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Q07869

- PPARA_HUMAN

UniProt

Q07869 - PPARA_HUMAN

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Protein

Peroxisome proliferator-activated receptor alpha

Gene

PPARA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 PER2.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei280 – 2801Synthetic agonist5 Publications
Binding sitei314 – 3141Synthetic agonist5 Publications
Sitei433 – 4331Essential for heterodimerization with RXRA
Binding sitei440 – 4401Synthetic agonist5 Publications
Binding sitei464 – 4641Synthetic agonist5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi99 – 17375Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri102 – 12221NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri139 – 16123NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. drug binding Source: UniProtKB
  3. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
  4. lipid binding Source: UniProtKB
  5. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
  7. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  8. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  9. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  10. sequence-specific DNA binding Source: BHF-UCL
  11. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  12. steroid hormone receptor activity Source: BHF-UCL
  13. ubiquitin conjugating enzyme binding Source: BHF-UCL
  14. zinc ion binding Source: InterPro

GO - Biological processi

  1. behavioral response to nicotine Source: Ensembl
  2. cellular lipid metabolic process Source: Reactome
  3. circadian regulation of gene expression Source: UniProtKB
  4. enamel mineralization Source: Ensembl
  5. epidermis development Source: Ensembl
  6. fatty acid metabolic process Source: ProtInc
  7. fatty acid transport Source: UniProtKB
  8. gene expression Source: Reactome
  9. heart development Source: Ensembl
  10. intracellular receptor signaling pathway Source: GOC
  11. lipid metabolic process Source: ProtInc
  12. lipoprotein metabolic process Source: Ensembl
  13. negative regulation of appetite Source: UniProtKB
  14. negative regulation of blood pressure Source: Ensembl
  15. negative regulation of cholesterol storage Source: BHF-UCL
  16. negative regulation of glycolytic process Source: BHF-UCL
  17. negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  18. negative regulation of neuron death Source: Ensembl
  19. negative regulation of protein binding Source: Ensembl
  20. negative regulation of receptor biosynthetic process Source: BHF-UCL
  21. negative regulation of sequestering of triglyceride Source: BHF-UCL
  22. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  23. negative regulation of transcription regulatory region DNA binding Source: Ensembl
  24. positive regulation of fatty acid beta-oxidation Source: UniProtKB
  25. positive regulation of fatty acid oxidation Source: BHF-UCL
  26. positive regulation of gluconeogenesis Source: Ensembl
  27. positive regulation of transcription, DNA-templated Source: UniProtKB
  28. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  29. regulation of cellular ketone metabolic process by positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  30. regulation of circadian rhythm Source: UniProtKB
  31. regulation of glycolytic by positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  32. regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  33. response to hypoxia Source: Ensembl
  34. response to insulin Source: Ensembl
  35. small molecule metabolic process Source: Reactome
  36. transcription initiation from RNA polymerase II promoter Source: Reactome
  37. wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Lipid-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates circadian gene expression.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_118789. REV-ERBA represses gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_15525. Nuclear Receptor transcription pathway.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_24941. Circadian Clock.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiQ07869.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisome proliferator-activated receptor alpha
Short name:
PPAR-alpha
Alternative name(s):
Nuclear receptor subfamily 1 group C member 1
Gene namesi
Name:PPARA
Synonyms:NR1C1, PPAR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:9232. PPARA.

Subcellular locationi

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi122 – 1221C → G: Prevents DNA binding but no effect on heterodimerization with RXRA. 1 Publication
Mutagenesisi304 – 3041D → A: Reduced heterodimerization with RXRA. Reduced DNA binding. 1 Publication
Mutagenesisi370 – 3701L → R: Abolishes heterodimerization with RXRA. No DNA binding. 1 Publication
Mutagenesisi391 – 3911L → R: Abolishes heterodimerization with RXRA. No DNA binding. 1 Publication
Mutagenesisi422 – 4221L → R: No effect on heterodimerization with RXRA nor on DNA binding and transactivation activity. 1 Publication
Mutagenesisi431 – 4311A → T: No effect on heterodimerization with RXRA nor on DNA binding. 1 Publication
Mutagenesisi433 – 4331L → R: Abolishes heterodimerization with RXRA, DNA binding and transactivation activity. 1 Publication

Organism-specific databases

MIMi170998. gene+phenotype.
PharmGKBiPA280.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Peroxisome proliferator-activated receptor alphaPRO_0000053481Add
BLAST

Proteomic databases

PaxDbiQ07869.
PRIDEiQ07869.

PTM databases

PhosphoSiteiQ07869.

Expressioni

Tissue specificityi

Skeletal muscle, liver, heart and kidney.2 Publications

Gene expression databases

BgeeiQ07869.
CleanExiHS_PPARA.
ExpressionAtlasiQ07869. baseline and differential.
GenevestigatoriQ07869.

