NONO_HUMAN
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 03-AUG-2022, entry version 225.
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-
CC ARNTL/BMAL1 heterodimer (By similarity). Important for the functional
CC organization of GABAergic synapses (By similarity). Plays a specific
CC and important role in the regulation of synaptic RNAs and GPHN/gephyrin
CC scaffold structure, through the regulation of GABRA2 transcript (By
CC similarity). Plays a key role during neuronal differentiation by
CC recruiting TET1 to genomic loci and thereby regulating 5-
CC hydroxymethylcytosine levels (By similarity). 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 (PubMed:28712728, PubMed:30270045).
CC Promotes activation of the cGAS-STING pathway in response to HIV-2
CC infection: acts by interacting with HIV-2 Capsid protein p24, thereby
CC promoting detection of viral DNA by CGAS, leading to CGAS-mediated
CC inmmune activation (PubMed:30270045). In contrast, the weak interaction
CC with HIV-1 Capsid protein p24 does not allow activation of the cGAS-
CC STING pathway (PubMed:30270045). {ECO:0000250|UniProtKB:Q99K48,
CC ECO:0000269|PubMed:10858305, ECO:0000269|PubMed:11525732,
CC ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:12403470,
CC ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:22416126,
CC ECO:0000269|PubMed:26571461, ECO:0000269|PubMed:28712728,
CC 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 (By similarity). Interacts with RNF43 (PubMed:18655028). Interacts with
CC PER1 and PER2 (By similarity). Part of the HDP-RNP complex composed of
CC at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO,
CC PSPC1, RBM14, and MATR3) and NEAT1 RNA (PubMed:28712728). Interacts
CC (via second RRM domain) with WASL; the interaction is direct
CC (PubMed:16767080). Component of a multiprotein complex with WASL and
CC SFPQ (PubMed:16767080). Interacts with ERCC6 (PubMed:26030138).
CC Interacts (via DNA-binding domain) with TET1 (By similarity).
CC {ECO:0000250|UniProtKB:Q99K48, ECO:0000269|PubMed:11525732,
CC ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:12403470,
CC ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:16148043,
CC ECO:0000269|PubMed:16767080, ECO:0000269|PubMed:18655028,
CC ECO:0000269|PubMed:22416126, ECO:0000269|PubMed:26030138,
CC ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:8439294,
CC 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="http://atlasgeneticsoncology.org/Genes/NONOID168.html";
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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; 437.
DR CORUM; Q15233; -.
DR DIP; DIP-29951N; -.
DR IntAct; Q15233; 119.
DR MINT; Q15233; -.
DR STRING; 9606.ENSP00000276079; -.
DR GlyGen; Q15233; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15233; -.
DR MetOSite; Q15233; -.
DR PhosphoSitePlus; Q15233; -.
DR SwissPalm; Q15233; -.
DR BioMuta; NONO; -.
DR DMDM; 67469924; -.
DR REPRODUCTION-2DPAGE; IPI00304596; -.
DR SWISS-2DPAGE; Q15233; -.
DR EPD; Q15233; -.
DR jPOST; Q15233; -.
DR MassIVE; Q15233; -.
DR MaxQB; Q15233; -.
DR PaxDb; Q15233; -.
DR PeptideAtlas; Q15233; -.
DR PRIDE; Q15233; -.
DR ProteomicsDB; 24887; -.
DR ProteomicsDB; 60494; -. [Q15233-1]
DR TopDownProteomics; Q15233-1; -. [Q15233-1]
DR ABCD; Q15233; 3 sequenced antibodies.
DR Antibodypedia; 13516; 565 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 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; NHTPRKQ; -.
DR PhylomeDB; Q15233; -.
DR TreeFam; TF315795; -.
DR PathwayCommons; Q15233; -.
DR SignaLink; Q15233; -.
DR SIGNOR; Q15233; -.
DR BioGRID-ORCS; 4841; 43 hits in 718 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 121 other tissues.
DR ExpressionAtlas; Q15233; baseline and differential.
DR Genevisible; Q15233; HS.
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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
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:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
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; 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
