NCOA3_HUMAN
ID NCOA3_HUMAN Reviewed; 1424 AA.
AC Q9Y6Q9; A4LAZ5; Q0VF45; Q5JYD9; Q5JYE0; Q9BR49; Q9UPC9; Q9UPG4; Q9UPG7;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Nuclear receptor coactivator 3;
DE Short=NCoA-3;
DE EC=2.3.1.48;
DE AltName: Full=ACTR;
DE AltName: Full=Amplified in breast cancer 1 protein;
DE Short=AIB-1;
DE AltName: Full=CBP-interacting protein;
DE Short=pCIP;
DE AltName: Full=Class E basic helix-loop-helix protein 42;
DE Short=bHLHe42;
DE AltName: Full=Receptor-associated coactivator 3;
DE Short=RAC-3;
DE AltName: Full=Steroid receptor coactivator protein 3;
DE Short=SRC-3;
DE AltName: Full=Thyroid hormone receptor activator molecule 1;
DE Short=TRAM-1;
GN Name=NCOA3; Synonyms=AIB1, BHLHE42, RAC3, TRAM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND INTERACTION WITH CREBBP;
RP PCAF; RARA; RXRA; THRA AND ESR.
RC TISSUE=Pituitary;
RX PubMed=9346901; DOI=10.1074/jbc.272.44.27629;
RA Takeshita A., Cardona G.R., Koibuchi N., Suen C.-S., Chin W.W.;
RT "TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule,
RT exhibits distinct properties from steroid receptor coactivator-1.";
RL J. Biol. Chem. 272:27629-27634(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ENZYME ACTIVITY, AND VARIANT
RP 1248-GLN--GLN-1250 DEL.
RC TISSUE=Leukemia;
RX PubMed=9267036; DOI=10.1016/s0092-8674(00)80516-4;
RA Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L.,
RA Privalsky M.L., Nakatani Y., Evans R.M.;
RT "Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and
RT forms a multimeric activation complex with P/CAF and CBP/p300.";
RL Cell 90:569-580(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND INTERACTION WITH ESR.
RC TISSUE=Lung;
RX PubMed=9252329; DOI=10.1126/science.277.5328.965;
RA Anzick S.L., Kononen J., Walker R.L., Azorsa D.O., Tanner M.M., Guan X.-Y.,
RA Sauter G., Kallioniemi O.-P., Trent J.M., Meltzer P.S.;
RT "AIB1, a steroid receptor coactivator amplified in breast and ovarian
RT cancer.";
RL Science 277:965-968(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH VDR; RARA; PPARA;
RP RXRA; THRA AND ESR, AND VARIANT 1248-GLN--GLN-1250 DEL.
RC TISSUE=Brain;
RX PubMed=9238002; DOI=10.1073/pnas.94.16.8479;
RA Li H., Gomes P.J., Chen J.D.;
RT "RAC3, a steroid/nuclear receptor-associated coactivator that is related to
RT SRC-1 and TIF2.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8479-8484(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-218; ILE-220; VAL-556;
RP SER-559; HIS-586; ALA-777; LEU-1247 AND LYS-1247.
RG NIEHS SNPs program;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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 [9]
RP POLYMORPHISM OF POLY-GLN REGION.
RX PubMed=9727751; DOI=10.1111/j.1399-0004.1998.tb03704.x;
RA Shirazi S.K., Bober M.A., Coetzee G.A.;
RT "Polymorphic exonic CAG microsatellites in the gene amplified in breast
RT cancer (AIB1 gene).";
RL Clin. Genet. 54:102-103(1998).
RN [10]
RP ACETYLATION AT LYS-616; LYS-619 AND LYS-620 BY CREBBP, AND MUTAGENESIS OF
RP LYS-616; 619-LYS-LYS-620; LYS-647; LYS-681; LYS-687; LYS-700 AND LYS-708.
RX PubMed=10490106; DOI=10.1016/s0092-8674(00)80054-9;
RA Chen H., Lin R.J., Xie W., Wilpitz D., Evans R.M.;
RT "Regulation of hormone-induced histone hyperacetylation and gene activation
RT via acetylation of an acetylase.";
RL Cell 98:675-686(1999).
RN [11]
RP INTERACTION WITH NFKB1.
RX PubMed=11094166; DOI=10.1016/s0014-5793(00)02223-7;
RA Werbajh S., Nojek I., Lanz R., Costas M.A.;
RT "RAC-3 is a NF-kappa B coactivator.";
RL FEBS Lett. 485:195-199(2000).
RN [12]
RP INTERACTION WITH DDX5.
RX PubMed=11250900; DOI=10.1093/emboj/20.6.1341;
RA Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S., Arao Y.,
RA Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y., Kato S.;
RT "A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor
RT alpha coactivator through the N-terminal activation domain (AF-1) with an
RT RNA coactivator, SRA.";
RL EMBO J. 20:1341-1352(2001).
RN [13]
RP SUBUNIT OF A COMPLEX CONTAINING CREBBP; NCOA2; IKKA; IKKB AND IKBKG, AND
RP PHOSPHORYLATION.
RX PubMed=11971985; DOI=10.1128/mcb.22.10.3549-3561.2002;
RA Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J.,
RA O'Malley B.W.;
RT "Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by
RT I kappa B kinase.";
RL Mol. Cell. Biol. 22:3549-3561(2002).
RN [14]
RP INTERACTION WITH NR3C1.
RX PubMed=12917342; DOI=10.1128/mcb.23.17.6210-6220.2003;
RA Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
RT "BAF60a mediates critical interactions between nuclear receptors and the
RT BRG1 chromatin-remodeling complex for transactivation.";
RL Mol. Cell. Biol. 23:6210-6220(2003).
RN [15]
RP INTERACTION WITH NPAS2.
RX PubMed=14645221; DOI=10.1074/jbc.m311973200;
RA Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M.,
RA Chakravarti D., FitzGerald G.A., McNamara P.;
RT "Histone acetyltransferase-dependent chromatin remodeling and the vascular
RT clock.";
RL J. Biol. Chem. 279:7091-7097(2004).
RN [16]
RP INTERACTION WITH CASP8AP2.
RX PubMed=15698540; DOI=10.1016/j.jsbmb.2004.09.003;
RA Kino T., Ichijo T., Chrousos G.P.;
RT "FLASH interacts with p160 coactivator subtypes and differentially
RT suppresses transcriptional activity of steroid hormone receptors.";
RL J. Steroid Biochem. Mol. Biol. 92:357-363(2004).
RN [17]
RP SUBUNIT.
RX PubMed=16951154; DOI=10.1158/0008-5472.can-06-1636;
RA Ma A.H., Xia L., Desai S.J., Boucher D.L., Guan Y., Shih H.M., Shi X.B.,
RA deVere White R.W., Chen H.W., Tepper C.G., Kung H.J.;
RT "Male germ cell-associated kinase, a male-specific kinase regulated by
RT androgen, is a coactivator of androgen receptor in prostate cancer cells.";
RL Cancer Res. 66:8439-8447(2006).
RN [18]
RP INTERACTION WITH PSMB9.
RX PubMed=16957778; DOI=10.1038/sj.emboj.7601306;
RA Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R.,
RA Sun X., Shang Y.;
RT "The catalytic subunit of the proteasome is engaged in the entire process
RT of estrogen receptor-regulated transcription.";
RL EMBO J. 25:4223-4233(2006).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857 AND SER-867, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [20]
RP INTERACTION WITH ATAD2.
RX PubMed=17998543; DOI=10.1073/pnas.0705814104;
RA Zou J.X., Revenko A.S., Li L.B., Gemo A.T., Chen H.-W.;
RT "ANCCA, an estrogen-regulated AAA+ ATPase coactivator for ERalpha, is
RT required for coregulator occupancy and chromatin modification.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18067-18072(2007).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-551; SER-728 AND
RP SER-857, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP PHOSPHORYLATION AT SER-601 BY CSNK1D/CK1, AND INTERACTION WITH CSNK1D.
