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Nuclear receptor coactivator 1 (NCoA-1) (EC 2.3.1.48) (Class E basic helix-loop-helix protein 74) (bHLHe74) (Protein Hin-2) (RIP160) (Renal carcinoma antigen NY-REN-52) (Steroid receptor coactivator 1) (SRC-1)

 NCOA1_HUMAN             Reviewed;        1441 AA.
Q15788; O00150; O43792; O43793; Q13071; Q13420; Q2T9G5; Q53SX3;
Q6GVI5; Q7KYV3;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 3.
25-OCT-2017, entry version 168.
RecName: Full=Nuclear receptor coactivator 1;
Short=NCoA-1;
EC=2.3.1.48;
AltName: Full=Class E basic helix-loop-helix protein 74;
Short=bHLHe74;
AltName: Full=Protein Hin-2;
AltName: Full=RIP160;
AltName: Full=Renal carcinoma antigen NY-REN-52;
AltName: Full=Steroid receptor coactivator 1;
Short=SRC-1;
Name=NCOA1; Synonyms=BHLHE74, SRC1;
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 3), INTERACTION WITH GTF2B, AND
VARIANTS LYS-457; LYS-466; PRO-474; THR-591; ALA-685; PHE-999 AND
THR-1154.
PubMed=8754792; DOI=10.1210/endo.137.8.8754792;
Takeshita A., Yen P.M., Misiti S., Cardona G.R., Liu Y., Chin W.W.;
"Molecular cloning and properties of a full-length putative thyroid
hormone receptor coactivator.";
Endocrinology 137:3594-3597(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
SPECIFICITY, AND MUTAGENESIS OF 636-LEU-LEU-637; 693-LEU-LEU-694 AND
752-LEU-LEU-753.
PubMed=9427757; DOI=10.1093/emboj/17.1.232;
Kalkhoven E., Valentine J.E., Heery D.M., Parker M.G.;
"Isoforms of steroid receptor coactivator 1 differ in their ability to
potentiate transcription by the oestrogen receptor.";
EMBO J. 17:232-243(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS LYS-457; LYS-466;
PRO-474; THR-591; ALA-685; PHE-999 AND THR-1154.
TISSUE=Heart muscle, and Skeletal muscle;
PubMed=9575154; DOI=10.1074/jbc.273.20.12101;
Onate S.A., Boonyaratanakornkit V., Spencer T.E., Tsai S.Y.,
Tsai M.-J., Edwards D.P., O'Malley B.W.;
"The steroid receptor coactivator-1 contains multiple receptor
interacting and activation domains that cooperatively enhance the
activation function 1 (AF1) and AF2 domains of steroid receptors.";
J. Biol. Chem. 273:12101-12108(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-1238 AND SER-1272.
SeattleSNPs variation discovery resource;
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 363-1441 (ISOFORM 1), FUNCTION,
INTERACTION WITH ESR1; RXRA; GCCR; PGR AND THRA, AND VARIANTS LYS-457;
LYS-466; PRO-474; THR-591; ALA-685; ALA-794; PHE-999 AND THR-1154.
PubMed=7481822; DOI=10.1126/science.270.5240.1354;
Onate S.A., Tsai S.Y., Tsai M.-J., O'Malley B.W.;
"Sequence and characterization of a coactivator for the steroid
hormone receptor superfamily.";
Science 270:1354-1357(1995).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 865-1441 (ISOFORM 2).
PubMed=11831720; DOI=10.1006/viro.1995.1161;
Raineri I., Soler M., Senn H.-P.;
"Analysis of human immunodeficiency virus type 1 promoter insertion in
vivo.";
Virology 208:359-364(1995).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 868-1441 (ISOFORM 2), CHROMOSOMAL
TRANSLOCATION WITH PAX3, AND TISSUE SPECIFICITY.
PubMed=15313887; DOI=10.1158/0008-5472.CAN-04-0844;
Wachtel M., Dettling M., Koscielniak E., Stegmaier S., Treuner J.,
Simon-Klingenstein K., Buehlmann P., Niggli F.K., Schaefer B.W.;
"Gene expression signatures identify rhabdomyosarcoma subtypes and
detect a novel t(2;2)(q35;p23) translocation fusing PAX3 to NCOA1.";
Cancer Res. 64:5539-5545(2004).
[11]
IDENTIFICATION (ISOFORM 2), FUNCTION, AND ALTERNATIVE SPLICING.
PubMed=9223431; DOI=10.1006/bbrc.1997.6911;
Hayashi Y., Ohmori S., Ito T., Seo H.;
"A splicing variant of steroid receptor coactivator-1 (SRC-1E): the
major isoform of SRC-1 to mediate thyroid hormone action.";
Biochem. Biophys. Res. Commun. 236:83-87(1997).
[12]
FUNCTION AS A HISTONE ACETYLTRANSFERASE, AND INTERACTION WITH PCAF.
PubMed=9296499; DOI=10.1038/38304;
Spencer T.E., Jenster G., Burcin M.M., Allis C.D., Zhou J.,
Mizzen C.A., McKenna N.J., Onate S.A., Tsai S.Y., Tsai M.-J.,
O'Malley B.W.;
"Steroid receptor coactivator-1 is a histone acetyltransferase.";
Nature 389:194-198(1997).
[13]
FUNCTION.
PubMed=9223281; DOI=10.1073/pnas.94.15.7879;
Jenster G., Spencer T.E., Burcin M.M., Tsai S.Y., Tsai M.-J.,
O'Malley B.W.;
"Steroid receptor induction of gene transcription: a two-step model.";
Proc. Natl. Acad. Sci. U.S.A. 94:7879-7884(1997).
[14]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[15]
INTERACTION WITH NCOA6.
PubMed=10567404; DOI=10.1074/jbc.274.48.34283;
Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y.,
Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D.,
Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.;
"A nuclear factor ASC-2, as a cancer-amplified transcriptional
coactivator essential for ligand-dependent transactivation by nuclear
receptors in vivo.";
J. Biol. Chem. 274:34283-34293(1999).
[16]
FUNCTION.
PubMed=10449719; DOI=10.1073/pnas.96.17.9485;
Liu Z., Wong J., Tsai S.Y., Tsai M.-J., O'Malley B.W.;
"Steroid receptor coactivator-1 (SRC-1) enhances ligand-dependent and
receptor-dependent cell-free transcription of chromatin.";
Proc. Natl. Acad. Sci. U.S.A. 96:9485-9490(1999).
[17]
PHOSPHORYLATION AT SER-372; SER-395; SER-517; SER-569; SER-1033;
THR-1179 AND SER-1185.
PubMed=10660621; DOI=10.1074/jbc.275.6.4475;
Rowan B.G., Weigel N.L., O'Malley B.W.;
"Phosphorylation of steroid receptor coactivator-1. Identification of
the phosphorylation sites and phosphorylation through the mitogen-
activated protein kinase pathway.";
J. Biol. Chem. 275:4475-4483(2000).
[18]
INTERACTION WITH COPS5.
PubMed=10722692; DOI=10.1074/jbc.275.12.8540;
Chauchereau A., Georgiakaki M., Perrin-Wolff M., Milgrom E.,
Loosfelt H.;
"JAB1 interacts with both the progesterone receptor and SRC-1.";
J. Biol. Chem. 275:8540-8548(2000).
[19]
INTERACTION WITH NCOA2.
PubMed=10594042; DOI=10.1128/MCB.20.1.402-415.2000;
Carrero P., Okamoto K., Coumailleau P., O'Brien S., Tanaka H.,
Poellinger L.;
"Redox-regulated recruitment of the transcriptional coactivators CREB-
binding protein and SRC-1 to hypoxia-inducible factor 1alpha.";
Mol. Cell. Biol. 20:402-415(2000).
[20]
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).
[21]
INTERACTION WITH STAT3.
PubMed=11773079; DOI=10.1074/jbc.M111486200;
Giraud S., Bienvenu F., Avril S., Gascan H., Heery D.M., Coqueret O.;
"Functional interaction of STAT3 transcription factor with the
coactivator NcoA/SRC1a.";
J. Biol. Chem. 277:8004-8011(2002).
[22]
INTERACTION WITH PRMT2.
PubMed=12039952; DOI=10.1074/jbc.M201053200;
Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
"Identification of protein arginine methyltransferase 2 as a
coactivator for estrogen receptor alpha.";
J. Biol. Chem. 277:28624-28630(2002).
[23]
INTERACTION WITH STAT6.
PubMed=12138096; DOI=10.1074/jbc.M203556200;
Litterst C.M., Pfitzner E.;
"An LXXLL motif in the transactivation domain of STAT6 mediates
recruitment of NCoA-1/SRC-1.";
J. Biol. Chem. 277:36052-36060(2002).
[24]
SUMOYLATION AT LYS-732 AND LYS-774, UBIQUITINATION, AND MUTAGENESIS OF
LYS-732; LYS-774; LYS-800; LYS-846 AND LYS-1378.
PubMed=12529333; DOI=10.1074/jbc.M207148200;
Chauchereau A., Amazit L., Quesne M., Guiochon-Mantel A., Milgrom E.;
"Sumoylation of the progesterone receptor and of the steroid receptor
coactivator SRC-1.";
J. Biol. Chem. 278:12335-12343(2003).
[25]
FUNCTION, AND INTERACTION WITH STAT5A AND STAT5B.
PubMed=12954634; DOI=10.1074/jbc.M303644200;
Litterst C.M., Kliem S., Marilley D., Pfitzner E.;
"NCoA-1/SRC-1 is an essential coactivator of STAT5 that binds to the
FDL motif in the alpha-helical region of the STAT5 transactivation
domain.";
J. Biol. Chem. 278:45340-45351(2003).
[26]
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).
[27]
INTERACTION WITH UBE2L3.
PubMed=15367689; DOI=10.1128/MCB.24.19.8716-8726.2004;
Verma S., Ismail A., Gao X., Fu G., Li X., O'Malley B.W., Nawaz Z.;
"The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for
steroid hormone receptors.";
Mol. Cell. Biol. 24:8716-8726(2004).
[28]
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).
[29]
INTERACTION WITH ASXL1.
PubMed=16606617; DOI=10.1074/jbc.M512616200;
Cho Y.S., Kim E.J., Park U.H., Sin H.S., Um S.J.;
"Additional sex comb-like 1 (ASXL1), in cooperation with SRC-1, acts
as a ligand-dependent coactivator for retinoic acid receptor.";
J. Biol. Chem. 281:17588-17598(2006).
[30]
INTERACTION WITH TTLL5.
TISSUE=Testis;
PubMed=17116691; DOI=10.1128/MCB.01360-06;
He Y., Simons S.S. Jr.;
"STAMP, a novel predicted factor assisting TIF2 actions in
glucocorticoid receptor-mediated induction and repression.";
Mol. Cell. Biol. 27:1467-1485(2007).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[33]
INTERACTION WITH RXRA.
PubMed=19786558; DOI=10.1124/mol.109.057000;
Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K.,
Kato Y., Makishima M.;
"The basic helix-loop-helix proteins differentiated embryo chondrocyte
(DEC) 1 and DEC2 function as corepressors of retinoid X receptors.";
Mol. Pharmacol. 76:1360-1369(2009).
[34]
INTERACTION WITH PRMT6.
PubMed=20047962; DOI=10.1093/nar/gkp1203;
Harrison M.J., Tang Y.H., Dowhan D.H.;
"Protein arginine methyltransferase 6 regulates multiple aspects of
gene expression.";
Nucleic Acids Res. 38:2201-2216(2010).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, 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).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-372; SER-395;
SER-698 AND SER-1372, 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).
[37]
INTERACTION WITH TRIP4.
PubMed=25219498; DOI=10.1016/j.molcel.2014.08.007;
Yoo H.M., Kang S.H., Kim J.Y., Lee J.E., Seong M.W., Lee S.W.,
Ka S.H., Sou Y.S., Komatsu M., Tanaka K., Lee S.T., Noh D.Y.,
Baek S.H., Jeon Y.J., Chung C.H.;
"Modification of ASC1 by UFM1 is crucial for ERalpha transactivation
and breast cancer development.";
Mol. Cell 56:261-274(2014).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-846, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[39]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 623-710 IN COMPLEX WITH
PPARG.
PubMed=9744270; DOI=10.1038/25931;
Nolte R.T., Wisely G.B., Westin S., Cobb J.E., Lambert M.H.,
Kurokawa R., Rosenfeld M.G., Willson T.M., Glass C.K., Milburn M.V.;
"Ligand binding and co-activator assembly of the peroxisome
proliferator-activated receptor-gamma.";
Nature 395:137-143(1998).
[40]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 687-696 IN COMPLEX WITH
PPARA.
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).
[41]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 686-700 IN COMPLEX WITH
ESRRG.
PubMed=11864604; DOI=10.1016/S1097-2765(02)00444-6;
Greschik H., Wurtz J.-M., Sanglier S., Bourguet W., van Dorsselaer A.,
Moras D., Renaud J.-P.;
"Structural and functional evidence for ligand-independent
transcriptional activation by the estrogen-related receptor 3.";
Mol. Cell 9:303-313(2002).
[42]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 257-385 IN COMPLEX WITH
795-808 OF STAT6.
PubMed=14757047; DOI=10.1016/j.jmb.2003.12.057;
Razeto A., Ramakrishnan V., Litterst C.M., Giller K., Griesinger C.,
Carlomagno T., Lakomek N., Heimburg T., Lodrini M., Pfitzner E.,
Becker S.;
"Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif
of the STAT6 transactivation domain.";
J. Mol. Biol. 336:319-329(2004).
-!- FUNCTION: Nuclear receptor coactivator that directly binds nuclear
receptors and stimulates the transcriptional activities in a
hormone-dependent fashion. Involved in the coactivation of
different nuclear receptors, such as for steroids (PGR, GR and
ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids
(PPARs). Also involved in coactivation mediated by STAT3, STAT5A,
STAT5B and STAT6 transcription factors. Displays histone
acetyltransferase activity toward H3 and H4; the relevance of such
activity remains however unclear. Plays a central role in creating
multisubunit coactivator complexes that act via remodeling of
chromatin, and possibly acts by participating in both chromatin
remodeling and recruitment of general transcription factors.
