ID NONO_MOUSE Reviewed; 473 AA. AC Q99K48; Q63887; Q9CYQ4; Q9DBP2; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 3. DT 27-MAR-2024, entry version 191. DE RecName: Full=Non-POU domain-containing octamer-binding protein {ECO:0000303|PubMed:8355702}; DE Short=NonO protein {ECO:0000303|PubMed:8355702}; GN Name=Nono {ECO:0000303|PubMed:8355702, ECO:0000312|MGI:MGI:1855692}; 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 1), PROTEIN SEQUENCE OF 195-201; RP 260-274; 300-306; 387-400 AND 438-445, AND FUNCTION. RX PubMed=8355702; DOI=10.1128/mcb.13.9.5593-5603.1993; RA Yang Y.-S., Hanke J.H., Carayannopoulos L., Craft C.M., Capra J.D., RA Tucker P.W.; RT "NonO, a non-POU-domain-containing, octamer-binding protein, is the RT mammalian homolog of Drosophila nonAdiss."; RL Mol. Cell. Biol. 13:5593-5603(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Embryo, and Lung; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J, and FVB/N; RC TISSUE=Mammary tumor, and Olfactory epithelium; 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 [4] RP PROTEIN SEQUENCE OF 298-312, AND INTERACTION WITH SPI1 AND SPIB. RX PubMed=8626664; DOI=10.1074/jbc.271.19.11177; RA Hallier M., Tavitian A., Moreau-Gachelin F.; RT "The transcription factor Spi-1/PU.1 binds RNA and interferes with the RNA- RT binding protein p54nrb."; RL J. Biol. Chem. 271:11177-11181(1996). RN [5] RP FUNCTION IN TRANSCRIPTIONAL REGULATION, AND DNA-BINDING. RX PubMed=9001221; DOI=10.1128/mcb.17.2.677; RA Basu A., Dong B., Krainer A.R., Howe C.C.; RT "The intracisternal A-particle proximal enhancer-binding protein activates RT transcription and is identical to the RNA- and DNA-binding protein RT p54nrb/NonO."; RL Mol. Cell. Biol. 17:677-686(1997). RN [6] RP INTERACTION WITH CPNE4. RX PubMed=12522145; DOI=10.1074/jbc.m212632200; RA Tomsig J.L., Snyder S.L., Creutz C.E.; RT "Identification of targets for calcium signaling through the copine family RT of proteins. Characterization of a coiled-coil copine-binding motif."; RL J. Biol. Chem. 278:10048-10054(2003). RN [7] RP INTERACTION WITH PSPC1. RX PubMed=15140795; DOI=10.1095/biolreprod.104.028159; RA Myojin R., Kuwahara S., Yasaki T., Matsunaga T., Sakurai T., Kimura M., RA Uesugi S., Kurihara Y.; RT "Expression and functional significance of mouse paraspeckle protein 1 on RT spermatogenesis."; RL Biol. Reprod. 71:926-932(2004). RN [8] RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=15860628; DOI=10.1126/science.1107373; RA Brown S.A., Ripperger J., Kadener S., Fleury-Olela F., Vilbois F., RA Rosbash M., Schibler U.; RT "PERIOD1-associated proteins modulate the negative limb of the mammalian RT circadian oscillator."; RL Science 308:693-696(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-452, AND IDENTIFICATION BY RP 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-452, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Kidney, Lung, 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 [11] RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH PER1 AND PER2. RX PubMed=22966205; DOI=10.1128/mcb.00334-12; RA Kowalska E., Ripperger J.A., Muheim C., Maier B., Kurihara Y., Fox A.H., RA Kramer A., Brown S.A.; RT "Distinct roles of DBHS family members in the circadian transcriptional RT feedback loop."; RL Mol. Cell. Biol. 32:4585-4594(2012). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-5; LYS-11; LYS-200; RP LYS-297 AND LYS-373, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [13] RP FUNCTION, INTERACTION WITH TET1, SUBCELLULAR LOCATION, AND DISRUPTION RP PHENOTYPE. RX PubMed=32286661; DOI=10.1093/nar/gkaa213; RA Li W., Karwacki-Neisius V., Ma C., Tan L., Shi Y., Wu F., Shi Y.G.; RT "Nono deficiency compromises TET1 chromatin association and impedes RT neuronal differentiation of mouse embryonic stem cells."; RL Nucleic Acids Res. 48:4827-4838(2020). RN [14] RP STRUCTURE BY NMR OF 68-153. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the N-terminal RNA recognition motif of NonO."; RL Submitted (NOV-2005) to the PDB data bank. RN [15] RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=26571461; DOI=10.1038/nn.4169; RG DDD Study; RA Mircsof D., Langouet M., Rio M., Moutton S., Siquier-Pernet K., RA Bole-Feysot C., Cagnard N., Nitschke P., Gaspar L., Znidaric M., Alibeu O., RA Fritz A.K., Wolfer D.P., Schroeter A., Bosshard G., Rudin M., Koester C., RA Crestani F., Seebeck P., Boddaert N., Prescott K., Hines R., Moss S.J., RA Fritschy J.M., Munnich A., Amiel J., Brown S.A., Tyagarajan S.K., RA Colleaux L.; RT "Mutations in NONO lead to syndromic intellectual disability and inhibitory RT synaptic defects."; RL Nat. Neurosci. 18:1731-1736(2015). CC -!- FUNCTION: DNA- and RNA binding protein, involved in several nuclear CC processes. Binds the conventional octamer sequence in double-stranded CC DNA (PubMed:8355702). Also binds single-stranded DNA and RNA at a site CC independent of the duplex site (By similarity). Involved in pre-mRNA CC splicing, probably as a heterodimer with SFPQ (By similarity). CC Interacts with U5 snRNA, probably by binding to a purine-rich sequence CC located on the 3' side of U5 snRNA stem 1b (By similarity). Together CC with PSPC1, required for the formation of nuclear paraspeckles (By CC similarity). The SFPQ-NONO heteromer associated with MATR3 may play a CC role in nuclear retention of defective RNAs (By similarity). The SFPQ- CC NONO heteromer may be involved in DNA unwinding by modulating the CC function of topoisomerase I/TOP1 (By similarity). The SFPQ-NONO CC heteromer may be involved in DNA non-homologous end joining (NHEJ) CC required for double-strand break repair and V(D)J recombination and may CC stabilize paired DNA ends (By similarity). In vitro, the complex CC strongly stimulates DNA end joining, binds directly to the DNA CC substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to CC establish a functional preligation complex (By similarity). NONO is CC involved in transcriptional regulation (By similarity). The SFPQ-NONO- CC NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP- CC dependent transcriptional activity (By similarity). NONO binds to an CC enhancer element in long terminal repeats of endogenous intracisternal CC A particles (IAPs) and activates transcription (PubMed:9001221). CC Regulates the circadian clock by repressing the transcriptional CC activator activity of the CLOCK-BMAL1 heterodimer (PubMed:22966205). CC Important for the functional organization of GABAergic synapses CC (PubMed:26571461). Plays a specific and important role in the CC regulation of synaptic RNAs and GPHN/gephyrin scaffold structure, CC through the regulation of GABRA2 transcript (PubMed:26571461). Plays a CC key role during neuronal differentiation by recruiting TET1 to genomic CC loci and thereby regulating 5-hydroxymethylcytosine levels CC (PubMed:32286661). Plays a role in the regulation of DNA virus-mediated CC innate immune response by assembling into the HDP-RNP complex, a CC complex that serves as a platform for IRF3 phosphorylation and CC subsequent innate immune response activation through the cGAS-STING CC pathway (By similarity). {ECO:0000250|UniProtKB:Q15233, CC ECO:0000269|PubMed:22966205, ECO:0000269|PubMed:26571461, CC ECO:0000269|PubMed:32286661, ECO:0000269|PubMed:8355702, CC ECO:0000269|PubMed:9001221}. CC -!- SUBUNIT: Monomer and component of the SFPQ-NONO complex, which is CC probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) CC subunits. NONO is a component of spliceosome and U5.4/6 snRNP complexes CC (By similarity). Interacts with CPNE4 (via VWFA domain) CC (PubMed:12522145). Forms heterodimers with PSPC1; this involves CC formation of a coiled coil domain by helices from both proteins CC (PubMed:15140795). Part of complex consisting of SFPQ, NONO and MATR3. CC Part of a complex consisting of SFPQ, NONO and NR5A1. Part of a complex CC consisting of SFPQ, NONO and TOP1. Interacts with SPI1 and SPIB CC (PubMed:8626664). Interacts with RNF43 (By similarity). Interacts with CC PER1 and PER2 (PubMed:22966205). Part of the HDP-RNP complex composed CC of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, CC NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA. Interacts (via second RRM CC domain) with WASL; the interaction is direct. Component of a CC multiprotein complex with WASL and SFPQ (By similarity). Interacts with CC ERCC6 (By similarity). Interacts (via DNA-binding domain) with TET1 CC (PubMed:32286661). {ECO:0000250|UniProtKB:Q15233, CC ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:15140795, CC ECO:0000269|PubMed:22966205, ECO:0000269|PubMed:32286661, CC ECO:0000269|PubMed:8626664}. CC -!- INTERACTION: CC Q99K48; A0A087WPF7: Auts2; NbExp=4; IntAct=EBI-607499, EBI-27122375; CC Q99K48; P17433: Spi1; NbExp=3; IntAct=EBI-607499, EBI-607588; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15860628, CC ECO:0000269|PubMed:26571461}. Nucleus, nucleolus CC {ECO:0000250|UniProtKB:Q15233}. Nucleus speckle CC {ECO:0000250|UniProtKB:Q15233}. Chromosome CC {ECO:0000269|PubMed:32286661}. Note=Detected in punctate subnuclear CC structures often located adjacent to splicing speckles, called CC paraspeckles. {ECO:0000250|UniProtKB:Q15233}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q99K48-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99K48-2; Sequence=VSP_013981; CC -!- TISSUE SPECIFICITY: Expressed in liver and suprachiasmatic nuclei, CC hippocampus and neocortex (at protein level). Expression is strongest CC in neurons in CA1 and CA3 pyramidal regions and granule cells of the CC dentate gyrus. Detected in testis and kidney. CC {ECO:0000269|PubMed:15860628, ECO:0000269|PubMed:22966205, CC ECO:0000269|PubMed:26571461}. CC -!- DISRUPTION PHENOTYPE: Mutant mice display flattened nose and a smaller CC cerebellum. Behaviorally, mice show impaired spatial memory, as well as CC a marked anxiety phenotype and increased risk aversion CC (PubMed:26571461). Deletion leads to a significant dissociation of TET1 CC from chromatin and dysregulation of DNA hydroxymethylation of neuronal CC genes (PubMed:32286661). {ECO:0000269|PubMed:26571461, CC ECO:0000269|PubMed:32286661}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB23598.