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Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1-alpha) (PPAR-gamma coactivator 1-alpha) (PPARGC-1-alpha) (Ligand effect modulator 6)

 PRGC1_HUMAN             Reviewed;         798 AA.
Q9UBK2; B7Z406; G8DM16; I3RTT5; I3RTT6; I3RTT7; I3RTT8; I3RTT9;
Q3LIG1; Q4W5M7; Q9UN32;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
18-JUL-2018, entry version 172.
RecName: Full=Peroxisome proliferator-activated receptor gamma coactivator 1-alpha;
Short=PGC-1-alpha;
Short=PPAR-gamma coactivator 1-alpha;
Short=PPARGC-1-alpha;
AltName: Full=Ligand effect modulator 6;
Name=PPARGC1A; Synonyms=LEM6, PGC1, PGC1A, PPARGC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
SPECIFICITY.
PubMed=10585775; DOI=10.1006/geno.1999.5977;
Esterbauer H., Oberkofler H., Krempler F., Patsch W.;
"Human peroxisome proliferator activated receptor gamma coactivator 1
(PPARGC1) gene: cDNA sequence, genomic organization, chromosomal
localization, and tissue expression.";
Genomics 62:98-102(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANT SER-482.
TISSUE=Skeletal muscle;
PubMed=10643692; DOI=10.1038/sj.ijo.0801106;
Larrouy D., Vidal H., Andreelli F., Laville M., Langin D.;
"Cloning and mRNA tissue distribution of human PPARgamma coactivator-
1.";
Int. J. Obes. Relat. Metab. Disord. 23:1327-1332(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=10713165; DOI=10.1128/MCB.20.7.2411-2422.2000;
Knutti D., Kaul A., Kralli A.;
"A tissue-specific coactivator of steroid receptors, identified in a
functional genetic screen.";
Mol. Cell. Biol. 20:2411-2422(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9), AND SUBCELLULAR LOCATION
(ISOFORM 9).
TISSUE=Liver;
PubMed=22009745; DOI=10.1074/jbc.M111.227496;
Felder T.K., Soyal S.M., Oberkofler H., Hahne P., Auer S., Weiss R.,
Gadermaier G., Miller K., Krempler F., Esterbauer H., Patsch W.;
"Characterization of novel peroxisome proliferator-activated receptor
gamma coactivator-1alpha (PGC-1alpha) isoform in human liver.";
J. Biol. Chem. 286:42923-42936(2011).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B4; B4-3EXT; B4-8A; B5 AND
B5-NT), ALTERNATIVE PROMOTER USAGE, ALTERNATIVE SPLICING, AND
SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=22589246; DOI=10.1093/hmg/dds177;
Soyal S.M., Felder T.K., Auer S., Hahne P., Oberkofler H., Witting A.,
Paulmichl M., Landwehrmeyer G.B., Weydt P., Patsch W.;
"A greatly extended PPARGC1A genomic locus encodes several new brain-
specific isoforms and influences Huntington disease age of onset.";
Hum. Mol. Genet. 21:3461-3473(2012).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NT-7A), AND ALTERNATIVE SPLICING.
TISSUE=Skeletal muscle;
Endo H.;
"Isoform of PGC-1 generated by alternative splicing.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8A).
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Rieder M.J., Johanson E.J., da Ponte S.H., Stanaway I.B., Ahearn M.O.,
Bertucci C.B., Wong M.W., Yi Q., Nickerson D.A.;
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[11]
INTERACTION WITH LRPPRC.
PubMed=17050673; DOI=10.1101/gad.1483906;
Cooper M.P., Qu L., Rohas L.M., Lin J., Yang W., Erdjument-Bromage H.,
Tempst P., Spiegelman B.M.;
"Defects in energy homeostasis in Leigh syndrome French Canadian
variant through PGC-1alpha/LRP130 complex.";
Genes Dev. 20:2996-3009(2006).
[12]
FUNCTION, AND REGULATION BY ACETYLATION.
PubMed=20005308; DOI=10.1016/j.bbapap.2009.11.023;
Dominy J.E. Jr., Lee Y., Gerhart-Hines Z., Puigserver P.;
"Nutrient-dependent regulation of PGC-1alpha's acetylation state and
metabolic function through the enzymatic activities of Sirt1/GCN5.";
Biochim. Biophys. Acta 1804:1676-1683(2010).
[13]
FUNCTION, AND INDUCTION.
PubMed=21376232; DOI=10.1016/j.cell.2011.02.010;
Shin J.H., Ko H.S., Kang H., Lee Y., Lee Y.I., Pletinkova O.,
Troconso J.C., Dawson V.L., Dawson T.M.;
"PARIS (ZNF746) repression of PGC-1alpha contributes to
neurodegeneration in Parkinson's disease.";
Cell 144:689-702(2011).
[14]
UBIQUITINATION BY RNF34, AND INTERACTION WITH RNF34.
PubMed=22064484; DOI=10.1128/MCB.05674-11;
Wei P., Pan D., Mao C., Wang Y.X.;
"RNF34 is a cold-regulated E3 ubiquitin ligase for PGC-1alpha and
modulates brown fat cell metabolism.";
Mol. Cell. Biol. 32:266-275(2012).
[15]
FUNCTION.
PubMed=23836911; DOI=10.1074/jbc.M113.489674;
Cho Y., Hazen B.C., Russell A.P., Kralli A.;
"Peroxisome proliferator-activated receptor gamma coactivator 1 (PGC-
1)- and estrogen-related receptor (ERR)-induced regulator in muscle 1
(Perm1) is a tissue-specific regulator of oxidative capacity in
skeletal muscle cells.";
J. Biol. Chem. 288:25207-25218(2013).
-!- FUNCTION: Transcriptional coactivator for steroid receptors and
nuclear receptors. Greatly increases the transcriptional activity
of PPARG and thyroid hormone receptor on the uncoupling protein
promoter. Can regulate key mitochondrial genes that contribute to
the program of adaptive thermogenesis. Plays an essential role in
metabolic reprogramming in response to dietary availability
through coordination of the expression of a wide array of genes
involved in glucose and fatty acid metabolism. Induces the
expression of PERM1 in the skeletal muscle in an ESRRA-dependent
manner. Also involved in the integration of the circadian rhythms
and energy metabolism. Required for oscillatory expression of
clock genes, such as ARNTL/BMAL1 and NR1D1, through the
coactivation of RORA and RORC, and metabolic genes, such as PDK4
and PEPCK. {ECO:0000269|PubMed:10713165,
ECO:0000269|PubMed:20005308, ECO:0000269|PubMed:21376232,
ECO:0000269|PubMed:23836911}.
-!- SUBUNIT: Homooligomer. Interacts with MYBBP1A; inhibits MYBBP1A
transcriptional activation (By similarity). Interacts with PRDM16,
LPIN1 and PML (By similarity). Interacts (via LXXLL motif) with
RORA and RORC (via AF-2 motif); activates RORA and RORC
transcriptional activation (By similarity). Interacts with LRPPRC.
Interacts with RNF34 (via RING-type zinc finger).
{ECO:0000250|UniProtKB:O70343, ECO:0000269|PubMed:10713165,
ECO:0000269|PubMed:17050673, ECO:0000269|PubMed:22064484}.
-!- INTERACTION:
P11474:ESRRA; NbExp=5; IntAct=EBI-765486, EBI-372412;
P62508:ESRRG; NbExp=4; IntAct=EBI-765486, EBI-2834260;
P41235:HNF4A; NbExp=4; IntAct=EBI-765486, EBI-1049011;
P42704:LRPPRC; NbExp=2; IntAct=EBI-765486, EBI-1050853;
P37231:PPARG; NbExp=2; IntAct=EBI-765486, EBI-781384;
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus. Nucleus, PML body.
-!- SUBCELLULAR LOCATION: Isoform B4: Nucleus.
-!- SUBCELLULAR LOCATION: Isoform B4-8a: Cytoplasm. Nucleus.
-!- SUBCELLULAR LOCATION: Isoform B5: Nucleus. Nucleus, PML body.
-!- SUBCELLULAR LOCATION: Isoform 9: Nucleus
{ECO:0000269|PubMed:22009745}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=9;
Name=1;
IsoId=Q9UBK2-1; Sequence=Displayed;
Name=NT-7a;
IsoId=Q9UBK2-2; Sequence=VSP_047684, VSP_047685;
Name=B5;
IsoId=Q9UBK2-3; Sequence=VSP_053724;
Note=Produced by alternative promoter usage.;
Name=B4;
IsoId=Q9UBK2-4; Sequence=VSP_053725;
Note=Produced by alternative promoter usage.;
Name=B4-8a;
IsoId=Q9UBK2-5; Sequence=VSP_053725, VSP_053728, VSP_053729;
Note=Produced by alternative promoter usage.;
Name=B5-NT;
IsoId=Q9UBK2-6; Sequence=VSP_053724, VSP_047684, VSP_047685;
Note=Produced by alternative promoter usage.;
Name=B4-3ext;
IsoId=Q9UBK2-7; Sequence=VSP_053725, VSP_053726, VSP_053727;
Note=Produced by alternative promoter usage.;
Name=8a;
IsoId=Q9UBK2-8; Sequence=VSP_053728, VSP_053729;
Name=9; Synonyms=L-PGG-1alpha;
IsoId=Q9UBK2-9; Sequence=VSP_053770;
Note=Produced by alternative promoter usage. May be involved in
gluconeogenesis, liver-specific.;
-!- TISSUE SPECIFICITY: Heart, skeletal muscle, liver and kidney.
Expressed at lower levels in brain and pancreas and at very low
levels in the intestine and white adipose tissue. In skeletal
muscle, levels were lower in obese than in lean subjects and
fasting induced a 2-fold increase in levels in the skeletal muscle
in obese subjects. {ECO:0000269|PubMed:10585775,
ECO:0000269|PubMed:10643692, ECO:0000269|PubMed:10713165}.
-!- INDUCTION: Transcription is repressed by ZNF746 which binds to
'insulin response sequences' its promoter.
{ECO:0000269|PubMed:21376232}.
-!- PTM: Phosphorylation by AMPK in skeletal muscle increases
activation of its own promoter. Phosphorylated by CLK2.
{ECO:0000250}.
-!- PTM: Heavily acetylated by GCN5 and biologically inactive under
conditions of high nutrients. Deacetylated by SIRT1 in low
nutrients/high NAD conditions.
-!- PTM: Ubiquitinated. Ubiquitination by RNF34 induces proteasomal
degradation. {ECO:0000269|PubMed:22064484}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/ppargc1a/";
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EMBL; AF108205; AAF19083.1; -; Genomic_DNA.
EMBL; AF108193; AAF19083.1; JOINED; Genomic_DNA.
EMBL; AF108194; AAF19083.1; JOINED; Genomic_DNA.
EMBL; AF108195; AAF19083.1; JOINED; Genomic_DNA.
EMBL; AF108196; AAF19083.1; JOINED; Genomic_DNA.
EMBL; AF108197; AAF19083.1; JOINED; Genomic_DNA.
EMBL; AF108198; AAF19083.1; JOINED; Genomic_DNA.
EMBL; AF108199; AAF19083.1; JOINED; Genomic_DNA.
EMBL; AF108200; AAF19083.1; JOINED; Genomic_DNA.
EMBL; AF108201; AAF19083.1; JOINED; Genomic_DNA.
EMBL; AF108202; AAF19083.1; JOINED; Genomic_DNA.
EMBL; AF108203; AAF19083.1; JOINED; Genomic_DNA.
EMBL; AF108204; AAF19083.1; JOINED; Genomic_DNA.
EMBL; AF106698; AAF18573.1; -; mRNA.
EMBL; AF159714; AAD51615.1; -; mRNA.
EMBL; AF186379; AAD56250.1; -; mRNA.
EMBL; HQ695733; ADW77180.1; -; mRNA.
EMBL; JQ772116; AFK29753.1; -; mRNA.
EMBL; JQ772117; AFK29754.1; -; mRNA.
EMBL; JQ772118; AFK29755.1; -; mRNA.
EMBL; JQ772119; AFK29756.1; -; mRNA.
EMBL; JQ772120; AFK29757.1; -; mRNA.
EMBL; AB061325; BAE46508.1; -; mRNA.
