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Q07869

- PPARA_HUMAN

UniProt

Q07869 - PPARA_HUMAN

Protein

Peroxisome proliferator-activated receptor alpha

Gene

PPARA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei280 – 2801Synthetic agonist5 Publications
    Binding sitei314 – 3141Synthetic agonist5 Publications
    Sitei433 – 4331Essential for heterodimerization with RXRA
    Binding sitei440 – 4401Synthetic agonist5 Publications
    Binding sitei464 – 4641Synthetic agonist5 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi99 – 17375Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri102 – 12221NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri139 – 16123NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. drug binding Source: UniProtKB
    3. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
    4. lipid binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    7. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
    8. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    9. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
    10. sequence-specific DNA binding Source: BHF-UCL
    11. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    12. steroid hormone receptor activity Source: BHF-UCL
    13. ubiquitin conjugating enzyme binding Source: BHF-UCL
    14. zinc ion binding Source: InterPro

    GO - Biological processi

    1. behavioral response to nicotine Source: Ensembl
    2. cellular lipid metabolic process Source: Reactome
    3. circadian regulation of gene expression Source: UniProtKB
    4. enamel mineralization Source: Ensembl
    5. epidermis development Source: Ensembl
    6. fatty acid metabolic process Source: ProtInc
    7. fatty acid transport Source: UniProtKB
    8. gene expression Source: Reactome
    9. heart development Source: Ensembl
    10. intracellular receptor signaling pathway Source: GOC
    11. lipid metabolic process Source: ProtInc
    12. lipoprotein metabolic process Source: Ensembl
    13. negative regulation of appetite Source: UniProtKB
    14. negative regulation of blood pressure Source: Ensembl
    15. negative regulation of cholesterol storage Source: BHF-UCL
    16. negative regulation of glycolytic process Source: BHF-UCL
    17. negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
    18. negative regulation of neuron death Source: Ensembl
    19. negative regulation of protein binding Source: Ensembl
    20. negative regulation of receptor biosynthetic process Source: BHF-UCL
    21. negative regulation of sequestering of triglyceride Source: BHF-UCL
    22. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    23. negative regulation of transcription regulatory region DNA binding Source: Ensembl
    24. positive regulation of fatty acid beta-oxidation Source: UniProtKB
    25. positive regulation of fatty acid oxidation Source: BHF-UCL
    26. positive regulation of transcription, DNA-templated Source: UniProtKB
    27. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    28. regulation of cellular ketone metabolic process by positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    29. regulation of circadian rhythm Source: UniProtKB
    30. regulation of glycolytic by positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    31. regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    32. response to hypoxia Source: Ensembl
    33. response to insulin Source: Ensembl
    34. small molecule metabolic process Source: Reactome
    35. transcription initiation from RNA polymerase II promoter Source: Reactome
    36. wound healing Source: Ensembl

    Keywords - Molecular functioni

    Activator, Receptor

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Lipid-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_15525. Nuclear Receptor transcription pathway.
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_24941. Circadian Clock.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinkiQ07869.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisome proliferator-activated receptor alpha
    Short name:
    PPAR-alpha
    Alternative name(s):
    Nuclear receptor subfamily 1 group C member 1
    Gene namesi
    Name:PPARA
    Synonyms:NR1C1, PPAR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:9232. PPARA.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi122 – 1221C → G: Prevents DNA binding but no effect on heterodimerization with RXRA. 1 Publication
    Mutagenesisi304 – 3041D → A: Reduced heterodimerization with RXRA. Reduced DNA binding. 1 Publication
    Mutagenesisi370 – 3701L → R: Abolishes heterodimerization with RXRA. No DNA binding. 1 Publication
    Mutagenesisi391 – 3911L → R: Abolishes heterodimerization with RXRA. No DNA binding. 1 Publication
    Mutagenesisi422 – 4221L → R: No effect on heterodimerization with RXRA nor on DNA binding and transactivation activity. 1 Publication
    Mutagenesisi431 – 4311A → T: No effect on heterodimerization with RXRA nor on DNA binding. 1 Publication
    Mutagenesisi433 – 4331L → R: Abolishes heterodimerization with RXRA, DNA binding and transactivation activity. 1 Publication

    Organism-specific databases

    MIMi170998. gene+phenotype.
    PharmGKBiPA280.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 468468Peroxisome proliferator-activated receptor alphaPRO_0000053481Add
    BLAST

    Proteomic databases

    PaxDbiQ07869.
    PRIDEiQ07869.

    PTM databases

    PhosphoSiteiQ07869.

    Expressioni

    Tissue specificityi

    Skeletal muscle, liver, heart and kidney.2 Publications

    Gene expression databases

    ArrayExpressiQ07869.
    BgeeiQ07869.
    CleanExiHS_PPARA.
    GenevestigatoriQ07869.

    Interactioni

    Subunit structurei

    Heterodimer; with RXRA. This heterodimerization is required for DNA binding and transactivation activity. Interacts with NCOA3 coactivator. Interacts with CITED2; the interaction stimulates its transcriptional activity. Also interacts with PPARBP in vitro. Interacts with AKAP13, LPIN1, PRDM16 and coactivator NCOA6. Interacts with ASXL1 AND ASXL2. Interacts with PER2.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CHD9Q3L8U1-32EBI-78615,EBI-960730
    NCOR1O753762EBI-78615,EBI-347233

    Protein-protein interaction databases

    BioGridi111461. 36 interactions.
    DIPiDIP-241N.
    IntActiQ07869. 12 interactions.
    MINTiMINT-232229.
    STRINGi9606.ENSP00000262735.

    Structurei

    Secondary structure

    1
    468
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi203 – 21715
    Helixi222 – 2298
    Beta strandi233 – 2353
    Beta strandi239 – 2413
    Helixi244 – 25411
    Helixi256 – 2594
    Helixi263 – 2653
    Helixi268 – 29023
    Helixi291 – 2933
    Turni295 – 2995
    Helixi302 – 32120
    Helixi322 – 3243
    Beta strandi329 – 3324
    Turni333 – 3364
    Beta strandi337 – 3404
    Helixi341 – 3466
    Turni349 – 3513
    Helixi352 – 36615
    Helixi372 – 38312
    Helixi394 – 41522
    Helixi422 – 45029
    Beta strandi453 – 4564
    Helixi458 – 4647
    Turni465 – 4673

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I7GX-ray2.20A196-468[»]
    1K7LX-ray2.50A/C/E/G192-468[»]
    1KKQX-ray3.00A/B/C/D200-468[»]
    2NPAX-ray2.30A/C199-468[»]
    2P54X-ray1.79A202-468[»]
    2REWX-ray2.35A196-468[»]
    2ZNNX-ray2.01A200-468[»]
    3ET1X-ray2.50A/B199-468[»]
    3FEIX-ray2.40A202-468[»]
    3G8IX-ray2.20A199-468[»]
    3KDTX-ray2.70A/B196-468[»]
    3KDUX-ray2.07A/B196-468[»]
    3SP6X-ray2.21A196-468[»]
    3VI8X-ray1.75A200-468[»]
    4BCRX-ray2.50A/B195-468[»]
    ProteinModelPortaliQ07869.
    SMRiQ07869. Positions 95-468.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ07869.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni280 – 468189Ligand-bindingAdd
    BLAST
    Regioni304 – 433130Required for heterodimerization with RXRAAdd
    BLAST

    Sequence similaritiesi

    Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri102 – 12221NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri139 – 16123NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG266867.
    HOGENOMiHOG000261626.
    HOVERGENiHBG106004.
    InParanoidiQ07869.
    KOiK07294.
    OMAiTESPICP.
    PhylomeDBiQ07869.
    TreeFamiTF316304.

    Family and domain databases

    Gene3Di1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProiIPR003074. 1Cnucl_rcpt.
    IPR003076. 1Cnucl_rcpt_A.
    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.
    PR01289. PROXISOMPAAR.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q07869-1) [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

    MVDTESPLCP LSPLEAGDLE SPLSEEFLQE MGNIQEISQS IGEDSSGSFG    50
    FTEYQYLGSC PGSDGSVITD TLSPASSPSS VTYPVVPGSV DESPSGALNI 100
    ECRICGDKAS GYHYGVHACE GCKGFFRRTI RLKLVYDKCD RSCKIQKKNR 150
    NKCQYCRFHK CLSVGMSHNA IRFGRMPRSE KAKLKAEILT CEHDIEDSET 200
    ADLKSLAKRI YEAYLKNFNM NKVKARVILS GKASNNPPFV IHDMETLCMA 250
    EKTLVAKLVA NGIQNKEAEV RIFHCCQCTS VETVTELTEF AKAIPGFANL 300
    DLNDQVTLLK YGVYEAIFAM LSSVMNKDGM LVAYGNGFIT REFLKSLRKP 350
    FCDIMEPKFD FAMKFNALEL DDSDISLFVA AIICCGDRPG LLNVGHIEKM 400
    QEGIVHVLRL HLQSNHPDDI FLFPKLLQKM ADLRQLVTEH AQLVQIIKKT 450
    ESDAALHPLL QEIYRDMY 468
    Length:468
    Mass (Da):52,225
    Last modified:July 15, 1998 - v2
    Checksum:i850846FD51ADA883
    GO
    Isoform 2 (identifier: Q07869-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         171-174: IRFG → FCHT
         175-468: Missing.

    Show »
    Length:174
    Mass (Da):18,942
    Checksum:i8587321146D06A03
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711T → M in CAA68898. (PubMed:8993548)Curated
    Sequence conflicti123 – 1231K → M in CAA68898. (PubMed:8993548)Curated
    Sequence conflicti296 – 2961G → A in AAA36468. (PubMed:7684926)Curated
    Sequence conflicti444 – 4441V → A in CAA68898. (PubMed:8993548)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti127 – 1271R → Q.
    Corresponds to variant rs1800204 [ dbSNP | Ensembl ].
    VAR_016110
    Natural varianti162 – 1621L → V.1 Publication
    Corresponds to variant rs1800206 [ dbSNP | Ensembl ].
    VAR_016111
    Natural varianti227 – 2271V → A.
    Corresponds to variant rs1800234 [ dbSNP | Ensembl ].
    VAR_016112
    Natural varianti268 – 2681A → V.1 Publication
    Corresponds to variant rs1042311 [ dbSNP | Ensembl ].
    VAR_016113
    Natural varianti304 – 3041D → N.
    Corresponds to variant rs1800242 [ dbSNP | Ensembl ].
    VAR_016114
    Natural varianti395 – 3951G → R.
    Corresponds to variant rs2229245 [ dbSNP | Ensembl ].
    VAR_050578
    Natural varianti409 – 4091R → T.
    Corresponds to variant rs1800243 [ dbSNP | Ensembl ].
    VAR_016115

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei171 – 1744IRFG → FCHT in isoform 2. 1 PublicationVSP_047571
    Alternative sequencei175 – 468294Missing in isoform 2. 1 PublicationVSP_047572Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02932 mRNA. Translation: AAA36468.1.
    S74349 mRNA. Translation: AAB32649.1.
    Y07619 mRNA. Translation: CAA68898.1.
    AB307690 mRNA. Translation: BAH02281.1.
    EU650667 mRNA. Translation: ACD12656.1.
    EU395809 mRNA. Translation: ABY73535.1.
    CR456547 mRNA. Translation: CAG30433.1.
    AK289821 mRNA. Translation: BAF82510.1.
    CR457435 mRNA. Translation: CAG33716.1.
    AY206718 Genomic DNA. Translation: AAO13489.1.
    AL049856, AL078611 Genomic DNA. Translation: CAI22450.1.
    Z94161 Genomic DNA. No translation available.
    CH471138 Genomic DNA. Translation: EAW73402.1.
    CCDSiCCDS33669.1. [Q07869-1]
    PIRiA49289.
    I56603.
    RefSeqiNP_001001928.1. NM_001001928.2. [Q07869-1]
    NP_005027.2. NM_005036.4. [Q07869-1]
    XP_005261710.1. XM_005261653.2. [Q07869-1]
    XP_005261712.1. XM_005261655.1. [Q07869-1]
    XP_005261713.1. XM_005261656.1. [Q07869-1]
    XP_005261714.1. XM_005261657.1. [Q07869-1]
    XP_006724332.1. XM_006724269.1. [Q07869-1]
    XP_006724333.1. XM_006724270.1. [Q07869-1]
    UniGeneiHs.103110.
    Hs.710044.

    Genome annotation databases

    EnsembliENST00000262735; ENSP00000262735; ENSG00000186951. [Q07869-1]
    ENST00000402126; ENSP00000385246; ENSG00000186951. [Q07869-1]
    ENST00000407236; ENSP00000385523; ENSG00000186951. [Q07869-1]
    GeneIDi5465.
    KEGGihsa:5465.
    UCSCiuc003bgw.1. human. [Q07869-1]

    Polymorphism databases

    DMDMi3041727.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Peroxisome proliferator-activated receptor entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02932 mRNA. Translation: AAA36468.1 .
    S74349 mRNA. Translation: AAB32649.1 .
    Y07619 mRNA. Translation: CAA68898.1 .
    AB307690 mRNA. Translation: BAH02281.1 .
    EU650667 mRNA. Translation: ACD12656.1 .
    EU395809 mRNA. Translation: ABY73535.1 .
    CR456547 mRNA. Translation: CAG30433.1 .
    AK289821 mRNA. Translation: BAF82510.1 .
    CR457435 mRNA. Translation: CAG33716.1 .
    AY206718 Genomic DNA. Translation: AAO13489.1 .
    AL049856 , AL078611 Genomic DNA. Translation: CAI22450.1 .
    Z94161 Genomic DNA. No translation available.
    CH471138 Genomic DNA. Translation: EAW73402.1 .
    CCDSi CCDS33669.1. [Q07869-1 ]
    PIRi A49289.
    I56603.
    RefSeqi NP_001001928.1. NM_001001928.2. [Q07869-1 ]
    NP_005027.2. NM_005036.4. [Q07869-1 ]
    XP_005261710.1. XM_005261653.2. [Q07869-1 ]
    XP_005261712.1. XM_005261655.1. [Q07869-1 ]
    XP_005261713.1. XM_005261656.1. [Q07869-1 ]
    XP_005261714.1. XM_005261657.1. [Q07869-1 ]
    XP_006724332.1. XM_006724269.1. [Q07869-1 ]
    XP_006724333.1. XM_006724270.1. [Q07869-1 ]
    UniGenei Hs.103110.
    Hs.710044.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I7G X-ray 2.20 A 196-468 [» ]
    1K7L X-ray 2.50 A/C/E/G 192-468 [» ]
    1KKQ X-ray 3.00 A/B/C/D 200-468 [» ]
    2NPA X-ray 2.30 A/C 199-468 [» ]
    2P54 X-ray 1.79 A 202-468 [» ]
    2REW X-ray 2.35 A 196-468 [» ]
    2ZNN X-ray 2.01 A 200-468 [» ]
    3ET1 X-ray 2.50 A/B 199-468 [» ]
    3FEI X-ray 2.40 A 202-468 [» ]
    3G8I X-ray 2.20 A 199-468 [» ]
    3KDT X-ray 2.70 A/B 196-468 [» ]
    3KDU X-ray 2.07 A/B 196-468 [» ]
    3SP6 X-ray 2.21 A 196-468 [» ]
    3VI8 X-ray 1.75 A 200-468 [» ]
    4BCR X-ray 2.50 A/B 195-468 [» ]
    ProteinModelPortali Q07869.
    SMRi Q07869. Positions 95-468.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111461. 36 interactions.
    DIPi DIP-241N.
    IntActi Q07869. 12 interactions.
    MINTi MINT-232229.
    STRINGi 9606.ENSP00000262735.

    Chemistry

    BindingDBi Q07869.
    ChEMBLi CHEMBL239.
    DrugBanki DB01076. Atorvastatin.
    DB01393. Bezafibrate.
    DB00636. Clofibrate.
    DB01039. Fenofibrate.
    DB01241. Gemfibrozil.
    DB00641. Simvastatin.
    GuidetoPHARMACOLOGYi 593.

    PTM databases

    PhosphoSitei Q07869.

    Polymorphism databases

    DMDMi 3041727.

    Proteomic databases

    PaxDbi Q07869.
    PRIDEi Q07869.

    Protocols and materials databases

    DNASUi 5465.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262735 ; ENSP00000262735 ; ENSG00000186951 . [Q07869-1 ]
    ENST00000402126 ; ENSP00000385246 ; ENSG00000186951 . [Q07869-1 ]
    ENST00000407236 ; ENSP00000385523 ; ENSG00000186951 . [Q07869-1 ]
    GeneIDi 5465.
    KEGGi hsa:5465.
    UCSCi uc003bgw.1. human. [Q07869-1 ]

    Organism-specific databases

    CTDi 5465.
    GeneCardsi GC22P046546.
    HGNCi HGNC:9232. PPARA.
    MIMi 170998. gene+phenotype.
    neXtProti NX_Q07869.
    PharmGKBi PA280.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG266867.
    HOGENOMi HOG000261626.
    HOVERGENi HBG106004.
    InParanoidi Q07869.
    KOi K07294.
    OMAi TESPICP.
    PhylomeDBi Q07869.
    TreeFami TF316304.

    Enzyme and pathway databases

    Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_15525. Nuclear Receptor transcription pathway.
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_24941. Circadian Clock.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinki Q07869.

    Miscellaneous databases

    EvolutionaryTracei Q07869.
    GeneWikii Peroxisome_proliferator-activated_receptor_alpha.
    GenomeRNAii 5465.
    NextBioi 21152.
    PROi Q07869.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q07869.
    Bgeei Q07869.
    CleanExi HS_PPARA.
    Genevestigatori Q07869.

    Family and domain databases

    Gene3Di 1.10.565.10. 2 hits.
    3.30.50.10. 1 hit.
    InterProi IPR003074. 1Cnucl_rcpt.
    IPR003076. 1Cnucl_rcpt_A.
    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.
    PR01289. PROXISOMPAAR.
    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. "cDNA cloning, chromosomal mapping, and functional characterization of the human peroxisome proliferator activated receptor."
      Sher T., Yi H.F., McBride O.W., Gonzales F.J.
      Biochemistry 32:5598-5604(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANT VAL-268.
      Tissue: Liver.
    2. "Human and rat peroxisome proliferator activated receptors (PPARs) demonstrate similar tissue distribution but different responsiveness to PPAR activators."
      Mukherjee R., Jow L., Noonan D., McDonnell D.P.
      J. Steroid Biochem. Mol. Biol. 51:157-166(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Liver.
    3. "Peroxisome proliferator-activated receptors: structures and function."
      Tugwood J.D., Aldridge T.C., Lambe K.G., Macdonald N., Woodyatt N.J.
      Ann. N. Y. Acad. Sci. 804:252-265(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    4. "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).
    5. "Optimization of an enzyme-linked immunosorbent assay to screen ligand of Peroxisome proliferator-activated receptor alpha."
      Cho M.-C., Lee S., Choi H.S., Yang Y., Tae Hong J., Kim S.J., Yoon D.-Y.
      Immunopharmacol. Immunotoxicol. 31:459-467(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. "A novel alternatively spliced peroxisome proliferator-activated receptor alpha."
      Jiang Y., Xie Z., Liu H., Liu M., Liu F.
      Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "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] (ISOFORM 1).
      Tissue: Brain.
    9. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    10. SeattleSNPs variation discovery resource
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-162.
    11. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. "Peroxisome proliferator-activated receptor mediates cross-talk with thyroid hormone receptor by competition for retinoid X receptor. Possible role of a leucine zipper-like heptad repeat."
      Juge-Aubry C.E., Gorla-Bajszczak A., Pernin A., Lemberger T., Wahli W., Burger A.G., Meier C.A.
      J. Biol. Chem. 270:18117-18122(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: HETERODIMERIZATION WITH RXRA, FUNCTION, MUTAGENESIS OF CYS-122; LEU-422 AND LEU-433.
    14. "RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2."
      Li H., Gomes P.J., Chen J.D.
      Proc. Natl. Acad. Sci. U.S.A. 94:8479-8484(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA3.
    15. "Regulation of peroxisome proliferator-activated receptor alpha-induced transactivation by the nuclear orphan receptor TAK1/TR4."
      Yan Z.H., Karam W.G., Staudinger J.L., Medvedev A., Ghanayem B.I., Jetten A.M.
      J. Biol. Chem. 273:10948-10957(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Conserved amino acids in the ligand-binding and tau(i) domains of the peroxisome proliferator-activated receptor alpha are necessary for heterodimerization with RXR."
      Gorla-Bajszczak A., Juge-Aubry C., Pernin A., Burger A.G., Meier C.A.
      Mol. Cell. Endocrinol. 147:37-47(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: HETERODIMERIZATION WITH RXRA, FUNCTION, MUTAGENESIS OF ASP-304; LEU-370; LEU-391 AND ALA-431.
    17. "Cloning and characterization of RAP250, a nuclear receptor coactivator."
      Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.
      J. Biol. Chem. 275:5308-5317(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA6.
    18. "Interaction of hepatitis C virus core protein with retinoid X receptor alpha modulates its transcriptional activity."
      Tsutsumi T., Suzuki T., Shimoike T., Suzuki R., Moriya K., Shintani Y., Fujie H., Matsuura Y., Koike K., Miyamura T.
      Hepatology 35:937-946(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: HETERODIMERIZATION WITH RXRA.
    19. "Oleylethanolamide regulates feeding and body weight through activation of the nuclear receptor PPAR-alpha."
      Fu J., Gaetani S., Oveisi F., Lo Verme J., Serrano A., Rodriguez De Fonseca F., Rosengarth A., Luecke H., Di Giacomo B., Tarzia G., Piomelli D.
      Nature 425:90-93(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS RECEPTOR FOR OLEYLETHANOLAMIDE.
    20. "Additional sex comb-like (ASXL) proteins 1 and 2 play opposite roles in adipogenesis via reciprocal regulation of peroxisome proliferator-activated receptor {gamma}."
      Park U.H., Yoon S.K., Park T., Kim E.J., Um S.J.
      J. Biol. Chem. 286:1354-1363(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ASXL1 AND ASXL2.
    21. "Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors."
      Xu H.E., Lambert M.H., Montana V.G., Plunket K.D., Moore L.B., Collins J.L., Oplinger J.A., Kliewer S.A., Gampe R.T. Jr., McKee D.D., Moore J.T., Willson T.M.
      Proc. Natl. Acad. Sci. U.S.A. 98:13919-13924(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 192-468 IN COMPLEX WITH SYNTHETIC AGONIST.
    22. "Structure of the PPARalpha and -gamma ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family."
      Cronet P., Petersen J.F.W., Folmer R., Blomberg N., Sjoeblom K., Karlsson U., Lindstedt E.-L., Bamberg K.
      Structure 9:699-706(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 196-468 IN COMPLEX WITH SYNTHETIC AGONIST.
    23. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 200-468 IN COMPLEX WITH SYNTHETIC AGONIST.
    24. "Design and synthesis of oxime ethers of alpha-acyl-beta-phenylpropanoic acids as PPAR dual agonists."
      Oon Han H., Kim S.H., Kim K.-H., Hur G.-C., Joo Yim H., Chung H.-K., Ho Woo S., Dong Koo K., Lee C.-S., Sung Koh J., Kim G.T.
      Bioorg. Med. Chem. Lett. 17:937-941(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 199-468 IN COMPLEX WITH SYNTHETIC AGONIST.
    25. Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 202-468 IN COMPLEX WITH SYNTHETIC AGONIST.
    26. "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 (2.01 ANGSTROMS) OF 200-468 IN COMPLEX WITH THE SYNTHETIC AGONIST TIPP-703.
    27. "Aleglitazar, a new, potent, and balanced dual PPARalpha/gamma agonist for the treatment of type II diabetes."
      Benardeau A., Benz J., Binggeli A., Blum D., Boehringer M., Grether U., Hilpert H., Kuhn B., Maerki H.P., Meyer M., Puentener K., Raab S., Ruf A., Schlatter D., Mohr P.
      Bioorg. Med. Chem. Lett. 19:2468-2473(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 199-468 IN COMPLEX WITH ALEGLITAZAR.
    28. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 199-468 IN COMPLEX WITH INDEGLITAZAR.

    Entry informationi

    Entry nameiPPARA_HUMAN
    AccessioniPrimary (citable) accession number: Q07869
    Secondary accession number(s): B0G0X3
    , Q16241, Q6I9S0, Q92486, Q92689, Q9Y3N1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 175 of the entry and version 2 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 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3