ID NONO_HUMAN Reviewed; 471 AA. AC Q15233; B7Z4C2; D3DVV4; F5GYZ3; O00201; P30807; Q12786; Q9BQC5; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 4. DT 27-MAR-2024, entry version 234. DE RecName: Full=Non-POU domain-containing octamer-binding protein {ECO:0000303|PubMed:9393982}; DE Short=NonO protein {ECO:0000303|PubMed:9393982}; DE AltName: Full=54 kDa nuclear RNA- and DNA-binding protein {ECO:0000303|PubMed:9341872}; DE Short=p54(nrb) {ECO:0000303|PubMed:9341872}; DE Short=p54nrb {ECO:0000303|PubMed:9341872}; DE AltName: Full=55 kDa nuclear protein {ECO:0000303|PubMed:9360842}; DE Short=NMT55 {ECO:0000303|PubMed:9360842}; DE AltName: Full=DNA-binding p52/p100 complex, 52 kDa subunit {ECO:0000303|PubMed:8439294}; GN Name=NONO {ECO:0000303|PubMed:9393982, ECO:0000312|HGNC:HGNC:7871}; GN Synonyms=NRB54 {ECO:0000303|PubMed:9341872}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 252-267; RP 273-279 AND 283-289. RX PubMed=8371983; DOI=10.1093/nar/21.17.4085; RA Dong B., Horowitz D.S., Kobayashi R., Krainer A.R.; RT "Purification and cDNA cloning of HeLa cell p54nrb, a nuclear protein with RT two RNA recognition motifs and extensive homology to human splicing factor RT PSF and Drosophila NONA/BJ6."; RL Nucleic Acids Res. 21:4085-4092(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Mammary carcinoma; RX PubMed=9360842; DOI=10.1097/00019606-199708000-00005; RA Traish A.M., Huang Y.-H., Ashba J., Pronovost M., Pavao M., McAneny D.B., RA Moreland R.B.; RT "Loss of expression of a 55 kDa nuclear protein (nmt55) in estrogen RT receptor-negative human breast cancer."; RL Diagn. Mol. Pathol. 6:209-221(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RC TISSUE=Blood; RX PubMed=9341872; DOI=10.1007/s004390050553; RA Peters U., Haberhausen G., Kostrzewa M., Nolte D., Mueller U.; RT "AFX1 and p54nrb: fine mapping, genomic structure, and exclusion as RT candidate genes of X-linked dystonia parkinsonism."; RL Hum. Genet. 100:569-572(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Honore B., Rasmussen H.H., Celis J.E.; RT "54 kDa human protein."; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix, Kidney, Muscle, and Skin; 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 [10] RP PROTEIN SEQUENCE OF 2-21 AND 133-153, BLOCKAGE OF N-TERMINUS, AND SUBUNIT. RX PubMed=8439294; DOI=10.1042/bj2900267; RA Zhang W.-W., Zhang L.-X., Busch R.K., Farres J., Busch H.; RT "Purification and characterization of a DNA-binding heterodimer of 52 and RT 100 kDa from HeLa cells."; RL Biochem. J. 290:267-272(1993). RN [11] RP PROTEIN SEQUENCE OF 76-91; 127-135; 177-184; 257-270 AND 435-456, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [12] RP CHROMOSOMAL TRANSLOCATION WITH TFE3. RX PubMed=9393982; DOI=10.1038/sj.onc.1201394; RA Clark J., Lu Y.-J., Sidhar S.K., Parker C., Gill S., Smedley D., RA Hamoudi R., Linehan W.M., Shipley J., Cooper C.S.; RT "Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3 gene in RT papillary renal cell carcinoma."; RL Oncogene 15:2233-2239(1997). RN [13] RP IDENTIFICATION IN A COMPLEX WITH SFPQ AND TOP1. RX PubMed=9756848; DOI=10.1074/jbc.273.41.26261; RA Straub T., Grue P., Uhse A., Lisby M., Knudsen B.R., Tange T.O., RA Westergaard O., Boege F.; RT "The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I activity by a RT direct interaction."; RL J. Biol. Chem. 273:26261-26264(1998). RN [14] RP FUNCTION IN DNA UNWINDING. RX PubMed=10858305; DOI=10.1021/bi992898e; RA Straub T., Knudsen B.R., Boege F.; RT "PSF/p54(nrb) stimulates 'jumping' of DNA topoisomerase I between separate RT DNA helices."; RL Biochemistry 39:7552-7558(2000). RN [15] RP FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, AND IDENTIFICATION IN RP A COMPLEX WITH NONO AND MATR3. RX PubMed=11525732; DOI=10.1016/s0092-8674(01)00466-4; RA Zhang Z., Carmichael G.G.; RT "The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates RT the nuclear retention of promiscuously A-to-I edited RNAs."; RL Cell 106:465-475(2001). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION IN TRANSCRIPTION REGULATION, RP AND IDENTIFICATION IN A COMPLEX WITH SFPQ AND NR5A1. RX PubMed=11897684; DOI=10.1210/endo.143.4.8748; RA Sewer M.B., Nguyen V.Q., Huang C.J., Tucker P.W., Kagawa N., Waterman M.R.; RT "Transcriptional activation of human CYP17 in H295R adrenocortical cells RT depends on complex formation among p54(nrb)/NonO, protein-associated RT splicing factor, and SF-1, a complex that also participates in repression RT of transcription."; RL Endocrinology 143:1280-1290(2002). RN [17] RP FUNCTION, INTERACTION WITH PSQF AND U5 SNRNA, AND IDENTIFICATION IN U5/4/6 RP SNRNP AND SPLICEOSOME COMPLEXES. RX PubMed=12403470; DOI=10.1017/s1355838202022070; RA Peng R., Dye B.T., Perez I., Barnard D.C., Thompson A.B., Patton J.G.; RT "PSF and p54nrb bind a conserved stem in U5 snRNA."; RL RNA 8:1334-1347(2002). RN [18] RP FUNCTION IN DNA REPAIR, IDENTIFICATION BY MASS SPECTROMETRY, DNA-BINDING, RP AND SUBUNIT. RX PubMed=15590677; DOI=10.1074/jbc.m412758200; RA Bladen C.L., Udayakumar D., Takeda Y., Dynan W.S.; RT "Identification of the polypyrimidine tract binding protein-associated RT splicing factor.p54(nrb) complex as a candidate DNA double-strand break RT rejoining factor."; RL J. Biol. Chem. 280:5205-5210(2005). RN [19] RP INTERACTION WITH PSPC1. RX PubMed=16148043; DOI=10.1091/mbc.e05-06-0587; RA Fox A.H., Bond C.S., Lamond A.I.; RT "P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles in an RT RNA-dependent manner."; RL Mol. Biol. Cell 16:5304-5315(2005). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [22] RP IDENTIFICATION IN A COMPLEX WITH SFPQ AND WASL, AND INTERACTION WITH WASL. RX PubMed=16767080; DOI=10.1038/ncb1433; RA Wu X., Yoo Y., Okuhama N.N., Tucker P.W., Liu G., Guan J.L.; RT "Regulation of RNA-polymerase-II-dependent transcription by N-WASP and its RT nuclear-binding partners."; RL Nat. Cell Biol. 8:756-763(2006). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200; RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling RT network: indicating the involvement of ribonucleoside-diphosphate reductase RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal RT transduction."; RL Mol. Cell. Proteomics 6:1952-1967(2007). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [28] RP INTERACTION WITH RNF43. RX PubMed=18655028; DOI=10.1002/pmic.200800083; RA Miyamoto K., Sakurai H., Sugiura T.; RT "Proteomic identification of a PSF/p54nrb heterodimer as RNF43 oncoprotein- RT interacting proteins."; RL Proteomics 8:2907-2910(2008). RN [29] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [31] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-11 AND LYS-198, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; THR-440 AND THR-450, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [33] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [35] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=22002106; DOI=10.1074/mcp.m111.013680; RA Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.; RT "Systematic analysis of protein pools, isoforms, and