NCOA1_MOUSE
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 03-AUG-2022, entry version 203.
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]
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 NCOA6 and NCOA2. Interacts with the FDL motif
CC of STAT5A and STAT5B. Interacts with the LXXLL motif of STAT6.
CC Interacts with STAT3 following IL-6 stimulation. Interacts with the
CC basal transcription factor GTF2B. Interacts with COPS5, NR3C1, PCAF and
CC TTLL5/STAMP. Interacts with the histone acetyltransferases EP300 and
CC CREBBP, and the methyltransferase CARM1. Interacts with PSMB9.
CC Interacts with UBE2L3; they functionally interact to regulate
CC progesterone receptor transcriptional activity. Interacts with PRMT2
CC and DDX5. Interacts with ASXL1. Interacts with PRMT6. Interacts (via
CC LXXLL 1, 2 and 3 motifs) with RORC (via AF-2 motif). Interacts in a
CC ligand-dependent fashion with RXRA. Interacts with TRIP4. Interacts
CC with NR4A3 (PubMed:12709428). 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}.
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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. [P70365-1]
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 iPTMnet; P70365; -.
DR PhosphoSitePlus; P70365; -.
DR EPD; P70365; -.
DR jPOST; P70365; -.
DR MaxQB; P70365; -.
DR PaxDb; P70365; -.
DR PeptideAtlas; P70365; -.
DR PRIDE; P70365; -.
DR ProteomicsDB; 293632; -. [P70365-1]
DR ProteomicsDB; 293633; -. [P70365-2]
DR ProteomicsDB; 293634; -. [P70365-3]
DR ProteomicsDB; 293635; -. [P70365-4]
DR Antibodypedia; 27525; 433 antibodies from 40 providers.
DR DNASU; 17977; -.
DR Ensembl; ENSMUST00000085814; ENSMUSP00000082971; ENSMUSG00000020647. [P70365-2]
DR Ensembl; ENSMUST00000217794; ENSMUSP00000151716; ENSMUSG00000020647. [P70365-4]
DR Ensembl; ENSMUST00000220434; ENSMUSP00000151358; ENSMUSG00000020647. [P70365-1]
DR GeneID; 17977; -.
DR KEGG; mmu:17977; -.
DR UCSC; uc007mxr.2; mouse. [P70365-1]
DR UCSC; uc007mxs.2; mouse. [P70365-2]
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; GVQGQFN; -.
DR OrthoDB; 59971at2759; -.
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 76 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 270 other tissues.
DR ExpressionAtlas; P70365; baseline and differential.
DR Genevisible; P70365; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO: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:0033142; F:nuclear progesterone 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:0047485; F:protein N-terminus binding; ISO:MGI.
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:0043967; P:histone H4 acetylation; IMP:GO_Central.
DR GO; GO:0060713; P:labyrinthine layer morphogenesis; IGI:MGI.
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; IC:ComplexPortal.
DR GO; GO:1904179; P:positive regulation of adipose tissue development; IC:ComplexPortal.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP: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:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IC:ComplexPortal.
DR GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; 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; cd00130; PAS; 1.
DR Gene3D; 4.10.280.10; -; 1.
DR Gene3D; 6.10.140.410; -; 1.
DR IDEAL; IID50084; -.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR010011; NCO_DUF1518.
DR InterPro; IPR028819; NCOA1.
DR InterPro; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ.
DR InterPro; IPR037077; Nuc_rcpt_coact_Ncoa_int_sf.
DR InterPro; IPR017426; Nuclear_rcpt_coactivator.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR014935; SRC/p160_LXXLL.
DR PANTHER; PTHR10684; PTHR10684; 1.
DR PANTHER; PTHR10684:SF1; PTHR10684:SF1; 1.
DR Pfam; PF07469; DUF1518; 2.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF08815; Nuc_rec_co-act; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08832; SRC-1; 1.
DR PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1.
DR SMART; SM01151; DUF1518; 2.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF69125; SSF69125; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Acyltransferase;
KW Alternative splicing; 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
