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Protein

Peroxisome proliferator-activated receptor delta

Gene

PPARD

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

Functioni

Ligand-activated transcription factor. Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Has a preference for poly-unsaturated fatty acids, such as gamma-linoleic acid and eicosapentanoic acid. Once activated by a ligand, the receptor binds to promoter elements of target genes. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the acyl-CoA oxidase gene. Decreases expression of NPC1L1 once activated by a ligand.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi71 – 14575Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri74 – 9421NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri111 – 13323NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. drug binding Source: UniProtKB
  3. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
  4. linoleic acid binding Source: UniProtKB
  5. lipid binding Source: UniProtKB
  6. sequence-specific DNA binding Source: InterPro
  7. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  8. steroid hormone receptor activity Source: ProtInc
  9. transcription coactivator activity Source: Ensembl
  10. zinc ion binding Source: InterPro

GO - Biological processi

  1. adipose tissue development Source: Ensembl
  2. apoptotic signaling pathway Source: UniProtKB
  3. axon ensheathment Source: UniProtKB
  4. cell differentiation Source: Ensembl
  5. cell proliferation Source: UniProtKB
  6. cell-substrate adhesion Source: Ensembl
  7. cellular response to hypoxia Source: Ensembl
  8. cholesterol metabolic process Source: UniProtKB
  9. decidualization Source: UniProtKB
  10. embryo implantation Source: UniProtKB
  11. fatty acid beta-oxidation Source: UniProtKB
  12. fatty acid catabolic process Source: UniProtKB
  13. fatty acid transport Source: UniProtKB
  14. gene expression Source: Reactome
  15. generation of precursor metabolites and energy Source: ProtInc
  16. glucose metabolic process Source: UniProtKB
  17. glucose transport Source: UniProtKB
  18. heart development Source: Ensembl
  19. intracellular receptor signaling pathway Source: GOC
  20. keratinocyte migration Source: Ensembl
  21. keratinocyte proliferation Source: Ensembl
  22. lipid metabolic process Source: UniProtKB
  23. mRNA transcription Source: Ensembl
  24. negative regulation of apoptotic process Source: Ensembl
  25. negative regulation of cell growth Source: Ensembl
  26. negative regulation of collagen biosynthetic process Source: Ensembl
  27. negative regulation of epithelial cell proliferation Source: Ensembl
  28. negative regulation of inflammatory response Source: Ensembl
  29. negative regulation of smooth muscle cell migration Source: Ensembl
  30. negative regulation of smooth muscle cell proliferation Source: Ensembl
  31. negative regulation of transcription, DNA-templated Source: UniProtKB
  32. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  33. phospholipid biosynthetic process Source: Ensembl
  34. positive regulation of cell proliferation Source: Ensembl
  35. positive regulation of epidermis development Source: Ensembl
  36. positive regulation of fat cell differentiation Source: UniProtKB
  37. positive regulation of insulin secretion Source: Ensembl
  38. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  39. positive regulation of transcription, DNA-templated Source: UniProtKB
  40. positive regulation of vasodilation Source: Ensembl
  41. proteoglycan metabolic process Source: Ensembl
  42. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  43. response to activity Source: Ensembl
  44. response to glucose Source: Ensembl
  45. response to vitamin A Source: Ensembl
  46. transcription initiation from RNA polymerase II promoter Source: Reactome
  47. vitamin A metabolic process Source: Ensembl
  48. wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_15525. Nuclear Receptor transcription pathway.
REACT_267785. Signaling by Retinoic Acid.
SignaLinkiQ03181.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisome proliferator-activated receptor delta
Short name:
PPAR-delta
Alternative name(s):
NUCI
Nuclear hormone receptor 1
Short name:
NUC1
Nuclear receptor subfamily 1 group C member 2
Peroxisome proliferator-activated receptor beta
Short name:
PPAR-beta
Gene namesi
Name:PPARD
Synonyms:NR1C2, PPARB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:9235. PPARD.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33557.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Peroxisome proliferator-activated receptor deltaPRO_0000053486Add
BLAST

Proteomic databases

MaxQBiQ03181.
PaxDbiQ03181.
PRIDEiQ03181.

PTM databases

PhosphoSiteiQ03181.

Expressioni

Tissue specificityi

Ubiquitous with maximal levels in placenta and skeletal muscle.

Gene expression databases

BgeeiQ03181.
CleanExiHS_PPARD.
ExpressionAtlasiQ03181. baseline and differential.
GenevestigatoriQ03181.

Organism-specific databases

HPAiCAB017635.

