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Q07869 (PPARA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisome proliferator-activated receptor alpha

Short name=PPAR-alpha
Alternative name(s):
Nuclear receptor subfamily 1 group C member 1
Gene names
Name:PPARA
Synonyms:NR1C1, PPAR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. May be required for the propagation of clock information to metabolic pathways regulated by PER2. Ref.1 Ref.13 Ref.15 Ref.16

Subunit structure

Heterodimer; with RXRA. This heterodimerization is required for DNA binding and transactivation activity. Interacts with NCOA3 coactivator. Interacts with CITED2; the interaction stimulates its transcriptional activity. Also interacts with PPARBP in vitro. Interacts with AKAP13, LPIN1, PRDM16 and coactivator NCOA6. Interacts with ASXL1 AND ASXL2. Interacts with PER2. Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.20

Subcellular location

Nucleus.

Tissue specificity

Skeletal muscle, liver, heart and kidney. Ref.2 Ref.3

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processBiological rhythms
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandDNA-binding
Lipid-binding
Metal-binding
Zinc
   Molecular functionActivator
Receptor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to nicotine

Inferred from electronic annotation. Source: Ensembl

cellular lipid metabolic process

Traceable author statement. Source: Reactome

circadian regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

enamel mineralization

Inferred from electronic annotation. Source: Ensembl

epidermis development

Inferred from electronic annotation. Source: Ensembl

fatty acid metabolic process

Traceable author statement PubMed 10377439. Source: ProtInc

fatty acid transport

Traceable author statement PubMed 16271724. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

heart development

Inferred from electronic annotation. Source: Ensembl

intracellular receptor signaling pathway

Inferred from direct assay Ref.19PubMed 19955185. Source: GOC

lipid metabolic process

Traceable author statement Ref.1PubMed 9792666. Source: ProtInc

lipoprotein metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of appetite

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

negative regulation of cholesterol storage

Inferred from direct assay PubMed 19114110. Source: BHF-UCL

negative regulation of glycolytic process

Inferred by curator PubMed 19955185. Source: BHF-UCL

negative regulation of macrophage derived foam cell differentiation

Inferred from direct assay PubMed 19114110. Source: BHF-UCL

negative regulation of neuron death

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of receptor biosynthetic process

Inferred from direct assay PubMed 12700342. Source: BHF-UCL

negative regulation of sequestering of triglyceride

Inferred from direct assay PubMed 12700342. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12700342. Source: BHF-UCL

negative regulation of transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of fatty acid beta-oxidation

Traceable author statement PubMed 16271724. Source: UniProtKB

positive regulation of fatty acid oxidation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19955185PubMed 20837115. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.19. Source: UniProtKB

regulation of cellular ketone metabolic process by positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19955185. Source: BHF-UCL

regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of glycolytic by positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19955185. Source: BHF-UCL

regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19955185. Source: BHF-UCL

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement PubMed 16271724. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement PubMed 10860941. Source: ProtInc

RNA polymerase II repressing transcription factor binding

Inferred from physical interaction PubMed 19955185. Source: BHF-UCL

drug binding

Inferred from direct assay Ref.19. Source: UniProtKB

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay Ref.19. Source: UniProtKB

lipid binding

Inferred from direct assay Ref.19. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.18PubMed 9653119. Source: UniProtKB

sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 19955185. Source: BHF-UCL

steroid hormone receptor activity

Inferred from direct assay PubMed 19955185. Source: BHF-UCL

ubiquitin conjugating enzyme binding

Inferred from physical interaction PubMed 19955185. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CHD9Q3L8U1-32EBI-78615,EBI-960730

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q07869-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q07869-2)

The sequence of this isoform differs from the canonical sequence as follows:
     171-174: IRFG → FCHT
     175-468: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 468468Peroxisome proliferator-activated receptor alpha
PRO_0000053481

Regions

DNA binding99 – 17375Nuclear receptor
Zinc finger102 – 12221NR C4-type
Zinc finger139 – 16123NR C4-type
Region280 – 468189Ligand-binding
Region304 – 433130Required for heterodimerization with RXRA

Sites

Binding site2801Synthetic agonist
Binding site3141Synthetic agonist
Binding site4401Synthetic agonist
Binding site4641Synthetic agonist
Site4331Essential for heterodimerization with RXRA