EMBL; EU280319; ABX44665.1; -; Genomic_DNA.
EMBL; AK296591; BAH12392.1; -; mRNA.
EMBL; AC092834; AAY41058.1; -; Genomic_DNA.
EMBL; AC097508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471069; EAW92811.1; -; Genomic_DNA.
CCDS; CCDS3429.1; -. [Q9UBK2-1]
RefSeq; NP_001317680.1; NM_001330751.1. [Q9UBK2-3]
RefSeq; NP_001317681.1; NM_001330752.1. [Q9UBK2-4]
RefSeq; NP_001317682.1; NM_001330753.1. [Q9UBK2-9]
RefSeq; NP_037393.1; NM_013261.4. [Q9UBK2-1]
RefSeq; XP_011512073.1; XM_011513771.1. [Q9UBK2-9]
UniGene; Hs.527078; -.
PDB; 1XB7; X-ray; 2.50 A; P=205-216.
PDB; 3B1M; X-ray; 1.60 A; B=136-154.
PDB; 3CS8; X-ray; 2.30 A; B=141-152.
PDB; 3D24; X-ray; 2.11 A; B/D=198-219.
PDB; 3U9Q; X-ray; 1.52 A; B=142-150.
PDB; 3V9T; X-ray; 1.65 A; C=136-154.
PDB; 3V9V; X-ray; 1.60 A; C=136-154.
PDB; 4QJR; X-ray; 2.40 A; B=139-152.
PDB; 4QK4; X-ray; 2.81 A; B=139-152.
PDB; 5Q0I; X-ray; 1.70 A; B=141-152.
PDB; 5TWO; X-ray; 1.93 A; B=138-152.
PDB; 5UNJ; X-ray; 1.96 A; C=139-152.
PDBsum; 1XB7; -.
PDBsum; 3B1M; -.
PDBsum; 3CS8; -.
PDBsum; 3D24; -.
PDBsum; 3U9Q; -.
PDBsum; 3V9T; -.
PDBsum; 3V9V; -.
PDBsum; 4QJR; -.
PDBsum; 4QK4; -.
PDBsum; 5Q0I; -.
PDBsum; 5TWO; -.
PDBsum; 5UNJ; -.
ProteinModelPortal; Q9UBK2; -.
SMR; Q9UBK2; -.
BioGrid; 116097; 66.
CORUM; Q9UBK2; -.
DIP; DIP-38449N; -.
ELM; Q9UBK2; -.
IntAct; Q9UBK2; 18.
MINT; Q9UBK2; -.
STRING; 9606.ENSP00000264867; -.
ChEMBL; CHEMBL6116; -.
iPTMnet; Q9UBK2; -.
PhosphoSitePlus; Q9UBK2; -.
BioMuta; PPARGC1A; -.
DMDM; 47117335; -.
MaxQB; Q9UBK2; -.
PaxDb; Q9UBK2; -.
PeptideAtlas; Q9UBK2; -.
PRIDE; Q9UBK2; -.
ProteomicsDB; 83978; -.
DNASU; 10891; -.
Ensembl; ENST00000264867; ENSP00000264867; ENSG00000109819. [Q9UBK2-1]
Ensembl; ENST00000506055; ENSP00000423075; ENSG00000109819. [Q9UBK2-2]
Ensembl; ENST00000513205; ENSP00000421632; ENSG00000109819. [Q9UBK2-8]
Ensembl; ENST00000613098; ENSP00000481498; ENSG00000109819. [Q9UBK2-9]
GeneID; 10891; -.
KEGG; hsa:10891; -.
UCSC; uc003gqs.3; human. [Q9UBK2-1]
CTD; 10891; -.
DisGeNET; 10891; -.
EuPathDB; HostDB:ENSG00000109819.8; -.
GeneCards; PPARGC1A; -.
HGNC; HGNC:9237; PPARGC1A.
HPA; HPA063136; -.
MalaCards; PPARGC1A; -.
MIM; 604517; gene.
neXtProt; NX_Q9UBK2; -.
OpenTargets; ENSG00000109819; -.
Orphanet; 803; Amyotrophic lateral sclerosis.
PharmGKB; PA33558; -.
eggNOG; ENOG410IIVU; Eukaryota.
eggNOG; ENOG410YQI0; LUCA.
GeneTree; ENSGT00530000063196; -.
HOGENOM; HOG000082404; -.
HOVERGEN; HBG053678; -.
InParanoid; Q9UBK2; -.
KO; K07202; -.
OMA; ENGYTLR; -.
OrthoDB; EOG091G029M; -.
PhylomeDB; Q9UBK2; -.
TreeFam; TF343068; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-2151209; Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
SIGNOR; Q9UBK2; -.
ChiTaRS; PPARGC1A; human.
EvolutionaryTrace; Q9UBK2; -.
GeneWiki; PPARGC1A; -.
GenomeRNAi; 10891; -.
PRO; PR:Q9UBK2; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000109819; -.
CleanEx; HS_PPARGC1A; -.
ExpressionAtlas; Q9UBK2; baseline and differential.
Genevisible; Q9UBK2; HS.
GO; GO:0097440; C:apical dendrite; IEA:Ensembl.
GO; GO:0022626; C:cytosolic ribosome; IEA:Ensembl.
GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; TAS:UniProtKB.
GO; GO:1990844; C:interfibrillar mitochondrion; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005719; C:nuclear euchromatin; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:1990843; C:subsarcolemmal mitochondrion; IEA:Ensembl.
GO; GO:0043014; F:alpha-tubulin binding; IEA:Ensembl.
GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IEA:Ensembl.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; IPI:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:BHF-UCL.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IEA:Ensembl.
GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; TAS:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003712; F:transcription coregulator activity; TAS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; TAS:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:1990845; P:adaptive thermogenesis; IEA:Ensembl.
GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0008209; P:androgen metabolic process; IEA:Ensembl.
GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
GO; GO:0000422; P:autophagy of mitochondrion; IEA:Ensembl.
GO; GO:0050873; P:brown fat cell differentiation; TAS:UniProtKB.
GO; GO:0001678; P:cellular glucose homeostasis; NAS:UniProtKB.
GO; GO:0045333; P:cellular respiration; TAS:UniProtKB.
GO; GO:0071313; P:cellular response to caffeine; IEA:Ensembl.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl.
GO; GO:0071332; P:cellular response to fructose stimulus; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
GO; GO:1904637; P:cellular response to ionomycin; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071250; P:cellular response to nitrite; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
GO; GO:0035865; P:cellular response to potassium ion; IEA:Ensembl.
GO; GO:1904639; P:cellular response to resveratrol; IEA:Ensembl.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0007623; P:circadian rhythm; TAS:Reactome.
GO; GO:0007586; P:digestion; TAS:UniProtKB.
GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
GO; GO:0019395; P:fatty acid oxidation; NAS:UniProtKB.
GO; GO:0051552; P:flavone metabolic process; IEA:Ensembl.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0006012; P:galactose metabolic process; IEA:Ensembl.
GO; GO:0006094; P:gluconeogenesis; NAS:UniProtKB.
GO; GO:0007005; P:mitochondrion organization; TAS:Reactome.
GO; GO:0006397; P:mRNA processing; TAS:UniProtKB.
GO; GO:0045820; P:negative regulation of glycolytic process; IEA:Ensembl.
GO; GO:0090258; P:negative regulation of mitochondrial fission; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:1901215; P:negative regulation of neuron death; IGI:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:2000272; P:negative regulation of signaling receptor activity; IEA:Ensembl.
GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IEA:Ensembl.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISS:UniProtKB.
GO; GO:1901857; P:positive regulation of cellular respiration; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0046321; P:positive regulation of fatty acid oxidation; TAS:UniProtKB.
GO; GO:1904635; P:positive regulation of glomerular visceral epithelial cell apoptotic process; IEA:Ensembl.
GO; GO:0045722; P:positive regulation of gluconeogenesis; TAS:UniProtKB.
GO; GO:0035066; P:positive regulation of histone acetylation; TAS:UniProtKB.
GO; GO:1901860; P:positive regulation of mitochondrial DNA metabolic process; IEA:Ensembl.
GO; GO:0010822; P:positive regulation of mitochondrion organization; IMP:ParkinsonsUK-UCL.