Interactioni

Subunit structurei

Heterodimer with the retinoid X receptor.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KDM1AO603412EBI-6426768,EBI-710124

Protein-protein interaction databases

BioGridi111463. 47 interactions.
IntActiQ03181. 5 interactions.
MINTiMINT-1200178.
STRINGi9606.ENSP00000310928.

Structurei

Secondary structure

1
441
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi75 – 773Combined sources
Beta strandi83 – 853Combined sources
Beta strandi88 – 903Combined sources
Helixi92 – 10312Combined sources
Beta strandi122 – 1243Combined sources
Helixi127 – 13610Combined sources
Helixi172 – 18918Combined sources
Helixi194 – 2018Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi211 – 2133Combined sources
Helixi216 – 22510Combined sources
Beta strandi229 – 2313Combined sources
Helixi232 – 2343Combined sources
Beta strandi235 – 2384Combined sources
Helixi241 – 26525Combined sources
Turni268 – 2725Combined sources
Helixi275 – 29420Combined sources
Helixi295 – 2973Combined sources
Beta strandi302 – 3054Combined sources
Helixi306 – 3083Combined sources
Beta strandi310 – 3134Combined sources
Helixi314 – 3185Combined sources
Turni322 – 3243Combined sources
Helixi325 – 33915Combined sources
Helixi345 – 35612Combined sources
Helixi367 – 38822Combined sources
Helixi395 – 42329Combined sources
Turni424 – 4263Combined sources
Helixi431 – 4388Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GWXX-ray2.50A/B171-441[»]
1Y0SX-ray2.65A/B170-441[»]
2AWHX-ray2.00A/B174-441[»]
2B50X-ray2.00A/B169-440[»]
2BAWX-ray2.30A/B175-441[»]
2ENVNMR-A72-146[»]
2GWXX-ray2.30A/B175-441[»]
2J14X-ray2.80A/B165-441[»]
2Q5GX-ray2.70A/B165-441[»]
2XYJX-ray2.30A/B165-441[»]
2XYWX-ray3.14A/B165-441[»]
2XYXX-ray2.70A/B165-441[»]
2ZNPX-ray3.00A/B170-441[»]
2ZNQX-ray2.65A/B170-441[»]
3D5FX-ray2.20A/B175-441[»]
3DY6X-ray2.90A/B171-441[»]
3ET2X-ray2.24A/B165-441[»]
3GWXX-ray2.40A/B171-441[»]
3GZ9X-ray2.00A171-439[»]
3OZ0X-ray3.00A165-441[»]
3PEQX-ray2.40A/B171-441[»]
3SP9X-ray2.30A/B173-441[»]
3TKMX-ray1.95A171-441[»]
ProteinModelPortaliQ03181.
SMRiQ03181. Positions 65-441.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03181.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni254 – 441188Ligand-bindingAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri74 – 9421NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri111 – 13323NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG266867.
GeneTreeiENSGT00780000121834.
HOGENOMiHOG000261626.
HOVERGENiHBG106004.
InParanoidiQ03181.
KOiK04504.
OMAiMNVPQVE.
OrthoDBiEOG7X9G7F.
PhylomeDBiQ03181.
TreeFamiTF316304.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR003074. 1Cnucl_rcpt.
IPR003075. 1Cnucl_rcpt_B.
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.
PR01290. PROXISOMPABR.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q03181-1) [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
MEQPQEEAPE VREEEEKEEV AEAEGAPELN GGPQHALPSS SYTDLSRSSS
60 70 80 90 100
PPSLLDQLQM GCDGASCGSL NMECRVCGDK ASGFHYGVHA CEGCKGFFRR
110 120 130 140 150
TIRMKLEYEK CERSCKIQKK NRNKCQYCRF QKCLALGMSH NAIRFGRMPE
160 170 180 190 200
AEKRKLVAGL TANEGSQYNP QVADLKAFSK HIYNAYLKNF NMTKKKARSI
210 220 230 240 250
LTGKASHTAP FVIHDIETLW QAEKGLVWKQ LVNGLPPYKE ISVHVFYRCQ
260 270 280 290 300
CTTVETVREL TEFAKSIPSF SSLFLNDQVT LLKYGVHEAI FAMLASIVNK
310 320 330 340 350
DGLLVANGSG FVTREFLRSL RKPFSDIIEP KFEFAVKFNA LELDDSDLAL
360 370 380 390 400
FIAAIILCGD RPGLMNVPRV EAIQDTILRA LEFHLQANHP DAQYLFPKLL
410 420 430 440
QKMADLRQLV TEHAQMMQRI KKTETETSLH PLLQEIYKDM Y
Length:441
Mass (Da):49,903
Last modified:September 30, 1993 - v1
Checksum:i94FBB2A4B46521E8
GO
Isoform 2 (identifier: Q03181-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     360-361: DR → GE
     362-441: Missing.