RX PubMed=19339517; DOI=10.1093/nar/gkp136;
RA Giamas G., Castellano L., Feng Q., Knippschild U., Jacob J., Thomas R.S.,
RA Coombes R.C., Smith C.L., Jiao L.R., Stebbing J.;
RT "CK1delta modulates the transcriptional activity of ERalpha via AIB1 in an
RT estrogen-dependent manner and regulates ERalpha-AIB1 interactions.";
RL Nucleic Acids Res. 37:3110-3123(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-687, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-857 AND SER-867, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-551; SER-694;
RP SER-728; SER-857; SER-1033 AND SER-1330, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [31]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1171; ARG-1177 AND ARG-1188, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
CC -!- FUNCTION: Nuclear receptor coactivator that directly binds nuclear
CC receptors and stimulates the transcriptional activities in a hormone-
CC dependent fashion. Plays a central role in creating a multisubunit
CC coactivator complex, which probably acts via remodeling of chromatin.
CC Involved in the coactivation of different nuclear receptors, such as
CC for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone
CC (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone
CC acetyltransferase activity. Also involved in the coactivation of the
CC NF-kappa-B pathway via its interaction with the NFKB1 subunit.
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 Evidence={ECO:0000269|PubMed:9267036};
CC -!- ACTIVITY REGULATION: Coactivator activity on nuclear receptors and NF-
CC kappa-B pathways is enhanced by various hormones, and the TNF cytokine,
CC respectively. TNF stimulation probably enhances phosphorylation, which
CC in turn activates coactivator function. In contrast, acetylation by
CC CREBBP apparently suppresses coactivation of target genes by disrupting
CC its association with nuclear receptors. Binds to CSNK1D.
CC -!- SUBUNIT: Interacts with CARM1 (By similarity). Present in a complex
CC containing NCOA2, IKKA, IKKB, IKBKG and the histone acetyltransferase
CC protein CREBBP. Interacts with CASP8AP2, NR3C1 and PCAF. Interacts with
CC ATAD2 and this interaction is enhanced by estradiol. Found in a complex
CC containing NCOA3, AR and MAK. Interacts with DDX5. Interacts with
CC PSMB9. Interacts with NPAS2. Interacts with NR4A3 (By similarity).
CC Interacts with ESRRB; mediates the interaction between ESRRB and RNA
CC polymerase II complexes and allows NCOA3 corecruitment to ESRRB, KLF4,
CC NANOG, and SOX2 enhancer regions to trigger ESRRB-dependent gene
CC activation involved in self-renewal and pluripotency (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:O09000,
CC ECO:0000269|PubMed:11094166, ECO:0000269|PubMed:11250900,
CC ECO:0000269|PubMed:11971985, ECO:0000269|PubMed:12917342,
CC ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:15698540,
CC ECO:0000269|PubMed:16951154, ECO:0000269|PubMed:16957778,
CC ECO:0000269|PubMed:17998543, ECO:0000269|PubMed:19339517,
CC ECO:0000269|PubMed:9238002, ECO:0000269|PubMed:9252329,
CC ECO:0000269|PubMed:9346901}.
CC -!- INTERACTION:
CC Q9Y6Q9; Q6PL18: ATAD2; NbExp=2; IntAct=EBI-81196, EBI-6598454;
CC Q9Y6Q9; Q86X55: CARM1; NbExp=13; IntAct=EBI-81196, EBI-2339854;
CC Q9Y6Q9; P03372: ESR1; NbExp=4; IntAct=EBI-81196, EBI-78473;
CC Q9Y6Q9; O14920: IKBKB; NbExp=3; IntAct=EBI-81196, EBI-81266;
CC Q9Y6Q9; P28065: PSMB9; NbExp=3; IntAct=EBI-81196, EBI-603300;
CC Q9Y6Q9; P61289: PSME3; NbExp=5; IntAct=EBI-81196, EBI-355546;
CC Q9Y6Q9; P60484: PTEN; NbExp=2; IntAct=EBI-81196, EBI-696162;
CC Q9Y6Q9; P10276: RARA; NbExp=2; IntAct=EBI-81196, EBI-413374;
CC Q9Y6Q9; O43791: SPOP; NbExp=6; IntAct=EBI-81196, EBI-743549;
CC Q9Y6Q9; Q8VIM5-1: Myocd; Xeno; NbExp=5; IntAct=EBI-81196, EBI-15626132;
CC Q9Y6Q9; P48281: Vdr; Xeno; NbExp=2; IntAct=EBI-81196, EBI-346797;
CC Q9Y6Q9-5; Q96CV9: OPTN; NbExp=3; IntAct=EBI-11057583, EBI-748974;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly cytoplasmic and
CC weakly nuclear. Upon TNF activation and subsequent phosphorylation, it
CC translocates from the cytoplasm to the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9Y6Q9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6Q9-2; Sequence=VSP_003407;
CC Name=3;
CC IsoId=Q9Y6Q9-3; Sequence=VSP_003405, VSP_003407, VSP_003408;
CC Name=4;
CC IsoId=Q9Y6Q9-4; Sequence=VSP_003405, VSP_003406, VSP_003407,
CC VSP_003408;
CC Name=5;
CC IsoId=Q9Y6Q9-5; Sequence=VSP_003408;
CC -!- TISSUE SPECIFICITY: Widely expressed. High expression in heart,
CC skeletal muscle, pancreas and placenta. Low expression in brain, and
CC very low in lung, liver and kidney.
CC -!- DOMAIN: Contains three Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Motifs 1 and
CC 2 are essential for the association with nuclear receptors, and
CC constitute the RID domain (Receptor-interacting domain).
CC -!- PTM: Acetylated by CREBBP. Acetylation occurs in the RID domain, and
CC disrupts the interaction with nuclear receptors and regulates its
CC function. {ECO:0000269|PubMed:10490106}.
CC -!- PTM: Methylated by CARM1. {ECO:0000250}.
CC -!- PTM: Phosphorylated by IKK complex. Regulated its function.
CC Phosphorylation at Ser-601 by CK1 promotes coactivator function.
CC {ECO:0000269|PubMed:11971985, ECO:0000269|PubMed:19339517}.
CC -!- POLYMORPHISM: The length of the poly-Gln region is polymorphic in the
CC normal population. {ECO:0000269|PubMed:9727751}.
CC -!- MISCELLANEOUS: NCOA3 is frequently amplified or overexpressed in breast
CC and ovarian cancers.
CC -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NCOA3ID505ch20q13.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ncoa3/";
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DR EMBL; AF016031; AAC51849.1; -; mRNA.
DR EMBL; AF036892; AAB92368.1; -; mRNA.
DR EMBL; AF012108; AAC51677.1; -; mRNA.
DR EMBL; AF010227; AAC51663.1; -; mRNA.
DR EMBL; EF488684; ABO43042.1; -; Genomic_DNA.
DR EMBL; AL034418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75698.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75702.1; -; Genomic_DNA.
DR EMBL; BC119001; AAI19002.1; -; mRNA.
DR CCDS; CCDS13406.1; -. [Q9Y6Q9-5]
DR CCDS; CCDS13407.1; -. [Q9Y6Q9-1]
DR CCDS; CCDS54472.1; -. [Q9Y6Q9-3]
DR PIR; T03851; T03851.
DR RefSeq; NP_001167559.1; NM_001174088.1. [Q9Y6Q9-3]
DR RefSeq; NP_006525.2; NM_006534.3. [Q9Y6Q9-5]
DR RefSeq; NP_858045.1; NM_181659.2. [Q9Y6Q9-1]
DR PDB; 1KBH; NMR; -; A=1045-1091.
DR PDB; 3L3X; X-ray; 1.55 A; B=618-629.
DR PDB; 3L3Z; X-ray; 2.00 A; B=735-746.
DR PDB; 6ES7; NMR; -; A=1045-1086.
DR PDB; 6SQC; X-ray; 2.28 A; B=1045-1091.
DR PDBsum; 1KBH; -.
DR PDBsum; 3L3X; -.
DR PDBsum; 3L3Z; -.
DR PDBsum; 6ES7; -.
DR PDBsum; 6SQC; -.
DR AlphaFoldDB; Q9Y6Q9; -.
DR BMRB; Q9Y6Q9; -.
DR SMR; Q9Y6Q9; -.
DR BioGRID; 113841; 165.
DR CORUM; Q9Y6Q9; -.
DR DIP; DIP-30876N; -.
DR ELM; Q9Y6Q9; -.
DR IntAct; Q9Y6Q9; 92.
DR MINT; Q9Y6Q9; -.
DR STRING; 9606.ENSP00000361066; -.
DR BindingDB; Q9Y6Q9; -.
DR ChEMBL; CHEMBL1615382; -.
DR MoonDB; Q9Y6Q9; Predicted.
DR GlyGen; Q9Y6Q9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y6Q9; -.
DR PhosphoSitePlus; Q9Y6Q9; -.
DR SwissPalm; Q9Y6Q9; -.
DR BioMuta; NCOA3; -.
DR DMDM; 23396777; -.
DR CPTAC; CPTAC-1256; -.
DR CPTAC; CPTAC-1257; -.
DR EPD; Q9Y6Q9; -.
DR jPOST; Q9Y6Q9; -.
DR MassIVE; Q9Y6Q9; -.
DR MaxQB; Q9Y6Q9; -.
DR PaxDb; Q9Y6Q9; -.
DR PeptideAtlas; Q9Y6Q9; -.
DR PRIDE; Q9Y6Q9; -.
DR ProteomicsDB; 86766; -. [Q9Y6Q9-1]
DR ProteomicsDB; 86767; -. [Q9Y6Q9-2]
DR ProteomicsDB; 86768; -. [Q9Y6Q9-3]
DR ProteomicsDB; 86769; -. [Q9Y6Q9-4]
DR ProteomicsDB; 86770; -. [Q9Y6Q9-5]
DR Antibodypedia; 4069; 596 antibodies from 45 providers.
DR DNASU; 8202; -.
DR Ensembl; ENST00000371997.3; ENSP00000361065.3; ENSG00000124151.19. [Q9Y6Q9-3]
DR Ensembl; ENST00000371998.8; ENSP00000361066.3; ENSG00000124151.19. [Q9Y6Q9-1]
DR Ensembl; ENST00000372004.7; ENSP00000361073.1; ENSG00000124151.19. [Q9Y6Q9-5]
DR GeneID; 8202; -.
DR KEGG; hsa:8202; -.
DR MANE-Select; ENST00000371998.8; ENSP00000361066.3; NM_181659.3; NP_858045.1.
DR UCSC; uc002xtk.4; human. [Q9Y6Q9-1]
DR CTD; 8202; -.
DR DisGeNET; 8202; -.
DR GeneCards; NCOA3; -.
DR HGNC; HGNC:7670; NCOA3.
DR HPA; ENSG00000124151; Low tissue specificity.
DR MIM; 601937; gene.
DR neXtProt; NX_Q9Y6Q9; -.
DR OpenTargets; ENSG00000124151; -.
DR PharmGKB; PA31472; -.
DR VEuPathDB; HostDB:ENSG00000124151; -.
DR eggNOG; KOG3561; Eukaryota.
DR GeneTree; ENSGT00950000183021; -.
DR HOGENOM; CLU_001988_0_0_1; -.
DR InParanoid; Q9Y6Q9; -.
DR OMA; RGPPESK; -.
DR OrthoDB; 59971at2759; -.
DR PhylomeDB; Q9Y6Q9; -.
DR TreeFam; TF332652; -.
DR BRENDA; 2.3.1.48; 2681.
DR PathwayCommons; Q9Y6Q9; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; Q9Y6Q9; -.
DR SIGNOR; Q9Y6Q9; -.
DR BioGRID-ORCS; 8202; 27 hits in 1100 CRISPR screens.
DR ChiTaRS; NCOA3; human.
DR EvolutionaryTrace; Q9Y6Q9; -.
DR GeneWiki; Nuclear_receptor_coactivator_3; -.
DR GenomeRNAi; 8202; -.
DR Pharos; Q9Y6Q9; Tchem.
DR PRO; PR:Q9Y6Q9; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9Y6Q9; protein.
DR Bgee; ENSG00000124151; Expressed in endometrium epithelium and 214 other tissues.
DR Genevisible; Q9Y6Q9; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IBA:GO_Central.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; NAS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0043697; P:cell dedifferentiation; ISS:UniProtKB.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:BHF-UCL.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:UniProtKB.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0035624; P:receptor transactivation; TAS:UniProtKB.
DR GO; GO:2000035; P:regulation of stem cell division; ISS:UniProtKB.
DR CDD; cd00130; PAS; 1.
DR DisProt; DP00343; -.
DR Gene3D; 4.10.280.10; -; 1.
DR Gene3D; 6.10.140.410; -; 1.
DR IDEAL; IID00110; -.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR010011; NCO_DUF1518.
DR InterPro; IPR032565; NCOA2/3_DUF4927.
DR InterPro; IPR028818; NCOA3.
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:SF3; PTHR10684:SF3; 1.
DR Pfam; PF07469; DUF1518; 1.
DR Pfam; PF16279; DUF4927; 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; 1.
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; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1424
FT /note="Nuclear receptor coactivator 3"
FT /id="PRO_0000094406"
FT DOMAIN 25..82
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 110..180
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1093
FT /note="Interaction with CREBBP"
FT /evidence="ECO:0000269|PubMed:9346901"
FT REGION 1097..1304
FT /note="Acetyltransferase"
FT REGION 1273..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 685..689
FT /note="LXXLL motif 1"
FT MOTIF 738..742
FT /note="LXXLL motif 2"
FT MOTIF 1057..1061
FT /note="LXXLL motif 3"
FT COMPBIAS 503..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09000"
FT MOD_RES 601
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:19339517"
FT MOD_RES 616
FT /note="N6-acetyllysine; by CREBBP"
FT /evidence="ECO:0000269|PubMed:10490106"
FT MOD_RES 619
FT /note="N6-acetyllysine; by CREBBP"
FT /evidence="ECO:0000269|PubMed:10490106"
FT MOD_RES 620
FT /note="N6-acetyllysine; by CREBBP"
FT /evidence="ECO:0000269|PubMed:10490106"
FT MOD_RES 687
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09000"
FT MOD_RES 867
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1171
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1177
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1188
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 321
FT /note="E -> EVTSDGIFSPT (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9267036"
FT /id="VSP_003405"
FT VAR_SEQ 837..901
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9267036"
FT /id="VSP_003406"
FT VAR_SEQ 903..917
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9267036,
FT ECO:0000303|PubMed:9346901"
FT /id="VSP_003407"
FT VAR_SEQ 1214..1217
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9238002, ECO:0000303|PubMed:9252329,
FT ECO:0000303|PubMed:9267036"
FT /id="VSP_003408"
FT VARIANT 218
FT /note="R -> C (in dbSNP:rs6094752)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_053527"
FT VARIANT 220
FT /note="R -> I (in dbSNP:rs72645252)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_060695"
FT VARIANT 369
FT /note="L -> F (in dbSNP:rs6094756)"
FT /id="VAR_053528"
FT VARIANT 460
FT /note="G -> R (in dbSNP:rs1052765)"
FT /id="VAR_013831"
FT VARIANT 556
FT /note="I -> V (in dbSNP:rs72645272)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_060696"
FT VARIANT 559
FT /note="P -> S (in dbSNP:rs2230781)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_013832"
FT VARIANT 586
FT /note="Q -> H (in dbSNP:rs2230782)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_013833"
FT VARIANT 777
FT /note="S -> A (in dbSNP:rs2230783)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_053529"
FT VARIANT 1247
FT /note="M -> K (in dbSNP:rs72645299)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_060697"
FT VARIANT 1247
FT /note="M -> L (in dbSNP:rs72645298)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_060698"
FT VARIANT 1248..1250
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:9238002,
FT ECO:0000269|PubMed:9267036"
FT /id="VAR_013834"
FT MUTAGEN 616
FT /note="K->Q: Strongly reduces acetylation by CREBBP."
FT /evidence="ECO:0000269|PubMed:10490106"
FT MUTAGEN 619..620
FT /note="KK->QQ: Abolishes acetylation by CREBBP."
FT /evidence="ECO:0000269|PubMed:10490106"
FT MUTAGEN 647
FT /note="K->Q: Does not affect acetylation by CREBBP."
FT /evidence="ECO:0000269|PubMed:10490106"
FT MUTAGEN 681
FT /note="K->Q: Does not affect acetylation by CREBBP."
FT /evidence="ECO:0000269|PubMed:10490106"
FT MUTAGEN 687
FT /note="K->Q: Does not affect acetylation by CREBBP."
FT /evidence="ECO:0000269|PubMed:10490106"
FT MUTAGEN 700
FT /note="K->Q: Does not affect acetylation by CREBBP."
FT /evidence="ECO:0000269|PubMed:10490106"
FT MUTAGEN 708
FT /note="K->Q: Does not affect acetylation by CREBBP."