modifications RT affecting turnover and subcellular localization."; RL Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012). RN [36] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; SER-262 AND THR-450, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [37] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [38] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-456, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [39] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5 AND LYS-371, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [40] RP INTERACTION WITH ERCC6. RX PubMed=26030138; DOI=10.1371/journal.pone.0128558; RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G., RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.; RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin RT Dynamics."; RL PLoS ONE 10:E0128558-E0128558(2015). RN [41] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [42] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRKDC; XRCC5; XRCC6; RP SFPQ; HEXIM1; PSPC1; RBM14 AND MATR3. RX PubMed=28712728; DOI=10.1016/j.molcel.2017.06.020; RA Morchikh M., Cribier A., Raffel R., Amraoui S., Cau J., Severac D., RA Dubois E., Schwartz O., Bennasser Y., Benkirane M.; RT "HEXIM1 and NEAT1 Long non-coding RNA form a multi-subunit complex that RT regulates DNA-mediated innate immune response."; RL Mol. Cell 67:387-399(2017). RN [43] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-60; LYS-96; LYS-99; RP LYS-126; LYS-190; LYS-198; LYS-243; LYS-249; LYS-371 AND LYS-467, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [44] RP FUNCTION, INTERACTION WITH HIV-1 CAPSID PROTEIN P24 (MICROBIAL INFECTION), RP AND INTERACTION WITH HIV-2 CAPSID PROTEIN P24 (MICROBIAL INFECTION). RX PubMed=30270045; DOI=10.1016/j.cell.2018.08.062; RA Lahaye X., Gentili M., Silvin A., Conrad C., Picard L., Jouve M., Zueva E., RA Maurin M., Nadalin F., Knott G.J., Zhao B., Du F., Rio M., Amiel J., RA Fox A.H., Li P., Etienne L., Bond C.S., Colleaux L., Manel N.; RT "NONO detects the nuclear HIV capsid to promote cGAS-mediated innate immune RT activation."; RL Cell 175:488-501(2018). RN [45] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 53-312 IN COMPLEX WITH PSPC1, RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-267 AND TRP-271. RX PubMed=22416126; DOI=10.1073/pnas.1120792109; RA Passon D.M., Lee M., Rackham O., Stanley W.A., Sadowska A., Filipovska A., RA Fox A.H., Bond C.S.; RT "Structure of the heterodimer of human NONO and paraspeckle protein RT component 1 and analysis of its role in subnuclear body formation."; RL Proc. Natl. Acad. Sci. U.S.A. 109:4846-4850(2012). RN [46] RP INVOLVEMENT IN MRXS34, AND FUNCTION. 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 (PubMed:11525732, PubMed:12403470, PubMed:26571461). Binds CC the conventional octamer sequence in double-stranded DNA CC (PubMed:11525732, PubMed:12403470, PubMed:26571461). Also binds single- CC stranded DNA and RNA at a site independent of the duplex site CC (PubMed:11525732, PubMed:12403470, PubMed:26571461). Involved in pre- CC mRNA splicing, probably as a heterodimer with SFPQ (PubMed:11525732, CC PubMed:12403470, PubMed:26571461). Interacts with U5 snRNA, probably by CC binding to a purine-rich sequence located on the 3' side of U5 snRNA CC stem 1b (PubMed:12403470). Together with PSPC1, required for the CC formation of nuclear paraspeckles (PubMed:22416126). The SFPQ-NONO CC heteromer associated with MATR3 may play a role in nuclear retention of CC defective RNAs (PubMed:11525732). The SFPQ-NONO heteromer may be CC involved in DNA unwinding by modulating the function of topoisomerase CC I/TOP1 (PubMed:10858305). The SFPQ-NONO heteromer may be involved in CC DNA non-homologous end joining (NHEJ) required for double-strand break CC repair and V(D)J recombination and may stabilize paired DNA ends CC (PubMed:15590677). In vitro, the complex strongly stimulates DNA end CC joining, binds directly to the DNA substrates and cooperates with the CC Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation CC complex (PubMed:15590677). NONO is involved in transcriptional CC regulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and CC regulates basal and cAMP-dependent transcriptional activity CC (PubMed:11897684). NONO binds to an enhancer element in long terminal CC repeats of endogenous intracisternal A particles (IAPs) and activates CC transcription (By similarity). Regulates the circadian clock by CC repressing the transcriptional activator activity of the CLOCK-BMAL1 CC heterodimer (By similarity). Important for the functional organization CC of GABAergic synapses (By similarity). 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 (By similarity). CC Plays a key role during neuronal differentiation by recruiting TET1 to CC genomic loci and thereby regulating 5-hydroxymethylcytosine levels (By CC similarity). 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 (PubMed:28712728, PubMed:30270045). Promotes activation of the CC cGAS-STING pathway in response to HIV-2 infection: acts by interacting CC with HIV-2 Capsid protein p24, thereby promoting detection of viral DNA CC by CGAS, leading to CGAS-mediated inmmune activation (PubMed:30270045). CC In contrast, the weak interaction with HIV-1 Capsid protein p24 does CC not allow activation of the cGAS-STING pathway (PubMed:30270045). CC {ECO:0000250|UniProtKB:Q99K48, ECO:0000269|PubMed:10858305, CC ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:11897684, CC ECO:0000269|PubMed:12403470, ECO:0000269|PubMed:15590677, CC ECO:0000269|PubMed:22416126, ECO:0000269|PubMed:26571461, CC ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:30270045}. 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 (PubMed:8439294, PubMed:15590677). NONO is a component of CC spliceosome and U5.4/6 snRNP complexes (PubMed:12403470). Interacts CC with CPNE4 (via VWFA domain) (By similarity). Forms heterodimers with CC PSPC1; this involves formation of a coiled coil domain by helices from CC both proteins (PubMed:16148043, PubMed:22416126). Part of complex CC consisting of SFPQ, NONO and MATR3 (PubMed:11525732). Part of a complex CC consisting of SFPQ, NONO and NR5A1 (PubMed:11897684). Part of a complex CC consisting of SFPQ, NONO and TOP1 (PubMed:9756848). Interacts with SPI1 CC and SPIB (By similarity). Interacts with RNF43 (PubMed:18655028). CC Interacts with PER1 and PER2 (By similarity). Part of the HDP-RNP CC complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle CC proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA CC (PubMed:28712728). Interacts (via second RRM domain) with WASL; the CC interaction is direct (PubMed:16767080). Component of a multiprotein CC complex with WASL and SFPQ (PubMed:16767080). Interacts with ERCC6 CC (PubMed:26030138). Interacts (via DNA-binding domain) with TET1 (By CC similarity). {ECO:0000250|UniProtKB:Q99K48, CC ECO:0000269|PubMed:11525732, ECO:0000269|PubMed:11897684, CC ECO:0000269|PubMed:12403470, ECO:0000269|PubMed:15590677, CC ECO:0000269|PubMed:16148043, ECO:0000269|PubMed:16767080, CC ECO:0000269|PubMed:18655028, ECO:0000269|PubMed:22416126, CC ECO:0000269|PubMed:26030138, ECO:0000269|PubMed:28712728, CC ECO:0000269|PubMed:8439294, ECO:0000269|PubMed:9756848}. CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-2 Capsid protein p24; CC interacts with high affinity (PubMed:30270045). Interacts with HIV-1 CC Capsid protein p24; interacts with low affinity (PubMed:30270045). CC {ECO:0000269|PubMed:30270045}. CC -!