NCOA3_MOUSE
ID NCOA3_MOUSE Reviewed; 1398 AA.
AC O09000; Q9CRD5;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Nuclear receptor coactivator 3;
DE Short=NCoA-3;
DE EC=2.3.1.48;
DE AltName: Full=Amplified in breast cancer-1 protein homolog;
DE Short=AIB-1;
DE AltName: Full=CBP-interacting protein;
DE Short=p/CIP;
DE Short=pCIP;
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=ACTR;
DE Short=TRAM-1;
GN Name=Ncoa3; Synonyms=Aib1, Pcip, Rac3, Tram1;
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], AND INTERACTION WITH CREBBP; ESR AND RARA.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1360-1398.
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
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 [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=10823921; DOI=10.1073/pnas.120166297;
RA Xu J., Liao L., Ning G., Yoshida-Komiya H., Deng C., O'Malley B.W.;
RT "The steroid receptor coactivator SRC-3 (p/CIP/RAC3/AIB1/ACTR/TRAM-1) is
RT required for normal growth, puberty, female reproductive function, and
RT mammary gland development.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6379-6384(2000).
RN [4]
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 [5]
RP METHYLATION BY CARM1.
RX PubMed=11701890; DOI=10.1126/science.1065961;
RA Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M.,
RA Evans R.M.;
RT "A transcriptional switch mediated by cofactor methylation.";
RL Science 294:2507-2511(2001).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-544; SER-720;
RP SER-847 AND SER-850, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-544; SER-562;
RP SER-847 AND SER-850, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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 [9]
RP INTERACTION WITH ESRRB.
RX PubMed=23019124; DOI=10.1101/gad.195545.112;
RA Percharde M., Lavial F., Ng J.H., Kumar V., Tomaz R.A., Martin N.,
RA Yeo J.C., Gil J., Prabhakar S., Ng H.H., Parker M.G., Azuara V.;
RT "Ncoa3 functions as an essential Esrrb coactivator to sustain embryonic
RT stem cell self-renewal and reprogramming.";
RL Genes Dev. 26:2286-2298(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-609; LYS-612 AND LYS-613, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1178; ARG-1184 AND ARG-1195, AND
RP 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).
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, probably via remodeling of chromatin. Involved in
CC the coactivation of different nuclear receptors, such as for steroids
CC (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin
CC D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase
CC activity. Also involved in the coactivation of the NF-kappa-B pathway
CC via its interaction with the NFKB1 subunit (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:10823921}.
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 -!- 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the histone acetyltransferase protein CREBBP.
CC These two proteins are present in a complex containing NCOA2, IKKA,
CC IKKB and IKBKG. Interacts with PCAF and NR3C1 (By similarity).
CC Interacts with CARM1. Interacts with CASP8AP2. Interacts with ATAD2 and
CC this interaction is enhanced by estradiol (By similarity). Interacts
CC with PSMB9. Binds to CSNK1D (By similarity). Found in a complex
CC containing NCOA3, AR and MAK. Interacts with DDX5. Interacts with NPAS2
CC (By similarity). Interacts with NR4A3 (via AF-1 domain)
CC (PubMed:12709428). Interacts with ESRRB; mediates the interaction
CC between ESRRB and RNA polymerase II complexes and allows NCOA3
CC corecruitment to ESRRB, KLF4, NANOG, and SOX2 enhancer regions to
CC trigger ESRRB-dependent gene activation involved in self-renewal and
CC pluripotency (PubMed:23019124). {ECO:0000250,
CC ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:23019124}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00981}. Note=Mainly cytoplasmic and
CC weakly nuclear. Upon TNF activation and subsequent phosphorylation, it
CC translocates from the cytoplasm to the nucleus (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Not expressed in all steroid sensitive tissues.
CC Highly expressed in the female reproductive system, in both oocyte and
CC smooth muscle cells of the oviduct, but not expressed in the uterine
CC endometrium. Highly expressed in mammary glands. Expressed moderately
CC in smooth muscle cells of both blood vessels and intestines, and weakly
CC expressed in hepatocytes. In brain, highly expressed in neurons of the
CC hippocampus, and in mitral cell and granule layers of the olfactory
CC bulb. Expressed moderately in the internal layer of cerebellum. Not
CC expressed in the spinal chord, cardiac muscle, skeletal muscle, thymus
CC and pancreas. {ECO:0000269|PubMed:10823921}.
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) (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Acetylated by CREBBP. Acetylation occurs in the RID domain, and
CC disrupts the interaction with nuclear receptors and regulates its
CC function (By similarity). {ECO:0000250}.
CC -!- PTM: Methylated by CARM1. {ECO:0000269|PubMed:11701890}.
CC -!- PTM: Phosphorylated by IKK complex. Regulated its function (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Defects result in diverse phenotype of postnatal
CC growth retardation, such as dwarfism, delayed puberty, abnormal
CC reproductive function and mammary gland growth retardation.
CC {ECO:0000269|PubMed:10823921}.
CC -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC family. {ECO:0000305}.
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DR EMBL; AF000581; AAC05020.1; -; mRNA.
DR EMBL; AK021229; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; O09000; -.
DR DIP; DIP-44921N; -.
DR IntAct; O09000; 16.
DR MINT; O09000; -.
DR STRING; 10090.ENSMUSP00000085416; -.
DR iPTMnet; O09000; -.
DR PhosphoSitePlus; O09000; -.
DR EPD; O09000; -.
DR jPOST; O09000; -.
DR PaxDb; O09000; -.
DR PeptideAtlas; O09000; -.
DR PRIDE; O09000; -.
DR ProteomicsDB; 287454; -.
DR MGI; MGI:1276535; Ncoa3.
DR eggNOG; KOG3561; Eukaryota.
DR InParanoid; O09000; -.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR ChiTaRS; Ncoa3; mouse.
DR PRO; PR:O09000; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O09000; protein.
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:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISO:MGI.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:MGI.
DR GO; GO:0042975; F:peroxisome proliferator activated 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:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
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:0043697; P:cell dedifferentiation; IMP:UniProtKB.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:MGI.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR GO; GO:0060713; P:labyrinthine layer morphogenesis; IGI:MGI.
DR GO; GO:0060744; P:mammary gland branching involved in thelarche; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; ISO:MGI.
DR GO; GO:0033145; P:positive regulation of intracellular steroid hormone receptor signaling pathway; ISO:MGI.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISO:MGI.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:2000035; P:regulation of stem cell division; IMP:UniProtKB.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IMP:MGI.
DR GO; GO:0072091; P:regulation of stem cell proliferation; IMP:MGI.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 4.10.280.10; -; 1.
DR Gene3D; 6.10.140.410; -; 1.
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 Acetylation; Activator; Acyltransferase; Cytoplasm; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6Q9"
FT CHAIN 2..1398
FT /note="Nuclear receptor coactivator 3"
FT /id="PRO_0000094407"
FT DOMAIN 26..83
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 111..181
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1113
FT /note="Interaction with CREBBP"
FT /evidence="ECO:0000250"
FT REGION 1104..1278
FT /note="Acetyltransferase"
FT REGION 1296..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 678..682
FT /note="LXXLL motif 1"
FT MOTIF 730..734
FT /note="LXXLL motif 2"
FT MOTIF 1041..1045
FT /note="LXXLL motif 3"
FT COMPBIAS 396..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6Q9"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 594
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6Q9"
FT MOD_RES 609
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 612
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 613
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 680
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6Q9"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6Q9"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1040
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6Q9"
FT MOD_RES 1178
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1184
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1195
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6Q9"
SQ SEQUENCE 1398 AA; 151574 MW; EF44E92735816C24 CRC64;
MSGLGESSLD PLAAESRKRK LPCDAPGQGL VYSGEKWRRE QESKYIEELA ELISANLSDI
DNFNVKPDKC AILKETVRQI RQIKEQGKTI SSDDDVQKAD VSSTGQGVID KDSLGPLLLQ
ALDGFLFVVN RDGNIVFVSE NVTQYLQYKQ EDLVNTSVYS ILHEPRRKDF LNTYQNPQLM
EFLGLMRTRD KKAPYILIVR MLMKTHDILE DVNASPETRQ RYETMQCFAL SQPRAMLEEG
EDLQCCMICV ARRVTAPFPS SPESFITRHD LSGKVVNIDT NSLRSSMRPG FEDIIRRCIQ
RFFSLNDGQS WSQKRHYQEA YVHGHAETPV YRFSLADGTI VSAQTKSKLF RNPVTNDRHG
FISTHFLQRE QNGYRPNPIP QDKGIRPPAA GCGVSMSPNQ NVQMMGSRTY GVPDPSNTGQ
MGGARYGASS SVASLTPGQS LQSPSSYQNS SYGLSMSSPP HGSPGLGPNQ QNIMISPRNR
GSPKMASHQF SPAAGAHSPM GPSGNTGSHS FSSSSLSALQ AISEGVGTSL LSTLSSPGPK
LDNSPNMNIS QPSKVSGQDS KSPLGLYCEQ NPVESSVCQS NSRDPQVKKE SKESSGEVSE
TPRGPLESKG HKKLLQLLTC SSDDRGHSSL TNSPLDPNCK DSSVSVTSPS GVSSSTSGTV
SSTSNVHGSL LQEKHRILHK LLQNGNSPAE VAKITAEATG KDTSSTASCG EGTTRQEQLS
PKKKENNALL RYLLDRDDPS DVLAKELQPQ ADSGDSKLSQ CSCSTNPSSG QEKDPKIKTE
TNDEVSGDLD NLDAILGDLT SSDFYNNPTN GGHPGAKQQM FAGPSSLGLR SPQPVQSVRP
PYNRAVSLDS PVSVGSGPPV KNVSAFPGLP KQPILAGNPR MMDSQENYGA NMGPNRNVPV
NPTSSPGDWG LANSRASRME PLASSPLGRT GADYSATLPR PAMGGSVPTL PLRSNRLPGA
RPSLQQQQQQ QQQQQQQQQQ QQQQQQQMLQ MRTGEIPMGM GVNPYSPAVQ SNQPGSWPEG
MLSMEQGPHG SQNRPLLRNS LDDLLGPPSN AEGQSDERAL LDQLHTFLSN TDATGLEEID
RALGIPELVN QGQALESKQD VFQGQEAAVM MDQKAALYGQ TYPAQGPPLQ GGFNLQGQSP
SFNSMMGQIS QQGSFPLQGM HPRAGLVRPR TNTPKQLRMQ LQQRLQGQQF LNQSRQALEM
KMENPAGTAV MRPMMPQAFF NAQMAAQQKR ELMSHHLQQQ RMAMMMSQPQ PQAFSPPPNV
TASPSMDGVL AGSAMPQAPP QQFPYPANYG MGQPPEPAFG RGSSPPSAMM SSRMGPSQNA
MVQHPQPTPM YQPSDMKGWP SGNLARNGSF PQQQFAPQGN PAAYNMVHMN SSGGHLGQMA
MTPMPMSGMP MGPDQKYC
