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Q03181

- PPARD_HUMAN

UniProt

Q03181 - PPARD_HUMAN

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Protein
Peroxisome proliferator-activated receptor delta
Gene
PPARD, NR1C2, PPARB
Organism
Homo sapiens (Human)
Status
Reviewed - 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 receptor
Add
BLAST
Zinc fingeri74 – 9421NR C4-type
Add
BLAST
Zinc fingeri111 – 13323NR C4-type
Add
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. protein binding Source: IntAct
  7. sequence-specific DNA binding Source: InterPro
  8. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  9. steroid hormone receptor activity Source: ProtInc
  10. transcription coactivator activity Source: Ensembl
  11. zinc ion binding Source: InterPro

GO - Biological processi

  1. adipose tissue development Source: Ensembl
  2. anagen Source: Ensembl
  3. apoptotic signaling pathway Source: UniProtKB
  4. axon ensheathment Source: UniProtKB
  5. cell differentiation Source: Ensembl
  6. cell proliferation Source: UniProtKB
  7. cell-substrate adhesion 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 from RNA polymerase II promoter Source: UniProtKB
  32. negative regulation of transcription, DNA-templated 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_15525. Nuclear Receptor transcription pathway.
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: 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 delta
PRO_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

ArrayExpressiQ03181.
BgeeiQ03181.
CleanExiHS_PPARD.
GenevestigatoriQ03181.

Organism-specific databases

HPAiCAB017635.

Interactioni

Subunit structurei

Heterodimer with the retinoid X receptor.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111463. 33 interactions.
IntActiQ03181. 4 interactions.
MINTiMINT-1200178.
STRINGi9606.ENSP00000310928.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ03181.

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG266867.
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. Align

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

MEQPQEEAPE VREEEEKEEV AEAEGAPELN GGPQHALPSS SYTDLSRSSS    50
PPSLLDQLQM GCDGASCGSL NMECRVCGDK ASGFHYGVHA CEGCKGFFRR 100
TIRMKLEYEK CERSCKIQKK NRNKCQYCRF QKCLALGMSH NAIRFGRMPE 150
AEKRKLVAGL TANEGSQYNP QVADLKAFSK HIYNAYLKNF NMTKKKARSI 200
LTGKASHTAP FVIHDIETLW QAEKGLVWKQ LVNGLPPYKE ISVHVFYRCQ 250
CTTVETVREL TEFAKSIPSF SSLFLNDQVT LLKYGVHEAI FAMLASIVNK 300
DGLLVANGSG FVTREFLRSL RKPFSDIIEP KFEFAVKFNA LELDDSDLAL 350
FIAAIILCGD RPGLMNVPRV EAIQDTILRA LEFHLQANHP DAQYLFPKLL 400
QKMADLRQLV TEHAQMMQRI KKTETETSLH PLLQEIYKDM Y 441
Length:441
Mass (Da):49,903
Last modified:October 1, 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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 4342EQPQE…SSSYT → HQR in isoform 3.
VSP_043787Add
BLAST
Alternative sequencei44 – 14198Missing in isoform 4.
VSP_046104Add
BLAST
Alternative sequencei360 – 3612DR → GE in isoform 2.
VSP_010133
Alternative sequencei362 – 44180Missing in isoform 2.
VSP_010134Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791D → G in BAF84350. 1 Publication
Sequence conflicti134 – 1341L → P in BAH02282. 1 Publication
Sequence conflicti191 – 1911N → D in BAG65615. 1 Publication
Sequence conflicti217 – 2171E → K in BAG65615. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
ENST00000444397; ENSP00000410837; ENSG00000112033. [Q03181-2]
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4803.1. [Q03181-1 ]
CCDS4804.1. [Q03181-2 ]
CCDS54994.1. [Q03181-3 ]
CCDS54995.1. [Q03181-4 ]
PIRi A45360.
RefSeqi NP_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 ]
UniGenei Hs.696032.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GWX X-ray 2.50 A/B 171-441 [» ]
1Y0S X-ray 2.65 A/B 170-441 [» ]
2AWH X-ray 2.00 A/B 174-441 [» ]
2B50 X-ray 2.00 A/B 169-440 [» ]
2BAW X-ray 2.30 A/B 175-441 [» ]
2ENV NMR - A 72-146 [» ]
2GWX X-ray 2.30 A/B 175-441 [» ]
2J14 X-ray 2.80 A/B 165-441 [» ]
2Q5G X-ray 2.70 A/B 165-441 [» ]
2XYJ X-ray 2.30 A/B 165-441 [» ]
2XYW X-ray 3.14 A/B 165-441 [» ]
2XYX X-ray 2.70 A/B 165-441 [» ]
2ZNP X-ray 3.00 A/B 170-441 [» ]
2ZNQ X-ray 2.65 A/B 170-441 [» ]
3D5F X-ray 2.20 A/B 175-441 [» ]
3DY6 X-ray 2.90 A/B 171-441 [» ]
3ET2 X-ray 2.24 A/B 165-441 [» ]
3GWX X-ray 2.40 A/B 171-441 [» ]
3GZ9 X-ray 2.00 A 171-439 [» ]
3OZ0 X-ray 3.00 A 165-441 [» ]
3PEQ X-ray 2.40 A/B 171-441 [» ]
3SP9 X-ray 2.30 A/B 173-441 [» ]
3TKM X-ray 1.95 A 171-441 [» ]
ProteinModelPortali Q03181.
SMRi Q03181. Positions 65-441.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111463. 33 interactions.
IntActi Q03181. 4 interactions.
MINTi MINT-1200178.
STRINGi 9606.ENSP00000310928.