GO; GO:1901863; P:positive regulation of muscle tissue development; IEA:Ensembl.
GO; GO:2000184; P:positive regulation of progesterone biosynthetic process; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0050821; P:protein stabilization; TAS:UniProtKB.
GO; GO:0065003; P:protein-containing complex assembly; TAS:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:2000310; P:regulation of NMDA receptor activity; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0022904; P:respiratory electron transport chain; ISS:UniProtKB.
GO; GO:0009409; P:response to cold; IEA:Ensembl.
GO; GO:0002021; P:response to dietary excess; IEA:Ensembl.
GO; GO:0014878; P:response to electrical stimulus involved in regulation of muscle adaptation; IEA:Ensembl.
GO; GO:0071871; P:response to epinephrine; IEA:Ensembl.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:0043201; P:response to leucine; IEA:Ensembl.
GO; GO:1901558; P:response to metformin; IEA:Ensembl.
GO; GO:1904640; P:response to methionine; IEA:Ensembl.
GO; GO:0014850; P:response to muscle activity; ISS:BHF-UCL.
GO; GO:0071873; P:response to norepinephrine; IEA:Ensembl.
GO; GO:0000302; P:response to reactive oxygen species; IEA:Ensembl.
GO; GO:0042594; P:response to starvation; NAS:UniProtKB.
GO; GO:0008380; P:RNA splicing; TAS:UniProtKB.
GO; GO:0014732; P:skeletal muscle atrophy; IEA:Ensembl.
GO; GO:0001659; P:temperature homeostasis; TAS:UniProtKB.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:UniProtKB.
CDD; cd12623; RRM_PPARGC1A; 1.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR034605; PGC-1.
InterPro; IPR034625; PGC-1alpha.
InterPro; IPR034833; PPARGC1A_RRM.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR15528; PTHR15528; 1.
PANTHER; PTHR15528:SF10; PTHR15528:SF10; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative promoter usage;
Alternative splicing; Biological rhythms; Complete proteome;
Cytoplasm; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 798 Peroxisome proliferator-activated
receptor gamma coactivator 1-alpha.
/FTId=PRO_0000081732.
DOMAIN 677 753 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 293 339 Interaction with PPARG.
REGION 350 798 Mediates interaction with RNF34.
{ECO:0000269|PubMed:22064484}.
MOTIF 144 148 LXXLL motif.
COMPBIAS 566 599 Arg/Ser-rich.
COMPBIAS 621 633 Arg/Ser-rich.
MOD_RES 79 79 N6-acetyllysine.
{ECO:0000250|UniProtKB:O70343}.
MOD_RES 146 146 N6-acetyllysine.
{ECO:0000250|UniProtKB:O70343}.
MOD_RES 178 178 Phosphothreonine; by AMPK.
{ECO:0000250|UniProtKB:O70343}.
MOD_RES 184 184 N6-acetyllysine.
{ECO:0000250|UniProtKB:O70343}.
MOD_RES 254 254 N6-acetyllysine.
{ECO:0000250|UniProtKB:O70343}.
MOD_RES 271 271 N6-acetyllysine.
{ECO:0000250|UniProtKB:O70343}.
MOD_RES 278 278 N6-acetyllysine.
{ECO:0000250|UniProtKB:O70343}.
MOD_RES 321 321 N6-acetyllysine.
{ECO:0000250|UniProtKB:O70343}.
MOD_RES 347 347 N6-acetyllysine.
{ECO:0000250|UniProtKB:O70343}.
MOD_RES 413 413 N6-acetyllysine.
{ECO:0000250|UniProtKB:O70343}.
MOD_RES 442 442 N6-acetyllysine.
{ECO:0000250|UniProtKB:O70343}.
MOD_RES 451 451 N6-acetyllysine.
{ECO:0000250|UniProtKB:O70343}.
MOD_RES 539 539 Phosphoserine; by AMPK.
{ECO:0000250|UniProtKB:O70343}.
MOD_RES 758 758 N6-acetyllysine.
{ECO:0000250|UniProtKB:O70343}.
MOD_RES 779 779 N6-acetyllysine.
{ECO:0000250|UniProtKB:O70343}.
VAR_SEQ 1 127 Missing (in isoform 9).