Required with NCOA2 to control energy balance between white and
brown adipose tissues. Required for mediating steroid hormone
response. Isoform 2 has a higher thyroid hormone-dependent
transactivation activity than isoform 1 and isoform 3.
{ECO:0000269|PubMed:10449719, ECO:0000269|PubMed:12954634,
ECO:0000269|PubMed:7481822, ECO:0000269|PubMed:9223281,
ECO:0000269|PubMed:9223431, ECO:0000269|PubMed:9296499,
ECO:0000269|PubMed:9427757}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine.
-!- SUBUNIT: Interacts with the methyltransferase CARM1 (By
similarity). Interacts with NCOA6 and NCOA2. Interacts with the
FDL motif of STAT5A and STAT5B. Interacts with the LXXLL motif of
STAT6. Interacts with STAT3 following IL-6 stimulation. Interacts
with the basal transcription factor GTF2B. Interacts with the
histone acetyltransferases EP300 and CREBBP. Interacts with PCAF,
COPS5, NR3C1 and TTLL5/STAMP. Interacts with PSMB9. Interacts with
UBE2L3; they functionally interact to regulate progesterone
receptor transcriptional activity. Interacts with PRMT2 and DDX5.
Interacts with ASXL1. Interacts with PRMT6. Interacts (via LXXLL
1, 2 and 3 motifs) with RORC (via AF-2 motif). Interacts in a
ligand-dependent fashion with RXRA. Interacts with TRIP4.
Interacts with NR4A3 (By similarity).
{ECO:0000250|UniProtKB:P70365, ECO:0000269|PubMed:10567404,
ECO:0000269|PubMed:10594042, ECO:0000269|PubMed:10722692,
ECO:0000269|PubMed:11250900, ECO:0000269|PubMed:11698662,
ECO:0000269|PubMed:11773079, ECO:0000269|PubMed:11864604,
ECO:0000269|PubMed:12039952, ECO:0000269|PubMed:12138096,
ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:12954634,
ECO:0000269|PubMed:14757047, ECO:0000269|PubMed:15367689,
ECO:0000269|PubMed:16606617, ECO:0000269|PubMed:16957778,
ECO:0000269|PubMed:17116691, ECO:0000269|PubMed:19786558,
ECO:0000269|PubMed:20047962, ECO:0000269|PubMed:25219498,
ECO:0000269|PubMed:7481822, ECO:0000269|PubMed:8754792,
ECO:0000269|PubMed:9296499, ECO:0000269|PubMed:9744270}.
-!- INTERACTION:
P59598:Asxl1 (xeno); NbExp=2; IntAct=EBI-455189, EBI-5743705;
P03372:ESR1; NbExp=10; IntAct=EBI-455189, EBI-78473;
P19785:Esr1 (xeno); NbExp=2; IntAct=EBI-455189, EBI-346765;
Q63ZY3:KANK2; NbExp=4; IntAct=EBI-455189, EBI-2556193;
P25799:Nfkb1 (xeno); NbExp=2; IntAct=EBI-455189, EBI-643958;
Q13133:NR1H3; NbExp=15; IntAct=EBI-455189, EBI-781356;
Q96RI1:NR1H4; NbExp=4; IntAct=EBI-455189, EBI-1250177;
Q96RI1-2:NR1H4; NbExp=5; IntAct=EBI-455189, EBI-9640524;
O75469:NR1I2; NbExp=5; IntAct=EBI-455189, EBI-3905991;
P06536:Nr3c1 (xeno); NbExp=2; IntAct=EBI-455189, EBI-1187143;
Q9BTK6:PAGR1; NbExp=4; IntAct=EBI-455189, EBI-2372223;
P28065:PSMB9; NbExp=3; IntAct=EBI-455189, EBI-603300;
P10276:RARA; NbExp=7; IntAct=EBI-455189, EBI-413374;
P51449:RORC; NbExp=2; IntAct=EBI-455189, EBI-3908771;
P19793:RXRA; NbExp=14; IntAct=EBI-455189, EBI-78598;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00981}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=SRC-1A, SRC1a;
IsoId=Q15788-1; Sequence=Displayed;
Name=2; Synonyms=SRC-1E, SRC1e;
IsoId=Q15788-2; Sequence=VSP_011739;
Note=Major form. Contains a domain at its C-terminus (1241-1399)
that is able to mediate transactivation.;
Name=3; Synonyms=SRC-1 (-Q);
IsoId=Q15788-3; Sequence=VSP_011738;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:15313887, ECO:0000269|PubMed:9427757}.
-!- DOMAIN: The C-terminal (1107-1441) part mediates the histone
acetyltransferase (HAT) activity.
-!- DOMAIN: Contains 7 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. LXXLL
motifs 3, 4 and 5 are essential for the association with nuclear
receptors. LXXLL motif 7, which is not present in isoform 2,
increases the affinity for steroid receptors in vitro.
-!- PTM: Sumoylated; sumoylation increases its interaction with PGR
and prolongs its retention in the nucleus. It does not prevent its
ubiquitination and does not exert a clear effect on the stability
of the protein. {ECO:0000269|PubMed:12529333}.
-!- PTM: Ubiquitinated; leading to proteasome-mediated degradation.
Ubiquitination and sumoylation take place at different sites.
{ECO:0000269|PubMed:12529333}.
-!- DISEASE: Note=A chromosomal aberration involving NCOA1 is a cause
of rhabdomyosarcoma. Translocation t(2;2)(q35;p23) with PAX3
generates the NCOA1-PAX3 oncogene consisting of the N-terminus
part of PAX3 and the C-terminus part of NCOA1. The fusion protein
acts as a transcriptional activator. Rhabdomyosarcoma is the most
common soft tissue carcinoma in childhood, representing 5-8% of
all malignancies in children. {ECO:0000269|PubMed:15313887}.
-!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA64187.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAC50305.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/ncoa1/";
-----------------------------------------------------------------------
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EMBL; U59302; AAC50631.1; -; mRNA.
EMBL; AJ000881; CAA04371.1; -; mRNA.
EMBL; AJ000882; CAA04372.1; -; mRNA.
EMBL; U90661; AAB50242.1; -; mRNA.
EMBL; EF660499; ABS29266.1; -; Genomic_DNA.
EMBL; AC013459; AAX93184.1; -; Genomic_DNA.
EMBL; AC093798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471053; EAX00746.1; -; Genomic_DNA.
EMBL; BC111533; AAI11534.1; -; mRNA.
EMBL; BC111534; AAI11535.1; -; mRNA.