Chemistry

BindingDBi Q03181.
ChEMBLi CHEMBL3979.
DrugBanki DB00159. Icosapent.
DB00605. Sulindac.
DB00374. Treprostinil.
GuidetoPHARMACOLOGYi 594.

PTM databases

PhosphoSitei Q03181.

Polymorphism databases

DMDMi 417522.

Proteomic databases

MaxQBi Q03181.
PaxDbi Q03181.
PRIDEi Q03181.

Protocols and materials databases

DNASUi 5467.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311565 ; ENSP00000310928 ; ENSG00000112033 . [Q03181-1 ]
ENST00000337400 ; ENSP00000337063 ; ENSG00000112033 . [Q03181-2 ]
ENST00000360694 ; ENSP00000353916 ; ENSG00000112033 . [Q03181-1 ]
ENST00000418635 ; ENSP00000413314 ; ENSG00000112033 . [Q03181-4 ]
ENST00000444397 ; ENSP00000410837 ; ENSG00000112033 . [Q03181-2 ]
ENST00000448077 ; ENSP00000414372 ; ENSG00000112033 . [Q03181-3 ]
GeneIDi 5467.
KEGGi hsa:5467.
UCSCi uc003okm.3. human. [Q03181-1 ]
uc011dtb.2. human. [Q03181-3 ]

Organism-specific databases

CTDi 5467.
GeneCardsi GC06P035310.
H-InvDB HIX0165038.
HGNCi HGNC:9235. PPARD.
HPAi CAB017635.
MIMi 600409. gene.
neXtProti NX_Q03181.
PharmGKBi PA33557.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG266867.
HOGENOMi HOG000261626.
HOVERGENi HBG106004.
InParanoidi Q03181.
KOi K04504.
OMAi MNVPQVE.
OrthoDBi EOG7X9G7F.
PhylomeDBi Q03181.
TreeFami TF316304.

Enzyme and pathway databases

Reactomei REACT_15525. Nuclear Receptor transcription pathway.
SignaLinki Q03181.

Miscellaneous databases

ChiTaRSi PPARD. human.
EvolutionaryTracei Q03181.
GeneWikii Peroxisome_proliferator-activated_receptor_delta.
GenomeRNAii 5467.
NextBioi 21160.
PROi Q03181.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q03181.
Bgeei Q03181.
CleanExi HS_PPARD.
Genevestigatori Q03181.

Family and domain databases

Gene3Di 1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProi IPR003074. 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 ]
Pfami PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR01288. PROXISOMEPAR.
PR01290. PROXISOMPABR.
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. "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(1992) [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(2000) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Human PPARdelta cDNA."
    Cho M.-C., Yoon D.-Y.
    Submitted (FEB-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(2004) [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 (OCT-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(2003) [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(2004) [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 (JAN-2003) 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(2005) [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(2000) [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(2006) [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(2006) [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(2009) [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 (APR-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: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 3, 2014
This is version 177 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

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