FT /evidence="ECO:0000269|PubMed:10490106"
FT CONFLICT 131..132
FT /note="DG -> EA (in Ref. 4; AAC51663)"
FT /evidence="ECO:0000305"
FT HELIX 619..626
FT /evidence="ECO:0007829|PDB:3L3X"
FT HELIX 736..743
FT /evidence="ECO:0007829|PDB:3L3Z"
FT HELIX 1049..1063
FT /evidence="ECO:0007829|PDB:6SQC"
FT HELIX 1067..1075
FT /evidence="ECO:0007829|PDB:6SQC"
FT HELIX 1078..1085
FT /evidence="ECO:0007829|PDB:6SQC"
FT HELIX 1086..1088
FT /evidence="ECO:0007829|PDB:1KBH"
SQ SEQUENCE 1424 AA; 155293 MW; 732CDF0423161679 CRC64;
MSGLGENLDP LASDSRKRKL PCDTPGQGLT CSGEKRRREQ ESKYIEELAE LISANLSDID
NFNVKPDKCA ILKETVRQIR QIKEQGKTIS NDDDVQKADV SSTGQGVIDK DSLGPLLLQA
LDGFLFVVNR DGNIVFVSEN VTQYLQYKQE DLVNTSVYNI LHEEDRKDFL KNLPKSTVNG
VSWTNETQRQ KSHTFNCRML MKTPHDILED INASPEMRQR YETMQCFALS QPRAMMEEGE
DLQSCMICVA RRITTGERTF PSNPESFITR HDLSGKVVNI DTNSLRSSMR PGFEDIIRRC
IQRFFSLNDG QSWSQKRHYQ EAYLNGHAET PVYRFSLADG TIVTAQTKSK LFRNPVTNDR
HGFVSTHFLQ REQNGYRPNP NPVGQGIRPP MAGCNSSVGG MSMSPNQGLQ MPSSRAYGLA
DPSTTGQMSG ARYGGSSNIA SLTPGPGMQS PSSYQNNNYG LNMSSPPHGS PGLAPNQQNI
MISPRNRGSP KIASHQFSPV AGVHSPMASS GNTGNHSFSS SSLSALQAIS EGVGTSLLST
LSSPGPKLDN SPNMNITQPS KVSNQDSKSP LGFYCDQNPV ESSMCQSNSR DHLSDKESKE
SSVEGAENQR GPLESKGHKK LLQLLTCSSD DRGHSSLTNS PLDSSCKESS VSVTSPSGVS
SSTSGGVSST SNMHGSLLQE KHRILHKLLQ NGNSPAEVAK ITAEATGKDT SSITSCGDGN
VVKQEQLSPK KKENNALLRY LLDRDDPSDA LSKELQPQVE GVDNKMSQCT SSTIPSSSQE
KDPKIKTETS EEGSGDLDNL DAILGDLTSS DFYNNSISSN GSHLGTKQQV FQGTNSLGLK
SSQSVQSIRP PYNRAVSLDS PVSVGSSPPV KNISAFPMLP KQPMLGGNPR MMDSQENYGS
SMGGPNRNVT VTQTPSSGDW GLPNSKAGRM EPMNSNSMGR PGGDYNTSLP RPALGGSIPT
LPLRSNSIPG ARPVLQQQQQ MLQMRPGEIP MGMGANPYGQ AAASNQLGSW PDGMLSMEQV
SHGTQNRPLL RNSLDDLVGP PSNLEGQSDE RALLDQLHTL LSNTDATGLE EIDRALGIPE
LVNQGQALEP KQDAFQGQEA AVMMDQKAGL YGQTYPAQGP PMQGGFHLQG QSPSFNSMMN
QMNQQGNFPL QGMHPRANIM RPRTNTPKQL RMQLQQRLQG QQFLNQSRQA LELKMENPTA
GGAAVMRPMM QPQVSSQQGF LNAQMVAQRS RELLSHHFRQ QRVAMMMQQQ QQQQQQQQQQ
QQQQQQQQQQ QQQQQQTQAF SPPPNVTASP SMDGLLAGPT MPQAPPQQFP YQPNYGMGQQ
PDPAFGRVSS PPNAMMSSRM GPSQNPMMQH PQAASIYQSS EMKGWPSGNL ARNSSFSQQQ
FAHQGNPAVY SMVHMNGSSG HMGQMNMNPM PMSGMPMGPD QKYC