Interactioni

Subunit structurei

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 PER2.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHD9Q3L8U1-32EBI-78615,EBI-960730
NCOR1O753762EBI-78615,EBI-347233

Protein-protein interaction databases

BioGridi111461. 36 interactions.
DIPiDIP-241N.
IntActiQ07869. 12 interactions.
MINTiMINT-232229.
STRINGi9606.ENSP00000262735.

Structurei

Secondary structure

1
468
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi203 – 21715
Helixi222 – 2298
Beta strandi233 – 2353
Beta strandi239 – 2413
Helixi244 – 25411
Helixi256 – 2594
Helixi263 – 2653
Helixi268 – 29023
Helixi291 – 2933
Turni295 – 2995
Helixi302 – 32120
Helixi322 – 3243
Beta strandi329 – 3324
Turni333 – 3364
Beta strandi337 – 3404
Helixi341 – 3466
Turni349 – 3513
Helixi352 – 36615
Helixi372 – 38312
Helixi394 – 41522
Helixi422 – 45029
Beta strandi453 – 4564
Helixi458 – 4647
Turni465 – 4673

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ07869.
SMRiQ07869. Positions 95-468.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07869.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni280 – 468189Ligand-bindingAdd
BLAST
Regioni304 – 433130Required for heterodimerization with RXRAAdd
BLAST

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri102 – 12221NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri139 – 16123NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG266867.
GeneTreeiENSGT00760000119049.
HOGENOMiHOG000261626.
HOVERGENiHBG106004.
InParanoidiQ07869.
KOiK07294.
OMAiTESPICP.
PhylomeDBiQ07869.
TreeFamiTF316304.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR003074. 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]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01288. PROXISOMEPAR.
PR01289. PROXISOMPAAR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q07869-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MVDTESPLCP LSPLEAGDLE SPLSEEFLQE MGNIQEISQS IGEDSSGSFG
60 70 80 90 100
FTEYQYLGSC PGSDGSVITD TLSPASSPSS VTYPVVPGSV DESPSGALNI
110 120 130 140 150
ECRICGDKAS GYHYGVHACE GCKGFFRRTI RLKLVYDKCD RSCKIQKKNR
160 170 180 190 200
NKCQYCRFHK CLSVGMSHNA IRFGRMPRSE KAKLKAEILT CEHDIEDSET
210 220 230 240 250
ADLKSLAKRI YEAYLKNFNM NKVKARVILS GKASNNPPFV IHDMETLCMA
260 270 280 290 300
EKTLVAKLVA NGIQNKEAEV RIFHCCQCTS VETVTELTEF AKAIPGFANL
310 320 330 340 350
DLNDQVTLLK YGVYEAIFAM LSSVMNKDGM LVAYGNGFIT REFLKSLRKP
360 370 380 390 400
FCDIMEPKFD FAMKFNALEL DDSDISLFVA AIICCGDRPG LLNVGHIEKM
410 420 430 440 450
QEGIVHVLRL HLQSNHPDDI FLFPKLLQKM ADLRQLVTEH AQLVQIIKKT
460
ESDAALHPLL QEIYRDMY
Length:468
Mass (Da):52,225
Last modified:July 15, 1998 - v2
Checksum:i850846FD51ADA883
GO
Isoform 2 (identifier: Q07869-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:174
Mass (Da):18,942
Checksum:i8587321146D06A03
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711T → M in CAA68898. (PubMed:8993548)Curated
Sequence conflicti123 – 1231K → M in CAA68898. (PubMed:8993548)Curated
Sequence conflicti296 – 2961G → A in AAA36468. (PubMed:7684926)Curated
Sequence conflicti444 – 4441V → A in CAA68898. (PubMed:8993548)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti127 – 1271R → Q.
Corresponds to variant rs1800204 [ dbSNP | Ensembl ].
VAR_016110
Natural varianti162 – 1621L → V.1 Publication
Corresponds to variant rs1800206 [ dbSNP | Ensembl ].
VAR_016111
Natural varianti227 – 2271V → A.
Corresponds to variant rs1800234 [ dbSNP | Ensembl ].
VAR_016112
Natural varianti268 – 2681A → V.1 Publication
Corresponds to variant rs1042311 [ dbSNP | Ensembl ].
VAR_016113
Natural varianti304 – 3041D → N.
Corresponds to variant rs1800242 [ dbSNP | Ensembl ].
VAR_016114
Natural varianti395 – 3951G → R.
Corresponds to variant rs2229245 [ dbSNP | Ensembl ].
VAR_050578
Natural varianti409 – 4091R → T.
Corresponds to variant rs1800243 [ dbSNP | Ensembl ].
VAR_016115

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei171 – 1744IRFG → FCHT in isoform 2. 1 PublicationVSP_047571
Alternative sequencei175 – 468294Missing in isoform 2. 1 PublicationVSP_047572Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS33669.1. [Q07869-1]
PIRiA49289.
I56603.
RefSeqiNP_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]
UniGeneiHs.103110.
Hs.710044.

Genome annotation databases

EnsembliENST00000262735; ENSP00000262735; ENSG00000186951. [Q07869-1]
ENST00000402126; ENSP00000385246; ENSG00000186951. [Q07869-1]
ENST00000407236; ENSP00000385523; ENSG00000186951. [Q07869-1]
GeneIDi5465.
KEGGihsa:5465.
UCSCiuc003bgw.1. human. [Q07869-1]

Polymorphism databases

DMDMi3041727.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Peroxisome proliferator-activated receptor entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS33669.1. [Q07869-1 ]
PIRi A49289.
I56603.
RefSeqi NP_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 ]
UniGenei Hs.103110.
Hs.710044.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1I7G X-ray 2.20 A 196-468 [» ]
1K7L X-ray 2.50 A/C/E/G 192-468 [» ]
1KKQ X-ray 3.00 A/B/C/D 200-468 [» ]
2NPA X-ray 2.30 A/C 199-468 [» ]
2P54 X-ray 1.79 A 202-468 [» ]
2REW X-ray 2.35 A 196-468 [» ]
2ZNN X-ray 2.01 A 200-468 [» ]
3ET1 X-ray 2.50 A/B 199-468 [» ]
3FEI X-ray 2.40 A 202-468 [» ]
3G8I X-ray 2.20 A 199-468 [» ]
3KDT X-ray 2.70 A/B 196-468 [» ]
3KDU X-ray 2.07 A/B 196-468 [» ]
3SP6 X-ray 2.21 A 196-468 [» ]
3VI8 X-ray 1.75 A 200-468 [» ]
4BCR X-ray 2.50 A/B 195-468 [» ]
ProteinModelPortali Q07869.
SMRi Q07869. Positions 95-468.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111461. 36 interactions.
DIPi DIP-241N.
IntActi Q07869. 12 interactions.
MINTi MINT-232229.
STRINGi 9606.ENSP00000262735.

Chemistry

BindingDBi Q07869.
ChEMBLi CHEMBL239.
DrugBanki DB01393. Bezafibrate.
DB00636. Clofibrate.
DB01039. Fenofibrate.
DB01241. Gemfibrozil.
DB00328. Indomethacin.
GuidetoPHARMACOLOGYi 593.

PTM databases

PhosphoSitei Q07869.

Polymorphism databases

DMDMi 3041727.

Proteomic databases

PaxDbi Q07869.
PRIDEi Q07869.

Protocols and materials databases

DNASUi 5465.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262735 ; ENSP00000262735 ; ENSG00000186951 . [Q07869-1 ]
ENST00000402126 ; ENSP00000385246 ; ENSG00000186951 . [Q07869-1 ]
ENST00000407236 ; ENSP00000385523 ; ENSG00000186951 . [Q07869-1 ]
GeneIDi 5465.
KEGGi hsa:5465.
UCSCi uc003bgw.1. human. [Q07869-1 ]

Organism-specific databases

CTDi 5465.
GeneCardsi GC22P046546.
HGNCi HGNC:9232. PPARA.
MIMi 170998. gene+phenotype.
neXtProti NX_Q07869.
PharmGKBi PA280.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG266867.
GeneTreei ENSGT00760000119049.
HOGENOMi HOG000261626.
HOVERGENi HBG106004.
InParanoidi Q07869.
KOi K07294.
OMAi TESPICP.
PhylomeDBi Q07869.
TreeFami TF316304.

Enzyme and pathway databases

Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates circadian gene expression.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_118789. REV-ERBA represses gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_15525. Nuclear Receptor transcription pathway.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_200608. Transcriptional activation of mitochondrial biogenesis.
REACT_24941. Circadian Clock.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinki Q07869.

Miscellaneous databases

EvolutionaryTracei Q07869.
GeneWikii Peroxisome_proliferator-activated_receptor_alpha.
GenomeRNAii 5465.
NextBioi 21152.
PROi Q07869.
SOURCEi Search...

Gene expression databases

Bgeei Q07869.
CleanExi HS_PPARA.
ExpressionAtlasi Q07869. baseline and differential.
Genevestigatori Q07869.

Family and domain databases

Gene3Di 1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProi 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.
[Graphical view ]
Pfami PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR01288. PROXISOMEPAR.
PR01289. PROXISOMPAAR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 199-468 IN COMPLEX WITH INDEGLITAZAR.

Entry informationi

Entry nameiPPARA_HUMAN
AccessioniPrimary (citable) accession number: Q07869
Secondary accession number(s): B0G0X3
, Q16241, Q6I9S0, Q92486, Q92689, Q9Y3N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 15, 1998
Last modified: October 29, 2014
This is version 176 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3