Show »
Length:361
Mass (Da):40,406
Checksum:iF97757AC266EF8BA
GO
Isoform 3 (identifier: Q03181-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-43: EQPQEEAPEVREEEEKEEVAEAEGAPELNGGPQHALPSSSYT → HQR

Show »
Length:402
Mass (Da):45,764
Checksum:i52A73C33151BCF8A
GO
Isoform 4 (identifier: Q03181-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     44-141: Missing.

Note: No experimental confirmation available.

Show »
Length:343
Mass (Da):38,855
Checksum:i54FB19E6FCE3B21D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791D → G in BAF84350 (PubMed:14702039).Curated
Sequence conflicti134 – 1341L → P in BAH02282 (PubMed:18619963).Curated
Sequence conflicti191 – 1911N → D in BAG65615 (PubMed:14702039).Curated
Sequence conflicti217 – 2171E → K in BAG65615 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 4342EQPQE…SSSYT → HQR in isoform 3. 1 PublicationVSP_043787Add
BLAST
Alternative sequencei44 – 14198Missing in isoform 4. 1 PublicationVSP_046104Add
BLAST
Alternative sequencei360 – 3612DR → GE in isoform 2. 1 PublicationVSP_010133
Alternative sequencei362 – 44180Missing in isoform 2. 1 PublicationVSP_010134Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07592 mRNA. Translation: AAA36469.1.
AF246303
, AF246299, AF246300, AF246301, AF246302 Genomic DNA. Translation: AAF62553.1.
AB307691 mRNA. Translation: BAH02282.1.
AY919140 mRNA. Translation: AAX14041.1.
AK291661 mRNA. Translation: BAF84350.1.
AK296425 mRNA. Translation: BAH12347.1.
AK304878 mRNA. Translation: BAG65615.1.
AK122614 mRNA. Translation: BAG53624.1.
AY442342 Genomic DNA. Translation: AAR05439.1.
AL022721 Genomic DNA. Translation: CAB38629.1.
AL022721 Genomic DNA. Translation: CAD92505.1.
CH471081 Genomic DNA. Translation: EAX03825.1.
BC002715 mRNA. Translation: AAH02715.1.
BC007578 mRNA. Translation: AAH07578.1.
AB099507 mRNA. Translation: BAC78903.1.
CCDSiCCDS4803.1. [Q03181-1]
CCDS4804.1. [Q03181-2]
CCDS54994.1. [Q03181-3]
CCDS54995.1. [Q03181-4]
PIRiA45360.
RefSeqiNP_001165289.1. NM_001171818.1.
NP_001165290.1. NM_001171819.1. [Q03181-3]
NP_001165291.1. NM_001171820.1. [Q03181-4]
NP_006229.1. NM_006238.4. [Q03181-1]
NP_803184.1. NM_177435.2. [Q03181-2]
XP_005249250.1. XM_005249193.1. [Q03181-1]
XP_006715183.1. XM_006715120.1. [Q03181-1]
XP_006715184.1. XM_006715121.1. [Q03181-1]
XP_006715185.1. XM_006715122.1. [Q03181-1]
XP_006715186.1. XM_006715123.1. [Q03181-1]
UniGeneiHs.696032.

Genome annotation databases

EnsembliENST00000311565; ENSP00000310928; ENSG00000112033. [Q03181-1]
ENST00000337400; ENSP00000337063; ENSG00000112033. [Q03181-2]
ENST00000360694; ENSP00000353916; ENSG00000112033. [Q03181-1]
ENST00000418635; ENSP00000413314; ENSG00000112033. [Q03181-4]
ENST00000448077; ENSP00000414372; ENSG00000112033. [Q03181-3]
GeneIDi5467.
KEGGihsa:5467.
UCSCiuc003okm.3. human. [Q03181-1]
uc011dtb.2. human. [Q03181-3]

