADL
K204 DSETADLKSLAKRIH
A230 VKARVILAGKTSNNP
Y311 DQVTLLKYGVYEAIF
Y314 TLLKYGVYEAIFTML
T319 GVYEAIFTMLSSLMN
K425 DDTFLFPKLLQKMVD
K429 LFPKLLQKMVDLRQL
K449 QLVQVIKKTESDAAL
S452 QVIKKTESDAALHPL
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