Q03181 (PPARD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PPARD
Synonyms:	NR1C2, PPARB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Receptor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adipose tissue development Inferred from electronic annotation. Source: Compara anagen Inferred from electronic annotation. Source: Compara apoptotic process 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: Compara cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB cell-substrate adhesion Inferred from electronic annotation. Source: Compara 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 transport Inferred from sequence or structural similarity. Source: UniProtKB 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 keratinocyte migration Inferred from electronic annotation. Source: Compara keratinocyte proliferation Inferred from electronic annotation. Source: Compara negative regulation of epithelial cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of fat cell differentiation Non-traceable author statement PubMed 10991946. Source: UniProtKB positive regulation of phosphatidylinositol 3-kinase cascade Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 12955147. Source: UniProtKB transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome wound healing Inferred from electronic annotation. Source: Compara
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA 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 sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro steroid hormone receptor activity Traceable author statement Ref.1. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 441

441

Peroxisome proliferator-activated receptor delta

PRO_0000053486

Regions

DNA binding

71 – 145

75

Nuclear receptor

Zinc finger

74 – 94

21

NR C4-type

Zinc finger

111 – 133

23

NR C4-type

Region

254 – 441

188

Ligand-binding

Natural variations

Alternative sequence

2 – 43

42

EQPQE…SSSYT → HQR in isoform 3.

VSP_043787

Alternative sequence

44 – 141

98

Missing in isoform 4.

VSP_046104

Alternative sequence

360 – 361

2

DR → GE in isoform 2.

VSP_010133

Alternative sequence

362 – 441

80

Missing in isoform 2.

VSP_010134

Experimental info

Sequence conflict

79

1

D → G in BAF84350. Ref.5

Sequence conflict

134

1

L → P in BAH02282. Ref.3

Sequence conflict

191

1

N → D in BAG65615. Ref.5

Sequence conflict

217

1

E → K in BAG65615. Ref.5

Secondary structure

1

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441

Helix Strand Turn

Details...

Beta strand

75 – 77

3

Beta strand

83 – 85

3

Beta strand

88 – 90

3

Helix

92 – 103

12

Beta strand

122 – 124

3

Helix

127 – 136

10

Helix

172 – 189

18

Helix

194 – 201

8

Beta strand

205 – 207

3

Beta strand

211 – 213

3

Helix

216 – 225

10

Beta strand

229 – 231

3

Helix

232 – 234

3

Beta strand

235 – 238

4

Helix

241 – 265

25

Turn

268 – 272

5

Helix

275 – 294

20

Helix

295 – 297

3

Beta strand

302 – 305

4

Helix

306 – 308

3

Beta strand

310 – 313

4

Helix

314 – 318

5

Turn

322 – 324

3

Helix

325 – 339

15

Helix

345 – 356

12

Helix

367 – 388

22

Helix

395 – 423

29

Turn

424 – 426

3

Helix

431 – 438

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 94FBB2A4B46521E8	FASTA	441	49,903
	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
	Isoform 2 [UniParc]. Checksum: F97757AC266EF8BA	FASTA	361	40,406
	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 FIAAIILCGG E
	Isoform 3 [UniParc]. Checksum: 52A73C33151BCF8A	FASTA	402	45,764
	10 20 30 40 50 60 MHQRDLSRSS SPPSLLDQLQ MGCDGASCGS LNMECRVCGD KASGFHYGVH ACEGCKGFFR 70 80 90 100 110 120 RTIRMKLEYE KCERSCKIQK KNRNKCQYCR FQKCLALGMS HNAIRFGRMP EAEKRKLVAG 130 140 150 160 170 180 LTANEGSQYN PQVADLKAFS KHIYNAYLKN FNMTKKKARS ILTGKASHTA PFVIHDIETL 190 200 210 220 230 240 WQAEKGLVWK QLVNGLPPYK EISVHVFYRC QCTTVETVRE LTEFAKSIPS FSSLFLNDQV 250 260 270 280 290 300 TLLKYGVHEA IFAMLASIVN KDGLLVANGS GFVTREFLRS LRKPFSDIIE PKFEFAVKFN 310 320 330 340 350 360 ALELDDSDLA LFIAAIILCG DRPGLMNVPR VEAIQDTILR ALEFHLQANH PDAQYLFPKL 370 380 390 400 LQKMADLRQL VTEHAQMMQR IKKTETETSL HPLLQEIYKD MY
	Isoform 4 [UniParc]. Checksum: 54FB19E6FCE3B21D	FASTA	343	38,855
	10 20 30 40 50 60 MEQPQEEAPE VREEEEKEEV AEAEGAPELN GGPQHALPSS SYTAIRFGRM PEAEKRKLVA 70 80 90 100 110 120 GLTANEGSQY NPQVADLKAF SKHIYNAYLK NFNMTKKKAR SILTGKASHT APFVIHDIET 130 140 150 160 170 180 LWQAEKGLVW KQLVNGLPPY KEISVHVFYR CQCTTVETVR ELTEFAKSIP SFSSLFLNDQ 190 200 210 220 230 240 VTLLKYGVHE AIFAMLASIV NKDGLLVANG SGFVTREFLR SLRKPFSDII EPKFEFAVKF 250 260 270 280 290 300 NALELDDSDL ALFIAAIILC GDRPGLMNVP RVEAIQDTIL RALEFHLQAN HPDAQYLFPK 310 320 330 340 LLQKMADLRQ LVTEHAQMMQ RIKKTETETS LHPLLQEIYK DMY