EMBL; U40396; AAC50305.1; ALT_INIT; mRNA.
EMBL; U19179; AAA64187.1; ALT_INIT; mRNA.
EMBL; AY633656; AAT47737.1; -; mRNA.
CCDS; CCDS1712.1; -. [Q15788-1]
CCDS; CCDS1713.1; -. [Q15788-2]
CCDS; CCDS42660.1; -. [Q15788-3]
PIR; A57620; A57620.
PIR; PC4363; PC4363.
PIR; PC4364; PC4364.
RefSeq; NP_003734.3; NM_003743.4. [Q15788-1]
RefSeq; NP_671756.1; NM_147223.2. [Q15788-2]
RefSeq; NP_671766.1; NM_147233.2. [Q15788-3]
RefSeq; XP_005264682.1; XM_005264625.1. [Q15788-1]
RefSeq; XP_005264683.1; XM_005264626.1. [Q15788-3]
RefSeq; XP_005264685.1; XM_005264628.1. [Q15788-2]
RefSeq; XP_016860657.1; XM_017005168.1. [Q15788-2]
RefSeq; XP_016860658.1; XM_017005169.1. [Q15788-2]
UniGene; Hs.596314; -.
PDB; 1FM6; X-ray; 2.10 A; B/E/V/Y=676-700.
PDB; 1FM9; X-ray; 2.10 A; B/E=676-700.
PDB; 1K4W; X-ray; 1.90 A; B=686-700.
PDB; 1K74; X-ray; 2.30 A; B/E=676-700.
PDB; 1K7L; X-ray; 2.50 A; B/D/F/H=680-700.
PDB; 1KV6; X-ray; 2.70 A; C/D=686-700.
PDB; 1N4H; X-ray; 2.10 A; B=686-700.
PDB; 1NQ7; X-ray; 1.50 A; B=687-696.
PDB; 1NRL; X-ray; 2.00 A; C/D=676-700.
PDB; 1P8D; X-ray; 2.80 A; C/D=676-700.
PDB; 1PZL; X-ray; 2.10 A; B=687-700.
PDB; 1RDT; X-ray; 2.40 A; B=676-700.
PDB; 1TFC; X-ray; 2.40 A; C/D=686-700.
PDB; 1U3R; X-ray; 2.21 A; C/D=630-640.
PDB; 1U3S; X-ray; 2.50 A; C/D=630-640.
PDB; 1X76; X-ray; 2.20 A; C/D=630-640.
PDB; 1X78; X-ray; 2.30 A; C/D=630-640.
PDB; 1X7B; X-ray; 2.30 A; C/D=630-640.
PDB; 1X7J; X-ray; 2.30 A; C/D=630-640.
PDB; 1XIU; X-ray; 2.50 A; E/F=686-700.
PDB; 1XV9; X-ray; 2.70 A; E/F/G/H=685-697.
PDB; 1XVP; X-ray; 2.60 A; E/F/G/H=685-697.
PDB; 1YY4; X-ray; 2.70 A; C/D=630-640.
PDB; 1YYE; X-ray; 2.03 A; C/D=630-640.
PDB; 1ZAF; X-ray; 2.20 A; C/D=630-640.
PDB; 2A3I; X-ray; 1.95 A; B=1430-1441.
PDB; 2C52; NMR; -; B=920-970.
PDB; 2FVJ; X-ray; 1.99 A; B=628-640.
PDB; 2GTK; X-ray; 2.10 A; B=631-640.
PDB; 2HBH; X-ray; 2.65 A; B=686-700.
PDB; 2HC4; X-ray; 2.20 A; B=686-700.
PDB; 2HCD; X-ray; 2.60 A; B=686-700.
PDB; 2HFP; X-ray; 2.00 A; B=680-700.
PDB; 2NPA; X-ray; 2.30 A; B/D=683-697.
PDB; 2NV7; X-ray; 2.10 A; C/D=631-640.
PDB; 2P54; X-ray; 1.79 A; B=686-696.
PDB; 2PRG; X-ray; 2.30 A; C=623-710.
PDB; 3BEJ; X-ray; 1.90 A; E/F=676-700.
PDB; 3BQD; X-ray; 2.50 A; B=1429-1441.
PDB; 3CTB; X-ray; 2.00 A; A/B=678-700.
PDB; 3CWD; X-ray; 2.40 A; C/D=685-700.
PDB; 3DCT; X-ray; 2.50 A; B=741-761.
PDB; 3DCU; X-ray; 2.95 A; B=741-761.
PDB; 3DR1; X-ray; 2.70 A; B=686-700.
PDB; 3ET1; X-ray; 2.50 A; P/Q=681-696.
PDB; 3ET3; X-ray; 1.95 A; P=680-695.
PDB; 3FEI; X-ray; 2.40 A; Z=744-756.
PDB; 3FEJ; X-ray; 2.01 A; B=628-640.
PDB; 3FUR; X-ray; 2.30 A; H=629-640.
PDB; 3FXV; X-ray; 2.26 A; B=744-756.
PDB; 3G8I; X-ray; 2.20 A; Z=744-756.
PDB; 3G9E; X-ray; 2.30 A; B=628-640.
PDB; 3GYT; X-ray; 2.40 A; B=1429-1441.
PDB; 3GYU; X-ray; 2.40 A; B=1429-1441.
PDB; 3H0A; X-ray; 2.10 A; B/E=629-640.
PDB; 3HC5; X-ray; 2.60 A; B=741-761.
PDB; 3HC6; X-ray; 3.20 A; B=741-761.
PDB; 3HVL; X-ray; 2.10 A; A/B=678-700.
PDB; 3IPQ; X-ray; 2.00 A; B=676-700.
PDB; 3IPS; X-ray; 2.26 A; C/D=676-700.
PDB; 3IPU; X-ray; 2.40 A; C/D=676-700.
PDB; 3KMR; X-ray; 1.80 A; C=686-698.
PDB; 3LMP; X-ray; 1.90 A; C=686-700.
PDB; 3OKH; X-ray; 2.50 A; B=744-757.
PDB; 3OKI; X-ray; 2.00 A; B/D=744-757.
PDB; 3OLF; X-ray; 1.90 A; B/D=744-757.
PDB; 3OLL; X-ray; 1.50 A; C/D=683-701.
PDB; 3OLS; X-ray; 2.20 A; C/D=683-701.
PDB; 3OMK; X-ray; 1.90 A; B/D=744-757.
PDB; 3OMM; X-ray; 2.10 A; B/D=744-757.
PDB; 3OMO; X-ray; 2.21 A; C/D=683-701.
PDB; 3OMP; X-ray; 2.05 A; C/D=683-701.
PDB; 3OMQ; X-ray; 1.97 A; C/D=683-701.
PDB; 3OOF; X-ray; 2.29 A; B/D=744-757.
PDB; 3OOK; X-ray; 2.29 A; B/D=744-757.
PDB; 3P88; X-ray; 2.95 A; B=745-755.
PDB; 3P89; X-ray; 2.30 A; B=745-755.
