NCOA1_HUMAN
ID NCOA1_HUMAN Reviewed; 1441 AA.
AC Q15788; O00150; O43792; O43793; Q13071; Q13420; Q2T9G5; Q53SX3; Q6GVI5;
AC Q7KYV3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 3.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Nuclear receptor coactivator 1;
DE Short=NCoA-1;
DE EC=2.3.1.48;
DE AltName: Full=Class E basic helix-loop-helix protein 74;
DE Short=bHLHe74;
DE AltName: Full=Protein Hin-2;
DE AltName: Full=RIP160;
DE AltName: Full=Renal carcinoma antigen NY-REN-52;
DE AltName: Full=Steroid receptor coactivator 1;
DE Short=SRC-1;
GN Name=NCOA1; Synonyms=BHLHE74, SRC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH GTF2B, AND
RP VARIANTS LYS-457; LYS-466; PRO-474; THR-591; ALA-685; PHE-999 AND THR-1154.
RX PubMed=8754792; DOI=10.1210/endo.137.8.8754792;
RA Takeshita A., Yen P.M., Misiti S., Cardona G.R., Liu Y., Chin W.W.;
RT "Molecular cloning and properties of a full-length putative thyroid hormone
RT receptor coactivator.";
RL Endocrinology 137:3594-3597(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF 636-LEU-LEU-637; 693-LEU-LEU-694 AND
RP 752-LEU-LEU-753.
RX PubMed=9427757; DOI=10.1093/emboj/17.1.232;
RA Kalkhoven E., Valentine J.E., Heery D.M., Parker M.G.;
RT "Isoforms of steroid receptor coactivator 1 differ in their ability to
RT potentiate transcription by the oestrogen receptor.";
RL EMBO J. 17:232-243(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS LYS-457; LYS-466;
RP PRO-474; THR-591; ALA-685; PHE-999 AND THR-1154.
RC TISSUE=Heart muscle, and Skeletal muscle;
RX PubMed=9575154; DOI=10.1074/jbc.273.20.12101;
RA Onate S.A., Boonyaratanakornkit V., Spencer T.E., Tsai S.Y., Tsai M.-J.,
RA Edwards D.P., O'Malley B.W.;
RT "The steroid receptor coactivator-1 contains multiple receptor interacting
RT and activation domains that cooperatively enhance the activation function 1
RT (AF1) and AF2 domains of steroid receptors.";
RL J. Biol. Chem. 273:12101-12108(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-1238 AND SER-1272.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 363-1441 (ISOFORM 1), FUNCTION, INTERACTION
RP WITH ESR1; RXRA; GCCR; PGR AND THRA, AND VARIANTS LYS-457; LYS-466;
RP PRO-474; THR-591; ALA-685; ALA-794; PHE-999 AND THR-1154.
RX PubMed=7481822; DOI=10.1126/science.270.5240.1354;
RA Onate S.A., Tsai S.Y., Tsai M.-J., O'Malley B.W.;
RT "Sequence and characterization of a coactivator for the steroid hormone
RT receptor superfamily.";
RL Science 270:1354-1357(1995).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 865-1441 (ISOFORM 2).
RX PubMed=11831720; DOI=10.1006/viro.1995.1161;
RA Raineri I., Soler M., Senn H.-P.;
RT "Analysis of human immunodeficiency virus type 1 promoter insertion in
RT vivo.";
RL Virology 208:359-364(1995).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 868-1441 (ISOFORM 2), CHROMOSOMAL
RP TRANSLOCATION WITH PAX3, AND TISSUE SPECIFICITY.
RX PubMed=15313887; DOI=10.1158/0008-5472.can-04-0844;
RA Wachtel M., Dettling M., Koscielniak E., Stegmaier S., Treuner J.,
RA Simon-Klingenstein K., Buehlmann P., Niggli F.K., Schaefer B.W.;
RT "Gene expression signatures identify rhabdomyosarcoma subtypes and detect a
RT novel t(2;2)(q35;p23) translocation fusing PAX3 to NCOA1.";
RL Cancer Res. 64:5539-5545(2004).
RN [11]
RP IDENTIFICATION (ISOFORM 2), FUNCTION, AND ALTERNATIVE SPLICING.
RX PubMed=9223431; DOI=10.1006/bbrc.1997.6911;
RA Hayashi Y., Ohmori S., Ito T., Seo H.;
RT "A splicing variant of steroid receptor coactivator-1 (SRC-1E): the major
RT isoform of SRC-1 to mediate thyroid hormone action.";
RL Biochem. Biophys. Res. Commun. 236:83-87(1997).
RN [12]
RP FUNCTION AS A HISTONE ACETYLTRANSFERASE, AND INTERACTION WITH PCAF.
RX PubMed=9296499; DOI=10.1038/38304;
RA Spencer T.E., Jenster G., Burcin M.M., Allis C.D., Zhou J., Mizzen C.A.,
RA McKenna N.J., Onate S.A., Tsai S.Y., Tsai M.-J., O'Malley B.W.;
RT "Steroid receptor coactivator-1 is a histone acetyltransferase.";
RL Nature 389:194-198(1997).
RN [13]
RP FUNCTION.
RX PubMed=9223281; DOI=10.1073/pnas.94.15.7879;
RA Jenster G., Spencer T.E., Burcin M.M., Tsai S.Y., Tsai M.-J.,
RA O'Malley B.W.;
RT "Steroid receptor induction of gene transcription: a two-step model.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7879-7884(1997).
RN [14]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [15]
RP INTERACTION WITH NCOA6.
RX PubMed=10567404; DOI=10.1074/jbc.274.48.34283;
RA Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K.,
RA Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H.,
RA Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.;
RT "A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator
RT essential for ligand-dependent transactivation by nuclear receptors in
RT vivo.";
RL J. Biol. Chem. 274:34283-34293(1999).
RN [16]
RP FUNCTION.
RX PubMed=10449719; DOI=10.1073/pnas.96.17.9485;
RA Liu Z., Wong J., Tsai S.Y., Tsai M.-J., O'Malley B.W.;
RT "Steroid receptor coactivator-1 (SRC-1) enhances ligand-dependent and
RT receptor-dependent cell-free transcription of chromatin.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:9485-9490(1999).
RN [17]
RP PHOSPHORYLATION AT SER-372; SER-395; SER-517; SER-569; SER-1033; THR-1179
RP AND SER-1185.
RX PubMed=10660621; DOI=10.1074/jbc.275.6.4475;
RA Rowan B.G., Weigel N.L., O'Malley B.W.;
RT "Phosphorylation of steroid receptor coactivator-1. Identification of the
RT phosphorylation sites and phosphorylation through the mitogen-activated
RT protein kinase pathway.";
RL J. Biol. Chem. 275:4475-4483(2000).
RN [18]
RP INTERACTION WITH COPS5.
RX PubMed=10722692; DOI=10.1074/jbc.275.12.8540;
RA Chauchereau A., Georgiakaki M., Perrin-Wolff M., Milgrom E., Loosfelt H.;
RT "JAB1 interacts with both the progesterone receptor and SRC-1.";
RL J. Biol. Chem. 275:8540-8548(2000).
RN [19]
RP INTERACTION WITH NCOA2.
RX PubMed=10594042; DOI=10.1128/mcb.20.1.402-415.2000;
RA Carrero P., Okamoto K., Coumailleau P., O'Brien S., Tanaka H.,
RA Poellinger L.;
RT "Redox-regulated recruitment of the transcriptional coactivators CREB-
RT binding protein and SRC-1 to hypoxia-inducible factor 1alpha.";
RL Mol. Cell. Biol. 20:402-415(2000).
RN [20]
RP INTERACTION WITH DDX5.
RX PubMed=11250900; DOI=10.1093/emboj/20.6.1341;
RA Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S., Arao Y.,
RA Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y., Kato S.;
RT "A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor
RT alpha coactivator through the N-terminal activation domain (AF-1) with an
RT RNA coactivator, SRA.";
RL EMBO J. 20:1341-1352(2001).
RN [21]
RP INTERACTION WITH STAT3.
RX PubMed=11773079; DOI=10.1074/jbc.m111486200;
RA Giraud S., Bienvenu F., Avril S., Gascan H., Heery D.M., Coqueret O.;
RT "Functional interaction of STAT3 transcription factor with the coactivator
RT NcoA/SRC1a.";
RL J. Biol. Chem. 277:8004-8011(2002).
RN [22]
RP INTERACTION WITH PRMT2.
RX PubMed=12039952; DOI=10.1074/jbc.m201053200;
RA Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
RT "Identification of protein arginine methyltransferase 2 as a coactivator
RT for estrogen receptor alpha.";
RL J. Biol. Chem. 277:28624-28630(2002).
RN [23]
RP INTERACTION WITH STAT6.
RX PubMed=12138096; DOI=10.1074/jbc.m203556200;
RA Litterst C.M., Pfitzner E.;
RT "An LXXLL motif in the transactivation domain of STAT6 mediates recruitment
RT of NCoA-1/SRC-1.";
RL J. Biol. Chem. 277:36052-36060(2002).
