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Nuclear receptor coactivator 3 (NCoA-3) (EC 2.3.1.48) (ACTR) (Amplified in breast cancer 1 protein) (AIB-1) (CBP-interacting protein) (pCIP) (Class E basic helix-loop-helix protein 42) (bHLHe42) (Receptor-associated coactivator 3) (RAC-3) (Steroid receptor coactivator protein 3) (SRC-3) (Thyroid hormone receptor activator molecule 1) (TRAM-1)

 NCOA3_HUMAN             Reviewed;        1424 AA.
Q9Y6Q9; A4LAZ5; Q0VF45; Q5JYD9; Q5JYE0; Q9BR49; Q9UPC9; Q9UPG4;
Q9UPG7;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
22-NOV-2017, entry version 192.
RecName: Full=Nuclear receptor coactivator 3;
Short=NCoA-3;
EC=2.3.1.48;
AltName: Full=ACTR;
AltName: Full=Amplified in breast cancer 1 protein;
Short=AIB-1;
AltName: Full=CBP-interacting protein;
Short=pCIP;
AltName: Full=Class E basic helix-loop-helix protein 42;
Short=bHLHe42;
AltName: Full=Receptor-associated coactivator 3;
Short=RAC-3;
AltName: Full=Steroid receptor coactivator protein 3;
Short=SRC-3;
AltName: Full=Thyroid hormone receptor activator molecule 1;
Short=TRAM-1;
Name=NCOA3; Synonyms=AIB1, BHLHE42, RAC3, TRAM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND INTERACTION WITH
CREBBP; PCAF; RARA; RXRA; THRA AND ESR.
TISSUE=Pituitary;
PubMed=9346901; DOI=10.1074/jbc.272.44.27629;
Takeshita A., Cardona G.R., Koibuchi N., Suen C.-S., Chin W.W.;
"TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule,
exhibits distinct properties from steroid receptor coactivator-1.";
J. Biol. Chem. 272:27629-27634(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ENZYME ACTIVITY, AND
VARIANT 1248-GLN--GLN-1250 DEL.
TISSUE=Leukemia;
PubMed=9267036; DOI=10.1016/S0092-8674(00)80516-4;
Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L.,
Privalsky M.L., Nakatani Y., Evans R.M.;
"Nuclear receptor coactivator ACTR is a novel histone
acetyltransferase and forms a multimeric activation complex with P/CAF
and CBP/p300.";
Cell 90:569-580(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND INTERACTION WITH ESR.
TISSUE=Lung;
PubMed=9252329; DOI=10.1126/science.277.5328.965;
Anzick S.L., Kononen J., Walker R.L., Azorsa D.O., Tanner M.M.,
Guan X.-Y., Sauter G., Kallioniemi O.-P., Trent J.M., Meltzer P.S.;
"AIB1, a steroid receptor coactivator amplified in breast and ovarian
cancer.";
Science 277:965-968(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH VDR; RARA;
PPARA; RXRA; THRA AND ESR, AND VARIANT 1248-GLN--GLN-1250 DEL.
TISSUE=Brain;
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-218; ILE-220;
VAL-556; SER-559; HIS-586; ALA-777; LEU-1247 AND LYS-1247.
NIEHS SNPs program;
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
POLYMORPHISM OF POLY-GLN REGION.
PubMed=9727751;
Shirazi S.K., Bober M.A., Coetzee G.A.;
"Polymorphic exonic CAG microsatellites in the gene amplified in
breast cancer (AIB1 gene).";
Clin. Genet. 54:102-103(1998).
[10]
ACETYLATION AT LYS-616; LYS-619 AND LYS-620 BY CREBBP, AND MUTAGENESIS
OF LYS-616; 619-LYS-LYS-620; LYS-647; LYS-681; LYS-687; LYS-700 AND
LYS-708.
PubMed=10490106; DOI=10.1016/S0092-8674(00)80054-9;
Chen H., Lin R.J., Xie W., Wilpitz D., Evans R.M.;
"Regulation of hormone-induced histone hyperacetylation and gene
activation via acetylation of an acetylase.";
Cell 98:675-686(1999).
[11]
INTERACTION WITH NFKB1.
PubMed=11094166; DOI=10.1016/S0014-5793(00)02223-7;
Werbajh S., Nojek I., Lanz R., Costas M.A.;
"RAC-3 is a NF-kappa B coactivator.";
FEBS Lett. 485:195-199(2000).
[12]
INTERACTION WITH DDX5.
PubMed=11250900; DOI=10.1093/emboj/20.6.1341;
Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S.,
Arao Y., Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y.,
Kato S.;
"A subfamily of RNA-binding DEAD-box proteins acts as an estrogen
receptor alpha coactivator through the N-terminal activation domain
(AF-1) with an RNA coactivator, SRA.";
EMBO J. 20:1341-1352(2001).
[13]
SUBUNIT OF A COMPLEX CONTAINING CREBBP; NCOA2; IKKA; IKKB AND IKBKG,
AND PHOSPHORYLATION.
PubMed=11971985; DOI=10.1128/MCB.22.10.3549-3561.2002;
Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J.,
O'Malley B.W.;
"Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator
activity by I kappa B kinase.";
Mol. Cell. Biol. 22:3549-3561(2002).
[14]
INTERACTION WITH NR3C1.
PubMed=12917342; DOI=10.1128/MCB.23.17.6210-6220.2003;
Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
"BAF60a mediates critical interactions between nuclear receptors and
the BRG1 chromatin-remodeling complex for transactivation.";
Mol. Cell. Biol. 23:6210-6220(2003).
[15]
INTERACTION WITH NPAS2.
PubMed=14645221; DOI=10.1074/jbc.M311973200;
Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M.,
Chakravarti D., FitzGerald G.A., McNamara P.;
"Histone acetyltransferase-dependent chromatin remodeling and the
vascular clock.";
J. Biol. Chem. 279:7091-7097(2004).
[16]
INTERACTION WITH CASP8AP2.
PubMed=15698540; DOI=10.1016/j.jsbmb.2004.09.003;
Kino T., Ichijo T., Chrousos G.P.;
"FLASH interacts with p160 coactivator subtypes and differentially
suppresses transcriptional activity of steroid hormone receptors.";
J. Steroid Biochem. Mol. Biol. 92:357-363(2004).
[17]
SUBUNIT.
PubMed=16951154; DOI=10.1158/0008-5472.CAN-06-1636;
Ma A.H., Xia L., Desai S.J., Boucher D.L., Guan Y., Shih H.M.,
Shi X.B., deVere White R.W., Chen H.W., Tepper C.G., Kung H.J.;
"Male germ cell-associated kinase, a male-specific kinase regulated by
androgen, is a coactivator of androgen receptor in prostate cancer
cells.";
Cancer Res. 66:8439-8447(2006).
[18]
INTERACTION WITH PSMB9.
PubMed=16957778; DOI=10.1038/sj.emboj.7601306;
Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R.,
Sun X., Shang Y.;
"The catalytic subunit of the proteasome is engaged in the entire
process of estrogen receptor-regulated transcription.";
EMBO J. 25:4223-4233(2006).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857 AND SER-867, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[20]
INTERACTION WITH ATAD2.
PubMed=17998543; DOI=10.1073/pnas.0705814104;
Zou J.X., Revenko A.S., Li L.B., Gemo A.T., Chen H.-W.;
"ANCCA, an estrogen-regulated AAA+ ATPase coactivator for ERalpha, is
required for coregulator occupancy and chromatin modification.";
Proc. Natl. Acad. Sci. U.S.A. 104:18067-18072(2007).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-551; SER-728
AND SER-857, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[23]
PHOSPHORYLATION AT SER-601 BY CSNK1D/CK1, AND INTERACTION WITH CSNK1D.
PubMed=19339517; DOI=10.1093/nar/gkp136;
Giamas G., Castellano L., Feng Q., Knippschild U., Jacob J.,
Thomas R.S., Coombes R.C., Smith C.L., Jiao L.R., Stebbing J.;
"CK1delta modulates the transcriptional activity of ERalpha via AIB1
in an estrogen-dependent manner and regulates ERalpha-AIB1
interactions.";
Nucleic Acids Res. 37:3110-3123(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-687, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-857 AND
SER-867, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-551; SER-694;
SER-728; SER-857; SER-1033 AND SER-1330, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[31]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1171; ARG-1177 AND ARG-1188,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Nuclear receptor coactivator that directly binds nuclear
receptors and stimulates the transcriptional activities in a
hormone-dependent fashion. Plays a central role in creating a
multisubunit coactivator complex, which probably acts via
remodeling of chromatin. Involved in the coactivation of different
nuclear receptors, such as for steroids (GR and ER), retinoids
(RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and
prostanoids (PPARs). Displays histone acetyltransferase activity.