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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. , 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

NIEHS-SNPs

Wikipedia

Peroxisome proliferator-activated receptor entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00009330.
IPI00219761.
IPI00908986.

PIR

A45360.

RefSeq

NP_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.

UniGene

Hs.696032.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q03181.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q03181. 1 interaction.

MINT

MINT-1200178.

STRING

9606.ENSP00000310928.

PTM databases

PhosphoSite

Q03181.

Polymorphism databases

DMDM

417522.

Proteomic databases

PaxDb

Q03181.

PRIDE

Q03181.

Protocols and materials databases

DNASU

5467.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000311565; ENSP00000310928; ENSG00000112033.
ENST00000337400; ENSP00000337063; ENSG00000112033.
ENST00000360694; ENSP00000353916; ENSG00000112033.
ENST00000418635; ENSP00000413314; ENSG00000112033.
ENST00000444397; ENSP00000410837; ENSG00000112033.
ENST00000448077; ENSP00000414372; ENSG00000112033.

GeneID

5467.

KEGG

hsa:5467.

UCSC

uc003okm.3. human.
uc011dtb.2. human.
uc011dtc.2. human.

Organism-specific databases

CTD

5467.

GeneCards

GC06P035310.

H-InvDB

HIX0165038.

HGNC

HGNC:9235. PPARD.

HPA

CAB017635.

MIM

600409. gene.

neXtProt

NX_Q03181.

PharmGKB

PA33557.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG266867.

HOGENOM

HOG000261626.

HOVERGEN

HBG106004.

InParanoid

Q03181.

KO

K04504.

OMA

SSLFLND.

OrthoDB

EOG4FFD1Q.

PhylomeDB

Q03181.

Enzyme and pathway databases

Pathway_Interaction_DB

ps1pathway. Presenilin action in Notch and Wnt signaling.
rxr_vdr_pathway. RXR and RAR hetrodimerization with other nuclear receptor.

Reactome

REACT_71. Gene Expression.

SignaLink

Q03181.

Gene expression databases

ArrayExpress

Q03181.

Bgee

Q03181.

CleanEx

HS_PPARD.

Genevestigator

Q03181.

GermOnline

ENSG00000112033. Homo sapiens.

Family and domain databases

Gene3D

1.10.565.10. 2 hits.
3.30.50.10. 1 hit.

InterPro

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]

Pfam

PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PRINTS

PR01288. PROXISOMEPAR.
PR01290. PROXISOMPABR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q03181.

ChEMBL

CHEMBL3979.

ChiTaRS

PPARD. human.

DrugBank

DB00159. Icosapent.
DB00605. Sulindac.
DB00374. Treprostinil.

EvolutionaryTrace

Q03181.

GenomeRNAi

5467.

NextBio

21160.

SOURCE

Search...

Entry information

Entry name

PPARD_HUMAN

Accession

Primary (citable) accession number: Q03181
Secondary accession number(s): A8K6J6 , 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:	May 29, 2013
This is version 163 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.