RN [24]
RP SUMOYLATION AT LYS-732 AND LYS-774, UBIQUITINATION, AND MUTAGENESIS OF
RP LYS-732; LYS-774; LYS-800; LYS-846 AND LYS-1378.
RX PubMed=12529333; DOI=10.1074/jbc.m207148200;
RA Chauchereau A., Amazit L., Quesne M., Guiochon-Mantel A., Milgrom E.;
RT "Sumoylation of the progesterone receptor and of the steroid receptor
RT coactivator SRC-1.";
RL J. Biol. Chem. 278:12335-12343(2003).
RN [25]
RP FUNCTION, AND INTERACTION WITH STAT5A AND STAT5B.
RX PubMed=12954634; DOI=10.1074/jbc.m303644200;
RA Litterst C.M., Kliem S., Marilley D., Pfitzner E.;
RT "NCoA-1/SRC-1 is an essential coactivator of STAT5 that binds to the FDL
RT motif in the alpha-helical region of the STAT5 transactivation domain.";
RL J. Biol. Chem. 278:45340-45351(2003).
RN [26]
RP INTERACTION WITH NR3C1.
RX PubMed=12917342; DOI=10.1128/mcb.23.17.6210-6220.2003;
RA Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
RT "BAF60a mediates critical interactions between nuclear receptors and the
RT BRG1 chromatin-remodeling complex for transactivation.";
RL Mol. Cell. Biol. 23:6210-6220(2003).
RN [27]
RP INTERACTION WITH UBE2L3.
RX PubMed=15367689; DOI=10.1128/mcb.24.19.8716-8726.2004;
RA Verma S., Ismail A., Gao X., Fu G., Li X., O'Malley B.W., Nawaz Z.;
RT "The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid
RT hormone receptors.";
RL Mol. Cell. Biol. 24:8716-8726(2004).
RN [28]
RP INTERACTION WITH PSMB9.
RX PubMed=16957778; DOI=10.1038/sj.emboj.7601306;
RA Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R.,
RA Sun X., Shang Y.;
RT "The catalytic subunit of the proteasome is engaged in the entire process
RT of estrogen receptor-regulated transcription.";
RL EMBO J. 25:4223-4233(2006).
RN [29]
RP INTERACTION WITH ASXL1.
RX PubMed=16606617; DOI=10.1074/jbc.m512616200;
RA Cho Y.S., Kim E.J., Park U.H., Sin H.S., Um S.J.;
RT "Additional sex comb-like 1 (ASXL1), in cooperation with SRC-1, acts as a
RT ligand-dependent coactivator for retinoic acid receptor.";
RL J. Biol. Chem. 281:17588-17598(2006).
RN [30]
RP INTERACTION WITH TTLL5.
RC TISSUE=Testis;
RX PubMed=17116691; DOI=10.1128/mcb.01360-06;
RA He Y., Simons S.S. Jr.;
RT "STAMP, a novel predicted factor assisting TIF2 actions in glucocorticoid
RT receptor-mediated induction and repression.";
RL Mol. Cell. Biol. 27:1467-1485(2007).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [33]
RP INTERACTION WITH RXRA.
RX PubMed=19786558; DOI=10.1124/mol.109.057000;
RA Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K., Kato Y.,
RA Makishima M.;
RT "The basic helix-loop-helix proteins differentiated embryo chondrocyte
RT (DEC) 1 and DEC2 function as corepressors of retinoid X receptors.";
RL Mol. Pharmacol. 76:1360-1369(2009).
RN [34]
RP INTERACTION WITH PRMT6.
RX PubMed=20047962; DOI=10.1093/nar/gkp1203;
RA Harrison M.J., Tang Y.H., Dowhan D.H.;
RT "Protein arginine methyltransferase 6 regulates multiple aspects of gene
RT expression.";
RL Nucleic Acids Res. 38:2201-2216(2010).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-372; SER-395; SER-698
RP AND SER-1372, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [37]
RP INTERACTION WITH TRIP4.
RX PubMed=25219498; DOI=10.1016/j.molcel.2014.08.007;
RA Yoo H.M., Kang S.H., Kim J.Y., Lee J.E., Seong M.W., Lee S.W., Ka S.H.,
RA Sou Y.S., Komatsu M., Tanaka K., Lee S.T., Noh D.Y., Baek S.H., Jeon Y.J.,
RA Chung C.H.;
RT "Modification of ASC1 by UFM1 is crucial for ERalpha transactivation and
RT breast cancer development.";
RL Mol. Cell 56:261-274(2014).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-846, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [39]
RP INTERACTION WITH VDR.
RX PubMed=28698609; DOI=10.1038/s41598-017-05081-x;
RA Tamura M., Ishizawa M., Isojima T., Oezen S., Oka A., Makishima M.,
RA Kitanaka S.;
RT "Functional analyses of a novel missense and other mutations of the vitamin
RT D receptor in association with alopecia.";
RL Sci. Rep. 7:5102-5102(2017).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 623-710 IN COMPLEX WITH PPARG.
RX PubMed=9744270; DOI=10.1038/25931;
RA Nolte R.T., Wisely G.B., Westin S., Cobb J.E., Lambert M.H., Kurokawa R.,
RA Rosenfeld M.G., Willson T.M., Glass C.K., Milburn M.V.;
RT "Ligand binding and co-activator assembly of the peroxisome proliferator-
RT activated receptor-gamma.";
RL Nature 395:137-143(1998).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 687-696 IN COMPLEX WITH PPARA.
RX PubMed=11698662; DOI=10.1073/pnas.241410198;
RA Xu H.E., Lambert M.H., Montana V.G., Plunket K.D., Moore L.B.,
RA Collins J.L., Oplinger J.A., Kliewer S.A., Gampe R.T. Jr., McKee D.D.,
RA Moore J.T., Willson T.M.;
RT "Structural determinants of ligand binding selectivity between the
RT peroxisome proliferator-activated receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13919-13924(2001).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 686-700 IN COMPLEX WITH ESRRG.
RX PubMed=11864604; DOI=10.1016/s1097-2765(02)00444-6;
RA Greschik H., Wurtz J.-M., Sanglier S., Bourguet W., van Dorsselaer A.,
RA Moras D., Renaud J.-P.;
RT "Structural and functional evidence for ligand-independent transcriptional
RT activation by the estrogen-related receptor 3.";
RL Mol. Cell 9:303-313(2002).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 257-385 IN COMPLEX WITH 795-808 OF
RP STAT6.
RX PubMed=14757047; DOI=10.1016/j.jmb.2003.12.057;
RA Razeto A., Ramakrishnan V., Litterst C.M., Giller K., Griesinger C.,
RA Carlomagno T., Lakomek N., Heimburg T., Lodrini M., Pfitzner E., Becker S.;
RT "Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the
RT STAT6 transactivation domain.";
RL J. Mol. Biol. 336:319-329(2004).
CC -!- FUNCTION: Nuclear receptor coactivator that directly binds nuclear
CC receptors and stimulates the transcriptional activities in a hormone-
CC dependent fashion. Involved in the coactivation of different nuclear
CC receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs),
CC thyroid hormone (TRs) and prostanoids (PPARs). Also involved in
CC coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription
CC factors. Displays histone acetyltransferase activity toward H3 and H4;
CC the relevance of such activity remains however unclear. Plays a central
CC role in creating multisubunit coactivator complexes that act via
CC remodeling of chromatin, and possibly acts by participating in both
CC chromatin remodeling and recruitment of general transcription factors.
CC Required with NCOA2 to control energy balance between white and brown
CC adipose tissues. Required for mediating steroid hormone response.
CC Isoform 2 has a higher thyroid hormone-dependent transactivation
CC activity than isoform 1 and isoform 3. {ECO:0000269|PubMed:10449719,
CC ECO:0000269|PubMed:12954634, ECO:0000269|PubMed:7481822,
CC ECO:0000269|PubMed:9223281, ECO:0000269|PubMed:9223431,
CC ECO:0000269|PubMed:9296499, ECO:0000269|PubMed:9427757}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC -!- SUBUNIT: Interacts with the methyltransferase CARM1 (By similarity).
CC Interacts with NCOA6 and NCOA2. Interacts with the FDL motif of STAT5A
CC and STAT5B. Interacts with the LXXLL motif of STAT6. Interacts with
CC STAT3 following IL-6 stimulation. Interacts with the basal
CC transcription factor GTF2B. Interacts with the histone
CC acetyltransferases EP300 and CREBBP. Interacts with PCAF, COPS5, NR3C1
CC and TTLL5/STAMP. Interacts with PSMB9. Interacts with UBE2L3; they
CC functionally interact to regulate progesterone receptor transcriptional
CC activity. Interacts with PRMT2 and DDX5. Interacts with ASXL1.
CC Interacts with PRMT6. Interacts (via LXXLL 1, 2 and 3 motifs) with RORC
CC (via AF-2 motif). Interacts in a ligand-dependent fashion with RXRA.