- INTERACTION: CC Q15233; Q9H3H3: C11orf68; NbExp=3; IntAct=EBI-350527, EBI-721765; CC Q15233; Q9H3H3-3: C11orf68; NbExp=3; IntAct=EBI-350527, EBI-12002214; CC Q15233; Q53ET0: CRTC2; NbExp=2; IntAct=EBI-350527, EBI-1181987; CC Q15233; P51114: FXR1; NbExp=2; IntAct=EBI-350527, EBI-713291; CC Q15233; Q15233: NONO; NbExp=5; IntAct=EBI-350527, EBI-350527; CC Q15233; Q13526: PIN1; NbExp=4; IntAct=EBI-350527, EBI-714158; CC Q15233; Q8WXF1: PSPC1; NbExp=11; IntAct=EBI-350527, EBI-1392258; CC Q15233; Q8WXF1-1: PSPC1; NbExp=7; IntAct=EBI-350527, EBI-15974663; CC Q15233; Q8WXF1-2: PSPC1; NbExp=4; IntAct=EBI-350527, EBI-12135327; CC Q15233; P23246: SFPQ; NbExp=5; IntAct=EBI-350527, EBI-355453; CC Q15233; Q8AZK7: EBNA-LP; Xeno; NbExp=2; IntAct=EBI-350527, EBI-1185167; CC Q15233-2; P26196: DDX6; NbExp=3; IntAct=EBI-10203843, EBI-351257; CC Q15233-2; P61968: LMO4; NbExp=3; IntAct=EBI-10203843, EBI-2798728; CC Q15233-2; Q13526: PIN1; NbExp=3; IntAct=EBI-10203843, EBI-714158; CC Q15233-2; P54646: PRKAA2; NbExp=3; IntAct=EBI-10203843, EBI-1383852; CC Q15233-2; Q8WXF1: PSPC1; NbExp=3; IntAct=EBI-10203843, EBI-1392258; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22416126, CC ECO:0000269|PubMed:28712728}. Nucleus, nucleolus. Nucleus speckle CC {ECO:0000269|PubMed:22416126, ECO:0000269|PubMed:28712728}. Chromosome CC {ECO:0000250|UniProtKB:Q99K48}. Note=Detected in punctate subnuclear CC structures often located adjacent to splicing speckles, called CC paraspeckles. {ECO:0000269|PubMed:22416126, CC ECO:0000269|PubMed:28712728}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q15233-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15233-2; Sequence=VSP_045470; CC -!- TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal CC muscle, kidney and pancreas. Also found in a number of breast tumor CC cell lines. {ECO:0000269|PubMed:9341872}. CC -!- PTM: The N-terminus is blocked. CC -!- DISEASE: Note=A chromosomal aberration involving NONO may be a cause of CC papillary renal cell carcinoma (PRCC). Translocation CC t(X;X)(p11.2;q13.1) with TFE3. {ECO:0000269|PubMed:9393982}. CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic 34 CC (MRXS34) [MIM:300967]: A syndrome characterized by intellectual CC deficit, delayed psychomotor development, poor speech, and dysmorphic CC features. {ECO:0000269|PubMed:26571461}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/168/NONO"; 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; L14599; AAC37578.1; -; mRNA. DR EMBL; U89867; AAC51852.1; -; mRNA. DR EMBL; Y11289; CAA72157.1; -; Genomic_DNA. DR EMBL; Y11290; CAA72157.1; JOINED; Genomic_DNA. DR EMBL; Y11291; CAA72157.1; JOINED; Genomic_DNA. DR EMBL; Y11292; CAA72157.1; JOINED; Genomic_DNA. DR EMBL; Y11293; CAA72157.1; JOINED; Genomic_DNA. DR EMBL; Y11294; CAA72157.1; JOINED; Genomic_DNA. DR EMBL; Y11295; CAA72157.1; JOINED; Genomic_DNA. DR EMBL; Y11296; CAA72157.1; JOINED; Genomic_DNA. DR EMBL; Y11297; CAA72157.1; JOINED; Genomic_DNA. DR EMBL; Y11298; CAA72157.1; JOINED; Genomic_DNA. DR EMBL; U02493; AAA03427.1; -; mRNA. DR