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB28857.1; Type=Frameshift; Evidence={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; S64860; AAB27887.1; -; mRNA. DR EMBL; AK004830; BAB23598.1; ALT_SEQ; mRNA. DR EMBL; AK013444; BAB28857.1; ALT_SEQ; mRNA. DR EMBL; AK028338; BAC25890.1; -; mRNA. DR EMBL; BC005465; AAH05465.1; -; mRNA. DR EMBL; BC083074; AAH83074.1; -; mRNA. DR CCDS; CCDS30316.1; -. [Q99K48-1] DR RefSeq; NP_001239447.1; NM_001252518.1. [Q99K48-1] DR RefSeq; NP_075633.2; NM_023144.2. [Q99K48-1] DR PDB; 2CPJ; NMR; -; A=68-153. DR PDB; 2RS8; NMR; -; A=68-153. DR PDBsum; 2CPJ; -. DR PDBsum; 2RS8; -. DR AlphaFoldDB; Q99K48; -. DR BMRB; Q99K48; -. DR SMR; Q99K48; -. DR BioGRID; 207330; 76. DR DIP; DIP-34308N; -. DR ELM; Q99K48; -. DR IntAct; Q99K48; 8. DR MINT; Q99K48; -. DR STRING; 10090.ENSMUSP00000033673; -. DR GlyGen; Q99K48; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q99K48; -. DR MetOSite; Q99K48; -. DR PhosphoSitePlus; Q99K48; -. DR SwissPalm; Q99K48; -. DR EPD; Q99K48; -. DR jPOST; Q99K48; -. DR MaxQB; Q99K48; -. DR PaxDb; 10090-ENSMUSP00000033673; -. DR PeptideAtlas; Q99K48; -. DR ProteomicsDB; 252988; -. [Q99K48-1] DR ProteomicsDB; 252989; -. [Q99K48-2] DR Pumba; Q99K48; -. DR TopDownProteomics; Q99K48-1; -. [Q99K48-1] DR Antibodypedia; 13516; 649 antibodies from 43 providers. DR DNASU; 53610; -. DR Ensembl; ENSMUST00000033673.7; ENSMUSP00000033673.7; ENSMUSG00000031311.18. [Q99K48-1] DR GeneID; 53610; -. DR KEGG; mmu:53610; -. DR UCSC; uc009txr.2; mouse. [Q99K48-2] DR UCSC; uc009txs.2; mouse. [Q99K48-1] DR AGR; MGI:1855692; -. DR CTD; 4841; -. DR MGI; MGI:1855692; Nono. DR VEuPathDB; HostDB:ENSMUSG00000031311; -. DR eggNOG; KOG0115; Eukaryota. DR GeneTree; ENSGT00940000154442; -. DR HOGENOM; CLU_027185_2_0_1; -. DR InParanoid; Q99K48; -. DR OMA; PNRPGEQ; -. DR OrthoDB; 5403433at2759; -. DR PhylomeDB; Q99K48; -. DR TreeFam; TF315795; -. DR BioGRID-ORCS; 53610; 11 hits in 114 CRISPR screens. DR ChiTaRS; Nono; mouse. DR EvolutionaryTrace; Q99K48; -. DR PRO; PR:Q99K48; -. DR Proteomes; UP000000589; Chromosome X. DR RNAct; Q99K48; Protein. DR Bgee; ENSMUSG00000031311; Expressed in undifferentiated genital tubercle and 211 other cell types or tissues. DR ExpressionAtlas; Q99K48; baseline and differential. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0001650; C:fibrillar center; ISO:MGI. DR GO; GO:0016363; C:nuclear matrix; ISO:MGI. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0042382; C:paraspeckles; ISO:MGI. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:BHF-UCL. DR GO; GO:0003682; F:chromatin binding; IDA:BHF-UCL. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0106222; F:lncRNA binding; ISO:MGI. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0002218; P:activation of innate immune response; ISO:MGI. DR GO; GO:1904385; P:cellular response to angiotensin; ISO:MGI. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISO:MGI. DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR CDD; cd12946; NOPS_p54nrb_PSF_PSPC1; 1. DR CDD; cd12588; RRM1_p54nrb; 1. DR Gene3D; 3.30.70.330; -; 2. DR Gene3D; 6.10.250.1170; -; 1. DR InterPro; IPR012975; NOPS. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR034552; p54nrb_RRM1. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR23189:SF15; NON-POU DOMAIN-CONTAINING OCTAMER-BINDING PROTEIN; 1. DR PANTHER; PTHR23189; RNA RECOGNITION MOTIF-CONTAINING; 1. DR Pfam; PF08075; NOPS; 1. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 2. DR Genevisible; Q99K48; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; KW Biological rhythms; Chromosome; Coiled coil; Direct protein sequencing; KW DNA damage; DNA recombination; DNA repair; DNA-binding; Immunity; KW Innate immunity; Isopeptide bond; Methylation; mRNA processing; KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Repressor; RNA-binding; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..473 FT /note="Non-POU domain-containing octamer-binding protein" FT /id="PRO_0000081684" FT DOMAIN 76..143 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 150..231 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 1..53 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 56..375 FT /note="DBHS" FT /evidence="ECO:0000250" FT REGION 445..473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 270..374 FT /evidence="ECO:0000255" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 5 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 11 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 149 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT MOD_RES 200 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 264 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT MOD_RES 297 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 373 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 430 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT MOD_RES 442 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT MOD_RES 452 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 458 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 5 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 62 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 98 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 101 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 128 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 192 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 200 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 245 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 251 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 373 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT CROSSLNK 469 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q15233" FT VAR_SEQ 220..473 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_013981" FT CONFLICT 76 FT /note="S -> T (in Ref. 2; BAB28857)" FT /evidence="ECO:0000305" FT CONFLICT 117 FT /note="R -> N (in Ref. 2; BAB28857)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="A -> V (in Ref. 1; AAB27887)" FT /evidence="ECO:0000305" FT CONFLICT 153 FT /note="T -> K (in Ref. 2; BAB28857)" FT /evidence="ECO:0000305" FT CONFLICT 167 FT /note="E -> G (in Ref. 2; BAB28857)" FT /evidence="ECO:0000305" FT CONFLICT 183 FT /note="V -> E (in Ref. 2; BAB28857)" FT /evidence="ECO:0000305" FT CONFLICT 188 FT /note="R -> W (in Ref. 2; BAB28857)" FT /evidence="ECO:0000305" FT CONFLICT 203..204 FT /note="AR -> VL (in Ref. 2; BAB28857)" FT /evidence="ECO:0000305" FT CONFLICT 222 FT /note="R -> W (in Ref. 1; AAB27887)" FT /evidence="ECO:0000305" FT STRAND 77..82 FT /evidence="ECO:0007829|PDB:2CPJ" FT HELIX 89..95 FT /evidence="ECO:0007829|PDB:2CPJ" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:2RS8" FT STRAND 103..108 FT /evidence="ECO:0007829|PDB:2CPJ" FT TURN 109..112 FT /evidence="ECO:0007829|PDB:2CPJ" FT STRAND 113..117 FT /evidence="ECO:0007829|PDB:2CPJ" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:2CPJ" FT HELIX 122..131 FT /evidence="ECO:0007829|PDB:2CPJ" FT STRAND 142..147 FT /evidence="ECO:0007829|PDB:2CPJ" SQ SEQUENCE 473 AA; 54541 MW; F65E6AE25D471A38 CRC64; MQSNKAFNLE KQNHTPRKHH QHHHQQHHQQ QQQQQQQQPP PPIPANGQQA SSQNEGLTID LKNFRKPGEK TFTQRSRLFV GNLPPDITEE EMRKLFEKYG KAGEVFIHKD KGFGFIRLET RTLAEIAKVE LDNMPLRGKQ LRVRFACHSA SLTVRNLPQY VSNELLEEAF SVFGQVERAV VIVDDRGRPS GKGIVEFSGK PAARKALDRC SEGSFLLTTF PRPVTVEPMD QLDDEEGLPE KLVIKNQQFH KEREQPPRFA QPGSFEYEYA MRWKALIEME KQQQDQVDRN IKEAREKLEM EMEAARHEHQ VMLMRQDLMR RQEELRRMEE LHNQEVQKRK QLELRQEEER RRREEEMRRQ QEEMMRRQQE GFKGTFPDAR EQEIRMGQMA MGGAMGINNR GAMPPAPVPP GTPAPPGPAT MMPDGTLGLT PPTTERFGQA ATMEGIGAIG GTPPAFNRPA PGAEFAPNKR RRY //