Also involved in the coactivation of the NF-kappa-B pathway via
its interaction with the NFKB1 subunit.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000269|PubMed:9267036}.
-!- ENZYME REGULATION: Coactivator activity on nuclear receptors and
NF-kappa-B pathways is enhanced by various hormones, and the TNF
cytokine, respectively. TNF stimulation probably enhances
phosphorylation, which in turn activates coactivator function. In
contrast, acetylation by CREBBP apparently suppresses coactivation
of target genes by disrupting its association with nuclear
receptors. Binds to CSNK1D.
-!- SUBUNIT: Interacts with CARM1 (By similarity). Present in a
complex containing NCOA2, IKKA, IKKB, IKBKG and the histone
acetyltransferase protein CREBBP. Interacts with CASP8AP2, NR3C1
and PCAF. Interacts with ATAD2 and this interaction is enhanced by
estradiol. Found in a complex containing NCOA3, AR and MAK.
Interacts with DDX5. Interacts with PSMB9. Interacts with NPAS2.
Interacts with NR4A3 (By similarity). Interacts with ESRRB;
mediates the interaction between ESRRB and RNA polymerase II
complexes and allows NCOA3 corecruitment to ESRRB, KLF4, NANOG,
and SOX2 enhancer regions to trigger ESRRB-dependent gene
activation involved in self-renewal and pluripotency (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:O09000,
ECO:0000269|PubMed:11094166, ECO:0000269|PubMed:11250900,
ECO:0000269|PubMed:11971985, ECO:0000269|PubMed:12917342,
ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:15698540,
ECO:0000269|PubMed:16951154, ECO:0000269|PubMed:16957778,
ECO:0000269|PubMed:17998543, ECO:0000269|PubMed:19339517,
ECO:0000269|PubMed:9238002, ECO:0000269|PubMed:9252329,
ECO:0000269|PubMed:9346901}.
-!- INTERACTION:
Q6PL18:ATAD2; NbExp=2; IntAct=EBI-81196, EBI-6598454;
Q86X55:CARM1; NbExp=13; IntAct=EBI-81196, EBI-2339854;
Q92841:DDX17; NbExp=2; IntAct=EBI-81196, EBI-746012;
Q09472:EP300; NbExp=2; IntAct=EBI-81196, EBI-447295;
P03372:ESR1; NbExp=4; IntAct=EBI-81196, EBI-78473;
O14920:IKBKB; NbExp=3; IntAct=EBI-81196, EBI-81266;
Q8VIM5-1:Myocd (xeno); NbExp=5; IntAct=EBI-81196, EBI-15626132;
P28065:PSMB9; NbExp=3; IntAct=EBI-81196, EBI-603300;
P61289:PSME3; NbExp=5; IntAct=EBI-81196, EBI-355546;
P60484:PTEN; NbExp=2; IntAct=EBI-81196, EBI-696162;
P10276:RARA; NbExp=2; IntAct=EBI-81196, EBI-413374;
O43791:SPOP; NbExp=6; IntAct=EBI-81196, EBI-743549;
P48281:Vdr (xeno); NbExp=2; IntAct=EBI-81196, EBI-346797;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly cytoplasmic
and weakly nuclear. Upon TNF activation and subsequent
phosphorylation, it translocates from the cytoplasm to the
nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q9Y6Q9-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y6Q9-2; Sequence=VSP_003407;
Name=3;
IsoId=Q9Y6Q9-3; Sequence=VSP_003405, VSP_003407, VSP_003408;
Name=4;
IsoId=Q9Y6Q9-4; Sequence=VSP_003405, VSP_003406, VSP_003407,
VSP_003408;
Name=5;
IsoId=Q9Y6Q9-5; Sequence=VSP_003408;
-!- TISSUE SPECIFICITY: Widely expressed. High expression in heart,
skeletal muscle, pancreas and placenta. Low expression in brain,
and very low in lung, liver and kidney.
