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Reviewed, UniProtKB/Swiss-Prot Q03181 (PPARD_HUMAN)

Last modified February 9, 2010. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peroxisome proliferator-activated receptor delta
      Short name=PPAR-delta
Alternative name(s):
    Peroxisome proliferator-activated receptor beta
      Short name=PPAR-beta
    Nuclear receptor subfamily 1 group C member 2
    Nuclear hormone receptor 1
      Short name=NUC1
    NUCI
Gene names
Name: PPARD
Synonyms: NR1C2, PPARB
OrganismHomo sapiens (Human) [Complete 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
Gene Ontology (GO)
   Biological processapoptosis

Inferred from mutant phenotype. Source: UniProtKB

axon ensheathment

Inferred from sequence or structural similarity. Source: UniProtKB

cholesterol metabolic process

Traceable author statement. Source: UniProtKB

decidualization

Traceable author statement. Source: UniProtKB

embryo implantation

Traceable author statement. Source: UniProtKB

fatty acid beta-oxidation

Traceable author statement. Source: UniProtKB

fatty acid transport

Inferred from sequence or structural similarity. Source: UniProtKB

generation of precursor metabolites and energy Ref.1

Traceable author statement. Source: ProtInc

glucose metabolic process

Non-traceable author statement. Source: UniProtKB

glucose transport

Non-traceable author statement. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of fat cell differentiation

Non-traceable author statement. Source: UniProtKB

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Non-traceable author statement. Source: UniProtKB

   Molecular functiondrug binding Ref.12

Inferred from direct assay. Source: UniProtKB

linoleic acid binding Ref.12

Inferred from direct assay. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

steroid hormone receptor activity Ref.1

Traceable author statement. Source: ProtInc

transcription activator activity

Inferred from direct assay. Source: UniProtKB

transcription factor activity

Inferred from direct assay. Source: UniProtKB

transcription repressor activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 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.

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 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

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.

Checksum: F97757AC266EF8BA
Show »

FASTA36140,406

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: 1333051] [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: 10851270] [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: 18619963] [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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[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: 14574404] [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: 15489334] [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: 15604518] [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: 10198642] [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: 10809235] [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: 16931011] [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: 16405912] [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: 16387648] [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: 17560785] [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: 18722772] [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: 19622862] [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: 19464171] [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: 19116277] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 165-441 IN COMPLEX WITH INDEGLITAZAR.
[22]"Solution sturcture 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

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.
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.
IPIIPI00009330.
IPI00219761.
PIRA45360.
RefSeqNP_006229.1.
NP_803184.1.
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[»]
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[»]
SMRQ03181. Positions 65-151.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ03181.

PTM databases

PhosphoSiteQ03181.

Proteomic databases

PRIDEQ03181.

Genome annotation databases

EnsemblENST00000311565; ENSP00000310928; ENSG00000112033; Homo sapiens. [Genome view]
ENST00000360694; ENSP00000353916; ENSG00000112033; Homo sapiens. [Genome view]
GeneID5467.
KEGGhsa:5467.
UCSCuc003okl.2. human.
uc003okm.1. human.

Organism-specific databases

CTD5467.
GeneCardsGC06P035418.
H-InvDBHIX0005804.
HGNCHGNC:9235. PPARD.
HPACAB017635.
MIM600409. gene.
PharmGKBPA33557.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG09323.
HOGENOMHBG446936.
HOVERGENQ03181.
InParanoidQ03181.
OMASSLFLND.
OrthoDBEOG9V45TJ.
PhylomeDBQ03181.

Enzyme and pathway databases

Pathway_Interaction_DBps1pathway. Presenilin action in Notch and Wnt signaling.
rxr_vdr_pathway. RXR and RAR hetrodimerization with other nuclear receptor.
ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ03181.
BgeeQ03181.
CleanExHS_PPARD.
GenevestigatorQ03181.
GermOnlineENSG00000112033. Homo sapiens.

Family and domain databases

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]
Gene3DG3DSA:1.10.565.10. Nucl_hrmn_rcpt_lig_bd. 1 hit.
G3DSA:3.30.50.10. Znf_NHR/GATA. 1 hit.
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]
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBQ03181.
DrugBankDB00159. Icosapent.
DB00605. Sulindac.
DB00374. Treprostinil.
NextBio21160.
SOURCESearch...

Entry information

Entry namePPARD_HUMAN
AccessionPrimary (citable) accession number: Q03181
Secondary accession number(s): A8K6J6 expand/collapse secondary AC list , B6ZGS1, Q5D1P0, Q7Z5K0, Q9BUD4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: February 9, 2010
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 6

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents