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Non-POU domain-containing octamer-binding protein (NonO protein) (54 kDa nuclear RNA- and DNA-binding protein) (55 kDa nuclear protein) (DNA-binding p52/p100 complex, 52 kDa subunit) (NMT55) (p54(nrb)) (p54nrb)

 NONO_HUMAN              Reviewed;         471 AA.
Q15233; B7Z4C2; D3DVV4; F5GYZ3; O00201; P30807; Q12786; Q9BQC5;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 4.
12-SEP-2018, entry version 199.
RecName: Full=Non-POU domain-containing octamer-binding protein;
Short=NonO protein;
AltName: Full=54 kDa nuclear RNA- and DNA-binding protein;
AltName: Full=55 kDa nuclear protein;
AltName: Full=DNA-binding p52/p100 complex, 52 kDa subunit;
AltName: Full=NMT55;
AltName: Full=p54(nrb);
Short=p54nrb;
Name=NONO; Synonyms=NRB54;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF
252-267; 273-279 AND 283-289.
PubMed=8371983; DOI=10.1093/nar/21.17.4085;
Dong B., Horowitz D.S., Kobayashi R., Krainer A.R.;
"Purification and cDNA cloning of HeLa cell p54nrb, a nuclear protein
with two RNA recognition motifs and extensive homology to human
splicing factor PSF and Drosophila NONA/BJ6.";
Nucleic Acids Res. 21:4085-4092(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Mammary carcinoma;
PubMed=9360842; DOI=10.1097/00019606-199708000-00005;
Traish A.M., Huang Y.-H., Ashba J., Pronovost M., Pavao M.,
McAneny D.B., Moreland R.B.;
"Loss of expression of a 55 kDa nuclear protein (nmt55) in estrogen
receptor-negative human breast cancer.";
Diagn. Mol. Pathol. 6:209-221(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
TISSUE=Blood;
PubMed=9341872; DOI=10.1007/s004390050553;
Peters U., Haberhausen G., Kostrzewa M., Nolte D., Mueller U.;
"AFX1 and p54nrb: fine mapping, genomic structure, and exclusion as
candidate genes of X-linked dystonia parkinsonism.";
Hum. Genet. 100:569-572(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Honore B., Rasmussen H.H., Celis J.E.;
"54 kDa human protein.";
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix, Kidney, Muscle, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 2-21 AND 133-153, BLOCKAGE OF N-TERMINUS, AND
SUBUNIT.
PubMed=8439294; DOI=10.1042/bj2900267;
Zhang W.-W., Zhang L.-X., Busch R.K., Farres J., Busch H.;
"Purification and characterization of a DNA-binding heterodimer of 52
and 100 kDa from HeLa cells.";
Biochem. J. 290:267-272(1993).
[11]
PROTEIN SEQUENCE OF 76-91; 127-135; 177-184; 257-270 AND 435-456, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[12]
CHROMOSOMAL TRANSLOCATION WITH TFE3.
PubMed=9393982; DOI=10.1038/sj.onc.1201394;
Clark J., Lu Y.-J., Sidhar S.K., Parker C., Gill S., Smedley D.,
Hamoudi R., Linehan W.M., Shipley J., Cooper C.S.;
"Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3
gene in papillary renal cell carcinoma.";
Oncogene 15:2233-2239(1997).
[13]
IDENTIFICATION IN A COMPLEX WITH SFPQ AND TOP1.
PubMed=9756848; DOI=10.1074/jbc.273.41.26261;
Straub T., Grue P., Uhse A., Lisby M., Knudsen B.R., Tange T.O.,
Westergaard O., Boege F.;
"The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I activity
by a direct interaction.";
J. Biol. Chem. 273:26261-26264(1998).
[14]
FUNCTION IN DNA UNWINDING.
PubMed=10858305; DOI=10.1021/bi992898e;
Straub T., Knudsen B.R., Boege F.;
"PSF/p54(nrb) stimulates 'jumping' of DNA topoisomerase I between
separate DNA helices.";
Biochemistry 39:7552-7558(2000).
[15]
FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, AND
IDENTIFICATION IN A COMPLEX WITH NONO AND MATR3.
PubMed=11525732; DOI=10.1016/S0092-8674(01)00466-4;
Zhang Z., Carmichael G.G.;
"The fate of dsRNA in the nucleus: a p54(nrb)-containing complex
mediates the nuclear retention of promiscuously A-to-I edited RNAs.";
Cell 106:465-475(2001).
[16]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION IN TRANSCRIPTION
REGULATION, AND IDENTIFICATION IN A COMPLEX WITH SFPQ AND NR5A1.
PubMed=11897684; DOI=10.1210/endo.143.4.8748;
Sewer M.B., Nguyen V.Q., Huang C.J., Tucker P.W., Kagawa N.,
Waterman M.R.;
"Transcriptional activation of human CYP17 in H295R adrenocortical
cells depends on complex formation among p54(nrb)/NonO, protein-
associated splicing factor, and SF-1, a complex that also participates
in repression of transcription.";
Endocrinology 143:1280-1290(2002).
[17]
INTERACTION WITH PSQF AND U5 SNRNA, AND IDENTIFICATION IN U5/4/6 SNRNP
AND SPLICEOSOME COMPLEXES.
PubMed=12403470; DOI=10.1017/S1355838202022070;
Peng R., Dye B.T., Perez I., Barnard D.C., Thompson A.B., Patton J.G.;
"PSF and p54nrb bind a conserved stem in U5 snRNA.";
RNA 8:1334-1347(2002).
[18]
FUNCTION IN DNA REPAIR, IDENTIFICATION BY MASS SPECTROMETRY,
DNA-BINDING, AND SUBUNIT.
PubMed=15590677; DOI=10.1074/jbc.M412758200;
Bladen C.L., Udayakumar D., Takeda Y., Dynan W.S.;
"Identification of the polypyrimidine tract binding protein-associated
splicing factor.p54(nrb) complex as a candidate DNA double-strand
break rejoining factor.";
J. Biol. Chem. 280:5205-5210(2005).
[19]
INTERACTION WITH PSPC1.
PubMed=16148043; DOI=10.1091/mbc.E05-06-0587;
Fox A.H., Bond C.S., Lamond A.I.;
"P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles
in an RNA-dependent manner.";
Mol. Biol. Cell 16:5304-5315(2005).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
network: indicating the involvement of ribonucleoside-diphosphate
reductase M2 subunit phosphorylation at residue serine 20 in canonical
Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[27]
INTERACTION WITH RNF43.
PubMed=18655028; DOI=10.1002/pmic.200800083;
Miyamoto K., Sakurai H., Sugiura T.;
"Proteomic identification of a PSF/p54nrb heterodimer as RNF43
oncoprotein-interacting proteins.";
Proteomics 8:2907-2910(2008).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-11 AND LYS-198, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; THR-440 AND
THR-450, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[34]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=22002106; DOI=10.1074/mcp.M111.013680;
Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
"Systematic analysis of protein pools, isoforms, and modifications
affecting turnover and subcellular localization.";
Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; SER-262 AND THR-450,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[37]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-456, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5 AND LYS-371, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[40]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRKDC; XRCC5;
XRCC6; SFPQ; HEXIM1; PSPC1; RBM14 AND MATR3.
PubMed=28712728; DOI=10.1016/j.molcel.2017.06.020;
Morchikh M., Cribier A., Raffel R., Amraoui S., Cau J., Severac D.,
Dubois E., Schwartz O., Bennasser Y., Benkirane M.;
"HEXIM1 and NEAT1 Long non-coding RNA form a multi-subunit complex
that regulates DNA-mediated innate immune response.";
Mol. Cell 67:387-399(2017).
[41]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-60; LYS-96; LYS-99;
LYS-126; LYS-190; LYS-198; LYS-243; LYS-249; LYS-371 AND LYS-467, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[42]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 53-312 IN COMPLEX WITH PSPC1,
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-267 AND
TRP-271.