EMBL; AK297144; BAH12508.1; -; mRNA. DR EMBL; CR456761; CAG33042.1; -; mRNA. DR EMBL; AL590762; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471132; EAX05298.1; -; Genomic_DNA. DR EMBL; CH471132; EAX05299.1; -; Genomic_DNA. DR EMBL; CH471132; EAX05300.1; -; Genomic_DNA. DR EMBL; BC002364; AAH02364.1; -; mRNA. DR EMBL; BC003129; AAH03129.1; -; mRNA. DR EMBL; BC012141; AAH12141.1; -; mRNA. DR EMBL; BC028299; AAH28299.1; -; mRNA. DR EMBL; BC069616; AAH69616.1; -; mRNA. DR EMBL; BC069639; AAH69639.1; -; mRNA. DR CCDS; CCDS14410.1; -. [Q15233-1] DR CCDS; CCDS55445.1; -. [Q15233-2] DR PIR; G01211; G01211. DR PIR; S29769; S29769. DR PIR; S41768; S41768. DR RefSeq; NP_001138880.1; NM_001145408.1. [Q15233-1] DR RefSeq; NP_001138881.1; NM_001145409.1. [Q15233-1] DR RefSeq; NP_001138882.1; NM_001145410.1. [Q15233-2] DR RefSeq; NP_031389.3; NM_007363.4. [Q15233-1] DR PDB; 3SDE; X-ray; 1.90 A; B=53-312. DR PDB; 5IFM; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=53-312. DR PDB; 6WMZ; X-ray; 2.85 A; B/D=53-312. DR PDB; 7LRQ; X-ray; 2.30 A; B=53-312. DR PDB; 7LRU; X-ray; 1.60 A; B=234-281. DR PDB; 7PU5; X-ray; 3.00 A; A/C/E/G/I/K=54-312. DR PDBsum; 3SDE; -. DR PDBsum; 5IFM; -. DR PDBsum; 6WMZ; -. DR PDBsum; 7LRQ; -. DR PDBsum; 7LRU; -. DR PDBsum; 7PU5; -. DR AlphaFoldDB; Q15233; -. DR BMRB; Q15233; -. DR SASBDB; Q15233; -. DR SMR; Q15233; -. DR BioGRID; 110904; 506. DR ComplexPortal; CPX-7765; SFPQ-NONO RNA-binding complex. DR ComplexPortal; CPX-7781; NONO RNA-binding homodimer. DR ComplexPortal; CPX-889; NONO-PSPC1 RNA-binding complex. DR CORUM; Q15233; -. DR DIP; DIP-29951N; -. DR IntAct; Q15233; 124. DR MINT; Q15233; -. DR STRING; 9606.ENSP00000276079; -. DR GlyCosmos; Q15233; 1 site, 1 glycan. DR GlyGen; Q15233; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q15233; -. DR MetOSite; Q15233; -. DR PhosphoSitePlus; Q15233; -. DR SwissPalm; Q15233; -. DR BioMuta; NONO; -. DR DMDM; 67469924; -. DR REPRODUCTION-2DPAGE; IPI00304596; -. DR EPD; Q15233; -. DR jPOST; Q15233; -. DR MassIVE; Q15233; -. DR MaxQB; Q15233; -. DR PaxDb; 9606-ENSP00000276079; -. DR PeptideAtlas; Q15233; -. DR ProteomicsDB; 24887; -. DR ProteomicsDB; 60494; -. [Q15233-1] DR Pumba; Q15233; -. DR TopDownProteomics; Q15233-1; -. [Q15233-1] DR ABCD; Q15233; 3 sequenced antibodies. DR Antibodypedia; 13516; 649 antibodies from 43 providers. DR DNASU; 4841; -. DR Ensembl; ENST00000276079.13; ENSP00000276079.8; ENSG00000147140.17. [Q15233-1] DR Ensembl; ENST00000373841.5; ENSP00000362947.1; ENSG00000147140.17. [Q15233-1] DR Ensembl; ENST00000420903.6; ENSP00000410299.2; ENSG00000147140.17. [Q15233-1] DR Ensembl; ENST00000450092.6; ENSP00000415777.2; ENSG00000147140.17. [Q15233-1] DR Ensembl; ENST00000454976.2; ENSP00000406673.2; ENSG00000147140.17. [Q15233-1] DR Ensembl; ENST00000535149.5; ENSP00000441364.1; ENSG00000147140.17. [Q15233-2] DR Ensembl; ENST00000676797.1; ENSP00000503920.1; ENSG00000147140.17. [Q15233-2] DR Ensembl; ENST00000677274.1; ENSP00000504314.1; ENSG00000147140.17. [Q15233-1] DR Ensembl; ENST00000677446.1; ENSP00000503031.1; ENSG00000147140.17. [Q15233-1] DR Ensembl; ENST00000677612.1; ENSP00000504351.1; ENSG00000147140.17. [Q15233-1] DR Ensembl; ENST00000678231.1; ENSP00000503233.1; ENSG00000147140.17. [Q15233-1] DR GeneID; 4841; -. DR KEGG; hsa:4841; -. DR MANE-Select; ENST00000276079.13; ENSP00000276079.8; NM_007363.5; NP_031389.3. DR UCSC; uc004dzn.5; human. [Q15233-1] DR AGR; HGNC:7871; -. DR CTD; 4841; -. DR DisGeNET; 4841; -. DR GeneCards; NONO; -. DR HGNC; HGNC:7871; NONO. DR HPA; ENSG00000147140; Low tissue specificity. DR MalaCards; NONO; -. DR MIM; 300084; gene. DR MIM; 300967; phenotype. DR neXtProt; NX_Q15233; -. DR OpenTargets; ENSG00000147140; -. DR Orphanet; 466791; Macrocephaly-intellectual disability-left ventricular non compaction syndrome. DR Orphanet; 319308; MiT family translocation renal cell carcinoma. DR PharmGKB; PA31680; -. DR VEuPathDB; HostDB:ENSG00000147140; -. DR eggNOG; KOG0115; Eukaryota. DR GeneTree; ENSGT00940000154442; -. DR HOGENOM; CLU_027185_2_0_1; -. DR InParanoid; Q15233; -. DR OMA; PNRPGEQ; -. DR OrthoDB; 5403433at2759; -. DR PhylomeDB; Q15233; -. DR TreeFam; TF315795; -. DR PathwayCommons; Q15233; -. DR SignaLink; Q15233; -. DR SIGNOR; Q15233; -. DR BioGRID-ORCS; 4841; 61 hits in 798 CRISPR screens. DR ChiTaRS; NONO; human. DR GeneWiki; NONO; -. DR GenomeRNAi; 4841; -. DR Pharos; Q15233; Tbio. DR PRO; PR:Q15233; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q15233; Protein. DR Bgee; ENSG00000147140; Expressed in oviduct epithelium and 123 other cell types or tissues. DR ExpressionAtlas; Q15233; baseline and differential. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0016363; C:nuclear matrix; IDA:BHF-UCL. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL. DR GO; GO:0042382; C:paraspeckles; IDA:MGI. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISS:BHF-UCL. DR GO; GO:0003682; F:chromatin binding; ISS:BHF-UCL. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0106222; F:lncRNA binding; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB. DR GO; GO:1904385; P:cellular response to angiotensin; IEA:Ensembl. 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; TAS:ProtInc. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc. 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 SWISS-2DPAGE; Q15233; -. DR Genevisible; Q15233; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; KW Biological rhythms; Chromosomal rearrangement; Chromosome; Coiled coil; KW Direct protein sequencing; DNA damage; DNA recombination; DNA repair; KW DNA-binding; Immunity; Innate immunity; Intellectual disability; KW Isopeptide bond; Methylation; mRNA processing; mRNA splicing; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding; KW Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..471 FT /note="Non-POU domain-containing octamer-binding protein" FT /id="PRO_0000081683" FT DOMAIN 74..141 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 148..229 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 1..51 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 54..373 FT /note="DBHS" FT REGION 443..471 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 268..372 FT /evidence="ECO:0000255" FT SITE 377..378 FT /note="Breakpoint for translocation to form NONO-TFE3" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q99K48" FT MOD_RES 5 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 6 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 11 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 147 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 198 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 262 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 295 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99K48" FT MOD_RES 371 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K48" FT MOD_RES 428 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17924679, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332" FT MOD_RES 440 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 450 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17693683, FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 456 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT CROSSLNK 5 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 60 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 96 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 99 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 126 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 190 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 198 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 243 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 249 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 371 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 467 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..89 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_045470" FT MUTAGEN 267 FT /note="Y->A: Abolishes interaction with PSPC1 and FT localization in nuclear paraspeckles; when associated with FT A-271." FT /evidence="ECO:0000269|PubMed:22416126" FT MUTAGEN 271 FT /note="W->A: Abolishes interaction with PSPC1 and FT localization in nuclear paraspeckles; when associated with FT A-267." FT /evidence="ECO:0000269|PubMed:22416126" FT CONFLICT 151 FT /note="T -> H (in Ref. 1; AAC37578)" FT /evidence="ECO:0000305" FT CONFLICT 358..359 FT /note="QQ -> HE (in Ref. 3; CAA72157 and 4; AAA03427)" FT /evidence="ECO:0000305" FT CONFLICT 366..367 FT /note="QQ -> HE (in Ref. 3; CAA72157 and 4; AAA03427)" FT /evidence="ECO:0000305" FT CONFLICT 387 FT /note="M -> I (in Ref. 5; BAH12508)" FT /evidence="ECO:0000305" FT STRAND 55..60 FT /evidence="ECO:0007829|PDB:5IFM" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 75..80 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 87..94 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 100..106 FT /evidence="ECO:0007829|PDB:3SDE" FT TURN 107..110 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 111..118 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 119..129 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 140..143 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 149..154 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 161..168 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 169..171 FT /evidence="ECO:0007829|PDB:7LRQ" FT STRAND 174..182 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 187..197 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 198..210 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 213..218 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 223..226 FT /evidence="ECO:0007829|PDB:3SDE" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:7LRQ" FT HELIX 238..240 FT /evidence="ECO:0007829|PDB:7LRU" FT HELIX 245..250 FT /evidence="ECO:0007829|PDB:7LRU" FT STRAND 255..257 FT /evidence="ECO:0007829|PDB:3SDE" FT HELIX 263..281 FT /evidence="ECO:0007829|PDB:7LRU" FT HELIX 308..311 FT /evidence="ECO:0007829|PDB:5IFM" SQ SEQUENCE 471 AA; 54232 MW; 26BBD3828F5B9E49 CRC64; MQSNKTFNLE KQNHTPRKHH QHHHQQQHHQ QQQQQPPPPP IPANGQQASS QNEGLTIDLK NFRKPGEKTF TQRSRLFVGN LPPDITEEEM RKLFEKYGKA GEVFIHKDKG FGFIRLETRT LAEIAKVELD NMPLRGKQLR VRFACHSASL TVRNLPQYVS NELLEEAFSV FGQVERAVVI VDDRGRPSGK GIVEFSGKPA ARKALDRCSE GSFLLTTFPR PVTVEPMDQL DDEEGLPEKL VIKNQQFHKE REQPPRFAQP GSFEYEYAMR WKALIEMEKQ QQDQVDRNIK EAREKLEMEM EAARHEHQVM LMRQDLMRRQ EELRRMEELH NQEVQKRKQL ELRQEEERRR REEEMRRQQE EMMRRQQEGF KGTFPDAREQ EIRMGQMAMG GAMGINNRGA MPPAPVPAGT PAPPGPATMM PDGTLGLTPP TTERFGQAAT MEGIGAIGGT PPAFNRAAPG AEFAPNKRRR Y //