Natural variations

Alternative sequence171 – 1744IRFG → FCHT in isoform 2.
VSP_047571
Alternative sequence175 – 468294Missing in isoform 2.
VSP_047572
Natural variant1271R → Q.
Corresponds to variant rs1800204 [ dbSNP | Ensembl ].
VAR_016110
Natural variant1621L → V. Ref.10
Corresponds to variant rs1800206 [ dbSNP | Ensembl ].
VAR_016111
Natural variant2271V → A.
Corresponds to variant rs1800234 [ dbSNP | Ensembl ].
VAR_016112
Natural variant2681A → V. Ref.1
Corresponds to variant rs1042311 [ dbSNP | Ensembl ].
VAR_016113
Natural variant3041D → N.
Corresponds to variant rs1800242 [ dbSNP | Ensembl ].
VAR_016114
Natural variant3951G → R.
Corresponds to variant rs2229245 [ dbSNP | Ensembl ].
VAR_050578
Natural variant4091R → T.
Corresponds to variant rs1800243 [ dbSNP | Ensembl ].
VAR_016115

Experimental info

Mutagenesis1221C → G: Prevents DNA binding but no effect on heterodimerization with RXRA. Ref.13
Mutagenesis3041D → A: Reduced heterodimerization with RXRA. Reduced DNA binding. Ref.16
Mutagenesis3701L → R: Abolishes heterodimerization with RXRA. No DNA binding. Ref.16
Mutagenesis3911L → R: Abolishes heterodimerization with RXRA. No DNA binding. Ref.16
Mutagenesis4221L → R: No effect on heterodimerization with RXRA nor on DNA binding and transactivation activity. Ref.13
Mutagenesis4311A → T: No effect on heterodimerization with RXRA nor on DNA binding. Ref.16
Mutagenesis4331L → R: Abolishes heterodimerization with RXRA, DNA binding and transactivation activity. Ref.13
Sequence conflict711T → M in CAA68898. Ref.3
Sequence conflict1231K → M in CAA68898. Ref.3
Sequence conflict2961G → A in AAA36468. Ref.1
Sequence conflict4441V → A in CAA68898. Ref.3

Secondary structure

.......................................... 468
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 850846FD51ADA883

FASTA46852,225
        10         20         30         40         50         60 
MVDTESPLCP LSPLEAGDLE SPLSEEFLQE MGNIQEISQS IGEDSSGSFG FTEYQYLGSC 

        70         80         90        100        110        120 
PGSDGSVITD TLSPASSPSS VTYPVVPGSV DESPSGALNI ECRICGDKAS GYHYGVHACE 

       130        140        150        160        170        180 
GCKGFFRRTI RLKLVYDKCD RSCKIQKKNR NKCQYCRFHK CLSVGMSHNA IRFGRMPRSE 

       190        200        210        220        230        240 
KAKLKAEILT CEHDIEDSET ADLKSLAKRI YEAYLKNFNM NKVKARVILS GKASNNPPFV 

       250        260        270        280        290        300 
IHDMETLCMA EKTLVAKLVA NGIQNKEAEV RIFHCCQCTS VETVTELTEF AKAIPGFANL 

       310        320        330        340        350        360 
DLNDQVTLLK YGVYEAIFAM LSSVMNKDGM LVAYGNGFIT REFLKSLRKP FCDIMEPKFD 

       370        380        390        400        410        420 
FAMKFNALEL DDSDISLFVA AIICCGDRPG LLNVGHIEKM QEGIVHVLRL HLQSNHPDDI 

       430        440        450        460 
FLFPKLLQKM ADLRQLVTEH AQLVQIIKKT ESDAALHPLL QEIYRDMY 

« Hide

Isoform 2 [UniParc].

Checksum: 8587321146D06A03
Show »

FASTA17418,942

References

« Hide 'large scale' references
[1]"cDNA cloning, chromosomal mapping, and functional characterization of the human peroxisome proliferator activated receptor."
Sher T., Yi H.F., McBride O.W., Gonzales F.J.
Biochemistry 32:5598-5604(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANT VAL-268.
Tissue: Liver.
[2]"Human and rat peroxisome proliferator activated receptors (PPARs) demonstrate similar tissue distribution but different responsiveness to PPAR activators."
Mukherjee R., Jow L., Noonan D., McDonnell D.P.
J. Steroid Biochem. Mol. Biol. 51:157-166(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Liver.
[3]"Peroxisome proliferator-activated receptors: structures and function."
Tugwood J.D., Aldridge T.C., Lambe K.G., Macdonald N., Woodyatt N.J.
Ann. N. Y. Acad. Sci. 804:252-265(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[4]"DNA-binding profiling of human hormone nuclear receptors via fluorescence correlation spectroscopy in a cell-free system."
Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T.
FEBS Lett. 582:2737-2744(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"Optimization of an enzyme-linked immunosorbent assay to screen ligand of Peroxisome proliferator-activated receptor alpha."
Cho M.-C., Lee S., Choi H.S., Yang Y., Tae Hong J., Kim S.J., Yoon D.-Y.
Immunopharmacol. Immunotoxicol. 31:459-467(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]"A novel alternatively spliced peroxisome proliferator-activated receptor alpha."
Jiang Y., Xie Z., Liu H., Liu M., Liu F.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[7]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[9]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[10]SeattleSNPs variation discovery resource
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-162.
[11]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]"Peroxisome proliferator-activated receptor mediates cross-talk with thyroid hormone receptor by competition for retinoid X receptor. Possible role of a leucine zipper-like heptad repeat."
Juge-Aubry C.E., Gorla-Bajszczak A., Pernin A., Lemberger T., Wahli W., Burger A.G., Meier C.A.
J. Biol. Chem. 270:18117-18122(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: HETERODIMERIZATION WITH RXRA, FUNCTION, MUTAGENESIS OF CYS-122; LEU-422 AND LEU-433.
[14]"RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2."
Li H., Gomes P.J., Chen J.D.
Proc. Natl. Acad. Sci. U.S.A. 94:8479-8484(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA3.
[15]"Regulation of peroxisome proliferator-activated receptor alpha-induced transactivation by the nuclear orphan receptor TAK1/TR4."
Yan Z.H., Karam W.G., Staudinger J.L., Medvedev A., Ghanayem B.I., Jetten A.M.
J. Biol. Chem. 273:10948-10957(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Conserved amino acids in the ligand-binding and tau(i) domains of the peroxisome proliferator-activated receptor alpha are necessary for heterodimerization with RXR."
Gorla-Bajszczak A., Juge-Aubry C., Pernin A., Burger A.G., Meier C.A.
Mol. Cell. Endocrinol. 147:37-47(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: HETERODIMERIZATION WITH RXRA, FUNCTION, MUTAGENESIS OF ASP-304; LEU-370; LEU-391 AND ALA-431.
[17]"Cloning and characterization of RAP250, a nuclear receptor coactivator."
Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.
J. Biol. Chem. 275:5308-5317(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA6.
[18]"Interaction of hepatitis C virus core protein with retinoid X receptor alpha modulates its transcriptional activity."
Tsutsumi T., Suzuki T., Shimoike T., Suzuki R., Moriya K., Shintani Y., Fujie H., Matsuura Y., Koike K., Miyamura T.
Hepatology 35:937-946(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: HETERODIMERIZATION WITH RXRA.
[19]"Oleylethanolamide regulates feeding and body weight through activation of the nuclear receptor PPAR-alpha."
Fu J., Gaetani S., Oveisi F., Lo Verme J., Serrano A., Rodriguez De Fonseca F., Rosengarth A., Luecke H., Di Giacomo B., Tarzia G., Piomelli D.