PDB; 3QT0; X-ray; 2.50 A; C=685-700.
PDB; 3RUT; X-ray; 3.00 A; B=745-755.
PDB; 3RUU; X-ray; 2.50 A; B=745-755.
PDB; 3RVF; X-ray; 3.10 A; B=741-761.
PDB; 3S9S; X-ray; 2.55 A; B=685-697.
PDB; 3T03; X-ray; 2.10 A; C/D=683-700.
PDB; 3UU7; X-ray; 2.20 A; F/G=686-698.
PDB; 3UUA; X-ray; 2.05 A; F/G=686-698.
PDB; 3UUD; X-ray; 1.60 A; C/D=686-698.
PDB; 3V9Y; X-ray; 2.10 A; B=686-700.
PDB; 3VN2; X-ray; 2.18 A; C=685-700.
PDB; 4DK7; X-ray; 2.45 A; B/D=745-756.
PDB; 4DK8; X-ray; 2.75 A; B/D=745-756.
PDB; 4DM6; X-ray; 1.90 A; E/F=676-700.
PDB; 4DM8; X-ray; 2.30 A; C/D=676-700.
PDB; 4DQM; X-ray; 2.75 A; B/D=1432-1441.
PDB; 4F9M; X-ray; 1.90 A; C=686-700.
PDB; 4FGY; X-ray; 2.84 A; B=686-696.
PDB; 4G1D; X-ray; 2.90 A; B=686-700.
PDB; 4G1Y; X-ray; 2.85 A; B=686-700.
PDB; 4G1Z; X-ray; 2.50 A; B=686-700.
PDB; 4G20; X-ray; 2.90 A; B=686-700.
PDB; 4G21; X-ray; 2.90 A; B=686-700.
PDB; 4G2H; X-ray; 2.50 A; B=686-700.
PDB; 4HEE; X-ray; 2.50 A; Y=676-700.
PDB; 4J5X; X-ray; 2.80 A; A/B/C/D=678-700.
PDB; 4JYG; X-ray; 2.35 A; F/G=686-698.
PDB; 4JYH; X-ray; 2.60 A; C/G=686-698.
PDB; 4JYI; X-ray; 1.90 A; F/G=686-698.
PDB; 4MG5; X-ray; 2.05 A; C/D=686-698.
PDB; 4MG6; X-ray; 2.10 A; C/D=686-698.
PDB; 4MG7; X-ray; 2.15 A; C/D=686-698.
PDB; 4MG8; X-ray; 1.85 A; C/D=686-698.
PDB; 4MG9; X-ray; 2.00 A; F/G=686-698.
PDB; 4MGA; X-ray; 1.80 A; C/D=686-698.
PDB; 4MGB; X-ray; 1.85 A; C/D=686-698.
PDB; 4MGC; X-ray; 2.15 A; F/G=686-698.
PDB; 4MGD; X-ray; 1.90 A; F/G=686-698.
PDB; 4RUJ; X-ray; 2.35 A; B=686-700.
PDB; 4RUP; X-ray; 2.75 A; B=686-700.
PDB; 4TUZ; X-ray; 1.90 A; F/G=686-698.
PDB; 4TV1; X-ray; 1.85 A; C/D=686-698.
PDB; 4UDA; X-ray; 2.03 A; B=1427-1441.
PDB; 4UDB; X-ray; 2.36 A; B=1427-1441.
PDB; 4Y29; X-ray; 1.98 A; B=1432-1441.
PDB; 5A86; X-ray; 2.25 A; C/D=682-698.
PDB; 5AVI; X-ray; 2.70 A; B/D=676-700.
PDB; 5AVL; X-ray; 2.80 A; B=676-700.
PDB; 5AZT; X-ray; 3.45 A; C=683-697.
PDB; 5DSH; X-ray; 2.95 A; B=685-700.
PDB; 5DV3; X-ray; 2.75 A; B=685-700.
PDB; 5DV6; X-ray; 2.80 A; B=685-700.
PDB; 5DV8; X-ray; 2.75 A; B=685-700.
PDB; 5DVC; X-ray; 2.30 A; B=685-700.
PDB; 5DWL; X-ray; 2.20 A; B=685-700.
PDB; 5E7V; X-ray; 2.40 A; B=686-700.
PDB; 5GTN; X-ray; 1.85 A; B=685-700.
PDB; 5GTO; X-ray; 2.10 A; B=685-700.
PDB; 5GTP; X-ray; 2.35 A; B=685-700.
PDB; 5HJS; X-ray; 1.72 A; C/D=676-700.
PDB; 5JI0; X-ray; 1.98 A; E/F=676-700.
PDB; 5JMM; X-ray; 2.10 A; F/G=686-698.
PDB; 5L7E; X-ray; 1.86 A; B=1432-1441.
PDB; 5L7G; X-ray; 2.01 A; B=1432-1441.
PDB; 5L7H; X-ray; 1.84 A; B=1432-1441.
PDB; 5NKY; X-ray; 2.10 A; B=686-700.
PDB; 5NMA; X-ray; 2.80 A; B=686-700.
PDB; 5NMB; X-ray; 2.50 A; B2=686-700.
PDB; 5X8U; X-ray; 2.00 A; B=686-700.
PDB; 5X8W; X-ray; 2.30 A; B=686-700.
PDBsum; 1FM6; -.
PDBsum; 1FM9; -.
PDBsum; 1K4W; -.
PDBsum; 1K74; -.
PDBsum; 1K7L; -.
PDBsum; 1KV6; -.
PDBsum; 1N4H; -.
PDBsum; 1NQ7; -.
PDBsum; 1NRL; -.
PDBsum; 1P8D; -.
PDBsum; 1PZL; -.
PDBsum; 1RDT; -.
PDBsum; 1TFC; -.
PDBsum; 1U3R; -.
PDBsum; 1U3S; -.
PDBsum; 1X76; -.
PDBsum; 1X78; -.
PDBsum; 1X7B; -.
PDBsum; 1X7J; -.
PDBsum; 1XIU; -.
PDBsum; 1XV9; -.
PDBsum; 1XVP; -.
PDBsum; 1YY4; -.
PDBsum; 1YYE; -.
PDBsum; 1ZAF; -.
PDBsum; 2A3I; -.
PDBsum; 2C52; -.
PDBsum; 2FVJ; -.
PDBsum; 2GTK; -.
PDBsum; 2HBH; -.
PDBsum; 2HC4; -.
PDBsum; 2HCD; -.
PDBsum; 2HFP; -.
PDBsum; 2NPA; -.
PDBsum; 2NV7; -.
PDBsum; 2P54; -.
PDBsum; 2PRG; -.
PDBsum; 3BEJ; -.
PDBsum; 3BQD; -.
PDBsum; 3CTB; -.
PDBsum; 3CWD; -.
PDBsum; 3DCT; -.
PDBsum; 3DCU; -.
PDBsum; 3DR1; -.
PDBsum; 3ET1; -.
PDBsum; 3ET3; -.
