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Q03181 (PPARD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisome proliferator-activated receptor 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 names
Name:PPARD
Synonyms:NR1C2, PPARB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.11

Subunit structure

Heterodimer with the retinoid X receptor.

Subcellular location

Nucleus.

Tissue specificity

Ubiquitous with maximal levels in placenta and skeletal muscle.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Receptor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadipose tissue development

Inferred from electronic annotation. Source: Ensembl

anagen

Inferred from electronic annotation. Source: Ensembl

apoptotic signaling pathway

Inferred from mutant phenotype PubMed 11551955. Source: UniProtKB

axon ensheathment

Inferred from sequence or structural similarity. Source: UniProtKB

cell differentiation

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

cell-substrate adhesion

Inferred from electronic annotation. Source: Ensembl

cholesterol metabolic process

Traceable author statement PubMed 15192438. Source: UniProtKB

decidualization

Traceable author statement PubMed 11551955. Source: UniProtKB

embryo implantation

Traceable author statement PubMed 11551955. Source: UniProtKB

fatty acid beta-oxidation

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid catabolic process

Traceable author statement PubMed 15192438. Source: UniProtKB

fatty acid transport

Inferred from sequence or structural similarity. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

generation of precursor metabolites and energy

Traceable author statement Ref.1. Source: ProtInc

glucose metabolic process

Non-traceable author statement PubMed 15793256. Source: UniProtKB

glucose transport

Non-traceable author statement PubMed 15793256. Source: UniProtKB

heart development

Inferred from electronic annotation. Source: Ensembl

intracellular receptor signaling pathway

Inferred from direct assay PubMed 12955147. Source: GOC

keratinocyte migration

Inferred from electronic annotation. Source: Ensembl

keratinocyte proliferation

Inferred from electronic annotation. Source: Ensembl

lipid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA transcription

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of collagen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

phospholipid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of epidermis development

Inferred from electronic annotation. Source: Ensembl

positive regulation of fat cell differentiation

Non-traceable author statement PubMed 10991946. Source: UniProtKB

positive regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12955147. Source: UniProtKB

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

proteoglycan metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

response to activity

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to vitamin A

Inferred from electronic annotation. Source: Ensembl

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

vitamin A metabolic process

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Non-traceable author statement PubMed 11551955. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

drug binding

Inferred from direct assay Ref.12. Source: UniProtKB

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

Inferred from direct assay PubMed 12955147. Source: UniProtKB

linoleic acid binding

Inferred from direct assay Ref.12. Source: UniProtKB

lipid binding

Inferred from direct assay PubMed 12955147. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12955147. Source: UniProtKB

steroid hormone receptor activity

Traceable author statement Ref.1. Source: ProtInc

transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KDM1AO603412EBI-6426768,EBI-710124

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q03181-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q03181-2)

The sequence of this isoform differs from the canonical sequence as follows:
     360-361: DR → GE
     362-441: Missing.
Isoform 3 (identifier: Q03181-3)

The sequence of this isoform differs from the canonical sequence as follows:
     2-43: EQPQEEAPEVREEEEKEEVAEAEGAPELNGGPQHALPSSSYT → HQR
Isoform 4 (identifier: Q03181-4)

The sequence of this isoform differs from the canonical sequence as follows:
     44-141: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 441441Peroxisome proliferator-activated receptor delta
PRO_0000053486

Regions

DNA binding71 – 14575Nuclear receptor
Zinc finger74 – 9421NR C4-type
Zinc finger111 – 13323NR C4-type
Region254 – 441188Ligand-binding

Natural variations

Alternative sequence2 – 4342EQPQE…SSSYT → HQR in isoform 3.
VSP_043787
Alternative sequence44 – 14198Missing in isoform 4.
VSP_046104
Alternative sequence360 – 3612DR → GE in isoform 2.
VSP_010133
Alternative sequence362 – 44180Missing in isoform 2.
VSP_010134

