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Database: UniProt
Entry: P70365
LinkDB: P70365
Original site: P70365 
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   02-JUN-2021, entry version 199.
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   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   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; 413 antibodies.
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   eggNOG; KOG3561; Eukaryota.
DR   GeneTree; ENSGT00950000183021; -.
DR   HOGENOM; CLU_001988_0_0_1; -.
DR   InParanoid; P70365; -.
DR   OMA; TPNRTNC; -.
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   BioGRID-ORCS; 17977; 0 hits in 52 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 325 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: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:0030331; F:estrogen receptor binding; ISO:MGI.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035257; F:nuclear hormone 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:0033142; F:progesterone 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:0042974; F:retinoic acid receptor binding; ISO:MGI.
DR   GO; GO:0046965; F:retinoid X receptor 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:0008134; F:transcription factor binding; IPI: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:0043967; P:histone H4 acetylation; IMP:UniProtKB.
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: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; IMP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:2001038; P:regulation of cellular response to drug; IMP:UniProtKB.
DR   GO; GO:2001141; P:regulation of RNA biosynthetic process; IMP:UniProtKB.
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; 1.10.287.1070; -; 1.
DR   Gene3D; 4.10.280.10; -; 1.
DR   IDEAL; IID50084; -.
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; 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
//
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