{ECO:0000303|PubMed:22009745}.
/FTId=VSP_053770.
VAR_SEQ 1 18 MAWDMCNQDSESVWSDIE -> MDEGYF (in isoform
B4, isoform B4-8a and isoform B4-3ext).
{ECO:0000303|PubMed:22589246}.
/FTId=VSP_053725.
VAR_SEQ 1 18 MAWDMCNQDSESVWSDIE -> MDETSPRLEEDWKKVLQRE
AGWQ (in isoform B5 and isoform B5-NT).
{ECO:0000303|PubMed:22589246}.
/FTId=VSP_053724.
VAR_SEQ 144 150 LKKLLLA -> VRTLPTV (in isoform B4-3ext).
{ECO:0000303|PubMed:22589246}.
/FTId=VSP_053726.
VAR_SEQ 151 798 Missing (in isoform B4-3ext).
{ECO:0000303|PubMed:22589246}.
/FTId=VSP_053727.
VAR_SEQ 269 271 DPK -> LFL (in isoform NT-7a and isoform
B5-NT). {ECO:0000303|PubMed:22589246,
ECO:0000303|Ref.6}.
/FTId=VSP_047684.
VAR_SEQ 272 798 Missing (in isoform NT-7a and isoform B5-
NT). {ECO:0000303|PubMed:22589246,
ECO:0000303|Ref.6}.
/FTId=VSP_047685.
VAR_SEQ 294 301 LTPPTTPP -> VKTNLISK (in isoform B4-8a
and isoform 8a).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:22589246}.
/FTId=VSP_053728.
VAR_SEQ 302 798 Missing (in isoform B4-8a and isoform
8a). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:22589246}.
/FTId=VSP_053729.
VARIANT 482 482 G -> S (in dbSNP:rs8192678).
{ECO:0000269|PubMed:10643692}.
/FTId=VAR_018450.
VARIANT 612 612 T -> M (in dbSNP:rs3736265).
/FTId=VAR_018451.
HELIX 143 149 {ECO:0000244|PDB:3U9Q}.
HELIX 208 214 {ECO:0000244|PDB:3D24}.
SEQUENCE 798 AA; 91027 MW; 97DDD3643051A5F1 CRC64;
MAWDMCNQDS ESVWSDIECA ALVGEDQPLC PDLPELDLSE LDVNDLDTDS FLGGLKWCSD
QSEIISNQYN NEPSNIFEKI DEENEANLLA VLTETLDSLP VDEDGLPSFD ALTDGDVTTD
NEASPSSMPD GTPPPQEAEE PSLLKKLLLA PANTQLSYNE CSGLSTQNHA NHNHRIRTNP
AIVKTENSWS NKAKSICQQQ KPQRRPCSEL LKYLTTNDDP PHTKPTENRN SSRDKCTSKK
KSHTQSQSQH LQAKPTTLSL PLTPESPNDP KGSPFENKTI ERTLSVELSG TAGLTPPTTP
PHKANQDNPF RASPKLKSSC KTVVPPPSKK PRYSESSGTQ GNNSTKKGPE QSELYAQLSK
SSVLTGGHEE RKTKRPSLRL FGDHDYCQSI NSKTEILINI SQELQDSRQL ENKDVSSDWQ
GQICSSTDSD QCYLRETLEA SKQVSPCSTR KQLQDQEIRA ELNKHFGHPS QAVFDDEADK
TGELRDSDFS NEQFSKLPMF INSGLAMDGL FDDSEDESDK LSYPWDGTQS YSLFNVSPSC
SSFNSPCRDS VSPPKSLFSQ RPQRMRSRSR SFSRHRSCSR SPYSRSRSRS PGSRSSSRSC
YYYESSHYRH RTHRNSPLYV RSRSRSPYSR RPRYDSYEEY QHERLKREEY RREYEKRESE
RAKQRERQRQ KAIEERRVIY VGKIRPDTTR TELRDRFEVF GEIEECTVNL RDDGDSYGFI
TYRYTCDAFA ALENGYTLRR SNETDFELYF CGRKQFFKSN YADLDSNSDD FDPASTKSKY
DSLDFDSLLK EAQRSLRR


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