Experimental info

Sequence conflict791D → G in BAF84350. Ref.5
Sequence conflict1341L → P in BAH02282. Ref.3
Sequence conflict1911N → D in BAG65615. Ref.5
Sequence conflict2171E → K in BAG65615. Ref.5

Secondary structure

.................................................... 441
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 1993. Version 1.
Checksum: 94FBB2A4B46521E8

FASTA44149,903
        10         20         30         40         50         60 
MEQPQEEAPE VREEEEKEEV AEAEGAPELN GGPQHALPSS SYTDLSRSSS PPSLLDQLQM 

        70         80         90        100        110        120 
GCDGASCGSL NMECRVCGDK ASGFHYGVHA CEGCKGFFRR TIRMKLEYEK CERSCKIQKK 

       130        140        150        160        170        180 
NRNKCQYCRF QKCLALGMSH NAIRFGRMPE AEKRKLVAGL TANEGSQYNP QVADLKAFSK 

       190        200        210        220        230        240 
HIYNAYLKNF NMTKKKARSI LTGKASHTAP FVIHDIETLW QAEKGLVWKQ LVNGLPPYKE 

       250        260        270        280        290        300 
ISVHVFYRCQ CTTVETVREL TEFAKSIPSF SSLFLNDQVT LLKYGVHEAI FAMLASIVNK 

       310        320        330        340        350        360 
DGLLVANGSG FVTREFLRSL RKPFSDIIEP KFEFAVKFNA LELDDSDLAL FIAAIILCGD 

       370        380        390        400        410        420 
RPGLMNVPRV EAIQDTILRA LEFHLQANHP DAQYLFPKLL QKMADLRQLV TEHAQMMQRI 

       430        440 
KKTETETSLH PLLQEIYKDM Y 

« Hide

Isoform 2 [UniParc].

Checksum: F97757AC266EF8BA
Show »

FASTA36140,406
Isoform 3 [UniParc].

Checksum: 52A73C33151BCF8A
Show »

FASTA40245,764
Isoform 4 [UniParc].

Checksum: 54FB19E6FCE3B21D
Show »

