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Database: UniProt
Entry: Q15788
LinkDB: Q15788
Original site: Q15788 
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   07-OCT-2020, entry version 196.
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/";
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; 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; 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   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; 6L96; -.
DR   PDBsum; 6NX1; -.
DR   PDBsum; 6P9F; -.
DR   PDBsum; 6SSQ; -.
DR   PDBsum; 6U25; -.
DR   PDBsum; 6W9H; -.
DR   PDBsum; 6W9I; -.
DR   SMR; Q15788; -.
DR   BioGRID; 114200; 120.
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; 46.
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   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; 403 antibodies.
DR   Ensembl; ENST00000288599; ENSP00000288599; ENSG00000084676. [Q15788-2]
DR   Ensembl; ENST00000348332; ENSP00000320940; ENSG00000084676. [Q15788-1]
DR   Ensembl; ENST00000395856; ENSP00000379197; ENSG00000084676. [Q15788-3]
DR   Ensembl; ENST00000405141; ENSP00000385097; ENSG00000084676. [Q15788-2]
DR   Ensembl; ENST00000406961; ENSP00000385216; ENSG00000084676. [Q15788-1]
DR   GeneID; 8648; -.
DR   KEGG; hsa:8648; -.
DR   UCSC; uc002rfj.4; human. [Q15788-1]
DR   CTD; 8648; -.
DR   DisGeNET; 8648; -.
DR   EuPathDB; HostDB:ENSG00000084676.15; -.
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   eggNOG; KOG3561; Eukaryota.
DR   GeneTree; ENSGT00950000183021; -.
DR   HOGENOM; CLU_001988_0_0_1; -.
DR   InParanoid; Q15788; -.
DR   KO; K09101; -.
DR   OMA; TPNRTNC; -.
DR   OrthoDB; 59971at2759; -.
DR   PhylomeDB; Q15788; -.
DR   TreeFam; TF332652; -.
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   SignaLink; Q15788; -.
DR   SIGNOR; Q15788; -.
DR   BioGRID-ORCS; 8648; 9 hits in 878 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 forebrain and 250 other tissues.
DR   ExpressionAtlas; Q15788; baseline and differential.
DR   Genevisible; Q15788; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
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:0017162; F:aryl hydrocarbon receptor binding; IPI:CAFA.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0030331; F:estrogen receptor binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035257; F:nuclear hormone receptor binding; IDA:UniProtKB.
DR   GO; GO:0016922; F:nuclear receptor binding; IPI:UniProtKB.
DR   GO; GO:0030374; F:nuclear receptor transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0033142; F:progesterone receptor binding; IEA:Ensembl.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0046965; F:retinoid X receptor binding; IEA:Ensembl.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0015721; P:bile acid and bile salt transport; TAS:Reactome.
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:0021549; P:cerebellum development; IEA:Ensembl.
DR   GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR   GO; GO:0044849; P:estrous cycle; IEA:Ensembl.
DR   GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR   GO; GO:0043967; P:histone H4 acetylation; IEA:Ensembl.
DR   GO; GO:0021854; P:hypothalamus development; IEA:Ensembl.
DR   GO; GO:0060713; P:labyrinthine layer morphogenesis; IEA:Ensembl.
DR   GO; GO:0007595; P:lactation; IEA:Ensembl.
DR   GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR   GO; GO:0060179; P:male mating behavior; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0045925; P:positive regulation of female receptivity; 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:2001038; P:regulation of cellular response to drug; IEA:Ensembl.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
DR   GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR   GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR   CDD; cd00083; HLH; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.1070; -; 1.
DR   Gene3D; 4.10.280.10; -; 1.
DR   IDEAL; IID00083; -.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR010011; DUF1518.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
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; Polymorphism; Proto-oncogene;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|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          361..567
FT                   /note="Interaction with STAT3"
FT                   /evidence="ECO:0000269|PubMed:11773079"
FT   REGION          781..988
FT                   /note="Interaction with CREBBP"
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        389..682
FT                   /note="Ser-rich"
FT   COMPBIAS        1053..1138
FT                   /note="Gln-rich"
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:0000244|PubMed:19413330"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         372
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163,
FT                   ECO:0000269|PubMed:10660621"
FT   MOD_RES         395
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:10660621"
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:0000244|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:0000244|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:0000244|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:0000244|PDB:5NWM"
FT   STRAND          272..276
FT                   /evidence="ECO:0000244|PDB:5NWM"
FT   HELIX           278..283
FT                   /evidence="ECO:0000244|PDB:5NWM"
FT   HELIX           288..299
FT                   /evidence="ECO:0000244|PDB:5NWM"
FT   HELIX           309..319
FT                   /evidence="ECO:0000244|PDB:5NWM"
FT   STRAND          320..324
FT                   /evidence="ECO:0000244|PDB:5NWM"
FT   STRAND          328..331
FT                   /evidence="ECO:0000244|PDB:5NWM"
FT   STRAND          337..347
FT                   /evidence="ECO:0000244|PDB:5NWM"
FT   STRAND          350..353
FT                   /evidence="ECO:0000244|PDB:5NWM"
FT   STRAND          357..365
FT                   /evidence="ECO:0000244|PDB:5NWM"
FT   HELIX           632..638
FT                   /evidence="ECO:0000244|PDB:2FVJ"
FT   HELIX           684..686
FT                   /evidence="ECO:0000244|PDB:5HJS"
FT   HELIX           688..695
FT                   /evidence="ECO:0000244|PDB:1NQ7"
FT   HELIX           747..753
FT                   /evidence="ECO:0000244|PDB:5Q0K"
FT   TURN            924..926
FT                   /evidence="ECO:0000244|PDB:2C52"
FT   HELIX           929..941
FT                   /evidence="ECO:0000244|PDB:2C52"
FT   HELIX           945..947
FT                   /evidence="ECO:0000244|PDB:2C52"
FT   HELIX           952..954
FT                   /evidence="ECO:0000244|PDB:2C52"
FT   TURN            958..962
FT                   /evidence="ECO:0000244|PDB:2C52"
FT   STRAND          964..966
FT                   /evidence="ECO:0000244|PDB:2C52"
FT   HELIX           1434..1440
FT                   /evidence="ECO:0000244|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
//
DBGET integrated database retrieval system