Polymorphism databases

DMDMi417522.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Peroxisome proliferator-activated receptor entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07592 mRNA. Translation: AAA36469.1.
AF246303
, AF246299, AF246300, AF246301, AF246302 Genomic DNA. Translation: AAF62553.1.
AB307691 mRNA. Translation: BAH02282.1.
AY919140 mRNA. Translation: AAX14041.1.
AK291661 mRNA. Translation: BAF84350.1.
AK296425 mRNA. Translation: BAH12347.1.
AK304878 mRNA. Translation: BAG65615.1.
AK122614 mRNA. Translation: BAG53624.1.
AY442342 Genomic DNA. Translation: AAR05439.1.
AL022721 Genomic DNA. Translation: CAB38629.1.
AL022721 Genomic DNA. Translation: CAD92505.1.
CH471081 Genomic DNA. Translation: EAX03825.1.
BC002715 mRNA. Translation: AAH02715.1.
BC007578 mRNA. Translation: AAH07578.1.
AB099507 mRNA. Translation: BAC78903.1.
CCDSiCCDS4803.1. [Q03181-1]
CCDS4804.1. [Q03181-2]
CCDS54994.1. [Q03181-3]
CCDS54995.1. [Q03181-4]
PIRiA45360.
RefSeqiNP_001165289.1. NM_001171818.1.
NP_001165290.1. NM_001171819.1. [Q03181-3]
NP_001165291.1. NM_001171820.1. [Q03181-4]
NP_006229.1. NM_006238.4. [Q03181-1]
NP_803184.1. NM_177435.2. [Q03181-2]
XP_005249250.1. XM_005249193.1. [Q03181-1]
XP_006715183.1. XM_006715120.1. [Q03181-1]
XP_006715184.1. XM_006715121.1. [Q03181-1]
XP_006715185.1. XM_006715122.1. [Q03181-1]
XP_006715186.1. XM_006715123.1. [Q03181-1]
UniGeneiHs.696032.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GWXX-ray2.50A/B171-441[»]
1Y0SX-ray2.65A/B170-441[»]
2AWHX-ray2.00A/B174-441[»]
2B50X-ray2.00A/B169-440[»]
2BAWX-ray2.30A/B175-441[»]
2ENVNMR-A72-146[»]
2GWXX-ray2.30A/B175-441[»]
2J14X-ray2.80A/B165-441[»]
2Q5GX-ray2.70A/B165-441[»]
2XYJX-ray2.30A/B165-441[»]
2XYWX-ray3.14A/B165-441[»]
2XYXX-ray2.70A/B165-441[»]
2ZNPX-ray3.00A/B170-441[»]
2ZNQX-ray2.65A/B170-441[»]
3D5FX-ray2.20A/B175-441[»]
3DY6X-ray2.90A/B171-441[»]
3ET2X-ray2.24A/B165-441[»]
3GWXX-ray2.40A/B171-441[»]
3GZ9X-ray2.00A171-439[»]
3OZ0X-ray3.00A165-441[»]
3PEQX-ray2.40A/B171-441[»]
3SP9X-ray2.30A/B173-441[»]
3TKMX-ray1.95A171-441[»]
ProteinModelPortaliQ03181.
SMRiQ03181. Positions 65-441.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111463. 47 interactions.
IntActiQ03181. 5 interactions.
MINTiMINT-1200178.
STRINGi9606.ENSP00000310928.

Chemistry

BindingDBiQ03181.
ChEMBLiCHEMBL2111371.
DrugBankiDB01393. Bezafibrate.
DB00159. Icosapent.
DB00605. Sulindac.
DB00374. Treprostinil.
GuidetoPHARMACOLOGYi594.

PTM databases

PhosphoSiteiQ03181.

Polymorphism databases

DMDMi417522.

Proteomic databases

MaxQBiQ03181.
PaxDbiQ03181.
PRIDEiQ03181.

Protocols and materials databases

DNASUi5467.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311565; ENSP00000310928; ENSG00000112033. [Q03181-1]
ENST00000337400; ENSP00000337063; ENSG00000112033. [Q03181-2]
ENST00000360694; ENSP00000353916; ENSG00000112033. [Q03181-1]
ENST00000418635; ENSP00000413314; ENSG00000112033. [Q03181-4]
ENST00000448077; ENSP00000414372; ENSG00000112033. [Q03181-3]
GeneIDi5467.
KEGGihsa:5467.
UCSCiuc003okm.3. human. [Q03181-1]
uc011dtb.2. human. [Q03181-3]

Organism-specific databases

CTDi5467.
GeneCardsiGC06P035310.
H-InvDBHIX0165038.
HGNCiHGNC:9235. PPARD.
HPAiCAB017635.
MIMi600409. gene.
neXtProtiNX_Q03181.
PharmGKBiPA33557.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG266867.
GeneTreeiENSGT00780000121834.
HOGENOMiHOG000261626.
HOVERGENiHBG106004.
InParanoidiQ03181.
KOiK04504.
OMAiMNVPQVE.
OrthoDBiEOG7X9G7F.
PhylomeDBiQ03181.
TreeFamiTF316304.

Enzyme and pathway databases

ReactomeiREACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_15525. Nuclear Receptor transcription pathway.
REACT_267785. Signaling by Retinoic Acid.
SignaLinkiQ03181.

Miscellaneous databases

ChiTaRSiPPARD. human.
EvolutionaryTraceiQ03181.
GeneWikiiPeroxisome_proliferator-activated_receptor_delta.
GenomeRNAii5467.
NextBioi21160.
PROiQ03181.
SOURCEiSearch...

Gene expression databases

BgeeiQ03181.
CleanExiHS_PPARD.
ExpressionAtlasiQ03181. baseline and differential.
GenevestigatoriQ03181.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR003074. 1Cnucl_rcpt.
IPR003075. 1Cnucl_rcpt_B.
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.
PR01290. PROXISOMPABR.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a new member of the steroid hormone receptor superfamily that is activated by a peroxisome proliferator and fatty acids."
    Schmidt A., Endo N., Rutledge S.J., Vogel R., Shinar D., Rodan G.A.
    Mol. Endocrinol. 6:1634-1641(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, FATTY ACID BINDING.
  2. "Characterization of the human peroxisome proliferator activated receptor delta gene and its expression."
    Skogsberg J., Kannisto K., Roshani L., Gagne E., Hamsten A., Larsson C., Ehrenborg E.
    Int. J. Mol. Med. 6:73-81(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    Tissue: Placenta.
  3. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Human PPARdelta cDNA."
    Cho M.-C., Yoon D.-Y.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Spleen.
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
    Tissue: Placenta and Thalamus.
  6. NIEHS SNPs program
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  10. "PPAR-delta 5'-complete cDNA fragment."
    Aoto T., Ishizuka M., Kazusaka A., Fujita S.
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 1-161.
  11. "Reduced cholesterol absorption upon PPARdelta activation coincides with decreased intestinal expression of NPC1L1."
    van der Veen J.N., Kruit J.K., Havinga R., Baller J.F.W., Chimini G., Lestavel S., Staels B., Groot P.H.E., Groen A.K., Kuipers F.
    J. Lipid Res. 46:526-534(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NPC1L1 EXPRESSION.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 171-441 IN COMPLEXES WITH EICOSAPENTAENOIC ACID AND THE SYNTHETIC AGONIST GW2433, UNSATURATED FATTY ACID BINDING.
  13. "Alteration of a single amino acid in peroxisome proliferator-activated receptor-alpha (PPAR alpha) generates a PPAR delta phenotype."
    Takada I., Yu R.T., Xu H.E., Lambert M.H., Montana V.G., Kliewer S.A., Evans R.M., Umesono K.
    Mol. Endocrinol. 14:733-740(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 170-441 IN COMPLEX WITH THE SYNTHETIC AGONIST GW2331.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 165-441 IN COMPLEX WITH SYNTHETIC AGONIST.
  15. "Recombinant human PPAR-beta/delta ligand-binding domain is locked in an activated conformation by endogenous fatty acids."
    Fyffe S.A., Alphey M.S., Buetow L., Smith T.K., Ferguson M.A., Soerensen M.D., Bjoerkling F., Hunter W.N.
    J. Mol. Biol. 356:1005-1013(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 169-440 IN COMPLEX WITH FATTY ACIDS.
  16. "Reevaluation of the PPAR-beta/delta ligand binding domain model reveals why it exhibits the activated form."
    Fyffe S.A., Alphey M.S., Buetow L., Smith T.K., Ferguson M.A., Soerensen M.D., Bjoerkling F., Hunter W.N.
    Mol. Cell 21:1-2(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 175-441.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 165-441 IN COMPLEX WITH SYNTHETIC AGONIST.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 171-441.
  19. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 170-441 IN COMPLEXES WITH THE SYNTHETIC AGONISTS TIPP-401 AND TIPP-204.
  20. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 171-439 IN COMPLEX WITH SYNTHETIC AGONIST.
  21. Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 165-441 IN COMPLEX WITH INDEGLITAZAR.
  22. "Solution structure of the C4-type zinc finger domain from human peroxisome proliferator-activated receptor delta."
    RIKEN structural genomics initiative (RSGI)
    Submitted (MAR-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 66-151.

Entry informationi

Entry nameiPPARD_HUMAN
AccessioniPrimary (citable) accession number: Q03181
Secondary accession number(s): A8K6J6
, B4E3V3, B6ZGS1, B7Z3W1, E9PE18, Q5D1P0, Q7Z5K0, Q9BUD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1993
Last sequence update: September 30, 1993
Last modified: March 31, 2015
This is version 184 of the entry and version 1 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.