Nature 425:90-93(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS RECEPTOR FOR OLEYLETHANOLAMIDE.
[20]"Additional sex comb-like (ASXL) proteins 1 and 2 play opposite roles in adipogenesis via reciprocal regulation of peroxisome proliferator-activated receptor {gamma}."
Park U.H., Yoon S.K., Park T., Kim E.J., Um S.J.
J. Biol. Chem. 286:1354-1363(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASXL1 AND ASXL2.
[21]"Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors."
Xu H.E., Lambert M.H., Montana V.G., Plunket K.D., Moore L.B., Collins J.L., Oplinger J.A., Kliewer S.A., Gampe R.T. Jr., McKee D.D., Moore J.T., Willson T.M.
Proc. Natl. Acad. Sci. U.S.A. 98:13919-13924(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 192-468 IN COMPLEX WITH SYNTHETIC AGONIST.
[22]"Structure of the PPARalpha and -gamma ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family."
Cronet P., Petersen J.F.W., Folmer R., Blomberg N., Sjoeblom K., Karlsson U., Lindstedt E.-L., Bamberg K.
Structure 9:699-706(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 196-468 IN COMPLEX WITH SYNTHETIC AGONIST.
[23]"Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha."
Xu H.E., Stanley T.B., Montana V.G., Lambert M.H., Shearer B.G., Cobb J.E., McKee D.D., Galardi C.M., Plunket K.D., Nolte R.T., Parks D.J., Moore J.T., Kliewer S.A., Willson T.M., Stimmel J.B.
Nature 415:813-817(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 200-468 IN COMPLEX WITH SYNTHETIC AGONIST.
[24]"Design and synthesis of oxime ethers of alpha-acyl-beta-phenylpropanoic acids as PPAR dual agonists."
Oon Han H., Kim S.H., Kim K.-H., Hur G.-C., Joo Yim H., Chung H.-K., Ho Woo S., Dong Koo K., Lee C.-S., Sung Koh J., Kim G.T.
Bioorg. Med. Chem. Lett. 17:937-941(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 199-468 IN COMPLEX WITH SYNTHETIC AGONIST.
[25]"Substituted 2-[(4-aminomethyl)phenoxy]-2-methylpropionic acid PPARalpha agonists. 1. Discovery of a novel series of potent HDLc raising agents."
Sierra M.L., Beneton V., Boullay A.-B., Boyer T., Brewster A.G., Donche F., Forest M.-C., Fouchet M.-H., Gellibert F.J., Grillot D.A., Lambert M.H., Laroze A., Le Grumelec C., Linget J.M., Montana V.G., Nguyen V.-L., Nicodeme E., Patel V. expand/collapse author list , Penfornis A., Pineau O., Pohin D., Potvain F., Poulain G., Ruault C.B., Saunders M., Toum J., Xu H.E., Xu R.X., Pianetti P.M.
J. Med. Chem. 50:685-695(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 202-468 IN COMPLEX WITH SYNTHETIC AGONIST.
[26]"Adaptability and selectivity of human peroxisome proliferator-activated receptor (PPAR) pan agonists revealed from crystal structures."
Oyama T., Toyota K., Waku T., Hirakawa Y., Nagasawa N., Kasuga J.I., Hashimoto Y., Miyachi H., Morikawa K.
Acta Crystallogr. D 65:786-795(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 200-468 IN COMPLEX WITH THE SYNTHETIC AGONIST TIPP-703.
[27]"Aleglitazar, a new, potent, and balanced dual PPARalpha/gamma agonist for the treatment of type II diabetes."
Benardeau A., Benz J., Binggeli A., Blum D., Boehringer M., Grether U., Hilpert H., Kuhn B., Maerki H.P., Meyer M., Puentener K., Raab S., Ruf A., Schlatter D., Mohr P.
Bioorg. Med. Chem. Lett. 19:2468-2473(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 199-468 IN COMPLEX WITH ALEGLITAZAR.
[28]"Scaffold-based discovery of indeglitazar, a PPAR pan-active anti-diabetic agent."
Artis D.R., Lin J.J., Zhang C., Wang W., Mehra U., Perreault M., Erbe D., Krupka H.I., England B.P., Arnold J., Plotnikov A.N., Marimuthu A., Nguyen H., Will S., Signaevsky M., Kral J., Cantwell J., Settachatgull C. expand/collapse author list , Yan D.S., Fong D., Oh A., Shi S., Womack P., Powell B., Habets G., West B.L., Zhang K.Y.J., Milburn M.V., Vlasuk G.P., Hirth K.P., Nolop K., Bollag G., Ibrahim P.N., Tobin J.F.
Proc. Natl. Acad. Sci. U.S.A. 106:262-267(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 199-468 IN COMPLEX WITH INDEGLITAZAR.
+Additional computationally mapped references.

Web resources

Wikipedia

Peroxisome proliferator-activated receptor entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02932 mRNA. Translation: AAA36468.1.
S74349 mRNA. Translation: AAB32649.1.
Y07619 mRNA. Translation: CAA68898.1.
AB307690 mRNA. Translation: BAH02281.1.
EU650667 mRNA. Translation: ACD12656.1.
EU395809 mRNA. Translation: ABY73535.1.
CR456547 mRNA. Translation: CAG30433.1.
AK289821 mRNA. Translation: BAF82510.1.
CR457435 mRNA. Translation: CAG33716.1.
AY206718 Genomic DNA. Translation: AAO13489.1.
AL049856, AL078611 Genomic DNA. Translation: CAI22450.1.
Z94161 Genomic DNA. No translation available.
CH471138 Genomic DNA. Translation: EAW73402.1.
CCDSCCDS33669.1. [Q07869-1]
PIRA49289.
I56603.
RefSeqNP_001001928.1. NM_001001928.2. [Q07869-1]
NP_005027.2. NM_005036.4. [Q07869-1]
XP_005261710.1. XM_005261653.2. [Q07869-1]
XP_005261712.1. XM_005261655.1. [Q07869-1]
XP_005261713.1. XM_005261656.1. [Q07869-1]
XP_005261714.1. XM_005261657.1. [Q07869-1]
XP_006724332.1. XM_006724269.1. [Q07869-1]
XP_006724333.1. XM_006724270.1. [Q07869-1]
UniGeneHs.103110.
Hs.710044.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I7GX-ray2.20A196-468[»]
1K7LX-ray2.50A/C/E/G192-468[»]
1KKQX-ray3.00A/B/C/D200-468[»]
2NPAX-ray2.30A/C199-468[»]
2P54X-ray1.79A202-468[»]
2REWX-ray2.35A196-468[»]
2ZNNX-ray2.01A200-468[»]
3ET1X-ray2.50A/B199-468[»]
3FEIX-ray2.40A202-468[»]
3G8IX-ray2.20A199-468[»]
3KDTX-ray2.70A/B196-468[»]
3KDUX-ray2.07A/B196-468[»]
3SP6X-ray2.21A196-468[»]
3VI8X-ray1.75A200-468[»]
4BCRX-ray2.50A/B195-468[»]
ProteinModelPortalQ07869.
SMRQ07869. Positions 95-468.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111461. 35 interactions.
DIPDIP-241N.
IntActQ07869. 10 interactions.
MINTMINT-232229.
STRING9606.ENSP00000262735.

Chemistry

BindingDBQ07869.
ChEMBLCHEMBL239.
DrugBankDB01076. Atorvastatin.
DB01393. Bezafibrate.
DB00636. Clofibrate.
DB01039. Fenofibrate.
DB01241. Gemfibrozil.
DB00641. Simvastatin.
GuidetoPHARMACOLOGY593.

PTM databases

PhosphoSiteQ07869.

Polymorphism databases

DMDM3041727.

Proteomic databases

PaxDbQ07869.
PRIDEQ07869.

Protocols and materials databases

DNASU5465.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262735; ENSP00000262735; ENSG00000186951. [Q07869-1]
ENST00000396000; ENSP00000379322; ENSG00000186951. [Q07869-1]
ENST00000402126; ENSP00000385246; ENSG00000186951. [Q07869-1]
ENST00000407236; ENSP00000385523; ENSG00000186951. [Q07869-1]
ENST00000434345; ENSP00000408149; ENSG00000186951. [Q07869-2]
GeneID5465.
KEGGhsa:5465.
UCSCuc003bgw.1. human. [Q07869-1]

Organism-specific databases

CTD5465.
GeneCardsGC22P046546.
HGNCHGNC:9232. PPARA.
MIM170998. gene+phenotype.
neXtProtNX_Q07869.
PharmGKBPA280.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266867.
HOGENOMHOG000261626.
HOVERGENHBG106004.
InParanoidQ07869.
KOK07294.
OMATESPICP.
PhylomeDBQ07869.
TreeFamTF316304.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_24941. Circadian Clock.
REACT_71. Gene Expression.
SignaLinkQ07869.

Gene expression databases

ArrayExpressQ07869.
BgeeQ07869.
CleanExHS_PPARA.
GenevestigatorQ07869.

Family and domain databases

Gene3D1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProIPR003074. 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.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR01288. PROXISOMEPAR.
PR01289. PROXISOMPAAR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ07869.
GeneWikiPeroxisome_proliferator-activated_receptor_alpha.
GenomeRNAi5465.
NextBio21152.
PROQ07869.
SOURCESearch...

Entry information

Entry namePPARA_HUMAN
AccessionPrimary (citable) accession number: Q07869
Secondary accession number(s): B0G0X3 expand/collapse secondary AC list , Q16241, Q6I9S0, Q92486, Q92689, Q9Y3N1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 15, 1998
Last modified: July 9, 2014
This is version 173 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM