ID NCOA1_MOUSE Reviewed; 1447 AA. AC P70365; P70366; Q61202; Q66JL7; Q8CBI9; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 2. DT 24-JAN-2024, entry version 211. DE RecName: Full=Nuclear receptor coactivator 1; DE Short=NCoA-1; DE EC=2.3.1.48; DE AltName: Full=Nuclear receptor coactivator protein 1; DE Short=mNRC-1; DE AltName: Full=Steroid receptor coactivator 1; DE Short=SRC-1; GN Name=Ncoa1; Synonyms=Src1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH RP EP300 AND CREBBP. RX PubMed=8616895; DOI=10.1016/s0092-8674(00)81118-6; RA Kamei Y., Xu L., Heinzel T., Torchia J., Kurokawa R., Gloss B., Lin S.-C., RA Heyman R.A., Rose D.W., Glass C.K., Rosenfeld M.G.; RT "A CBP integrator complex mediates transcriptional activation and AP-1 RT inhibition by nuclear receptors."; RL Cell 85:403-414(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9041124; RA Zhu Y., Qi C., Calandra C., Rao M.S., Reddy J.K.; RT "Cloning and identification of mouse steroid receptor coactivator-1 (mSRC- RT 1), as a coactivator of peroxisome proliferator-activated receptor gamma."; RL Gene Expr. 6:185-195(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND INTERACTION WITH EP300 AND RAR. RX PubMed=8855229; DOI=10.1073/pnas.93.20.10626; RA Yao T.-P., Ku G., Zhou N., Scully R., Livingston D.M.; RT "The nuclear hormone receptor coactivator SRC-1 is a specific target of RT p300."; RL Proc. Natl. Acad. Sci. U.S.A. 93:10626-10631(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC STRAIN=C57BL/6J; TISSUE=Cerebellum; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye; 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 [6] RP PROTEIN SEQUENCE OF 21-33, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [7] RP ROLE OF LXXLL MOTIFS, TISSUE SPECIFICITY, AND MUTAGENESIS OF RP 695-HIS--LEU-698 AND 756-ARG--LEU-759. RX PubMed=9192892; DOI=10.1038/42652; RA Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., RA Rosenfeld M.G.; RT "The transcriptional co-activator p/CIP binds CBP and mediates nuclear- RT receptor function."; RL Nature 387:677-684(1997). RN [8] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=9506940; DOI=10.1126/science.279.5358.1922; RA Xu J., Qiu Y., DeMayo F.J., Tsai S.Y., Tsai M.-J., O'Malley B.W.; RT "Partial hormone resistance in mice with disruption of the steroid receptor RT coactivator-1 (SRC-1) gene."; RL Science 279:1922-1925(1998). RN [9] RP INTERACTION WITH CARM1. RX PubMed=10381882; DOI=10.1126/science.284.5423.2174; RA Chen D., Ma H., Hong H., Koh S.S., Huang S.-M., Schurter B.T., Aswad D.W., RA Stallcup M.R.; RT "Regulation of transcription by a protein methyltransferase."; RL Science 284:2174-2177(1999). RN [10] RP FUNCTION. RX PubMed=12507421; DOI=10.1016/s0092-8674(02)01169-8; RA Picard F., Gehin M., Annicotte J.-S., Rocchi S., Champy M.-F., RA O'Malley B.W., Chambon P., Auwerx J.; RT "SRC-1 and TIF2 control energy balance between white and brown adipose RT tissues."; RL Cell 111:931-941(2002). RN [11] RP INTERACTION WITH NR4A3. RX PubMed=12709428; DOI=10.1074/jbc.m300088200; RA Wansa K.D., Harris J.M., Yan G., Ordentlich P., Muscat G.E.; RT "The AF-1 domain of the orphan nuclear receptor NOR-1 mediates trans- RT activation, coactivator recruitment, and activation by the purine anti- RT metabolite 6-mercaptopurine."; RL J. Biol. Chem. 278:24776-24790(2003). RN [12] RP FUNCTION AS COACTIVATOR, AND INTERACTION WITH RORC. RX PubMed=16148126; DOI=10.4049/jimmunol.175.6.3800; RA Xie H., Sadim M.S., Sun Z.; RT "RORgammat recruits steroid receptor coactivators to ensure thymocyte RT survival."; RL J. Immunol. 175:3800-3809(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-372 AND SER-702, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-559, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [15] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1079; ARG-1097; ARG-1130 AND RP ARG-1137, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [16] {ECO:0007744|PDB:1OJ5} RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 257-385 IN COMPLEX WITH 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:12507421, CC ECO:0000269|PubMed:16148126, ECO:0000269|PubMed:8616895, CC ECO:0000269|PubMed:9506940}. 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 PPARA; the interaction is direct (By CC similarity). Interacts with PPARG; the interaction is direct (By CC similarity). Interacts with ESRRG; the interaction is direct (By CC similarity). Interacts with STAT5A (via FDL motif) (By similarity). CC Interacts with STAT5B (via FDL motif) (By similarity). Interacts with CC STAT6 (via LXXLL motif) (PubMed:14757047). Interacts (via LXXLL 1, 2 CC and 3 motifs) with RORC (via AF-2 motif) (PubMed:16148126). Interacts CC with ASXL1 (By similarity). Interacts with the methyltransferase CARM1 CC (PubMed:10381882). Interacts with COPS5 (By similarity). Interacts with CC the histone acetyltransferase CREBBP (PubMed:8616895). Interacts with CC DDX5 (By similarity). Interacts with the histone acetyltransferase CC EP300 (PubMed:8616895, PubMed:8855229). Interacts with ESR1 (By CC similarity). Interacts with GCCR (By similarity). Interacts with the CC basal transcription factor GTF2B (By similarity). Interacts with NCOA6 CC (By similarity). Interacts with NCOA2 (By similarity). Interacts with CC NR3C1 (By similarity). Interacts with NR4A1/Nur77 (By similarity). CC Interacts with NR4A3 (PubMed:12709428). Interacts with PCAF (By CC similarity). Interacts with PGR (By similarity). Interacts with PRMT2 CC (By similarity). Interacts with PRMT6 (By similarity). Interacts with CC PSMB9 (By similarity). Interacts with RXRA, the interaction is ligand- CC dependent (By similarity). Interacts with STAT3 following IL-6 CC stimulation (By similarity). Interacts with TRA (By similarity). CC Interacts with TRIP4 (By similarity). Interacts with TTLL5/STAMP (By CC similarity). Interacts with UBE2L3; they functionally interact to CC regulate progesterone receptor transcriptional activity (By CC similarity). Interacts with VDR (By similarity). CC {ECO:0000250|UniProtKB:Q15788, ECO:0000269|PubMed:10381882, CC ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:14757047, CC ECO:0000269|PubMed:16148126, ECO:0000269|PubMed:8616895, CC ECO:0000269|PubMed:8855229}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, CC ECO:0000269|PubMed:8855229}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=SRC-1A, SRC1a; CC IsoId=P70365-1; Sequence=Displayed; CC Name=2; Synonyms=SRC-1E, SRC1e; CC IsoId=P70365-2; Sequence=VSP_011740; CC Name=3; CC IsoId=P70365-3; Sequence=VSP_011741; CC Name=4; CC IsoId=P70365-4; Sequence=VSP_027855, VSP_027856; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8855229, CC ECO:0000269|PubMed:9192892}. CC -!- DOMAIN: The C-terminal (1113-1447) part mediates the histone CC acetyltransferase (HAT) activity. {ECO:0000250}. 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 (By similarity). {ECO:0000250}. CC -!- PTM: Ubiquitinated; leading to proteasome-mediated degradation. CC Ubiquitination and sumoylation take place at different sites (By CC similarity). {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Mice show partial hormone resistance: target CC organs such as uterus, prostate, testis and mammary gland exhibiting CC decreased growth and development in response to steroid hormones. CC Moreover, such mice are prone to obesity due to reduced energy CC expenditure. {ECO:0000269|PubMed:9506940}. CC -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U56920; AAB01228.1; -; mRNA. DR EMBL; U64606; AAB06177.1; -; mRNA. DR EMBL; U64828; AAB38841.1; -; mRNA. DR EMBL; AK035922; BAC29244.1; -; mRNA. DR EMBL; BC068177; AAH68177.1; -; mRNA. DR EMBL; BC080866; AAH80866.1; -; mRNA. DR CCDS; CCDS25789.1; -. [P70365-2] DR RefSeq; NP_035011.1; NM_010881.2. [P70365-2] DR RefSeq; XP_006515068.1; XM_006515005.3. DR RefSeq; XP_006515069.1; XM_006515006.3. [P70365-1] DR RefSeq; XP_006515070.1; XM_006515007.3. [P70365-1] DR RefSeq; XP_011242143.1; XM_011243841.2. DR PDB; 1OJ5; X-ray; 2.20 A; A=257-385. DR PDB; 2O9I; X-ray; 2.80 A; C/D=686-700. DR PDB; 4DMA; X-ray; 2.30 A; E/F=690-704. DR PDB; 5NWX; X-ray; 2.51 A; A=257-385. DR PDB; 5Y7W; X-ray; 2.25 A; A/B=257-367. DR PDBsum; 1OJ5; -. DR PDBsum; 2O9I; -. DR PDBsum; 4DMA; -. DR PDBsum; 5NWX; -. DR PDBsum; 5Y7W; -. DR AlphaFoldDB; P70365; -. DR SMR; P70365; -. DR BioGRID; 201707; 14. DR ComplexPortal; CPX-5343; RXRalpha-NCOA1 activated retinoic acid receptor complex. DR ComplexPortal; CPX-644; PXR-NCOA1 activated nuclear receptor complex. DR ComplexPortal; CPX-667; RARalpha-NCOA1 activated retinoic acid receptor complex. DR ComplexPortal; CPX-864; PPARgamma-NCOA1 activated nuclear receptor complex. DR CORUM; P70365; -. DR IntAct; P70365; 3. DR MINT; P70365; -. DR STRING; 10090.ENSMUSP00000082971; -. DR GlyGen; P70365; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P70365; -. DR PhosphoSitePlus; P70365; -. DR EPD; P70365; -. DR jPOST; P70365; -. DR MaxQB; P70365; -. DR PaxDb; 10090-ENSMUSP00000082971; -. DR PeptideAtlas; P70365; -. DR ProteomicsDB; 293632; -. [P70365-1] DR ProteomicsDB; 293633; -. [P70365-2] DR ProteomicsDB; 293634; -. [P70365-3] DR ProteomicsDB; 293635; -. [P70365-4] DR Pumba; P70365; -. DR Antibodypedia; 27525; 477 antibodies from 40 providers. DR DNASU; 17977; -. DR Ensembl; ENSMUST00000085814.5; ENSMUSP00000082971.4; ENSMUSG00000020647.11. [P70365-2] DR Ensembl; ENSMUST00000217794.2; ENSMUSP00000151716.2; ENSMUSG00000020647.11. [P70365-4] DR Ensembl; ENSMUST00000220434.2; ENSMUSP00000151358.2; ENSMUSG00000020647.11. [P70365-1] DR GeneID; 17977; -. DR KEGG; mmu:17977; -. DR UCSC; uc007mxr.2; mouse. [P70365-1] DR UCSC; uc007mxs.2; mouse. [P70365-2] DR AGR; MGI:1276523; -. DR CTD; 8648; -. DR MGI; MGI:1276523; Ncoa1. DR VEuPathDB; HostDB:ENSMUSG00000020647; -. DR eggNOG; KOG3561; Eukaryota. DR GeneTree; ENSGT00950000183021; -. DR HOGENOM; CLU_001988_0_0_1; -. DR InParanoid; P70365; -. DR OMA; AQHVNIG; -. DR OrthoDB; 4230728at2759; -. DR PhylomeDB; P70365; -. DR TreeFam; TF332652; -. DR Reactome; R-MMU-159418; Recycling of bile acids and salts. DR Reactome; R-MMU-192105; Synthesis of bile acids and bile salts. DR Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol. DR Reactome; R-MMU-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol. DR Reactome; R-MMU-211976; Endogenous sterols. DR Reactome; R-MMU-3214847; HATs acetylate histones. DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors. DR Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha. DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression. DR Reactome; R-MMU-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux. DR Reactome; R-MMU-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis. DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1. DR BioGRID-ORCS; 17977; 3 hits in 82 CRISPR screens. DR ChiTaRS; Ncoa1; mouse. DR EvolutionaryTrace; P70365; -. DR PRO; PR:P70365; -. DR Proteomes; UP000000589; Chromosome 12. DR RNAct; P70365; Protein. DR Bgee; ENSMUSG00000020647; Expressed in rostral migratory stream and 272 other cell types or tissues. DR ExpressionAtlas; P70365; baseline and differential. DR GO; GO:0000785; C:chromatin; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI. DR GO; GO:0005667; C:transcription regulator complex; EXP:ComplexPortal. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI. DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI. DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI. DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; ISO:MGI. DR GO; GO:0046965; F:nuclear retinoid X receptor binding; ISO:MGI. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0032870; P:cellular response to hormone stimulus; ISO:MGI. DR GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IGI:MGI. 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:0021854; P:hypothalamus development; IEA:Ensembl. DR GO; GO:0060713; P:labyrinthine layer morphogenesis; IGI:MGI. 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; ISO:MGI. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; NAS:ComplexPortal. DR GO; GO:1904179; P:positive regulation of adipose tissue development; NAS:ComplexPortal. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0045925; P:positive regulation of female receptivity; ISO:MGI. DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; ISO:MGI. DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; NAS:ComplexPortal. DR GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; IGI:MGI. DR GO; GO:0032355; P:response to estradiol; ISO:MGI. DR GO; GO:0032570; P:response to progesterone; ISO:MGI. DR GO; GO:0032526; P:response to retinoic acid; ISO:MGI. DR CDD; cd18948; bHLH-PAS_NCoA1_SRC1; 1. DR CDD; cd00130; PAS; 1. DR Gene3D; 6.10.140.410; -; 1. DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1. DR Gene3D; 3.30.450.20; PAS domain; 2. DR IDEAL; IID50084; -. DR InterPro; IPR011598; bHLH_dom. DR InterPro; IPR036638; HLH_DNA-bd_sf. DR InterPro; IPR010011; NCO_DUF1518. DR InterPro; IPR028819; NCOA1_bHLH. 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; NUCLEAR RECEPTOR COACTIVATOR; 1. DR PANTHER; PTHR10684:SF1; NUCLEAR RECEPTOR COACTIVATOR 1; 1. DR Pfam; PF07469; DUF1518; 2. DR Pfam; PF16665; NCOA_u2; 1. DR Pfam; PF08815; Nuc_rec_co-act; 1. DR Pfam; PF00989; PAS; 1. DR Pfam; PF14598; PAS_11; 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; HLH, helix-loop-helix DNA-binding domain; 1. DR SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2. DR PROSITE; PS50888; BHLH; 1. DR PROSITE; PS50112; PAS; 1. DR Genevisible; P70365; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Acyltransferase; KW Alternative splicing; Direct protein sequencing; Isopeptide bond; KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Transcription; Transcription regulation; Transferase; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q15788" FT CHAIN 2..1447 FT /note="Nuclear receptor coactivator 1" FT /id="PRO_0000094401" 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..568 FT /note="Interaction with STAT3" FT REGION 368..446 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 459..478 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 548..632 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 663..688 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 700..735 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 787..994 FT /note="Interaction with CREBBP" FT /evidence="ECO:0000269|PubMed:8616895" FT REGION 1166..1195 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1268..1287 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1415..1447 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 637..641 FT /note="LXXLL motif 3" FT MOTIF 694..698 FT /note="LXXLL motif 4" FT MOTIF 755..759 FT /note="LXXLL motif 5" FT MOTIF 919..923 FT /note="LXXLL motif 6" FT MOTIF 1441..1445 FT /note="LXXLL motif 7" FT COMPBIAS 373..446 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 548..579 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 592..609 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 663..687 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 721..735 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1169..1183 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1420..1447 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:Q15788" FT MOD_RES 22 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 372 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319" FT MOD_RES 395 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15788" FT MOD_RES 518 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15788" FT MOD_RES 559 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 570 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15788" FT MOD_RES 702 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319" FT MOD_RES 1039 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15788" FT MOD_RES 1079 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1097 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1130 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1137 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1185 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q15788" FT MOD_RES 1191 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15788" FT MOD_RES 1378 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15788" FT CROSSLNK 738 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250" FT CROSSLNK 780 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250" FT CROSSLNK 852 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15788" FT VAR_SEQ 1300..1376 FT /note="NVFSQAVQSQPAPAQPGVYNNMSITVSMAGGNANIQNMNPMMGQMQMSSLQM FT PGMNTVCSEQMNDPALRHTGLYCNQ -> KWKRKHSEHESNDGPDANELSADARDEYCV FT L (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_027855" FT VAR_SEQ 1377..1447 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_027856" FT VAR_SEQ 1392..1447 FT /note="QVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQ FT LLTE -> DKKTEEFFSVVTTD (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8616895, ECO:0000303|PubMed:8855229" FT /id="VSP_011740" FT VAR_SEQ 1392..1447 FT /note="QVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQ FT LLTE -> VSKKDNPSAELADSITLDTWRTSHGIC (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_011741" FT MUTAGEN 695..698 FT /note="HRLL->AAAA: Abolishes the interactions with estrogen FT and retinoid-acids receptors." FT /evidence="ECO:0000269|PubMed:9192892" FT MUTAGEN 756..759 FT /note="RYLL->AAAA: Abolishes the interactions with estrogen FT and retinoid-acids receptors." FT /evidence="ECO:0000269|PubMed:9192892" FT CONFLICT 45 FT /note="E -> G (in Ref. 1; AAB01228)" FT /evidence="ECO:0000305" FT CONFLICT 223 FT /note="C -> R (in Ref. 2; AAB06177)" FT /evidence="ECO:0000305" FT CONFLICT 234 FT /note="E -> G (in Ref. 2; AAB06177)" FT /evidence="ECO:0000305" FT CONFLICT 237 FT /note="E -> K (in Ref. 5; AAH80866)" FT /evidence="ECO:0000305" FT CONFLICT 465..466 FT /note="SS -> TT (in Ref. 1; AAB01228)" FT /evidence="ECO:0000305" FT CONFLICT 699 FT /note="Q -> P (in Ref. 2; AAB06177)" FT /evidence="ECO:0000305" FT CONFLICT 1115 FT /note="L -> M (in Ref. 4; BAC29244)" FT /evidence="ECO:0000305" FT CONFLICT 1130 FT /note="R -> K (in Ref. 1; AAB01228)" FT /evidence="ECO:0000305" FT CONFLICT 1137..1138 FT /note="RA -> KP (in Ref. 1; AAB01228)" FT /evidence="ECO:0000305" FT CONFLICT 1142 FT /note="R -> K (in Ref. 1; AAB01228)" FT /evidence="ECO:0000305" FT CONFLICT 1162 FT /note="T -> D (in Ref. 1; AAB01228)" FT /evidence="ECO:0000305" FT CONFLICT 1164 FT /note="R -> S (in Ref. 2; AAB06177)" FT /evidence="ECO:0000305" FT CONFLICT 1166 FT /note="P -> L (in Ref. 1; AAB01228)" FT /evidence="ECO:0000305" FT STRAND 261..266 FT /evidence="ECO:0007829|PDB:1OJ5" FT STRAND 272..276 FT /evidence="ECO:0007829|PDB:1OJ5" FT HELIX 278..281 FT /evidence="ECO:0007829|PDB:1OJ5" FT HELIX 288..299 FT /evidence="ECO:0007829|PDB:1OJ5" FT HELIX 309..320 FT /evidence="ECO:0007829|PDB:1OJ5" FT STRAND 321..324 FT /evidence="ECO:0007829|PDB:1OJ5" FT STRAND 328..331 FT /evidence="ECO:0007829|PDB:1OJ5" FT STRAND 337..347 FT /evidence="ECO:0007829|PDB:1OJ5" FT STRAND 357..365 FT /evidence="ECO:0007829|PDB:1OJ5" FT TURN 687..690 FT /evidence="ECO:0007829|PDB:2O9I" FT HELIX 693..699 FT /evidence="ECO:0007829|PDB:4DMA" SQ SEQUENCE 1447 AA; 157016 MW; 65C08AFFCF14241D CRC64; MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG VPWPQEATRR NSHTFNCRML IHPPEDPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ SCLICIARRL PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ SPDMQPFIMG IHIIDREHSG LSPQDDSNSG MSIPRINPSV NPGISPAHGV TRSSTLPPSN NNMVSARVNR QQSSDLNSSS SHTNSSNNQG NFGCSPGNQI VANVALNQGQ AGSQSSNPSL NLNNSPMEGT GIALSQFMSP RRQANSGLAT RARMSNNSFP PNIPTLSSPV GITSGACNNN NRSYSNIPVT SLQGMNEGPN NSVGFSAGSP VLRQMSSQNS PSRLSMQPAK AESKDSKEIA SILNEMIQSD NSDNSANEGK PLDSGLLHNN DRLSEGDSKY SQTSHKLVQL LTTTAEQQLR HADIDTSCKD VLSCTGTSSS ASSNPSGGTC PSSHSSLTER HKILHRLLQE GSPSDITTLS VEPEKKDSVP ASTAVSVSGQ SQGSASIKLE LDAAKKKESK DHQLLRYLLD KDEKDLRSTP NLCLDDVKVK VEKKEQMDPC NTNPTPMTKP APEEVKLESQ SQFTADLDQF DQLLPTLEKA AQLPSLCETD RMDGAVTGVS IKAEVLPASL QPTTARAAPR LSRLPELELE AIDNQFGQPG AGDQIPWANN TLTTINQNKP EDQCISSQLD ELLCPPTTVE GRNDEKALLE QLVSFLSGKD ETELAELDRA LGIDKLVQGG GLDVLSERFP PQQATPPLMM EDRPTLYSQP YSSPSPTAGL SGPFQGMVRQ KPSLGAMPVQ VTPPRGTFSP NMGMQPRQTL NRPPAAPNQL RLQLQQRLQG QQQLMHQNRQ AILNQFAANA PVGMNMRSGM QQQITPQPPL NAQMLAQRQR ELYSQQHRQR QIIQQQRAML MRHQSFGNNI PPSSGLPVQM GTPRLPQGAP QQFPYPPNYG TNPGTPPAST SPFSQLAANP EASLATRSSM VNRGMAGNMG GQFGAGISPQ MQQNVFQYPG PGLVPQGEAT FAPSLSPGSS MVPMPVPPPQ SSLLQQTPPT SGYQSPDMKA WQQGTMGNNN VFSQAVQSQP APAQPGVYNN MSITVSMAGG NANIQNMNPM MGQMQMSSLQ MPGMNTVCSE QMNDPALRHT GLYCNQLSST DLLKTDADGN QQVQQVQVFA DVQCTVNLVG GDPYLNQPGP LGTQKPTSGP QTPQAQQKSL LQQLLTE //