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Q03181

- PPARD_HUMAN

UniProt

Q03181 - PPARD_HUMAN

Protein

Peroxisome proliferator-activated receptor delta

Gene

PPARD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 178 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    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. 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, 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

    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

    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

    ArrayExpressiQ03181.
    BgeeiQ03181.
    CleanExiHS_PPARD.
    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. 33 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 – 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.
    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.
    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

    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:
    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]
    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. 5 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 ]
    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

    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: October 1, 2014
    This is version 178 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