-!- DOMAIN: Contains three Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Motifs
1 and 2 are essential for the association with nuclear receptors,
and constitute the RID domain (Receptor-interacting domain).
-!- PTM: Acetylated by CREBBP. Acetylation occurs in the RID domain,
and disrupts the interaction with nuclear receptors and regulates
its function. {ECO:0000269|PubMed:10490106}.
-!- PTM: Methylated by CARM1. {ECO:0000250}.
-!- PTM: Phosphorylated by IKK complex. Regulated its function.
Phosphorylation at Ser-601 by CK1 promotes coactivator function.
{ECO:0000269|PubMed:11971985, ECO:0000269|PubMed:19339517}.
-!- POLYMORPHISM: The length of the poly-Gln region is polymorphic in
the normal population. {ECO:0000269|PubMed:9727751}.
-!- MISCELLANEOUS: NCOA3 is frequently amplified or overexpressed in
breast and ovarian cancers.
-!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NCOA3ID505ch20q13.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ncoa3/";
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EMBL; AF016031; AAC51849.1; -; mRNA.
EMBL; AF036892; AAB92368.1; -; mRNA.
EMBL; AF012108; AAC51677.1; -; mRNA.
EMBL; AF010227; AAC51663.1; -; mRNA.
EMBL; EF488684; ABO43042.1; -; Genomic_DNA.
EMBL; AL034418; CAB40662.1; -; Genomic_DNA.
EMBL; AL034418; CAC17693.1; -; Genomic_DNA.
EMBL; AL034418; CAI42141.1; -; Genomic_DNA.
EMBL; CH471077; EAW75698.1; -; Genomic_DNA.
EMBL; CH471077; EAW75702.1; -; Genomic_DNA.
EMBL; BC119001; AAI19002.1; -; mRNA.
CCDS; CCDS13406.1; -. [Q9Y6Q9-5]
CCDS; CCDS13407.1; -. [Q9Y6Q9-1]
CCDS; CCDS54472.1; -. [Q9Y6Q9-3]
PIR; T03851; T03851.
RefSeq; NP_001167559.1; NM_001174088.1. [Q9Y6Q9-3]
RefSeq; NP_006525.2; NM_006534.3. [Q9Y6Q9-5]
RefSeq; NP_858045.1; NM_181659.2. [Q9Y6Q9-1]
UniGene; Hs.592142; -.
PDB; 1KBH; NMR; -; A=1045-1091.
PDB; 3L3X; X-ray; 1.55 A; B=618-629.
PDB; 3L3Z; X-ray; 2.00 A; B=735-746.
PDBsum; 1KBH; -.
PDBsum; 3L3X; -.
PDBsum; 3L3Z; -.
DisProt; DP00343; -.
ProteinModelPortal; Q9Y6Q9; -.
SMR; Q9Y6Q9; -.
BioGrid; 113841; 110.
CORUM; Q9Y6Q9; -.
DIP; DIP-30876N; -.
ELM; Q9Y6Q9; -.
IntAct; Q9Y6Q9; 55.
MINT; MINT-231818; -.
STRING; 9606.ENSP00000361066; -.
BindingDB; Q9Y6Q9; -.
ChEMBL; CHEMBL1615382; -.
iPTMnet; Q9Y6Q9; -.
PhosphoSitePlus; Q9Y6Q9; -.
SwissPalm; Q9Y6Q9; -.
BioMuta; NCOA3; -.
DMDM; 23396777; -.
EPD; Q9Y6Q9; -.
PaxDb; Q9Y6Q9; -.
PeptideAtlas; Q9Y6Q9; -.
PRIDE; Q9Y6Q9; -.
Ensembl; ENST00000371997; ENSP00000361065; ENSG00000124151. [Q9Y6Q9-3]
Ensembl; ENST00000371998; ENSP00000361066; ENSG00000124151. [Q9Y6Q9-1]
Ensembl; ENST00000372004; ENSP00000361073; ENSG00000124151. [Q9Y6Q9-5]
GeneID; 8202; -.
KEGG; hsa:8202; -.
UCSC; uc002xtk.4; human. [Q9Y6Q9-1]
CTD; 8202; -.
DisGeNET; 8202; -.
EuPathDB; HostDB:ENSG00000124151.18; -.
GeneCards; NCOA3; -.
HGNC; HGNC:7670; NCOA3.
HPA; CAB009800; -.
HPA; HPA024210; -.
MIM; 601937; gene.
neXtProt; NX_Q9Y6Q9; -.
OpenTargets; ENSG00000124151; -.
PharmGKB; PA31472; -.
eggNOG; ENOG410IQ5R; Eukaryota.
eggNOG; ENOG410ZDZC; LUCA.
GeneTree; ENSGT00530000063109; -.
HOVERGEN; HBG052583; -.
InParanoid; Q9Y6Q9; -.
KO; K11256; -.
OMA; MQCFALS; -.
OrthoDB; EOG091G152H; -.
PhylomeDB; Q9Y6Q9; -.
TreeFam; TF332652; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
SignaLink; Q9Y6Q9; -.
SIGNOR; Q9Y6Q9; -.
ChiTaRS; NCOA3; human.
EvolutionaryTrace; Q9Y6Q9; -.
GeneWiki; Nuclear_receptor_coactivator_3; -.
GenomeRNAi; 8202; -.
PRO; PR:Q9Y6Q9; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000124151; -.
CleanEx; HS_NCOA3; -.
CleanEx; HS_RAC3; -.
CleanEx; HS_TRAM1; -.
Genevisible; Q9Y6Q9; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; IPI:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IBA:GO_Central.
GO; GO:0035257; F:nuclear hormone receptor binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IMP:CAFA.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0000993; F:RNA polymerase II core binding; ISS:UniProtKB.
GO; GO:0046966; F:thyroid hormone receptor binding; NAS:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
GO; GO:0043697; P:cell dedifferentiation; ISS:UniProtKB.
GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:BHF-UCL.
GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
GO; GO:0030522; P:intracellular receptor signaling pathway; IBA:GO_Central.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:UniProtKB.
GO; GO:1902459; P:positive regulation of stem cell population maintenance; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0035624; P:receptor transactivation; TAS:UniProtKB.
GO; GO:2001141; P:regulation of RNA biosynthetic process; IMP:UniProtKB.
GO; GO:2000035; P:regulation of stem cell division; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00083; HLH; 1.
CDD; cd00130; PAS; 1.
Gene3D; 1.10.287.1070; -; 1.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR010011; DUF1518.
InterPro; IPR032565; DUF4927.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR028818; NCOA3.
InterPro; IPR009110; Nuc_rcpt_coact.
InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ.
InterPro; IPR037077; Nuc_rcpt_coact_Ncoa_int_sf.
InterPro; IPR017426; Nuclear_rcpt_coactivator.
InterPro; IPR000014; PAS.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR013767; PAS_fold.
InterPro; IPR014935; SRC/p160_LXXLL.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
PANTHER; PTHR10684; PTHR10684; 1.
PANTHER; PTHR10684:SF3; PTHR10684:SF3; 1.
Pfam; PF07469; DUF1518; 1.
Pfam; PF16279; DUF4927; 1.
Pfam; PF08815; Nuc_rec_co-act; 1.
Pfam; PF00989; PAS; 1.
Pfam; PF08832; SRC-1; 1.
PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1.
SMART; SM01151; DUF1518; 1.
SMART; SM00353; HLH; 1.
SMART; SM00091; PAS; 1.
SUPFAM; SSF47459; SSF47459; 1.
SUPFAM; SSF55785; SSF55785; 2.
SUPFAM; SSF69125; SSF69125; 1.
PROSITE; PS50888; BHLH; 1.
PROSITE; PS50112; PAS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Acyltransferase;
Alternative splicing; Complete proteome; Cytoplasm; Methylation;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 1424 Nuclear receptor coactivator 3.
/FTId=PRO_0000094406.
DOMAIN 25 82 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 110 180 PAS. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
REGION 1023 1093 Interaction with CREBBP.
{ECO:0000269|PubMed:9346901}.
REGION 1097 1304 Acetyltransferase.
MOTIF 685 689 LXXLL motif 1.
MOTIF 738 742 LXXLL motif 2.
MOTIF 1057 1061 LXXLL motif 3.
COMPBIAS 505 671 Ser-rich.
COMPBIAS 976 980 Poly-Gln.
COMPBIAS 1248 1278 Poly-Gln.
COMPBIAS 1392 1417 Met-rich.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000250|UniProtKB:O09000}.
MOD_RES 601 601 Phosphoserine; by CK1.
{ECO:0000269|PubMed:19339517}.
MOD_RES 616 616 N6-acetyllysine; by CREBBP.
{ECO:0000269|PubMed:10490106}.
MOD_RES 619 619 N6-acetyllysine; by CREBBP.
{ECO:0000269|PubMed:10490106}.
MOD_RES 620 620 N6-acetyllysine; by CREBBP.
{ECO:0000269|PubMed:10490106}.
MOD_RES 687 687 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 694 694 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 728 728 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 857 857 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 860 860 Phosphoserine.
{ECO:0000250|UniProtKB:O09000}.
MOD_RES 867 867 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:20068231}.
MOD_RES 1033 1033 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1171 1171 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1177 1177 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1188 1188 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1330 1330 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 321 321 E -> EVTSDGIFSPT (in isoform 3 and
isoform 4). {ECO:0000303|PubMed:9267036}.
/FTId=VSP_003405.
VAR_SEQ 837 901 Missing (in isoform 4).
{ECO:0000303|PubMed:9267036}.
/FTId=VSP_003406.
VAR_SEQ 903 917 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:9267036,
ECO:0000303|PubMed:9346901}.
/FTId=VSP_003407.
VAR_SEQ 1214 1217 Missing (in isoform 3, isoform 4 and
isoform 5). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9238002,
ECO:0000303|PubMed:9252329,
ECO:0000303|PubMed:9267036}.
/FTId=VSP_003408.
VARIANT 218 218 R -> C (in dbSNP:rs6094752).
{ECO:0000269|Ref.5}.
/FTId=VAR_053527.
VARIANT 220 220 R -> I (in dbSNP:rs72645252).
{ECO:0000269|Ref.5}.
/FTId=VAR_060695.
VARIANT 369 369 L -> F (in dbSNP:rs6094756).
/FTId=VAR_053528.
VARIANT 460 460 G -> R (in dbSNP:rs1052765).
/FTId=VAR_013831.
VARIANT 556 556 I -> V (in dbSNP:rs72645272).
{ECO:0000269|Ref.5}.
/FTId=VAR_060696.
VARIANT 559 559 P -> S (in dbSNP:rs2230781).
{ECO:0000269|Ref.5}.
/FTId=VAR_013832.
VARIANT 586 586 Q -> H (in dbSNP:rs2230782).
{ECO:0000269|Ref.5}.
/FTId=VAR_013833.
VARIANT 777 777 S -> A (in dbSNP:rs2230783).
{ECO:0000269|Ref.5}.
/FTId=VAR_053529.
VARIANT 1247 1247 M -> K (in dbSNP:rs72645299).
{ECO:0000269|Ref.5}.
/FTId=VAR_060697.
VARIANT 1247 1247 M -> L (in dbSNP:rs72645298).
{ECO:0000269|Ref.5}.
/FTId=VAR_060698.
VARIANT 1248 1250 Missing. {ECO:0000269|PubMed:9238002,
ECO:0000269|PubMed:9267036}.
/FTId=VAR_013834.
MUTAGEN 616 616 K->Q: Strongly reduces acetylation by
CREBBP. {ECO:0000269|PubMed:10490106}.
MUTAGEN 619 620 KK->QQ: Abolishes acetylation by CREBBP.
{ECO:0000269|PubMed:10490106}.
MUTAGEN 647 647 K->Q: Does not affect acetylation by
CREBBP. {ECO:0000269|PubMed:10490106}.
MUTAGEN 681 681 K->Q: Does not affect acetylation by
CREBBP. {ECO:0000269|PubMed:10490106}.
MUTAGEN 687 687 K->Q: Does not affect acetylation by
CREBBP. {ECO:0000269|PubMed:10490106}.
MUTAGEN 700 700 K->Q: Does not affect acetylation by
CREBBP. {ECO:0000269|PubMed:10490106}.
MUTAGEN 708 708 K->Q: Does not affect acetylation by
CREBBP. {ECO:0000269|PubMed:10490106}.
CONFLICT 131 132 DG -> EA (in Ref. 4; AAC51663).
{ECO:0000305}.
HELIX 619 626 {ECO:0000244|PDB:3L3X}.
HELIX 736 743 {ECO:0000244|PDB:3L3Z}.
HELIX 1049 1060 {ECO:0000244|PDB:1KBH}.
HELIX 1069 1075 {ECO:0000244|PDB:1KBH}.
HELIX 1078 1084 {ECO:0000244|PDB:1KBH}.
HELIX 1086 1088 {ECO:0000244|PDB:1KBH}.
SEQUENCE 1424 AA; 155293 MW; 732CDF0423161679 CRC64;
MSGLGENLDP LASDSRKRKL PCDTPGQGLT CSGEKRRREQ ESKYIEELAE LISANLSDID
NFNVKPDKCA ILKETVRQIR QIKEQGKTIS NDDDVQKADV SSTGQGVIDK DSLGPLLLQA
LDGFLFVVNR DGNIVFVSEN VTQYLQYKQE DLVNTSVYNI LHEEDRKDFL KNLPKSTVNG
VSWTNETQRQ KSHTFNCRML MKTPHDILED INASPEMRQR YETMQCFALS QPRAMMEEGE
DLQSCMICVA RRITTGERTF PSNPESFITR HDLSGKVVNI DTNSLRSSMR PGFEDIIRRC
IQRFFSLNDG QSWSQKRHYQ EAYLNGHAET PVYRFSLADG TIVTAQTKSK LFRNPVTNDR
HGFVSTHFLQ REQNGYRPNP NPVGQGIRPP MAGCNSSVGG MSMSPNQGLQ MPSSRAYGLA
DPSTTGQMSG ARYGGSSNIA SLTPGPGMQS PSSYQNNNYG LNMSSPPHGS PGLAPNQQNI
MISPRNRGSP KIASHQFSPV AGVHSPMASS GNTGNHSFSS SSLSALQAIS EGVGTSLLST
LSSPGPKLDN SPNMNITQPS KVSNQDSKSP LGFYCDQNPV ESSMCQSNSR DHLSDKESKE
SSVEGAENQR GPLESKGHKK LLQLLTCSSD DRGHSSLTNS PLDSSCKESS VSVTSPSGVS
SSTSGGVSST SNMHGSLLQE KHRILHKLLQ NGNSPAEVAK ITAEATGKDT SSITSCGDGN
VVKQEQLSPK KKENNALLRY LLDRDDPSDA LSKELQPQVE GVDNKMSQCT SSTIPSSSQE
KDPKIKTETS EEGSGDLDNL DAILGDLTSS DFYNNSISSN GSHLGTKQQV FQGTNSLGLK
SSQSVQSIRP PYNRAVSLDS PVSVGSSPPV KNISAFPMLP KQPMLGGNPR MMDSQENYGS
SMGGPNRNVT VTQTPSSGDW GLPNSKAGRM EPMNSNSMGR PGGDYNTSLP RPALGGSIPT
LPLRSNSIPG ARPVLQQQQQ MLQMRPGEIP MGMGANPYGQ AAASNQLGSW PDGMLSMEQV
SHGTQNRPLL RNSLDDLVGP PSNLEGQSDE RALLDQLHTL LSNTDATGLE EIDRALGIPE
LVNQGQALEP KQDAFQGQEA AVMMDQKAGL YGQTYPAQGP PMQGGFHLQG QSPSFNSMMN
QMNQQGNFPL QGMHPRANIM RPRTNTPKQL RMQLQQRLQG QQFLNQSRQA LELKMENPTA
GGAAVMRPMM QPQVSSQQGF LNAQMVAQRS RELLSHHFRQ QRVAMMMQQQ QQQQQQQQQQ
QQQQQQQQQQ QQQQQQTQAF SPPPNVTASP SMDGLLAGPT MPQAPPQQFP YQPNYGMGQQ
PDPAFGRVSS PPNAMMSSRM GPSQNPMMQH PQAASIYQSS EMKGWPSGNL ARNSSFSQQQ
FAHQGNPAVY SMVHMNGSSG HMGQMNMNPM PMSGMPMGPD QKYC


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