CC Interacts with TRIP4. Interacts with NR4A3 (By similarity). Interacts
CC with VDR. {ECO:0000250|UniProtKB:P70365, ECO:0000269|PubMed:10567404,
CC ECO:0000269|PubMed:10594042, ECO:0000269|PubMed:10722692,
CC ECO:0000269|PubMed:11250900, ECO:0000269|PubMed:11698662,
CC ECO:0000269|PubMed:11773079, ECO:0000269|PubMed:11864604,
CC ECO:0000269|PubMed:12039952, ECO:0000269|PubMed:12138096,
CC ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:12954634,
CC ECO:0000269|PubMed:14757047, ECO:0000269|PubMed:15367689,
CC ECO:0000269|PubMed:16606617, ECO:0000269|PubMed:16957778,
CC ECO:0000269|PubMed:17116691, ECO:0000269|PubMed:19786558,
CC ECO:0000269|PubMed:20047962, ECO:0000269|PubMed:25219498,
CC ECO:0000269|PubMed:28698609, ECO:0000269|PubMed:7481822,
CC ECO:0000269|PubMed:8754792, ECO:0000269|PubMed:9296499,
CC ECO:0000269|PubMed:9744270}.
CC -!- INTERACTION:
CC Q15788; P03372: ESR1; NbExp=8; IntAct=EBI-455189, EBI-78473;
CC Q15788; Q63ZY3: KANK2; NbExp=4; IntAct=EBI-455189, EBI-2556193;
CC Q15788; Q13133: NR1H3; NbExp=15; IntAct=EBI-455189, EBI-781356;
CC Q15788; Q96RI1: NR1H4; NbExp=4; IntAct=EBI-455189, EBI-1250177;
CC Q15788; Q96RI1-2: NR1H4; NbExp=5; IntAct=EBI-455189, EBI-9640524;
CC Q15788; O75469: NR1I2; NbExp=5; IntAct=EBI-455189, EBI-3905991;
CC Q15788; Q9BTK6: PAGR1; NbExp=4; IntAct=EBI-455189, EBI-2372223;
CC Q15788; P28065: PSMB9; NbExp=3; IntAct=EBI-455189, EBI-603300;
CC Q15788; P10276: RARA; NbExp=7; IntAct=EBI-455189, EBI-413374;
CC Q15788; P51449: RORC; NbExp=2; IntAct=EBI-455189, EBI-3908771;
CC Q15788; P19793: RXRA; NbExp=14; IntAct=EBI-455189, EBI-78598;
CC Q15788; Q13569: TDG; NbExp=8; IntAct=EBI-455189, EBI-348333;
CC Q15788; P14373: TRIM27; NbExp=3; IntAct=EBI-455189, EBI-719493;
CC Q15788; P11473: VDR; NbExp=3; IntAct=EBI-455189, EBI-286357;
CC Q15788; P59598: Asxl1; Xeno; NbExp=2; IntAct=EBI-455189, EBI-5743705;
CC Q15788; P19785: Esr1; Xeno; NbExp=3; IntAct=EBI-455189, EBI-346765;
CC Q15788; P25799: Nfkb1; Xeno; NbExp=2; IntAct=EBI-455189, EBI-643958;
CC Q15788; P06536: Nr3c1; Xeno; NbExp=2; IntAct=EBI-455189, EBI-1187143;
CC Q15788; P56581: Tdg; Xeno; NbExp=4; IntAct=EBI-455189, EBI-4320525;
CC Q15788-2; Q13569: TDG; NbExp=2; IntAct=EBI-5327712, EBI-348333;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=SRC-1A, SRC1a;
CC IsoId=Q15788-1; Sequence=Displayed;
CC Name=2; Synonyms=SRC-1E, SRC1e;
CC IsoId=Q15788-2; Sequence=VSP_011739;
CC Name=3; Synonyms=SRC-1 (-Q);
CC IsoId=Q15788-3; Sequence=VSP_011738;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15313887,
CC ECO:0000269|PubMed:9427757}.
CC -!- DOMAIN: The C-terminal (1107-1441) part mediates the histone
CC acetyltransferase (HAT) activity.
CC -!- DOMAIN: Contains 7 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. LXXLL motifs 3,
CC 4 and 5 are essential for the association with nuclear receptors. LXXLL
CC motif 7, which is not present in isoform 2, increases the affinity for
CC steroid receptors in vitro.
CC -!- PTM: Sumoylated; sumoylation increases its interaction with PGR and
CC prolongs its retention in the nucleus. It does not prevent its
CC ubiquitination and does not exert a clear effect on the stability of
CC the protein. {ECO:0000269|PubMed:12529333}.
CC -!- PTM: Ubiquitinated; leading to proteasome-mediated degradation.
CC Ubiquitination and sumoylation take place at different sites.
CC {ECO:0000269|PubMed:12529333}.
CC -!- DISEASE: Note=A chromosomal aberration involving NCOA1 is a cause of
CC rhabdomyosarcoma. Translocation t(2;2)(q35;p23) with PAX3 generates the
CC NCOA1-PAX3 oncogene consisting of the N-terminus part of PAX3 and the
CC C-terminus part of NCOA1. The fusion protein acts as a transcriptional
CC activator. Rhabdomyosarcoma is the most common soft tissue carcinoma in
CC childhood, representing 5-8% of all malignancies in children.
CC {ECO:0000269|PubMed:15313887}.
CC -!- MISCELLANEOUS: [Isoform 2]: Major form. Contains a domain at its C-
CC terminus (1241-1399) that is able to mediate transactivation.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA64187.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC50305.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/ncoa1/";
CC ---------------------------------------------------------------------------
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DR EMBL; U59302; AAC50631.1; -; mRNA.
DR EMBL; AJ000881; CAA04371.1; -; mRNA.
DR EMBL; AJ000882; CAA04372.1; -; mRNA.
DR EMBL; U90661; AAB50242.1; -; mRNA.
DR EMBL; EF660499; ABS29266.1; -; Genomic_DNA.
DR EMBL; AC013459; AAX93184.1; -; Genomic_DNA.
DR EMBL; AC093798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00746.1; -; Genomic_DNA.
DR EMBL; BC111533; AAI11534.1; -; mRNA.
DR EMBL; BC111534; AAI11535.1; -; mRNA.
DR EMBL; U40396; AAC50305.1; ALT_INIT; mRNA.
DR EMBL; U19179; AAA64187.1; ALT_INIT; mRNA.
DR EMBL; AY633656; AAT47737.1; -; mRNA.
DR CCDS; CCDS1712.1; -. [Q15788-1]
DR CCDS; CCDS1713.1; -. [Q15788-2]
DR CCDS; CCDS42660.1; -. [Q15788-3]
DR PIR; A57620; A57620.
DR PIR; PC4363; PC4363.
DR PIR; PC4364; PC4364.
DR RefSeq; NP_003734.3; NM_003743.4. [Q15788-1]
DR RefSeq; NP_671756.1; NM_147223.2. [Q15788-2]
DR RefSeq; NP_671766.1; NM_147233.2. [Q15788-3]
DR RefSeq; XP_005264682.1; XM_005264625.1. [Q15788-1]
DR RefSeq; XP_005264683.1; XM_005264626.1. [Q15788-3]
DR RefSeq; XP_005264685.1; XM_005264628.1.
DR RefSeq; XP_016860657.1; XM_017005168.1.
DR RefSeq; XP_016860658.1; XM_017005169.1.
DR PDB; 1FM6; X-ray; 2.10 A; B/E/V/Y=676-700.
DR PDB; 1FM9; X-ray; 2.10 A; B/E=676-700.
DR PDB; 1K4W; X-ray; 1.90 A; B=686-700.
DR PDB; 1K74; X-ray; 2.30 A; B/E=676-700.
DR PDB; 1K7L; X-ray; 2.50 A; B/D/F/H=680-700.
DR PDB; 1KV6; X-ray; 2.70 A; C/D=686-700.
DR PDB; 1N4H; X-ray; 2.10 A; B=686-700.
DR PDB; 1NQ7; X-ray; 1.50 A; B=687-696.
DR PDB; 1NRL; X-ray; 2.00 A; C/D=676-700.
DR PDB; 1P8D; X-ray; 2.80 A; C/D=676-700.
DR PDB; 1PZL; X-ray; 2.10 A; B=687-700.
DR PDB; 1RDT; X-ray; 2.40 A; B=676-700.
DR PDB; 1TFC; X-ray; 2.40 A; C/D=686-700.
DR PDB; 1U3R; X-ray; 2.21 A; C/D=630-640.
DR PDB; 1U3S; X-ray; 2.50 A; C/D=630-640.
DR PDB; 1X76; X-ray; 2.20 A; C/D=630-640.
DR PDB; 1X78; X-ray; 2.30 A; C/D=630-640.
DR PDB; 1X7B; X-ray; 2.30 A; C/D=630-640.
DR PDB; 1X7J; X-ray; 2.30 A; C/D=630-640.
DR PDB; 1XIU; X-ray; 2.50 A; E/F=686-700.
DR PDB; 1XV9; X-ray; 2.70 A; E/F/G/H=685-697.
DR PDB; 1XVP; X-ray; 2.60 A; E/F/G/H=685-697.
DR PDB; 1YY4; X-ray; 2.70 A; C/D=630-640.
DR PDB; 1YYE; X-ray; 2.03 A; C/D=630-640.
DR PDB; 1ZAF; X-ray; 2.20 A; C/D=630-640.
DR PDB; 2A3I; X-ray; 1.95 A; B=1430-1441.
DR PDB; 2C52; NMR; -; B=920-970.
DR PDB; 2FVJ; X-ray; 1.99 A; B=628-640.
DR PDB; 2GTK; X-ray; 2.10 A; B=631-640.
DR PDB; 2HBH; X-ray; 2.65 A; B=686-700.
DR PDB; 2HC4; X-ray; 2.20 A; B=686-700.
DR PDB; 2HCD; X-ray; 2.60 A; B=686-700.
DR PDB; 2HFP; X-ray; 2.00 A; B=680-700.
DR PDB; 2NPA; X-ray; 2.30 A; B/D=683-697.
DR PDB; 2NV7; X-ray; 2.10 A; C/D=631-640.
DR PDB; 2P54; X-ray; 1.79 A; B=686-696.
DR PDB; 2PRG; X-ray; 2.30 A; C=623-710.
DR PDB; 3BEJ; X-ray; 1.90 A; E/F=676-700.
DR PDB; 3BQD; X-ray; 2.50 A; B=1429-1441.
DR PDB; 3CTB; X-ray; 2.00 A; A/B=678-700.
DR PDB; 3CWD; X-ray; 2.40 A; C/D=685-700.
DR PDB; 3DCT; X-ray; 2.50 A; B=741-761.
DR PDB; 3DCU; X-ray; 2.95 A; B=741-761.
DR PDB; 3DR1; X-ray; 2.70 A; B=686-700.
DR PDB; 3ET1; X-ray; 2.50 A; P/Q=681-696.
DR PDB; 3ET3; X-ray; 1.95 A; P=680-695.
DR PDB; 3FEI; X-ray; 2.40 A; Z=744-756.
DR PDB; 3FEJ; X-ray; 2.01 A; B=628-640.
DR PDB; 3FUR; X-ray; 2.30 A; H=629-640.
DR PDB; 3FXV; X-ray; 2.26 A; B=744-756.
DR PDB; 3G8I; X-ray; 2.20 A; Z=744-756.
DR PDB; 3G9E; X-ray; 2.30 A; B=628-640.
DR PDB; 3GYT; X-ray; 2.40 A; B=1429-1441.
DR PDB; 3GYU; X-ray; 2.40 A; B=1429-1441.
DR PDB; 3H0A; X-ray; 2.10 A; B/E=629-640.
DR PDB; 3HC5; X-ray; 2.60 A; B=741-761.
DR PDB; 3HC6; X-ray; 3.20 A; B=741-761.
DR PDB; 3HVL; X-ray; 2.10 A; A/B=678-700.
DR PDB; 3IPQ; X-ray; 2.00 A; B=676-700.
DR PDB; 3IPS; X-ray; 2.26 A; C/D=676-700.
DR PDB; 3IPU; X-ray; 2.40 A; C/D=676-700.
DR PDB; 3KMR; X-ray; 1.80 A; C=686-698.
DR PDB; 3LMP; X-ray; 1.90 A; C=686-700.
DR PDB; 3OKH; X-ray; 2.50 A; B=744-757.
DR PDB; 3OKI; X-ray; 2.00 A; B/D=744-757.
DR PDB; 3OLF; X-ray; 1.90 A; B/D=744-757.
DR PDB; 3OLL; X-ray; 1.50 A; C/D=683-701.
DR PDB; 3OLS; X-ray; 2.20 A; C/D=683-701.
DR PDB; 3OMK; X-ray; 1.90 A; B/D=744-757.
DR PDB; 3OMM; X-ray; 2.10 A; B/D=744-757.
DR PDB; 3OMO; X-ray; 2.21 A; C/D=683-701.
DR PDB; 3OMP; X-ray; 2.05 A; C/D=683-701.
DR PDB; 3OMQ; X-ray; 1.97 A; C/D=683-701.
DR PDB; 3OOF; X-ray; 2.29 A; B/D=744-757.
DR PDB; 3OOK; X-ray; 2.29 A; B/D=744-757.
DR PDB; 3P88; X-ray; 2.95 A; B=745-755.
DR PDB; 3P89; X-ray; 2.30 A; B=745-755.
DR PDB; 3QT0; X-ray; 2.50 A; C=685-700.
DR PDB; 3RUT; X-ray; 3.00 A; B=745-755.
DR PDB; 3RUU; X-ray; 2.50 A; B=745-755.
DR PDB; 3RVF; X-ray; 3.10 A; B=741-761.
DR PDB; 3S9S; X-ray; 2.55 A; B=685-697.
DR PDB; 3T03; X-ray; 2.10 A; C/D=683-700.
DR PDB; 3UU7; X-ray; 2.20 A; F/G=686-698.
DR PDB; 3UUA; X-ray; 2.05 A; F/G=686-698.
DR PDB; 3UUD; X-ray; 1.60 A; C/D=686-698.
DR PDB; 3V9Y; X-ray; 2.10 A; B=686-700.
DR PDB; 3VN2; X-ray; 2.18 A; C=685-700.
DR PDB; 4DK7; X-ray; 2.45 A; B/D=745-756.
DR PDB; 4DK8; X-ray; 2.75 A; B/D=745-756.
DR PDB; 4DM6; X-ray; 1.90 A; E/F=676-700.
DR PDB; 4DM8; X-ray; 2.30 A; C/D=676-700.
DR PDB; 4DQM; X-ray; 2.75 A; B/D=1432-1441.
DR PDB; 4F9M; X-ray; 1.90 A; C=686-700.
DR PDB; 4FGY; X-ray; 2.84 A; B=686-696.
DR PDB; 4G1D; X-ray; 2.90 A; B=686-700.
DR PDB; 4G1Y; X-ray; 2.85 A; B=686-700.
DR PDB; 4G1Z; X-ray; 2.50 A; B=686-700.
DR PDB; 4G20; X-ray; 2.90 A; B=686-700.
DR PDB; 4G21; X-ray; 2.90 A; B=686-700.
DR PDB; 4G2H; X-ray; 2.50 A; B=686-700.
DR PDB; 4HEE; X-ray; 2.50 A; Y=676-700.
DR PDB; 4J5X; X-ray; 2.80 A; A/B/C/D=678-700.
DR PDB; 4JYG; X-ray; 2.35 A; F/G=686-698.
DR PDB; 4JYH; X-ray; 2.60 A; C/G=686-698.
DR PDB; 4JYI; X-ray; 1.90 A; F/G=686-698.
DR PDB; 4MG5; X-ray; 2.05 A; C/D=686-698.
DR PDB; 4MG6; X-ray; 2.10 A; C/D=686-698.
DR PDB; 4MG7; X-ray; 2.15 A; C/D=686-698.
DR PDB; 4MG8; X-ray; 1.85 A; C/D=686-698.
DR PDB; 4MG9; X-ray; 2.00 A; F/G=686-698.
DR PDB; 4MGA; X-ray; 1.80 A; C/D=686-698.
DR PDB; 4MGB; X-ray; 1.85 A; C/D=686-698.
DR PDB; 4MGC; X-ray; 2.15 A; F/G=686-698.
DR PDB; 4MGD; X-ray; 1.90 A; F/G=686-698.
DR PDB; 4RUJ; X-ray; 2.35 A; B=686-700.
DR PDB; 4RUP; X-ray; 2.75 A; B=686-700.
DR PDB; 4TUZ; X-ray; 1.90 A; F/G=686-698.
DR PDB; 4TV1; X-ray; 1.85 A; C/D=686-698.
DR PDB; 4UDA; X-ray; 2.03 A; B=1427-1441.
DR PDB; 4UDB; X-ray; 2.36 A; B=1427-1441.
DR PDB; 4Y29; X-ray; 1.98 A; B=1432-1441.
DR PDB; 5A86; X-ray; 2.25 A; C/D=682-698.
DR PDB; 5AVI; X-ray; 2.70 A; B/D=676-700.
DR PDB; 5AVL; X-ray; 2.80 A; B=676-700.
DR PDB; 5AZT; X-ray; 3.45 A; C=683-697.
DR PDB; 5DSH; X-ray; 2.95 A; B=685-700.
DR PDB; 5DV3; X-ray; 2.75 A; B=685-700.
DR PDB; 5DV6; X-ray; 2.80 A; B=685-700.
DR PDB; 5DV8; X-ray; 2.75 A; B=685-700.
DR PDB; 5DVC; X-ray; 2.30 A; B=685-700.
DR PDB; 5DWL; X-ray; 2.20 A; B=685-700.
DR PDB; 5E7V; X-ray; 2.40 A; B=686-700.
DR PDB; 5GTN; X-ray; 1.85 A; B=685-700.
DR PDB; 5GTO; X-ray; 2.10 A; B=685-700.
DR PDB; 5GTP; X-ray; 2.35 A; B=685-700.
DR PDB; 5HJS; X-ray; 1.72 A; C/D=676-700.
DR PDB; 5JI0; X-ray; 1.98 A; E/F=676-700.
DR PDB; 5JMM; X-ray; 2.10 A; F/G=686-698.
DR PDB; 5L7E; X-ray; 1.86 A; B=1432-1441.
DR PDB; 5L7G; X-ray; 2.01 A; B=1432-1441.
DR PDB; 5L7H; X-ray; 1.84 A; B=1432-1441.
DR PDB; 5MWP; X-ray; 1.82 A; B=1427-1441.
DR PDB; 5MWY; X-ray; 1.75 A; B=1427-1441.
DR PDB; 5MX7; X-ray; 1.98 A; B1=686-700.
DR PDB; 5NKY; X-ray; 2.10 A; B=686-700.
DR PDB; 5NMA; X-ray; 2.80 A; B=686-700.
DR PDB; 5NMB; X-ray; 2.50 A; B2=686-700.
DR PDB; 5NWM; NMR; -; A=257-385.
DR PDB; 5OW7; X-ray; 2.10 A; B=686-700.
DR PDB; 5OW9; X-ray; 2.40 A; B=686-700.
DR PDB; 5OWD; X-ray; 2.15 A; B=686-700.
DR PDB; 5Q0J; X-ray; 2.00 A; B/D=744-757.
DR PDB; 5Q0K; X-ray; 1.80 A; B=744-757.
DR PDB; 5Q0L; X-ray; 2.50 A; B/D=744-757.
DR PDB; 5Q0M; X-ray; 2.20 A; B=744-757.
DR PDB; 5Q0N; X-ray; 2.40 A; B/D=744-757.
DR PDB; 5Q0O; X-ray; 1.90 A; B/D=744-757.
DR PDB; 5Q0P; X-ray; 1.80 A; B/D=744-757.
DR PDB; 5Q0Q; X-ray; 2.60 A; B/D=744-757.
DR PDB; 5Q0R; X-ray; 1.91 A; B=744-757.
DR PDB; 5Q0S; X-ray; 2.50 A; B/D=744-757.
DR PDB; 5Q0T; X-ray; 2.14 A; B=744-757.
DR PDB; 5Q0U; X-ray; 1.90 A; B/D=744-757.
DR PDB; 5Q0V; X-ray; 1.87 A; B/D=744-757.
DR PDB; 5Q0W; X-ray; 1.90 A; B=744-757.
DR PDB; 5Q0X; X-ray; 2.26 A; B=744-757.
DR PDB; 5Q0Y; X-ray; 2.20 A; B/D=744-757.
DR PDB; 5Q0Z; X-ray; 2.26 A; B/D=744-757.
DR PDB; 5Q10; X-ray; 2.20 A; B=744-757.
DR PDB; 5Q11; X-ray; 2.20 A; B=744-757.
DR PDB; 5Q12; X-ray; 2.00 A; B=744-757.
DR PDB; 5Q13; X-ray; 1.90 A; B/D=744-757.
DR PDB; 5Q14; X-ray; 1.85 A; B/D=744-757.
DR PDB; 5Q15; X-ray; 1.90 A; B/D=744-757.
DR PDB; 5Q16; X-ray; 2.00 A; B/D=744-757.
DR PDB; 5Q18; X-ray; 1.90 A; B/D=744-757.
DR PDB; 5Q19; X-ray; 1.98 A; B/D=744-757.
DR PDB; 5Q1A; X-ray; 2.00 A; B/D=744-757.
DR PDB; 5Q1B; X-ray; 2.30 A; B/D=744-757.
DR PDB; 5Q1C; X-ray; 2.30 A; B/D=744-757.
DR PDB; 5Q1D; X-ray; 1.89 A; B/D=744-757.
DR PDB; 5Q1E; X-ray; 1.85 A; B=744-757.
DR PDB; 5Q1F; X-ray; 2.30 A; B/D=744-757.
DR PDB; 5Q1G; X-ray; 2.00 A; B=744-757.
DR PDB; 5Q1H; X-ray; 2.20 A; B/D/F/H=744-757.
DR PDB; 5Q1I; X-ray; 1.95 A; B=744-757.
DR PDB; 5X0R; X-ray; 2.67 A; C/D=676-700.
DR PDB; 5X8U; X-ray; 2.00 A; B=686-700.
DR PDB; 5X8W; X-ray; 2.30 A; B=686-700.
DR PDB; 5Y44; X-ray; 2.35 A; B=745-755.
DR PDB; 5YCN; X-ray; 2.15 A; B=685-700.
DR PDB; 5YCP; X-ray; 2.00 A; B=685-700.
DR PDB; 5YP6; X-ray; 2.20 A; B=688-695.
DR PDB; 6A5W; X-ray; 2.88 A; B/D=745-756.
DR PDB; 6A5X; X-ray; 2.60 A; B=745-755.
DR PDB; 6A5Y; X-ray; 2.10 A; B/F=685-700.
DR PDB; 6A5Z; X-ray; 2.95 A; E/F/G/I=685-700.
DR PDB; 6A60; X-ray; 3.05 A; B/F=685-700.
DR PDB; 6BNS; X-ray; 2.56 A; A/B=678-710.
DR PDB; 6E3G; X-ray; 2.10 A; C/D=688-695.
DR PDB; 6FO7; X-ray; 2.59 A; B=686-700.
DR PDB; 6FO8; X-ray; 2.30 A; B=686-700.
DR PDB; 6FO9; X-ray; 2.70 A; B=686-700.
DR PDB; 6FOB; X-ray; 2.75 A; B=686-700.
DR PDB; 6FOD; X-ray; 2.50 A; B=686-700.
DR PDB; 6GEV; X-ray; 1.54 A; B=1427-1441.
DR PDB; 6GG8; X-ray; 1.80 A; B=1427-1441.
DR PDB; 6HTY; X-ray; 2.22 A; A/B=678-700.
DR PDB; 6ICJ; X-ray; 2.48 A; B=676-700.
DR PDB; 6IJR; X-ray; 2.85 A; B/D=685-700.
DR PDB; 6IJS; X-ray; 2.15 A; B=685-700.
DR PDB; 6ILQ; X-ray; 2.41 A; B=676-700.
DR PDB; 6ITM; X-ray; 2.50 A; B/D=744-757.
DR PDB; 6JNR; X-ray; 2.30 A; C/D=687-698.
DR PDB; 6JQ7; X-ray; 2.55 A; B=685-700.
DR PDB; 6KTM; X-ray; 2.70 A; B=685-700.
DR PDB; 6KTN; X-ray; 2.75 A; B=685-700.
DR PDB; 6L6K; X-ray; 1.80 A; B=687-698.
DR PDB; 6L96; X-ray; 3.20 A; C=686-698.
DR PDB; 6NX1; X-ray; 2.27 A; A/B=678-710.
DR PDB; 6P9F; X-ray; 2.80 A; A/B=683-696.
DR PDB; 6SSQ; X-ray; 2.30 A; F/G=686-698.
DR PDB; 6T2M; X-ray; 3.00 A; B=686-700.
DR PDB; 6TFI; X-ray; 1.85 A; A/B=681-700.
DR PDB; 6U25; X-ray; 2.61 A; A=683-696.
DR PDB; 6W9H; X-ray; 2.00 A; A=683-696.
DR PDB; 6W9I; X-ray; 1.61 A; A=683-696.
DR PDB; 6XP9; X-ray; 2.27 A; A/B=678-710.
DR PDB; 7AOS; X-ray; 2.55 A; C/D=686-712.
DR PDB; 7B39; X-ray; 2.13 A; B=686-700.
DR PDB; 7BNS; X-ray; 2.70 A; B2=686-700.
DR PDB; 7BNU; X-ray; 2.40 A; B2=686-700.
DR PDB; 7BO6; X-ray; 2.86 A; B=686-700.
DR PDB; 7BPY; X-ray; 2.09 A; B/D=683-697.
DR PDB; 7BPZ; X-ray; 2.43 A; B/D=683-697.
DR PDB; 7BQ0; X-ray; 1.77 A; B/D=683-697.
DR PDB; 7BQ1; X-ray; 1.52 A; B=683-697.
DR PDB; 7BQ2; X-ray; 1.52 A; B=683-697.
DR PDB; 7BQ3; X-ray; 1.98 A; B=683-697.
DR PDB; 7BQ4; X-ray; 1.62 A; B=683-697.
DR PDB; 7C6Q; X-ray; 2.76 A; B=682-699.
DR PDB; 7CHG; X-ray; 1.93 A; A/B=676-700.
DR PDB; 7CXF; X-ray; 2.35 A; B=685-700.
DR PDB; 7CXH; X-ray; 2.30 A; B=685-700.
DR PDB; 7CXI; X-ray; 2.30 A; B=685-700.
DR PDB; 7CXJ; X-ray; 2.65 A; B=685-700.
DR PDB; 7CXK; X-ray; 2.20 A; B=685-700.
DR PDB; 7CXL; X-ray; 2.70 A; B=685-700.
DR PDB; 7JYM; X-ray; 3.05 A; A=683-696.
DR PDB; 7KXD; X-ray; 1.62 A; A=683-696.
DR PDB; 7KXE; X-ray; 2.42 A; A=683-696.
DR PDB; 7KXF; X-ray; 2.14 A; A=683-696.
DR PDB; 7OXZ; X-ray; 2.20 A; B=686-700.
DR PDB; 7OY4; X-ray; 2.00 A; B=686-700.
DR PDBsum; 1FM6; -.
DR PDBsum; 1FM9; -.
DR PDBsum; 1K4W; -.
DR PDBsum; 1K74; -.
DR PDBsum; 1K7L; -.
DR PDBsum; 1KV6; -.
DR PDBsum; 1N4H; -.
DR PDBsum; 1NQ7; -.
DR PDBsum; 1NRL; -.
DR PDBsum; 1P8D; -.
DR PDBsum; 1PZL; -.
DR PDBsum; 1RDT; -.
DR PDBsum; 1TFC; -.
DR PDBsum; 1U3R; -.
DR PDBsum; 1U3S; -.
DR PDBsum; 1X76; -.
DR PDBsum; 1X78; -.
DR PDBsum; 1X7B; -.
DR PDBsum; 1X7J; -.
DR PDBsum; 1XIU; -.
DR PDBsum; 1XV9; -.
DR PDBsum; 1XVP; -.
DR PDBsum; 1YY4; -.
DR PDBsum; 1YYE; -.
DR PDBsum; 1ZAF; -.
DR PDBsum; 2A3I; -.
DR PDBsum; 2C52; -.
DR PDBsum; 2FVJ; -.
DR PDBsum; 2GTK; -.
DR PDBsum; 2HBH; -.
DR PDBsum; 2HC4; -.
DR PDBsum; 2HCD; -.
DR PDBsum; 2HFP; -.
DR PDBsum; 2NPA; -.
DR PDBsum; 2NV7; -.
DR PDBsum; 2P54; -.
DR PDBsum; 2PRG; -.
DR PDBsum; 3BEJ; -.
DR PDBsum; 3BQD; -.
DR PDBsum; 3CTB; -.
DR PDBsum; 3CWD; -.
DR PDBsum; 3DCT; -.
DR PDBsum; 3DCU; -.
DR PDBsum; 3DR1; -.
DR PDBsum; 3ET1; -.
DR PDBsum; 3ET3; -.
DR PDBsum; 3FEI; -.
DR PDBsum; 3FEJ; -.
DR PDBsum; 3FUR; -.
DR PDBsum; 3FXV; -.
DR PDBsum; 3G8I; -.
DR PDBsum; 3G9E; -.
DR PDBsum; 3GYT; -.
DR PDBsum; 3GYU; -.
DR PDBsum; 3H0A; -.
DR PDBsum; 3HC5; -.
DR PDBsum; 3HC6; -.
DR PDBsum; 3HVL; -.
DR PDBsum; 3IPQ; -.
DR PDBsum; 3IPS; -.
DR PDBsum; 3IPU; -.
DR PDBsum; 3KMR; -.
DR PDBsum; 3LMP; -.
DR PDBsum; 3OKH; -.
DR PDBsum; 3OKI; -.
DR PDBsum; 3OLF; -.
DR PDBsum; 3OLL; -.
DR PDBsum; 3OLS; -.
DR PDBsum; 3OMK; -.
DR PDBsum; 3OMM; -.
DR PDBsum; 3OMO; -.
DR PDBsum; 3OMP; -.
DR PDBsum; 3OMQ; -.
DR PDBsum; 3OOF; -.
DR PDBsum; 3OOK; -.
DR PDBsum; 3P88; -.
DR PDBsum; 3P89; -.
DR PDBsum; 3QT0; -.
DR PDBsum; 3RUT; -.
DR PDBsum; 3RUU; -.
DR PDBsum; 3RVF; -.
DR PDBsum; 3S9S; -.
DR PDBsum; 3T03; -.
DR PDBsum; 3UU7; -.
DR PDBsum; 3UUA; -.
DR PDBsum; 3UUD; -.
DR PDBsum; 3V9Y; -.
DR PDBsum; 3VN2; -.
DR PDBsum; 4DK7; -.
DR PDBsum; 4DK8; -.
DR PDBsum; 4DM6; -.
DR PDBsum; 4DM8; -.
DR PDBsum; 4DQM; -.
DR PDBsum; 4F9M; -.
DR PDBsum; 4FGY; -.
DR PDBsum; 4G1D; -.
DR PDBsum; 4G1Y; -.
DR PDBsum; 4G1Z; -.
DR PDBsum; 4G20; -.
DR PDBsum; 4G21; -.
DR PDBsum; 4G2H; -.
DR PDBsum; 4HEE; -.
DR PDBsum; 4J5X; -.
DR PDBsum; 4JYG; -.
DR PDBsum; 4JYH; -.
DR PDBsum; 4JYI; -.
DR PDBsum; 4MG5; -.
DR PDBsum; 4MG6; -.
DR PDBsum; 4MG7; -.
DR PDBsum; 4MG8; -.
DR PDBsum; 4MG9; -.
DR PDBsum; 4MGA; -.
DR PDBsum; 4MGB; -.
DR PDBsum; 4MGC; -.
DR PDBsum; 4MGD; -.
DR PDBsum; 4RUJ; -.
DR PDBsum; 4RUP; -.
DR PDBsum; 4TUZ; -.
DR PDBsum; 4TV1; -.
DR PDBsum; 4UDA; -.
DR PDBsum; 4UDB; -.
DR PDBsum; 4Y29; -.
DR PDBsum; 5A86; -.
DR PDBsum; 5AVI; -.
DR PDBsum; 5AVL; -.
DR PDBsum; 5AZT; -.
DR PDBsum; 5DSH; -.
DR PDBsum; 5DV3; -.
DR PDBsum; 5DV6; -.
DR PDBsum; 5DV8; -.
DR PDBsum; 5DVC; -.
DR PDBsum; 5DWL; -.
DR PDBsum; 5E7V; -.
DR PDBsum; 5GTN; -.
DR PDBsum; 5GTO; -.
DR PDBsum; 5GTP; -.
DR PDBsum; 5HJS; -.
DR PDBsum; 5JI0; -.
DR PDBsum; 5JMM; -.
DR PDBsum; 5L7E; -.
DR PDBsum; 5L7G; -.
DR PDBsum; 5L7H; -.
DR PDBsum; 5MWP; -.
DR PDBsum; 5MWY; -.
DR PDBsum; 5MX7; -.
DR PDBsum; 5NKY; -.
DR PDBsum; 5NMA; -.
DR PDBsum; 5NMB; -.
DR PDBsum; 5NWM; -.
DR PDBsum; 5OW7; -.
DR PDBsum; 5OW9; -.
DR PDBsum; 5OWD; -.
DR PDBsum; 5Q0J; -.
DR PDBsum; 5Q0K; -.
DR PDBsum; 5Q0L; -.
DR PDBsum; 5Q0M; -.
DR PDBsum; 5Q0N; -.
DR PDBsum; 5Q0O; -.
DR PDBsum; 5Q0P; -.
DR PDBsum; 5Q0Q; -.
DR PDBsum; 5Q0R; -.
DR PDBsum; 5Q0S; -.
DR PDBsum; 5Q0T; -.
DR PDBsum; 5Q0U; -.
DR PDBsum; 5Q0V; -.
DR PDBsum; 5Q0W; -.
DR PDBsum; 5Q0X; -.
DR PDBsum; 5Q0Y; -.
DR PDBsum; 5Q0Z; -.
DR PDBsum; 5Q10; -.
DR PDBsum; 5Q11; -.
DR PDBsum; 5Q12; -.
DR PDBsum; 5Q13; -.
DR PDBsum; 5Q14; -.
DR PDBsum; 5Q15; -.
DR PDBsum; 5Q16; -.
DR PDBsum; 5Q18; -.
DR PDBsum; 5Q19; -.
DR PDBsum; 5Q1A; -.
DR PDBsum; 5Q1B; -.
DR PDBsum; 5Q1C; -.
DR PDBsum; 5Q1D; -.
DR PDBsum; 5Q1E; -.
DR PDBsum; 5Q1F; -.
DR PDBsum; 5Q1G; -.
DR PDBsum; 5Q1H; -.
DR PDBsum; 5Q1I; -.
DR PDBsum; 5X0R; -.
DR PDBsum; 5X8U; -.
DR PDBsum; 5X8W; -.
DR PDBsum; 5Y44; -.
DR PDBsum; 5YCN; -.
DR PDBsum; 5YCP; -.
DR PDBsum; 5YP6; -.
DR PDBsum; 6A5W; -.
DR PDBsum; 6A5X; -.
DR PDBsum; 6A5Y; -.
DR PDBsum; 6A5Z; -.
DR PDBsum; 6A60; -.
DR PDBsum; 6BNS; -.
DR PDBsum; 6E3G; -.
DR PDBsum; 6FO7; -.
DR PDBsum; 6FO8; -.
DR PDBsum; 6FO9; -.
DR PDBsum; 6FOB; -.
DR PDBsum; 6FOD; -.
DR PDBsum; 6GEV; -.
DR PDBsum; 6GG8; -.
DR PDBsum; 6HTY; -.
DR PDBsum; 6ICJ; -.
DR PDBsum; 6IJR; -.
DR PDBsum; 6IJS; -.
DR PDBsum; 6ILQ; -.
DR PDBsum; 6ITM; -.
DR PDBsum; 6JNR; -.
DR PDBsum; 6JQ7; -.
DR PDBsum; 6KTM; -.
DR PDBsum; 6KTN; -.
DR PDBsum; 6L6K; -.
DR PDBsum; 6L96; -.
DR PDBsum; 6NX1; -.
DR PDBsum; 6P9F; -.
DR PDBsum; 6SSQ; -.
DR PDBsum; 6T2M; -.
DR PDBsum; 6TFI; -.
DR PDBsum; 6U25; -.
DR PDBsum; 6W9H; -.
DR PDBsum; 6W9I; -.
DR PDBsum; 6XP9; -.
DR PDBsum; 7AOS; -.
DR PDBsum; 7B39; -.
DR PDBsum; 7BNS; -.
DR PDBsum; 7BNU; -.
DR PDBsum; 7BO6; -.
DR PDBsum; 7BPY; -.
DR PDBsum; 7BPZ; -.
DR PDBsum; 7BQ0; -.
DR PDBsum; 7BQ1; -.
DR PDBsum; 7BQ2; -.
DR PDBsum; 7BQ3; -.
DR PDBsum; 7BQ4; -.
DR PDBsum; 7C6Q; -.
DR PDBsum; 7CHG; -.
DR PDBsum; 7CXF; -.
DR PDBsum; 7CXH; -.
DR PDBsum; 7CXI; -.
DR PDBsum; 7CXJ; -.
DR PDBsum; 7CXK; -.
DR PDBsum; 7CXL; -.
DR PDBsum; 7JYM; -.
DR PDBsum; 7KXD; -.
DR PDBsum; 7KXE; -.
DR PDBsum; 7KXF; -.
DR PDBsum; 7OXZ; -.
DR PDBsum; 7OY4; -.
DR AlphaFoldDB; Q15788; -.
DR SMR; Q15788; -.
DR BioGRID; 114200; 128.
DR ComplexPortal; CPX-517; PXR-NCOA1 activated nuclear receptor complex.
DR ComplexPortal; CPX-525; RARalpha-NCOA1 activated retinoic acid receptor complex.
DR ComplexPortal; CPX-5342; RXRalpha-NCOA1 activated retinoic acid receptor complex.
DR ComplexPortal; CPX-711; PPARgamma-NCOA1 activated nuclear receptor complex.
DR CORUM; Q15788; -.
DR DIP; DIP-30877N; -.
DR IntAct; Q15788; 51.
DR MINT; Q15788; -.
DR STRING; 9606.ENSP00000385216; -.
DR BindingDB; Q15788; -.
DR ChEMBL; CHEMBL1615387; -.
DR DrugBank; DB07530; (1R,3R)-5-[(2E)-3-{(1S,3R)-2,2,3-trimethyl-3-[6,6,6-trifluoro-5-hydroxy-5-(trifluoromethyl)hex-3-yn-1-yl]cyclopentyl}prop-2-en-1-ylidene]cyclohexane-1,3-diol.
DR DrugBank; DB06908; (2S)-3-(1-{[2-(2-CHLOROPHENYL)-5-METHYL-1,3-OXAZOL-4-YL]METHYL}-1H-INDOL-5-YL)-2-ETHOXYPROPANOIC ACID.
DR DrugBank; DB08220; (8alpha,10alpha,13alpha,17beta)-17-[(4-hydroxyphenyl)carbonyl]androsta-3,5-diene-3-carboxylic acid.
DR DrugBank; DB08742; 1,3-CYCLOHEXANEDIOL, 4-METHYLENE-5-[(2E)-[(1S,3AS,7AS)-OCTAHYDRO-1-(5-HYDROXY-5-METHYL-1,3-HEXADIYNYL)-7A-METHYL-4H-INDEN-4-YLIDENE]ETHYLIDENE]-, (1R,3S,5Z).
DR DrugBank; DB07119; 1-CHLORO-6-(4-HYDROXYPHENYL)-2-NAPHTHOL.
DR DrugBank; DB07009; 2-(5-HYDROXY-NAPHTHALEN-1-YL)-1,3-BENZOOXAZOL-6-OL.
DR DrugBank; DB07557; 3,20-Pregnanedione.
DR DrugBank; DB07236; 3-(6-HYDROXY-NAPHTHALEN-2-YL)-BENZO[D]ISOOXAZOL-6-OL.
DR DrugBank; DB07230; 3-BROMO-6-HYDROXY-2-(4-HYDROXYPHENYL)-1H-INDEN-1-ONE.
DR DrugBank; DB07150; 4-(4-HYDROXYPHENYL)-1-NAPHTHALDEHYDE OXIME.
DR DrugBank; DB07198; 5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-CARBONITRILE.
DR DrugBank; DB06927; [5-HYDROXY-2-(4-HYDROXYPHENYL)-1-BENZOFURAN-7-YL]ACETONITRILE.
DR DrugBank; DB08915; Aleglitazar.
DR DrugBank; DB04652; Corticosterone.
DR DrugBank; DB06875; ERB-196.
DR DrugBank; DB01645; Genistein.
DR DrugBank; DB07215; GW-590735.
DR DrugBank; DB07724; Indeglitazar.
DR DrugBank; DB08231; Myristic acid.
DR DrugBank; DB06832; Prinaberel.
DR DrugBank; DB07080; TO-901317.
DR GuidetoPHARMACOLOGY; 2693; -.
DR GlyGen; Q15788; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; Q15788; -.
DR PhosphoSitePlus; Q15788; -.
DR BioMuta; NCOA1; -.
DR DMDM; 158518533; -.
DR CPTAC; CPTAC-1255; -.
DR EPD; Q15788; -.
DR jPOST; Q15788; -.
DR MassIVE; Q15788; -.
DR MaxQB; Q15788; -.
DR PaxDb; Q15788; -.
DR PeptideAtlas; Q15788; -.
DR PRIDE; Q15788; -.
DR ProteomicsDB; 60761; -. [Q15788-1]
DR ProteomicsDB; 60762; -. [Q15788-2]
DR ProteomicsDB; 60763; -. [Q15788-3]
DR Antibodypedia; 27525; 433 antibodies from 40 providers.
DR DNASU; 8648; -.
DR Ensembl; ENST00000288599.9; ENSP00000288599.5; ENSG00000084676.16. [Q15788-2]
DR Ensembl; ENST00000348332.8; ENSP00000320940.5; ENSG00000084676.16. [Q15788-1]
DR Ensembl; ENST00000395856.3; ENSP00000379197.3; ENSG00000084676.16. [Q15788-3]
DR Ensembl; ENST00000405141.5; ENSP00000385097.1; ENSG00000084676.16. [Q15788-2]
DR Ensembl; ENST00000406961.5; ENSP00000385216.1; ENSG00000084676.16. [Q15788-1]
DR GeneID; 8648; -.
DR KEGG; hsa:8648; -.
DR MANE-Select; ENST00000348332.8; ENSP00000320940.5; NM_003743.5; NP_003734.3.
DR UCSC; uc002rfj.4; human. [Q15788-1]
DR CTD; 8648; -.
DR DisGeNET; 8648; -.
DR GeneCards; NCOA1; -.
DR HGNC; HGNC:7668; NCOA1.
DR HPA; ENSG00000084676; Low tissue specificity.
DR MIM; 602691; gene.
DR neXtProt; NX_Q15788; -.
DR OpenTargets; ENSG00000084676; -.
DR PharmGKB; PA31470; -.
DR VEuPathDB; HostDB:ENSG00000084676; -.
DR eggNOG; KOG3561; Eukaryota.
DR GeneTree; ENSGT00950000183021; -.
DR HOGENOM; CLU_001988_0_0_1; -.
DR InParanoid; Q15788; -.
DR OMA; GVQGQFN; -.
DR OrthoDB; 59971at2759; -.
DR PhylomeDB; Q15788; -.
DR TreeFam; TF332652; -.
DR BRENDA; 2.3.1.48; 2681.
DR PathwayCommons; Q15788; -.
DR Reactome; R-HSA-1368082; RORA activates gene expression.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR Reactome; R-HSA-159418; Recycling of bile acids and salts.
DR Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
DR Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-211976; Endogenous sterols.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-HSA-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; Q15788; -.
DR SIGNOR; Q15788; -.
DR BioGRID-ORCS; 8648; 17 hits in 1095 CRISPR screens.
DR ChiTaRS; NCOA1; human.
DR EvolutionaryTrace; Q15788; -.
DR GeneWiki; Nuclear_receptor_coactivator_1; -.
DR GenomeRNAi; 8648; -.
DR Pharos; Q15788; Tchem.
DR PRO; PR:Q15788; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q15788; protein.
DR Bgee; ENSG00000084676; Expressed in middle temporal gyrus and 214 other tissues.
DR ExpressionAtlas; Q15788; baseline and differential.
DR Genevisible; Q15788; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:ComplexPortal.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:CAFA.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0016922; F:nuclear receptor binding; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IEA:Ensembl.
DR GO; GO:0043967; P:histone H4 acetylation; IEA:Ensembl.
DR GO; GO:0060713; P:labyrinthine layer morphogenesis; IEA:Ensembl.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1904179; P:positive regulation of adipose tissue development; IC:ComplexPortal.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IC:ComplexPortal.
DR GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; IEA:Ensembl.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 4.10.280.10; -; 1.
DR Gene3D; 6.10.140.410; -; 1.
DR IDEAL; IID00083; -.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR010011; NCO_DUF1518.
DR InterPro; IPR028819; NCOA1.
DR InterPro; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ.
DR InterPro; IPR037077; Nuc_rcpt_coact_Ncoa_int_sf.
DR InterPro; IPR017426; Nuclear_rcpt_coactivator.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR014935; SRC/p160_LXXLL.
DR PANTHER; PTHR10684; PTHR10684; 1.
DR PANTHER; PTHR10684:SF1; PTHR10684:SF1; 1.
DR Pfam; PF07469; DUF1518; 2.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF08815; Nuc_rec_co-act; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08832; SRC-1; 1.
DR PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1.
DR SMART; SM01151; DUF1518; 2.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF69125; SSF69125; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Acyltransferase;
KW Alternative splicing; Chromosomal rearrangement; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1441
FT /note="Nuclear receptor coactivator 1"
FT /id="PRO_0000094400"
FT DOMAIN 23..80
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 109..180
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..567
FT /note="Interaction with STAT3"
FT /evidence="ECO:0000269|PubMed:11773079"
FT REGION 368..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..988
FT /note="Interaction with CREBBP"
FT REGION 1143..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1409..1441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 46..50
FT /note="LXXLL motif 1"
FT MOTIF 112..116
FT /note="LXXLL motif 2"
FT MOTIF 633..637
FT /note="LXXLL motif 3"
FT MOTIF 690..694
FT /note="LXXLL motif 4"
FT MOTIF 749..753
FT /note="LXXLL motif 5"
FT MOTIF 913..917
FT /note="LXXLL motif 6"
FT MOTIF 1435..1439
FT /note="LXXLL motif 7"
FT COMPBIAS 373..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1177
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 867..868
FT /note="Breakpoint for translocation to form PAX3-NCOA1
FT oncogene"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10660621,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10660621,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10660621"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70365"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10660621"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10660621"
FT MOD_RES 1073
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P70365"
FT MOD_RES 1091
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P70365"
FT MOD_RES 1124
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P70365"
FT MOD_RES 1131
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P70365"
FT MOD_RES 1179
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10660621"
FT MOD_RES 1185
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10660621"
FT MOD_RES 1372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 732
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:12529333"
FT CROSSLNK 774
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:12529333"
FT CROSSLNK 846
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1385
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8754792"
FT /id="VSP_011738"
FT VAR_SEQ 1386..1441
FT /note="QVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQ
FT LLTE -> DKKTEEFFSVVTTD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11831720,
FT ECO:0000303|PubMed:15313887, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9427757"
FT /id="VSP_011739"
FT VARIANT 457
FT /note="Q -> K (in dbSNP:rs1049015)"
FT /evidence="ECO:0000269|PubMed:7481822,
FT ECO:0000269|PubMed:8754792, ECO:0000269|PubMed:9575154"
FT /id="VAR_019768"
FT VARIANT 466
FT /note="N -> K (in dbSNP:rs1049016)"
FT /evidence="ECO:0000269|PubMed:7481822,
FT ECO:0000269|PubMed:8754792, ECO:0000269|PubMed:9575154"
FT /id="VAR_019769"
FT VARIANT 474
FT /note="S -> P (in dbSNP:rs1049018)"
FT /evidence="ECO:0000269|PubMed:7481822,
FT ECO:0000269|PubMed:8754792, ECO:0000269|PubMed:9575154"
FT /id="VAR_019770"
FT VARIANT 591
FT /note="I -> T (in dbSNP:rs1049020)"
FT /evidence="ECO:0000269|PubMed:7481822,
FT ECO:0000269|PubMed:8754792, ECO:0000269|PubMed:9575154"
FT /id="VAR_019771"
FT VARIANT 685
FT /note="E -> A (in dbSNP:rs1049021)"
FT /evidence="ECO:0000269|PubMed:7481822,
FT ECO:0000269|PubMed:8754792, ECO:0000269|PubMed:9575154"
FT /id="VAR_019772"
FT VARIANT 794
FT /note="P -> A (in dbSNP:rs1049025)"
FT /evidence="ECO:0000269|PubMed:7481822"
FT /id="VAR_019773"
FT VARIANT 999
FT /note="S -> F (in dbSNP:rs1049032)"
FT /evidence="ECO:0000269|PubMed:7481822,
FT ECO:0000269|PubMed:8754792, ECO:0000269|PubMed:9575154"
FT /id="VAR_019774"
FT VARIANT 1154
FT /note="M -> T (in dbSNP:rs1049038)"
FT /evidence="ECO:0000269|PubMed:7481822,
FT ECO:0000269|PubMed:8754792, ECO:0000269|PubMed:9575154"
FT /id="VAR_019775"
FT VARIANT 1238
FT /note="V -> I (in dbSNP:rs56099330)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_038832"
FT VARIANT 1272
FT /note="P -> S (in dbSNP:rs1804645)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_034882"
FT MUTAGEN 636..637
FT /note="LL->AA: Slightly affects interactions with steroid
FT receptors. Abolishes interactions with steroid receptors;
FT when associated with A-693; A-694; A-752 and A-753."
FT /evidence="ECO:0000269|PubMed:9427757"
FT MUTAGEN 693..694
FT /note="LL->AA: Slightly affects interactions with steroid
FT receptors. Abolishes interactions with steroid receptors;
FT when associated with A-636; A-637; A-752 and A-753."
FT /evidence="ECO:0000269|PubMed:9427757"
FT MUTAGEN 732
FT /note="K->R: Abolishes sumoylation; when associated with R-
FT 774."
FT /evidence="ECO:0000269|PubMed:12529333"
FT MUTAGEN 752..753
FT /note="LL->AA: Slightly affects interactions with steroid
FT receptors. Abolishes interactions with steroid receptors;
FT when associated with A-636; A-637; A-693 and A-694."
FT /evidence="ECO:0000269|PubMed:9427757"
FT MUTAGEN 774
FT /note="K->R: Abolishes sumoylation; when associated with R-
FT 732."
FT /evidence="ECO:0000269|PubMed:12529333"
FT MUTAGEN 800
FT /note="K->R: Does not affect sumoylation of the protein."
FT /evidence="ECO:0000269|PubMed:12529333"
FT MUTAGEN 846
FT /note="K->R: Does not affect sumoylation of the protein."
FT /evidence="ECO:0000269|PubMed:12529333"
FT MUTAGEN 1378
FT /note="K->R: Does not affect sumoylation of the protein."
FT /evidence="ECO:0000269|PubMed:12529333"
FT CONFLICT 1035
FT /note="Missing (in Ref. 10; AAT47737)"
FT /evidence="ECO:0000305"
FT CONFLICT 1370
FT /note="Q -> H (in Ref. 9; AAA64187)"
FT /evidence="ECO:0000305"
FT CONFLICT 1382
FT /note="D -> G (in Ref. 10; AAT47737)"
FT /evidence="ECO:0000305"
FT CONFLICT 1435
FT /note="L -> R (in Ref. 3; AAB50242)"
FT /evidence="ECO:0000305"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:5NWM"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:5NWM"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:5NWM"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:5NWM"
FT HELIX 309..319
FT /evidence="ECO:0007829|PDB:5NWM"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:5NWM"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:5NWM"
FT STRAND 337..347
FT /evidence="ECO:0007829|PDB:5NWM"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:5NWM"
FT STRAND 357..365
FT /evidence="ECO:0007829|PDB:5NWM"
FT HELIX 632..638
FT /evidence="ECO:0007829|PDB:2FVJ"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:5HJS"
FT HELIX 688..695
FT /evidence="ECO:0007829|PDB:1NQ7"
FT HELIX 747..753
FT /evidence="ECO:0007829|PDB:5Q0K"
FT TURN 924..926
FT /evidence="ECO:0007829|PDB:2C52"
FT HELIX 929..941
FT /evidence="ECO:0007829|PDB:2C52"
FT HELIX 945..947
FT /evidence="ECO:0007829|PDB:2C52"
FT HELIX 952..954
FT /evidence="ECO:0007829|PDB:2C52"
FT TURN 958..962
FT /evidence="ECO:0007829|PDB:2C52"
FT STRAND 964..966
FT /evidence="ECO:0007829|PDB:2C52"
FT HELIX 1434..1440
FT /evidence="ECO:0007829|PDB:6GEV"
SQ 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