FASTA34338,855

References

« Hide 'large scale' references
[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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]"Molecular recognition of fatty acids by peroxisome proliferator-activated receptors."
Xu H.E., Lambert M.H., Montana V.G., Parks D.J., Blanchard S.G., Brown P.J., Sternbach D.D., Lehmann J.M., Wisely G.B., Willson T.M., Kliewer S.A., Milburn M.V.
Mol. Cell 3:397-403(1999) [PubMed] [Europe PMC] [Abstract]
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]"3,4,5-trisubstituted isoxazoles as novel PPARdelta agonists. Part 2."
Epple R., Azimioara M., Russo R., Xie Y., Wang X., Cow C., Wityak J., Karanewsky D., Bursulaya B., Kreusch A., Tuntland T., Gerken A., Iskandar M., Saez E., Martin Seidel H., Tian S.-S.
Bioorg. Med. Chem. Lett. 16:5488-5492(2006) [PubMed] [Europe PMC] [Abstract]
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]"Design of a partial PPARdelta agonist."
Pettersson I., Ebdrup S., Havranek M., Pihera P., Korinek M., Mogensen J.P., Jeppesen C.B., Johansson E., Sauerberg P.
Bioorg. Med. Chem. Lett. 17:4625-4629(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 165-441 IN COMPLEX WITH SYNTHETIC AGONIST.
[18]"Discovery of a novel class of PPARdelta partial agonists."
Shearer B.G., Patel H.S., Billin A.N., Way J.M., Winegar D.A., Lambert M.H., Xu R.X., Leesnitzer L.M., Merrihew R.V., Huet S., Willson T.M.
Bioorg. Med. Chem. Lett. 18:5018-5022(2008) [PubMed] [Europe PMC] [Abstract]
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]"Identification of a PPARdelta agonist with partial agonistic activity on PPARgamma."
Connors R.V., Wang Z., Harrison M., Zhang A., Wanska M., Hiscock S., Fox B., Dore M., Labelle M., Sudom A., Johnstone S., Liu J., Walker N.P., Chai A., Siegler K., Li Y., Coward P.
Bioorg. Med. Chem. Lett. 19:3550-3554(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 171-439 IN COMPLEX WITH SYNTHETIC AGONIST.
[21]"Scaffold-based discovery of indeglitazar, a PPAR pan-active anti-diabetic agent."
Artis D.R., Lin J.J., Zhang C., Wang W., Mehra U., Perreault M., Erbe D., Krupka H.I., England B.P., Arnold J., Plotnikov A.N., Marimuthu A., Nguyen H., Will S., Signaevsky M., Kral J., Cantwell J., Settachatgull C. expand/collapse author list , Yan D.S., Fong D., Oh A., Shi S., Womack P., Powell B., Habets G., West B.L., Zhang K.Y.J., Milburn M.V., Vlasuk G.P., Hirth K.P., Nolop K., Bollag G., Ibrahim P.N., Tobin J.F.
Proc. Natl. Acad. Sci. U.S.A. 106:262-267(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.24 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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07592 mRNA. Translation: AAA36469.1.
AF246303 expand/collapse EMBL AC list , 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.
PIRA45360.
RefSeqNP_001165289.1. NM_001171818.1.
NP_001165290.1. NM_001171819.1.
NP_001165291.1. NM_001171820.1.
NP_006229.1. NM_006238.4.
NP_803184.1. NM_177435.2.
XP_005249250.1. XM_005249193.1.
UniGeneHs.696032.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ03181.
SMRQ03181. Positions 65-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111463. 33 interactions.
IntActQ03181. 4 interactions.
MINTMINT-1200178.
STRING9606.ENSP00000310928.

Chemistry

BindingDBQ03181.
ChEMBLCHEMBL3979.
DrugBankDB00159. Icosapent.
DB00605. Sulindac.
DB00374. Treprostinil.
GuidetoPHARMACOLOGY594.

PTM databases

PhosphoSiteQ03181.

Polymorphism databases

DMDM417522.

Proteomic databases

PaxDbQ03181.
PRIDEQ03181.

Protocols and materials databases

DNASU5467.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311565; 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]
GeneID5467.
KEGGhsa:5467.
UCSCuc003okm.3. human. [Q03181-1]
uc011dtb.2. human. [Q03181-3]

Organism-specific databases

CTD5467.
GeneCardsGC06P035310.
H-InvDBHIX0165038.
HGNCHGNC:9235. PPARD.
HPACAB017635.
MIM600409. gene.
neXtProtNX_Q03181.
PharmGKBPA33557.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266867.
HOGENOMHOG000261626.
HOVERGENHBG106004.
InParanoidQ03181.
KOK04504.
OMAMNVPQVE.
OrthoDBEOG7X9G7F.
PhylomeDBQ03181.
TreeFamTF316304.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkQ03181.

Gene expression databases

ArrayExpressQ03181.
BgeeQ03181.
CleanExHS_PPARD.
GenevestigatorQ03181.

Family and domain databases

Gene3D1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProIPR003074. 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]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR01288. PROXISOMEPAR.
PR01290. PROXISOMPABR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPARD. human.
EvolutionaryTraceQ03181.
GeneWikiPeroxisome_proliferator-activated_receptor_delta.
GenomeRNAi5467.
NextBio21160.
PROQ03181.
SOURCESearch...

Entry information

Entry namePPARD_HUMAN
AccessionPrimary (citable) accession number: Q03181
Secondary accession number(s): A8K6J6 expand/collapse secondary AC list , B4E3V3, B6ZGS1, B7Z3W1, E9PE18, Q5D1P0, Q7Z5K0, Q9BUD4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 173 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM