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Peroxisome proliferator-activated receptor alpha (PPAR-alpha) (Nuclear receptor subfamily 1 group C member 1)

 PPARA_HUMAN             Reviewed;         468 AA.
Q07869; B0G0X3; Q16241; Q6I9S0; Q92486; Q92689; Q9Y3N1;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
25-OCT-2017, entry version 207.
RecName: Full=Peroxisome proliferator-activated receptor alpha;
Short=PPAR-alpha;
AltName: Full=Nuclear receptor subfamily 1 group C member 1;
Name=PPARA; Synonyms=NR1C1, PPAR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANT VAL-268.
TISSUE=Liver;
PubMed=7684926; DOI=10.1021/bi00072a015;
Sher T., Yi H.F., McBride O.W., Gonzales F.J.;
"cDNA cloning, chromosomal mapping, and functional characterization of
the human peroxisome proliferator activated receptor.";
Biochemistry 32:5598-5604(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=7981125; DOI=10.1016/0960-0760(94)90089-2;
Mukherjee R., Jow L., Noonan D., McDonnell D.P.;
"Human and rat peroxisome proliferator activated receptors (PPARs)
demonstrate similar tissue distribution but different responsiveness
to PPAR activators.";
J. Steroid Biochem. Mol. Biol. 51:157-166(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=8993548; DOI=10.1111/j.1749-6632.1996.tb18620.x;
Tugwood J.D., Aldridge T.C., Lambe K.G., Macdonald N., Woodyatt N.J.;
"Peroxisome proliferator-activated receptors: structures and
function.";
Ann. N. Y. Acad. Sci. 804:252-265(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=18619963; DOI=10.1016/j.febslet.2008.07.003;
Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T.;
"DNA-binding profiling of human hormone nuclear receptors via
fluorescence correlation spectroscopy in a cell-free system.";
FEBS Lett. 582:2737-2744(2008).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=19263263; DOI=10.1080/08923970902785246;
Cho M.-C., Lee S., Choi H.S., Yang Y., Tae Hong J., Kim S.J.,
Yoon D.-Y.;
"Optimization of an enzyme-linked immunosorbent assay to screen ligand
of Peroxisome proliferator-activated receptor alpha.";
Immunopharmacol. Immunotoxicol. 31:459-467(2009).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Jiang Y., Xie Z., Liu H., Liu M., Liu F.;
"A novel alternatively spliced peroxisome proliferator-activated
receptor alpha.";
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-162.
SeattleSNPs variation discovery resource;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
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.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[13]
HETERODIMERIZATION WITH RXRA, FUNCTION, AND MUTAGENESIS OF CYS-122;
LEU-422 AND LEU-433.
PubMed=7629123; DOI=10.1074/jbc.270.30.18117;
Juge-Aubry C.E., Gorla-Bajszczak A., Pernin A., Lemberger T.,
Wahli W., Burger A.G., Meier C.A.;
"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.";
J. Biol. Chem. 270:18117-18122(1995).
[14]
INTERACTION WITH NCOA3.
PubMed=9238002; DOI=10.1073/pnas.94.16.8479;
Li H., Gomes P.J., Chen J.D.;
"RAC3, a steroid/nuclear receptor-associated coactivator that is
related to SRC-1 and TIF2.";
Proc. Natl. Acad. Sci. U.S.A. 94:8479-8484(1997).
[15]
FUNCTION.
PubMed=9556573; DOI=10.1074/jbc.273.18.10948;
Yan Z.H., Karam W.G., Staudinger J.L., Medvedev A., Ghanayem B.I.,
Jetten A.M.;
"Regulation of peroxisome proliferator-activated receptor alpha-
induced transactivation by the nuclear orphan receptor TAK1/TR4.";
J. Biol. Chem. 273:10948-10957(1998).
[16]
HETERODIMERIZATION WITH RXRA, FUNCTION, AND MUTAGENESIS OF ASP-304;
LEU-370; LEU-391 AND ALA-431.
PubMed=10195690; DOI=10.1016/S0303-7207(98)00217-2;
Gorla-Bajszczak A., Juge-Aubry C., Pernin A., Burger A.G., Meier C.A.;
"Conserved amino acids in the ligand-binding and tau(i) domains of the
peroxisome proliferator-activated receptor alpha are necessary for
heterodimerization with RXR.";
Mol. Cell. Endocrinol. 147:37-47(1999).
[17]
INTERACTION WITH NCOA6.
PubMed=10681503; DOI=10.1074/jbc.275.8.5308;
Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.;
"Cloning and characterization of RAP250, a nuclear receptor
coactivator.";
J. Biol. Chem. 275:5308-5317(2000).
[18]
HETERODIMERIZATION WITH RXRA.
PubMed=11915042; DOI=10.1053/jhep.2002.32470;
Tsutsumi T., Suzuki T., Shimoike T., Suzuki R., Moriya K.,
Shintani Y., Fujie H., Matsuura Y., Koike K., Miyamura T.;
"Interaction of hepatitis C virus core protein with retinoid X
receptor alpha modulates its transcriptional activity.";
Hepatology 35:937-946(2002).
[19]
IDENTIFICATION AS RECEPTOR FOR OLEYLETHANOLAMIDE.
PubMed=12955147; DOI=10.1038/nature01921;
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.;
"Oleylethanolamide regulates feeding and body weight through
activation of the nuclear receptor PPAR-alpha.";
Nature 425:90-93(2003).
[20]
INTERACTION WITH ASXL1 AND ASXL2.
PubMed=21047783; DOI=10.1074/jbc.M110.177816;
Park U.H., Yoon S.K., Park T., Kim E.J., Um S.J.;
"Additional sex comb-like (ASXL) proteins 1 and 2 play opposite roles
in adipogenesis via reciprocal regulation of peroxisome proliferator-
activated receptor {gamma}.";
J. Biol. Chem. 286:1354-1363(2011).
[21]
INTERACTION WITH SIRT1, AND FUNCTION.
PubMed=24043310; DOI=10.1128/MCB.00087-13;
Laurent G., de Boer V.C., Finley L.W., Sweeney M., Lu H., Schug T.T.,
Cen Y., Jeong S.M., Li X., Sauve A.A., Haigis M.C.;
"SIRT4 represses peroxisome proliferator-activated receptor alpha
activity to suppress hepatic fat oxidation.";
Mol. Cell. Biol. 33:4552-4561(2013).
[22]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 192-468 IN COMPLEX WITH
SYNTHETIC AGONIST.
PubMed=11698662; DOI=10.1073/pnas.241410198;
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.;
"Structural determinants of ligand binding selectivity between the
peroxisome proliferator-activated receptors.";
Proc. Natl. Acad. Sci. U.S.A. 98:13919-13924(2001).
[23]
X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 196-468 IN COMPLEX WITH
SYNTHETIC AGONIST.
PubMed=11587644; DOI=10.1016/S0969-2126(01)00634-7;
Cronet P., Petersen J.F.W., Folmer R., Blomberg N., Sjoeblom K.,
Karlsson U., Lindstedt E.-L., Bamberg K.;
"Structure of the PPARalpha and -gamma ligand binding domain in
complex with AZ 242; ligand selectivity and agonist activation in the
PPAR family.";
Structure 9:699-706(2001).
[24]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 200-468 IN COMPLEX WITH
SYNTHETIC AGONIST.
PubMed=11845213; DOI=10.1038/415813a;
Xu H.E., Stanley T.B., Montana V.G., Lambert M.H., Shearer B.G.,
Cobb J.E., McKee D.D., Galardi C.M., Plunket K.D., Nolte R.T.,
Parks D.J., Moore J.T., Kliewer S.A., Willson T.M., Stimmel J.B.;
"Structural basis for antagonist-mediated recruitment of nuclear co-
repressors by PPARalpha.";
Nature 415:813-817(2002).
[25]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 199-468 IN COMPLEX WITH
SYNTHETIC AGONIST.
PubMed=17157019; DOI=10.1016/j.bmcl.2006.11.050;
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.;
"Design and synthesis of oxime ethers of alpha-acyl-beta-
phenylpropanoic acids as PPAR dual agonists.";
Bioorg. Med. Chem. Lett. 17:937-941(2007).
[26]
X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 202-468 IN COMPLEX WITH
SYNTHETIC AGONIST.
PubMed=17243659; DOI=10.1021/jm058056x;
Sierra M.L., Beneton V., Boullay A.-B., Boyer T., Brewster A.G.,
Donche F., Forest M.-C., Fouchet M.-H., Gellibert F.J., Grillot D.A.,
Lambert M.H., Laroze A., Le Grumelec C., Linget J.M., Montana V.G.,
Nguyen V.-L., Nicodeme E., Patel V., Penfornis A., Pineau O.,
Pohin D., Potvain F., Poulain G., Ruault C.B., Saunders M., Toum J.,
Xu H.E., Xu R.X., Pianetti P.M.;
"Substituted 2-[(4-aminomethyl)phenoxy]-2-methylpropionic acid
PPARalpha agonists. 1. Discovery of a novel series of potent HDLc
raising agents.";
J. Med. Chem. 50:685-695(2007).
[27]
X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 200-468 IN COMPLEX WITH THE
SYNTHETIC AGONIST TIPP-703.
PubMed=19622862; DOI=10.1107/S0907444909015935;
Oyama T., Toyota K., Waku T., Hirakawa Y., Nagasawa N., Kasuga J.I.,
Hashimoto Y., Miyachi H., Morikawa K.;
"Adaptability and selectivity of human peroxisome proliferator-
activated receptor (PPAR) pan agonists revealed from crystal
structures.";
Acta Crystallogr. D 65:786-795(2009).
[28]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 199-468 IN COMPLEX WITH
ALEGLITAZAR.
PubMed=19349176; DOI=10.1016/j.bmcl.2009.03.036;
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.;
"Aleglitazar, a new, potent, and balanced dual PPARalpha/gamma agonist
for the treatment of type II diabetes.";
Bioorg. Med. Chem. Lett. 19:2468-2473(2009).
[29]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 199-468 IN COMPLEX WITH
INDEGLITAZAR.
PubMed=19116277; DOI=10.1073/pnas.0811325106;
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.;
"Scaffold-based discovery of indeglitazar, a PPAR pan-active anti-
diabetic agent.";
Proc. Natl. Acad. Sci. U.S.A. 106:262-267(2009).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:10195690, ECO:0000269|PubMed:24043310,
ECO:0000269|PubMed:7629123, ECO:0000269|PubMed:7684926,
ECO:0000269|PubMed:9556573}.
-!- SUBUNIT: 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. Interacts with SIRT1; the interaction seems to be modulated
by NAD(+) levels (PubMed:24043310). {ECO:0000250|UniProtKB:P23204,
ECO:0000250|UniProtKB:P37230, ECO:0000269|PubMed:10681503,
ECO:0000269|PubMed:11587644, ECO:0000269|PubMed:11698662,
ECO:0000269|PubMed:11845213, ECO:0000269|PubMed:17157019,
ECO:0000269|PubMed:17243659, ECO:0000269|PubMed:19116277,
ECO:0000269|PubMed:19349176, ECO:0000269|PubMed:19622862,
ECO:0000269|PubMed:21047783, ECO:0000269|PubMed:24043310,
ECO:0000269|PubMed:9238002}.
-!- INTERACTION:
Q3L8U1-3:CHD9; NbExp=2; IntAct=EBI-78615, EBI-960730;
P62993:GRB2; NbExp=3; IntAct=EBI-78615, EBI-401755;
O75376:NCOR1; NbExp=3; IntAct=EBI-78615, EBI-347233;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q07869-1; Sequence=Displayed;
Name=2;
IsoId=Q07869-2; Sequence=VSP_047571, VSP_047572;
-!- TISSUE SPECIFICITY: Skeletal muscle, liver, heart and kidney.
{ECO:0000269|PubMed:7981125, ECO:0000269|PubMed:8993548}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Peroxisome proliferator-
activated receptor entry;
URL="https://en.wikipedia.org/wiki/Peroxisome_proliferator-activated_receptor";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/ppara/";
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EMBL; L02932; AAA36468.1; -; mRNA.
EMBL; S74349; AAB32649.1; -; mRNA.
EMBL; Y07619; CAA68898.1; -; mRNA.
EMBL; AB307690; BAH02281.1; -; mRNA.
EMBL; EU650667; ACD12656.1; -; mRNA.
EMBL; EU395809; ABY73535.1; -; mRNA.
EMBL; CR456547; CAG30433.1; -; mRNA.
EMBL; AK289821; BAF82510.1; -; mRNA.
EMBL; CR457435; CAG33716.1; -; mRNA.
EMBL; AY206718; AAO13489.1; -; Genomic_DNA.
EMBL; AL049856; CAI22450.1; -; Genomic_DNA.
EMBL; AL078611; CAI22450.1; JOINED; Genomic_DNA.
EMBL; Z94161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471138; EAW73402.1; -; Genomic_DNA.
CCDS; CCDS33669.1; -. [Q07869-1]
PIR; A49289; A49289.
PIR; I56603; I56603.
RefSeq; NP_001001928.1; NM_001001928.2. [Q07869-1]
RefSeq; NP_005027.2; NM_005036.4. [Q07869-1]
RefSeq; XP_005261712.1; XM_005261655.3. [Q07869-1]
RefSeq; XP_005261713.1; XM_005261656.3. [Q07869-1]
RefSeq; XP_006724332.1; XM_006724269.3. [Q07869-1]
RefSeq; XP_006724333.1; XM_006724270.3. [Q07869-1]
RefSeq; XP_011528541.1; XM_011530239.2. [Q07869-1]
RefSeq; XP_011528542.1; XM_011530240.2. [Q07869-1]
RefSeq; XP_011528543.1; XM_011530241.2. [Q07869-1]
RefSeq; XP_011528544.1; XM_011530242.2. [Q07869-1]
RefSeq; XP_011528545.1; XM_011530243.2. [Q07869-1]
UniGene; Hs.103110; -.
UniGene; Hs.710044; -.
PDB; 1I7G; X-ray; 2.20 A; A=196-468.
PDB; 1K7L; X-ray; 2.50 A; A/C/E/G=192-468.
PDB; 1KKQ; X-ray; 3.00 A; A/B/C/D=200-468.
PDB; 2NPA; X-ray; 2.30 A; A/C=199-468.
PDB; 2P54; X-ray; 1.79 A; A=202-468.
PDB; 2REW; X-ray; 2.35 A; A=196-468.
PDB; 2ZNN; X-ray; 2.01 A; A=200-468.
PDB; 3ET1; X-ray; 2.50 A; A/B=199-468.
PDB; 3FEI; X-ray; 2.40 A; A=202-468.
PDB; 3G8I; X-ray; 2.20 A; A=199-468.
PDB; 3KDT; X-ray; 2.70 A; A/B=196-468.
PDB; 3KDU; X-ray; 2.07 A; A/B=196-468.
PDB; 3SP6; X-ray; 2.21 A; A=196-468.
PDB; 3VI8; X-ray; 1.75 A; A=200-468.
PDB; 4BCR; X-ray; 2.50 A; A/B=195-468.
PDB; 4CI4; X-ray; 2.30 A; A=195-468.
PDB; 5AZT; X-ray; 3.45 A; A/B=201-468.
PDB; 5HYK; X-ray; 1.83 A; A=200-468.
PDBsum; 1I7G; -.
PDBsum; 1K7L; -.
PDBsum; 1KKQ; -.
PDBsum; 2NPA; -.
PDBsum; 2P54; -.
PDBsum; 2REW; -.
PDBsum; 2ZNN; -.
PDBsum; 3ET1; -.
PDBsum; 3FEI; -.
PDBsum; 3G8I; -.
PDBsum; 3KDT; -.
PDBsum; 3KDU; -.
PDBsum; 3SP6; -.
PDBsum; 3VI8; -.
PDBsum; 4BCR; -.
PDBsum; 4CI4; -.
PDBsum; 5AZT; -.
PDBsum; 5HYK; -.
ProteinModelPortal; Q07869; -.
SMR; Q07869; -.
BioGrid; 111461; 43.
DIP; DIP-241N; -.
IntAct; Q07869; 18.
MINT; MINT-232229; -.
STRING; 9606.ENSP00000262735; -.
BindingDB; Q07869; -.
ChEMBL; CHEMBL239; -.
DrugBank; DB07724; 3-{5-methoxy-1-[(4-methoxyphenyl)sulfonyl]-1H-indol-3-yl}propanoic acid.
DrugBank; DB08915; Aleglitazar.
DrugBank; DB01393; Bezafibrate.
DrugBank; DB00636; Clofibrate.
DrugBank; DB01039; Fenofibrate.
DrugBank; DB01241; Gemfibrozil.
DrugBank; DB05187; GFT505.
DrugBank; DB00328; Indomethacin.
DrugBank; DB01708; Prasterone.
DrugBank; DB04971; Reglixane.
GuidetoPHARMACOLOGY; 593; -.
SwissLipids; SLP:000001644; -.
iPTMnet; Q07869; -.
PhosphoSitePlus; Q07869; -.
BioMuta; PPARA; -.
DMDM; 3041727; -.
PaxDb; Q07869; -.
PeptideAtlas; Q07869; -.
PRIDE; Q07869; -.
DNASU; 5465; -.
Ensembl; ENST00000262735; ENSP00000262735; ENSG00000186951. [Q07869-1]
Ensembl; ENST00000402126; ENSP00000385246; ENSG00000186951. [Q07869-1]
Ensembl; ENST00000407236; ENSP00000385523; ENSG00000186951. [Q07869-1]
GeneID; 5465; -.
KEGG; hsa:5465; -.
UCSC; uc003bgx.1; human. [Q07869-1]
CTD; 5465; -.
DisGeNET; 5465; -.
EuPathDB; HostDB:ENSG00000186951.16; -.
GeneCards; PPARA; -.
HGNC; HGNC:9232; PPARA.
HPA; HPA058901; -.
HPA; HPA067049; -.
MIM; 170998; gene+phenotype.
neXtProt; NX_Q07869; -.
OpenTargets; ENSG00000186951; -.
PharmGKB; PA280; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00870000136388; -.
HOGENOM; HOG000261626; -.
HOVERGEN; HBG106004; -.
InParanoid; Q07869; -.
KO; K07294; -.
OMA; FSFTEYQ; -.
OrthoDB; EOG091G05U8; -.
PhylomeDB; Q07869; -.
TreeFam; TF316304; -.
Reactome; R-HSA-1368082; RORA activates gene expression.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-8951671; RUNX3 regulates YAP1-mediated transcription.
SignaLink; Q07869; -.
SIGNOR; Q07869; -.
ChiTaRS; PPARA; human.
EvolutionaryTrace; Q07869; -.
GeneWiki; Peroxisome_proliferator-activated_receptor_alpha; -.
GenomeRNAi; 5465; -.
PRO; PR:Q07869; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000186951; -.
CleanEx; HS_PPARA; -.
ExpressionAtlas; Q07869; baseline and differential.
Genevisible; Q07869; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
GO; GO:0097371; F:MDM2/MDM4 family protein binding; IEA:Ensembl.
GO; GO:0051525; F:NFAT protein binding; IEA:Ensembl.
GO; GO:0019902; F:phosphatase binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL.
GO; GO:0004879; F:RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:BHF-UCL.
GO; GO:0003707; F:steroid hormone receptor activity; IDA:BHF-UCL.
GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; IEA:Ensembl.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0035095; P:behavioral response to nicotine; IEA:Ensembl.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0070166; P:enamel mineralization; IEA:Ensembl.
GO; GO:0008544; P:epidermis development; IEA:Ensembl.
GO; GO:0006631; P:fatty acid metabolic process; TAS:ProtInc.
GO; GO:0015908; P:fatty acid transport; TAS:UniProtKB.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0042157; P:lipoprotein metabolic process; IEA:Ensembl.
GO; GO:0032099; P:negative regulation of appetite; ISS:UniProtKB.
GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl.
GO; GO:0010887; P:negative regulation of cholesterol storage; IDA:BHF-UCL.
GO; GO:0045820; P:negative regulation of glycolytic process; IC:BHF-UCL.
GO; GO:0050728; P:negative regulation of inflammatory response; IDA:BHF-UCL.
GO; GO:1903038; P:negative regulation of leukocyte cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
GO; GO:1902894; P:negative regulation of pri-miRNA transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
GO; GO:0010871; P:negative regulation of receptor biosynthetic process; IDA:BHF-UCL.
GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IEA:Ensembl.
GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; TAS:UniProtKB.
GO; GO:0046321; P:positive regulation of fatty acid oxidation; ISS:BHF-UCL.
GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0072366; P:regulation of cellular ketone metabolic process by positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0072363; P:regulation of glycolytic process by positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0072369; P:regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR003074; 1Cnucl_rcpt.
InterPro; IPR003076; 1Cnucl_rcpt_A.
InterPro; IPR035500; NHR_like_domain.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR01288; PROXISOMEPAR.
PRINTS; PR01289; PROXISOMPAAR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Biological rhythms;
Complete proteome; DNA-binding; Lipid-binding; Metal-binding; Nucleus;
Polymorphism; Receptor; Reference proteome; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 468 Peroxisome proliferator-activated
receptor alpha.
/FTId=PRO_0000053481.
DNA_BIND 99 173 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 102 122 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 139 161 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 280 468 Ligand-binding.
REGION 304 433 Required for heterodimerization with
RXRA.
BINDING 280 280 Synthetic agonist.
{ECO:0000269|PubMed:11587644,
ECO:0000269|PubMed:11698662,
ECO:0000269|PubMed:11845213,
ECO:0000269|PubMed:17157019,
ECO:0000269|PubMed:17243659}.
BINDING 314 314 Synthetic agonist.
{ECO:0000269|PubMed:11587644,
ECO:0000269|PubMed:11698662,
ECO:0000269|PubMed:11845213,
ECO:0000269|PubMed:17157019,
ECO:0000269|PubMed:17243659}.
BINDING 440 440 Synthetic agonist.
{ECO:0000269|PubMed:11587644,
ECO:0000269|PubMed:11698662,
ECO:0000269|PubMed:11845213,
ECO:0000269|PubMed:17157019,
ECO:0000269|PubMed:17243659}.
BINDING 464 464 Synthetic agonist.
{ECO:0000269|PubMed:11587644,
ECO:0000269|PubMed:11698662,
ECO:0000269|PubMed:11845213,
ECO:0000269|PubMed:17157019,
ECO:0000269|PubMed:17243659}.
SITE 433 433 Essential for heterodimerization with
RXRA.
VAR_SEQ 171 174 IRFG -> FCHT (in isoform 2).
{ECO:0000303|Ref.6}.
/FTId=VSP_047571.
VAR_SEQ 175 468 Missing (in isoform 2).
{ECO:0000303|Ref.6}.
/FTId=VSP_047572.
VARIANT 127 127 R -> Q (in dbSNP:rs1800204).
/FTId=VAR_016110.
VARIANT 162 162 L -> V (in dbSNP:rs1800206).
{ECO:0000269|Ref.10}.
/FTId=VAR_016111.
VARIANT 227 227 V -> A (in dbSNP:rs1800234).
/FTId=VAR_016112.
VARIANT 268 268 A -> V (in dbSNP:rs1042311).
{ECO:0000269|PubMed:7684926}.
/FTId=VAR_016113.
VARIANT 304 304 D -> N (in dbSNP:rs1800242).
/FTId=VAR_016114.
VARIANT 395 395 G -> R (in dbSNP:rs2229245).
/FTId=VAR_050578.
VARIANT 409 409 R -> T (in dbSNP:rs1800243).
/FTId=VAR_016115.
MUTAGEN 122 122 C->G: Prevents DNA binding but no effect
on heterodimerization with RXRA.
{ECO:0000269|PubMed:7629123}.
MUTAGEN 304 304 D->A: Reduced heterodimerization with
RXRA. Reduced DNA binding.
{ECO:0000269|PubMed:10195690}.
MUTAGEN 370 370 L->R: Abolishes heterodimerization with
RXRA. No DNA binding.
{ECO:0000269|PubMed:10195690}.
MUTAGEN 391 391 L->R: Abolishes heterodimerization with
RXRA. No DNA binding.
{ECO:0000269|PubMed:10195690}.
MUTAGEN 422 422 L->R: No effect on heterodimerization
with RXRA nor on DNA binding and
transactivation activity.
{ECO:0000269|PubMed:7629123}.
MUTAGEN 431 431 A->T: No effect on heterodimerization
with RXRA nor on DNA binding.
{ECO:0000269|PubMed:10195690}.
MUTAGEN 433 433 L->R: Abolishes heterodimerization with
RXRA, DNA binding and transactivation
activity. {ECO:0000269|PubMed:7629123}.
CONFLICT 71 71 T -> M (in Ref. 3; CAA68898).
{ECO:0000305}.
CONFLICT 123 123 K -> M (in Ref. 3; CAA68898).
{ECO:0000305}.
CONFLICT 296 296 G -> A (in Ref. 1; AAA36468).
{ECO:0000305}.
CONFLICT 444 444 V -> A (in Ref. 3; CAA68898).
{ECO:0000305}.
HELIX 203 217 {ECO:0000244|PDB:3VI8}.
HELIX 222 229 {ECO:0000244|PDB:3VI8}.
STRAND 233 235 {ECO:0000244|PDB:1K7L}.
STRAND 239 241 {ECO:0000244|PDB:3VI8}.
HELIX 244 254 {ECO:0000244|PDB:3VI8}.
HELIX 256 259 {ECO:0000244|PDB:3VI8}.
HELIX 263 265 {ECO:0000244|PDB:2P54}.
HELIX 268 290 {ECO:0000244|PDB:3VI8}.
HELIX 291 293 {ECO:0000244|PDB:3VI8}.
TURN 295 299 {ECO:0000244|PDB:3VI8}.
HELIX 302 321 {ECO:0000244|PDB:3VI8}.
HELIX 322 324 {ECO:0000244|PDB:3VI8}.
STRAND 329 332 {ECO:0000244|PDB:3VI8}.
TURN 333 336 {ECO:0000244|PDB:3VI8}.
STRAND 337 340 {ECO:0000244|PDB:3VI8}.
HELIX 341 346 {ECO:0000244|PDB:3VI8}.
TURN 349 351 {ECO:0000244|PDB:3VI8}.
HELIX 352 366 {ECO:0000244|PDB:3VI8}.
HELIX 372 383 {ECO:0000244|PDB:3VI8}.
HELIX 394 415 {ECO:0000244|PDB:3VI8}.
HELIX 422 450 {ECO:0000244|PDB:3VI8}.
STRAND 453 456 {ECO:0000244|PDB:1KKQ}.
HELIX 458 464 {ECO:0000244|PDB:3VI8}.
TURN 465 467 {ECO:0000244|PDB:2ZNN}.
SEQUENCE 468 AA; 52225 MW; 850846FD51ADA883 CRC64;
MVDTESPLCP LSPLEAGDLE SPLSEEFLQE MGNIQEISQS IGEDSSGSFG FTEYQYLGSC
PGSDGSVITD TLSPASSPSS VTYPVVPGSV DESPSGALNI ECRICGDKAS GYHYGVHACE
GCKGFFRRTI RLKLVYDKCD RSCKIQKKNR NKCQYCRFHK CLSVGMSHNA IRFGRMPRSE
KAKLKAEILT CEHDIEDSET ADLKSLAKRI YEAYLKNFNM NKVKARVILS GKASNNPPFV
IHDMETLCMA EKTLVAKLVA NGIQNKEAEV RIFHCCQCTS VETVTELTEF AKAIPGFANL
DLNDQVTLLK YGVYEAIFAM LSSVMNKDGM LVAYGNGFIT REFLKSLRKP FCDIMEPKFD
FAMKFNALEL DDSDISLFVA AIICCGDRPG LLNVGHIEKM QEGIVHVLRL HLQSNHPDDI
FLFPKLLQKM ADLRQLVTEH AQLVQIIKKT ESDAALHPLL QEIYRDMY


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