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 27-NOV-2024, entry version 204. 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=L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] CC + CoA + H(+); Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA- CC COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, CC 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: Present in a complex containing NCOA2, IKKA, IKKB, IKBKG and CC the histone acetyltransferase protein CREBBP (By similarity). Found in CC a complex containing NCOA3, AR and MAK (By similarity). Interacts with CC ATAD2; the interaction is enhanced by estradiol (By similarity). CC Interacts with CARM1 (PubMed:10381882). Interacts with CASP8AP2 (By CC similarity). Interacts with CSNK1D (By similarity). Interacts with DDX5 CC (By similarity). Interacts with ESR (By similarity). Interacts with CC ESRRB; mediates the interaction between ESRRB and RNA polymerase II CC complexes and allows NCOA3 corecruitment to ESRRB, KLF4, NANOG, and CC SOX2 enhancer regions to trigger ESRRB-dependent gene activation CC involved in self-renewal and pluripotency (PubMed:23019124). Interacts CC with NFKB1 (By similarity). Interacts with NPAS2 (By similarity). CC Interacts with NR3C1 (By similarity). Interacts with NR4A1/Nur77 (By CC similarity). Interacts with NR4A3 (PubMed:12709428). Interacts with CC PCAF (By similarity). Interacts with PPARA (By similarity). Interacts CC with PSMB9 (By similarity). Interacts with RARA (By similarity). CC Interacts with RXRA (By similarity). Interacts with THRA (By CC similarity). Interacts with VDR (By similarity). CC {ECO:0000250|UniProtKB:Q9Y6Q9, ECO:0000269|PubMed:10381882, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 GlyGen; O09000; 5 sites, 1 O-linked glycan (5 sites). DR iPTMnet; O09000; -. DR PhosphoSitePlus; O09000; -. DR SwissPalm; O09000; -. DR jPOST; O09000; -. DR PaxDb; 10090-ENSMUSP00000085416; -. DR PeptideAtlas; O09000; -. DR ProteomicsDB; 287454; -. DR Pumba; O09000; -. DR AGR; MGI:1276535; -. 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:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA: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:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI. DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0016922; F:nuclear receptor binding; IEA:InterPro. DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:MGI. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0043697; P:cell dedifferentiation; IMP:UniProtKB. 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:2000737; P:negative regulation of stem cell differentiation; IMP:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IMP:UniProtKB. 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 FunFam; 3.30.450.20:FF:000008; Nuclear receptor coactivator; 1. DR FunFam; 4.10.280.10:FF:000008; Nuclear receptor coactivator; 1. DR FunFam; 3.30.450.20:FF:000341; Nuclear receptor coactivator 3; 1. DR Gene3D; 6.10.140.410; -; 1. DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1. DR Gene3D; 3.30.450.20; PAS domain; 2. DR InterPro; IPR011598; bHLH_dom. DR InterPro; IPR036638; HLH_DNA-bd_sf. DR InterPro; IPR010011; NCO_DUF1518. DR InterPro; IPR032565; NCOA2/3_DUF4927. DR InterPro; IPR009110; Nuc_rcpt_coact. DR InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ. DR InterPro; IPR037077; Nuc_rcpt_coact_Ncoa_int_sf. DR InterPro; IPR017426; Nuclear_rcpt_coactivator. DR InterPro; IPR000014; PAS. DR InterPro; IPR035965; PAS-like_dom_sf. DR InterPro; IPR013767; PAS_fold. DR InterPro; IPR014935; SRC/p160_LXXLL. DR PANTHER; PTHR10684; NUCLEAR RECEPTOR COACTIVATOR; 1. DR PANTHER; PTHR10684:SF3; NUCLEAR RECEPTOR COACTIVATOR 3; 1. DR Pfam; PF07469; DUF1518; 1. DR Pfam; PF16279; DUF4927; 1. DR Pfam; PF16665; NCOA_u2; 1. DR Pfam; PF08815; Nuc_rec_co-act; 1. DR Pfam; PF00989; PAS; 1. DR Pfam; PF14598; PAS_11; 1. DR Pfam; PF08832; SRC-1; 1. DR PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1. DR SMART; SM01151; DUF1518; 1. DR SMART; SM00353; HLH; 1. DR SMART; SM00091; PAS; 1. DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1. DR SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2. DR PROSITE; PS50888; BHLH; 1. DR PROSITE; PS50112; PAS; 1. 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 //