PDBsum; 3FEI; -.
PDBsum; 3FEJ; -.
PDBsum; 3FUR; -.
PDBsum; 3FXV; -.
PDBsum; 3G8I; -.
PDBsum; 3G9E; -.
PDBsum; 3GYT; -.
PDBsum; 3GYU; -.
PDBsum; 3H0A; -.
PDBsum; 3HC5; -.
PDBsum; 3HC6; -.
PDBsum; 3HVL; -.
PDBsum; 3IPQ; -.
PDBsum; 3IPS; -.
PDBsum; 3IPU; -.
PDBsum; 3KMR; -.
PDBsum; 3LMP; -.
PDBsum; 3OKH; -.
PDBsum; 3OKI; -.
PDBsum; 3OLF; -.
PDBsum; 3OLL; -.
PDBsum; 3OLS; -.
PDBsum; 3OMK; -.
PDBsum; 3OMM; -.
PDBsum; 3OMO; -.
PDBsum; 3OMP; -.
PDBsum; 3OMQ; -.
PDBsum; 3OOF; -.
PDBsum; 3OOK; -.
PDBsum; 3P88; -.
PDBsum; 3P89; -.
PDBsum; 3QT0; -.
PDBsum; 3RUT; -.
PDBsum; 3RUU; -.
PDBsum; 3RVF; -.
PDBsum; 3S9S; -.
PDBsum; 3T03; -.
PDBsum; 3UU7; -.
PDBsum; 3UUA; -.
PDBsum; 3UUD; -.
PDBsum; 3V9Y; -.
PDBsum; 3VN2; -.
PDBsum; 4DK7; -.
PDBsum; 4DK8; -.
PDBsum; 4DM6; -.
PDBsum; 4DM8; -.
PDBsum; 4DQM; -.
PDBsum; 4F9M; -.
PDBsum; 4FGY; -.
PDBsum; 4G1D; -.
PDBsum; 4G1Y; -.
PDBsum; 4G1Z; -.
PDBsum; 4G20; -.
PDBsum; 4G21; -.
PDBsum; 4G2H; -.
PDBsum; 4HEE; -.
PDBsum; 4J5X; -.
PDBsum; 4JYG; -.
PDBsum; 4JYH; -.
PDBsum; 4JYI; -.
PDBsum; 4MG5; -.
PDBsum; 4MG6; -.
PDBsum; 4MG7; -.
PDBsum; 4MG8; -.
PDBsum; 4MG9; -.
PDBsum; 4MGA; -.
PDBsum; 4MGB; -.
PDBsum; 4MGC; -.
PDBsum; 4MGD; -.
PDBsum; 4RUJ; -.
PDBsum; 4RUP; -.
PDBsum; 4TUZ; -.
PDBsum; 4TV1; -.
PDBsum; 4UDA; -.
PDBsum; 4UDB; -.
PDBsum; 4Y29; -.
PDBsum; 5A86; -.
PDBsum; 5AVI; -.
PDBsum; 5AVL; -.
PDBsum; 5AZT; -.
PDBsum; 5DSH; -.
PDBsum; 5DV3; -.
PDBsum; 5DV6; -.
PDBsum; 5DV8; -.
PDBsum; 5DVC; -.
PDBsum; 5DWL; -.
PDBsum; 5E7V; -.
PDBsum; 5GTN; -.
PDBsum; 5GTO; -.
PDBsum; 5GTP; -.
PDBsum; 5HJS; -.
PDBsum; 5JI0; -.
PDBsum; 5JMM; -.
PDBsum; 5L7E; -.
PDBsum; 5L7G; -.
PDBsum; 5L7H; -.
PDBsum; 5NKY; -.
PDBsum; 5NMA; -.
PDBsum; 5NMB; -.
PDBsum; 5X8U; -.
PDBsum; 5X8W; -.
ProteinModelPortal; Q15788; -.
SMR; Q15788; -.
BioGrid; 114200; 114.
CORUM; Q15788; -.
DIP; DIP-30877N; -.
IntAct; Q15788; 35.
MINT; MINT-153305; -.
STRING; 9606.ENSP00000320940; -.
BindingDB; Q15788; -.
ChEMBL; CHEMBL1615387; -.
DrugBank; DB07119; 1-CHLORO-6-(4-HYDROXYPHENYL)-2-NAPHTHOL.
DrugBank; DB06875; 3-(3-FLUORO-4-HYDROXYPHENYL)-7-HYDROXY-1-NAPHTHONITRILE.
DrugBank; DB07236; 3-(6-HYDROXY-NAPHTHALEN-2-YL)-BENZO[D]ISOOXAZOL-6-OL.
DrugBank; DB07230; 3-BROMO-6-HYDROXY-2-(4-HYDROXYPHENYL)-1H-INDEN-1-ONE.
DrugBank; DB07724; 3-{5-methoxy-1-[(4-methoxyphenyl)sulfonyl]-1H-indol-3-yl}propanoic acid.
DrugBank; DB07150; 4-(4-HYDROXYPHENYL)-1-NAPHTHALDEHYDE OXIME.
DrugBank; DB07198; 5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-CARBONITRILE.
DrugBank; DB06927; [5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-YL]ACETONITRILE.
DrugBank; DB08915; Aleglitazar.
DrugBank; DB01645; Genistein.
DrugBank; DB08231; MYRISTIC ACID.
GuidetoPHARMACOLOGY; 2693; -.
iPTMnet; Q15788; -.
PhosphoSitePlus; Q15788; -.
BioMuta; NCOA1; -.
DMDM; 158518533; -.
EPD; Q15788; -.
MaxQB; Q15788; -.
PaxDb; Q15788; -.
PeptideAtlas; Q15788; -.
PRIDE; Q15788; -.
Ensembl; ENST00000288599; ENSP00000288599; ENSG00000084676. [Q15788-2]
Ensembl; ENST00000348332; ENSP00000320940; ENSG00000084676. [Q15788-1]
Ensembl; ENST00000395856; ENSP00000379197; ENSG00000084676. [Q15788-3]
Ensembl; ENST00000405141; ENSP00000385097; ENSG00000084676. [Q15788-2]
Ensembl; ENST00000406961; ENSP00000385216; ENSG00000084676. [Q15788-1]
GeneID; 8648; -.
KEGG; hsa:8648; -.
UCSC; uc002rfj.4; human. [Q15788-1]
CTD; 8648; -.
DisGeNET; 8648; -.
EuPathDB; HostDB:ENSG00000084676.15; -.
GeneCards; NCOA1; -.
HGNC; HGNC:7668; NCOA1.
HPA; CAB019402; -.
HPA; HPA070213; -.
HPA; HPA070520; -.
MIM; 602691; gene.
neXtProt; NX_Q15788; -.
OpenTargets; ENSG00000084676; -.
PharmGKB; PA31470; -.
eggNOG; ENOG410IQ5S; Eukaryota.
eggNOG; ENOG410XPF9; LUCA.
GeneTree; ENSGT00530000063109; -.
HOVERGEN; HBG052583; -.
InParanoid; Q15788; -.
KO; K09101; -.
OMA; MVPMPIP; -.
OrthoDB; EOG091G00US; -.
PhylomeDB; Q15788; -.
TreeFam; TF332652; -.
Reactome; R-HSA-1368082; RORA activates gene expression.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-159418; Recycling of bile acids and salts.
Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
Reactome; R-HSA-211976; Endogenous sterols.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
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; Q15788; -.
SIGNOR; Q15788; -.
ChiTaRS; NCOA1; human.
EvolutionaryTrace; Q15788; -.
GeneWiki; Nuclear_receptor_coactivator_1; -.
GenomeRNAi; 8648; -.
PRO; PR:Q15788; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000084676; -.
ExpressionAtlas; Q15788; baseline and differential.
Genevisible; Q15788; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:CAFA.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; IPI:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:UniProtKB.
GO; GO:0035257; F:nuclear hormone receptor binding; IDA:UniProtKB.
GO; GO:0033142; F:progesterone receptor binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0046965; F:retinoid X receptor binding; IEA:Ensembl.
GO; GO:0001012; F:RNA polymerase II regulatory region DNA binding; IEA:Ensembl.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; NAS:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
GO; GO:0015721; P:bile acid and bile salt transport; TAS:Reactome.
GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IEA:Ensembl.
GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0044849; P:estrous cycle; IEA:Ensembl.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0043967; P:histone H4 acetylation; IEA:Ensembl.
GO; GO:0021854; P:hypothalamus development; IEA:Ensembl.
GO; GO:0030522; P:intracellular receptor signaling pathway; IBA:GO_Central.
GO; GO:0060713; P:labyrinthine layer morphogenesis; IEA:Ensembl.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0060179; P:male mating behavior; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0045925; P:positive regulation of female receptivity; IEA:Ensembl.
GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:2001038; P:regulation of cellular response to drug; IEA:Ensembl.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
CDD; cd00083; HLH; 1.
CDD; cd00130; PAS; 1.
Gene3D; 1.10.287.1070; -; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR010011; DUF1518.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR028819; NCOA1.
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.
PANTHER; PTHR10684; PTHR10684; 1.
PANTHER; PTHR10684:SF1; PTHR10684:SF1; 1.
Pfam; PF07469; DUF1518; 2.
Pfam; PF00010; HLH; 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; 2.
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; Chromosomal rearrangement; Complete proteome;
Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Proto-oncogene; Reference proteome; Repeat; Transcription;
Transcription regulation; Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 1441 Nuclear receptor coactivator 1.
/FTId=PRO_0000094400.
DOMAIN 23 80 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 109 180 PAS. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
REGION 361 567 Interaction with STAT3.
{ECO:0000269|PubMed:11773079}.
REGION 781 988 Interaction with CREBBP.
MOTIF 46 50 LXXLL motif 1.
MOTIF 112 116 LXXLL motif 2.
MOTIF 633 637 LXXLL motif 3.
MOTIF 690 694 LXXLL motif 4.
MOTIF 749 753 LXXLL motif 5.
MOTIF 913 917 LXXLL motif 6.
MOTIF 1435 1439 LXXLL motif 7.
COMPBIAS 389 682 Ser-rich.
COMPBIAS 1053 1138 Gln-rich.
SITE 867 868 Breakpoint for translocation to form
PAX3-NCOA1 oncogene.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10660621}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10660621}.
MOD_RES 517 517 Phosphoserine.
{ECO:0000269|PubMed:10660621}.
MOD_RES 558 558 Phosphoserine.
{ECO:0000250|UniProtKB:P70365}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000269|PubMed:10660621}.
MOD_RES 698 698 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1033 1033 Phosphoserine.
{ECO:0000269|PubMed:10660621}.
MOD_RES 1073 1073 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:P70365}.
MOD_RES 1091 1091 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:P70365}.
MOD_RES 1124 1124 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:P70365}.
MOD_RES 1131 1131 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:P70365}.
MOD_RES 1179 1179 Phosphothreonine.
{ECO:0000269|PubMed:10660621}.
MOD_RES 1185 1185 Phosphoserine.
{ECO:0000269|PubMed:10660621}.
MOD_RES 1372 1372 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 732 732 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:12529333}.
CROSSLNK 774 774 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:12529333}.
CROSSLNK 846 846 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1385 1385 Missing (in isoform 3).
{ECO:0000303|PubMed:8754792}.
/FTId=VSP_011738.
VAR_SEQ 1386 1441 QVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQT
PQAQQKSLLQQLLTE -> DKKTEEFFSVVTTD (in
isoform 2). {ECO:0000303|PubMed:11831720,
ECO:0000303|PubMed:15313887,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9427757}.
/FTId=VSP_011739.
VARIANT 457 457 Q -> K (in dbSNP:rs1049015).
{ECO:0000269|PubMed:7481822,
ECO:0000269|PubMed:8754792,
ECO:0000269|PubMed:9575154}.
/FTId=VAR_019768.
VARIANT 466 466 N -> K (in dbSNP:rs1049016).
{ECO:0000269|PubMed:7481822,
ECO:0000269|PubMed:8754792,
ECO:0000269|PubMed:9575154}.
/FTId=VAR_019769.
VARIANT 474 474 S -> P (in dbSNP:rs1049018).
{ECO:0000269|PubMed:7481822,
ECO:0000269|PubMed:8754792,
ECO:0000269|PubMed:9575154}.
/FTId=VAR_019770.
VARIANT 591 591 I -> T (in dbSNP:rs1049020).
{ECO:0000269|PubMed:7481822,
ECO:0000269|PubMed:8754792,
ECO:0000269|PubMed:9575154}.
/FTId=VAR_019771.
VARIANT 685 685 E -> A (in dbSNP:rs1049021).
{ECO:0000269|PubMed:7481822,
ECO:0000269|PubMed:8754792,
ECO:0000269|PubMed:9575154}.
/FTId=VAR_019772.
VARIANT 794 794 P -> A (in dbSNP:rs1049025).
{ECO:0000269|PubMed:7481822}.
/FTId=VAR_019773.
VARIANT 999 999 S -> F (in dbSNP:rs1049032).
{ECO:0000269|PubMed:7481822,
ECO:0000269|PubMed:8754792,
ECO:0000269|PubMed:9575154}.
/FTId=VAR_019774.
VARIANT 1154 1154 M -> T (in dbSNP:rs1049038).
{ECO:0000269|PubMed:7481822,
ECO:0000269|PubMed:8754792,
ECO:0000269|PubMed:9575154}.
/FTId=VAR_019775.
VARIANT 1238 1238 V -> I (in dbSNP:rs56099330).
{ECO:0000269|Ref.4}.
/FTId=VAR_038832.
VARIANT 1272 1272 P -> S (in dbSNP:rs1804645).
{ECO:0000269|Ref.4}.
/FTId=VAR_034882.
MUTAGEN 636 637 LL->AA: Slightly affects interactions
with steroid receptors. Abolishes
interactions with steroid receptors; when
associated with A-693; A-694; A-752 and
A-753. {ECO:0000269|PubMed:9427757}.
MUTAGEN 693 694 LL->AA: Slightly affects interactions
with steroid receptors. Abolishes
interactions with steroid receptors; when
associated with A-636; A-637; A-752 and
A-753. {ECO:0000269|PubMed:9427757}.
MUTAGEN 732 732 K->R: Abolishes sumoylation; when
associated with R-774.
{ECO:0000269|PubMed:12529333}.
MUTAGEN 752 753 LL->AA: Slightly affects interactions
with steroid receptors. Abolishes
interactions with steroid receptors; when
associated with A-636; A-637; A-693 and
A-694. {ECO:0000269|PubMed:9427757}.
MUTAGEN 774 774 K->R: Abolishes sumoylation; when
associated with R-732.
{ECO:0000269|PubMed:12529333}.
MUTAGEN 800 800 K->R: Does not affect sumoylation of the
protein. {ECO:0000269|PubMed:12529333}.
MUTAGEN 846 846 K->R: Does not affect sumoylation of the
protein. {ECO:0000269|PubMed:12529333}.
MUTAGEN 1378 1378 K->R: Does not affect sumoylation of the
protein. {ECO:0000269|PubMed:12529333}.
CONFLICT 1035 1035 Missing (in Ref. 10; AAT47737).
{ECO:0000305}.
CONFLICT 1370 1370 Q -> H (in Ref. 9; AAA64187).
{ECO:0000305}.
CONFLICT 1382 1382 D -> G (in Ref. 10; AAT47737).
{ECO:0000305}.
CONFLICT 1435 1435 L -> R (in Ref. 3; AAB50242).
{ECO:0000305}.
HELIX 632 638 {ECO:0000244|PDB:2FVJ}.
HELIX 684 686 {ECO:0000244|PDB:5HJS}.
HELIX 688 695 {ECO:0000244|PDB:1NQ7}.
HELIX 747 754 {ECO:0000244|PDB:3OLF}.
TURN 924 926 {ECO:0000244|PDB:2C52}.
HELIX 929 941 {ECO:0000244|PDB:2C52}.
HELIX 945 947 {ECO:0000244|PDB:2C52}.
HELIX 952 954 {ECO:0000244|PDB:2C52}.
TURN 958 962 {ECO:0000244|PDB:2C52}.
STRAND 964 966 {ECO:0000244|PDB:2C52}.
HELIX 1434 1440 {ECO:0000244|PDB:5L7H}.
SEQUENCE 1441 AA; 156757 MW; 25EF6F389489121E CRC64;
MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL
SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL
DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG
VPWPQEATRR NSHTFNCRML IHPPDEPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ
SCLICIARRL PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF
QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ SPDMQPFIMG
IHIIDREHSG LSPQDDTNSG MSIPRVNPSV NPSISPAHGV ARSSTLPPSN SNMVSTRINR
QQSSDLHSSS HSNSSNSQGS FGCSPGSQIV ANVALNQGQA SSQSSNPSLN LNNSPMEGTG
ISLAQFMSPR RQVTSGLATR PRMPNNSFPP NISTLSSPVG MTSSACNNNN RSYSNIPVTS
LQGMNEGPNN SVGFSASSPV LRQMSSQNSP SRLNIQPAKA ESKDNKEIAS ILNEMIQSDN
SSSDGKPLDS GLLHNNDRLS DGDSKYSQTS HKLVQLLTTT AEQQLRHADI DTSCKDVLSC
TGTSNSASAN SSGGSCPSSH SSLTERHKIL HRLLQEGSPS DITTLSVEPD KKDSASTSVS
VTGQVQGNSS IKLELDASKK KESKDHQLLR YLLDKDEKDL RSTPNLSLDD VKVKVEKKEQ
MDPCNTNPTP MTKPTPEEIK LEAQSQFTAD LDQFDQLLPT LEKAAQLPGL CETDRMDGAV
TSVTIKSEIL PASLQSATAR PTSRLNRLPE LELEAIDNQF GQPGTGDQIP WTNNTVTAIN
QSKSEDQCIS SQLDELLCPP TTVEGRNDEK ALLEQLVSFL SGKDETELAE LDRALGIDKL
VQGGGLDVLS ERFPPQQATP PLIMEERPNL YSQPYSSPSP TANLPSPFQG MVRQKPSLGT
MPVQVTPPRG AFSPGMGMQP RQTLNRPPAA PNQLRLQLQQ RLQGQQQLIH QNRQAILNQF
AATAPVGINM RSGMQQQITP QPPLNAQMLA QRQRELYSQQ HRQRQLIQQQ RAMLMRQQSF
GNNLPPSSGL PVQMGNPRLP QGAPQQFPYP PNYGTNPGTP PASTSPFSQL AANPEASLAN
RNSMVSRGMT GNIGGQFGTG INPQMQQNVF QYPGAGMVPQ GEANFAPSLS PGSSMVPMPI
PPPQSSLLQQ TPPASGYQSP DMKAWQQGAI GNNNVFSQAV QNQPTPAQPG VYNNMSITVS
MAGGNTNVQN MNPMMAQMQM SSLQMPGMNT VCPEQINDPA LRHTGLYCNQ LSSTDLLKTE
ADGTQQVQQV QVFADVQCTV NLVGGDPYLN QPGPLGTQKP TSGPQTPQAQ QKSLLQQLLT
E


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EIAAB14718 Basic helix-loop-helix protein N-twist,bHLHa31,BHLHA31,Class A basic helix-loop-helix protein 31,Fer3-like protein,FERD3L,Homo sapiens,Human,NATO3,Nephew of atonal 3,Neuronal twist,NTWIST
E2286h ELISA ARNT,ARNT protein,Aryl hydrocarbon receptor nuclear translocator,bHLHe2,BHLHE2,Class E basic helix-loop-helix protein 2,Dioxin receptor, nuclear translocator,HIF-1-beta,HIF1-beta,Homo sapiens,Hu 96T
E2286h ARNT,ARNT protein,Aryl hydrocarbon receptor nuclear translocator,bHLHe2,BHLHE2,Class E basic helix-loop-helix protein 2,Dioxin receptor, nuclear translocator,HIF-1-beta,HIF1-beta,Homo sapiens,Human,Hy
U2286h CLIA ARNT,ARNT protein,Aryl hydrocarbon receptor nuclear translocator,bHLHe2,BHLHE2,Class E basic helix-loop-helix protein 2,Dioxin receptor, nuclear translocator,HIF-1-beta,HIF1-beta,Homo sapiens,Hum 96T
U2286h CLIA kit ARNT,ARNT protein,Aryl hydrocarbon receptor nuclear translocator,bHLHe2,BHLHE2,Class E basic helix-loop-helix protein 2,Dioxin receptor, nuclear translocator,HIF-1-beta,HIF1-beta,Homo sapien 96T


 

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