NONO_MOUSE
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 03-AUG-2022, entry version 182.
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; 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.
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-ARNTL/BMAL1 heterodimer
CC (PubMed:22966205). Important for the functional organization of
CC GABAergic synapses (PubMed:26571461). Plays a specific and important
CC role in the regulation of synaptic RNAs and GPHN/gephyrin scaffold
CC structure, through the regulation of GABRA2 transcript
CC (PubMed:26571461). Plays a key role during neuronal differentiation by
CC recruiting TET1 to genomic loci and thereby regulating 5-
CC hydroxymethylcytosine levels (PubMed:32286661). Plays a role in the
CC regulation of DNA virus-mediated innate immune response by assembling
CC into the HDP-RNP complex, a complex that serves as a platform for IRF3
CC phosphorylation and subsequent innate immune response activation
CC through the cGAS-STING pathway (By similarity).
CC {ECO:0000250|UniProtKB:Q15233, ECO:0000269|PubMed:22966205,
CC ECO:0000269|PubMed:26571461, ECO:0000269|PubMed:32286661,
CC ECO:0000269|PubMed:8355702, 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
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};
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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; 75.
DR DIP; DIP-34308N; -.
DR ELM; Q99K48; -.
DR IntAct; Q99K48; 8.
DR MINT; Q99K48; -.
DR STRING; 10090.ENSMUSP00000033673; -.
DR iPTMnet; Q99K48; -.
DR PhosphoSitePlus; Q99K48; -.
DR SwissPalm; Q99K48; -.
DR EPD; Q99K48; -.
DR jPOST; Q99K48; -.
DR MaxQB; Q99K48; -.
DR PaxDb; Q99K48; -.
DR PeptideAtlas; Q99K48; -.
DR PRIDE; Q99K48; -.
DR ProteomicsDB; 252988; -. [Q99K48-1]
DR ProteomicsDB; 252989; -. [Q99K48-2]
DR TopDownProteomics; Q99K48-1; -. [Q99K48-1]
DR Antibodypedia; 13516; 565 antibodies from 43 providers.
DR DNASU; 53610; -.
DR Ensembl; ENSMUST00000033673; ENSMUSP00000033673; ENSMUSG00000031311. [Q99K48-1]
DR GeneID; 53610; -.
DR KEGG; mmu:53610; -.
DR UCSC; uc009txr.2; mouse. [Q99K48-2]
DR UCSC; uc009txs.2; mouse. [Q99K48-1]
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; NHTPRKQ; -.
DR PhylomeDB; Q99K48; -.
DR TreeFam; TF315795; -.
DR BioGRID-ORCS; 53610; 11 hits in 109 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 208 other tissues.
DR ExpressionAtlas; Q99K48; baseline and differential.
DR Genevisible; Q99K48; MM.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0002218; P:activation of innate immune response; ISO:MGI.
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:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12588; RRM1_p54nrb; 1.
DR Gene3D; 3.30.70.330; -; 2.
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 Pfam; PF08075; NOPS; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
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