PubMed=22416126; DOI=10.1073/pnas.1120792109;
Passon D.M., Lee M., Rackham O., Stanley W.A., Sadowska A.,
Filipovska A., Fox A.H., Bond C.S.;
"Structure of the heterodimer of human NONO and paraspeckle protein
component 1 and analysis of its role in subnuclear body formation.";
Proc. Natl. Acad. Sci. U.S.A. 109:4846-4850(2012).
[43]
INVOLVEMENT IN MRXS34, AND FUNCTION.
PubMed=26571461; DOI=10.1038/nn.4169;
DDD Study;
Mircsof D., Langouet M., Rio M., Moutton S., Siquier-Pernet K.,
Bole-Feysot C., Cagnard N., Nitschke P., Gaspar L., Znidaric M.,
Alibeu O., Fritz A.K., Wolfer D.P., Schroeter A., Bosshard G.,
Rudin M., Koester C., Crestani F., Seebeck P., Boddaert N.,
Prescott K., Hines R., Moss S.J., Fritschy J.M., Munnich A., Amiel J.,
Brown S.A., Tyagarajan S.K., Colleaux L.;
"Mutations in NONO lead to syndromic intellectual disability and
inhibitory synaptic defects.";
Nat. Neurosci. 18:1731-1736(2015).
-!- FUNCTION: DNA- and RNA binding protein, involved in several
nuclear processes. Binds the conventional octamer sequence in
double-stranded DNA. Also binds single-stranded DNA and RNA at a
site independent of the duplex site. Involved in pre-mRNA
splicing, probably as a heterodimer with SFPQ. Interacts with U5
snRNA, probably by binding to a purine-rich sequence located on
the 3' side of U5 snRNA stem 1b. Together with PSPC1, required for
the formation of nuclear paraspeckles. The SFPQ-NONO heteromer
associated with MATR3 may play a role in nuclear retention of
defective RNAs. The SFPQ-NONO heteromer may be involved in DNA
unwinding by modulating the function of topoisomerase I/TOP1. The
SFPQ-NONO heteromer may be involved in DNA non-homologous end
joining (NHEJ) required for double-strand break repair and V(D)J
recombination and may stabilize paired DNA ends. In vitro, the
complex strongly stimulates DNA end joining, binds directly to the
DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku)
dimer to establish a functional preligation complex. NONO is
involved in transcriptional regulation. The SFPQ-NONO-NR5A1
complex binds to the CYP17 promoter and regulates basal and cAMP-
dependent transcriptional activity. NONO binds to an enhancer
element in long terminal repeats of endogenous intracisternal A
particles (IAPs) and activates transcription. Regulates the
circadian clock by repressing the transcriptional activator
activity of the CLOCK-ARNTL/BMAL1 heterodimer. Important for the
functional organization of GABAergic synapses. Plays a specific
and important role in the regulation of synaptic RNAs and
GPHN/gephyrin scaffold structure, through the regulation of GABRA2
transcript. Plays a role in the regulation of DNA virus-mediated
innate immune response by assembling into the HDP-RNP complex, a
complex that serves as a platform for IRF3 phosphorylation and
subsequent innate immune response activation through the cGAS-
STING pathway (PubMed:28712728). {ECO:0000250|UniProtKB:Q99K48,
ECO:0000269|PubMed:10858305, ECO:0000269|PubMed:11525732,
ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:15590677,
ECO:0000269|PubMed:22416126, ECO:0000269|PubMed:26571461,
ECO:0000269|PubMed:28712728}.
-!- SUBUNIT: Interacts with CPNE4 (via VWFA domain) (By similarity).
Monomer and component of the SFPQ-NONO complex, which is probably
a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ)
subunits. NONO is a component of spliceosome and U5.4/6 snRNP
complexes. Forms heterodimers with PSPC1; this involves formation
of a coiled coil domain by helices from both proteins. Interacts
with PSPC1 and SNRPA/U1A. Part of complex consisting of SFPQ, NONO
and MATR3. Part of a complex consisting of SFPQ, NONO and NR5A1.
Part of a complex consisting of SFPQ, NONO and TOP1. Interacts
with SPI1. Interacts with RNF43. Interacts with PER1 and PER2.
Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC,
XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and
MATR3) and NEAT1 RNA (PubMed:28712728).
{ECO:0000250|UniProtKB:Q99K48, ECO:0000269|PubMed:11525732,
ECO:0000269|PubMed:11897684, ECO:0000269|PubMed:12403470,
ECO:0000269|PubMed:15590677, ECO:0000269|PubMed:16148043,
ECO:0000269|PubMed:18655028, ECO:0000269|PubMed:22416126,
ECO:0000269|PubMed:28712728, ECO:0000269|PubMed:8439294,
ECO:0000269|PubMed:9756848}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-350527, EBI-350527;
Q9H3H3:C11orf68; NbExp=3; IntAct=EBI-350527, EBI-721765;
Q53ET0:CRTC2; NbExp=2; IntAct=EBI-350527, EBI-1181987;
P26196:DDX6; NbExp=3; IntAct=EBI-10203843, EBI-351257;
Q8AZK7:EBNA-LP (xeno); NbExp=2; IntAct=EBI-350527, EBI-1185167;
P61968:LMO4; NbExp=3; IntAct=EBI-10203843, EBI-2798728;
Q13526:PIN1; NbExp=4; IntAct=EBI-350527, EBI-714158;
P54646:PRKAA2; NbExp=3; IntAct=EBI-10203843, EBI-1383852;
Q8WXF1:PSPC1; NbExp=11; IntAct=EBI-350527, EBI-1392258;
Q8WXF1-1:PSPC1; NbExp=7; IntAct=EBI-350527, EBI-15974663;
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Nucleus
speckle. Note=Detected in punctate subnuclear structures often
located adjacent to splicing speckles, called paraspeckles.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15233-1; Sequence=Displayed;
Name=2;
IsoId=Q15233-2; Sequence=VSP_045470;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal
muscle, kidney and pancreas. Also found in a number of breast
tumor cell lines. {ECO:0000269|PubMed:9341872}.
-!- PTM: The N-terminus is blocked.
-!- DISEASE: Note=A chromosomal aberration involving NONO may be a
cause of papillary renal cell carcinoma (PRCC). Translocation
t(X;X)(p11.2;q13.1) with TFE3. {ECO:0000269|PubMed:9393982}.
-!- DISEASE: Mental retardation, X-linked, syndromic, 34 (MRXS34)
[MIM:300967]: A mental retardation syndrome characterized by
intellectual deficit, delayed psychomotor development, poor
speech, and dysmorphic features. Mental retardation is defined by
significantly below average general intellectual functioning
associated with impairments in adaptive behavior and manifested
during the developmental period. {ECO:0000269|PubMed:26571461}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NONOID168.html";
-----------------------------------------------------------------------
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EMBL; L14599; AAC37578.1; -; mRNA.
EMBL; U89867; AAC51852.1; -; mRNA.
EMBL; Y11289; CAA72157.1; -; Genomic_DNA.
EMBL; Y11290; CAA72157.1; JOINED; Genomic_DNA.
EMBL; Y11291; CAA72157.1; JOINED; Genomic_DNA.
EMBL; Y11292; CAA72157.1; JOINED; Genomic_DNA.
EMBL; Y11293; CAA72157.1; JOINED; Genomic_DNA.
EMBL; Y11294; CAA72157.1; JOINED; Genomic_DNA.
EMBL; Y11295; CAA72157.1; JOINED; Genomic_DNA.
EMBL; Y11296; CAA72157.1; JOINED; Genomic_DNA.
EMBL; Y11297; CAA72157.1; JOINED; Genomic_DNA.
EMBL; Y11298; CAA72157.1; JOINED; Genomic_DNA.
EMBL; U02493; AAA03427.1; -; mRNA.
EMBL; AK297144; BAH12508.1; -; mRNA.
EMBL; CR456761; CAG33042.1; -; mRNA.
EMBL; AL590762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471132; EAX05298.1; -; Genomic_DNA.
EMBL; CH471132; EAX05299.1; -; Genomic_DNA.
EMBL; CH471132; EAX05300.1; -; Genomic_DNA.
EMBL; BC002364; AAH02364.1; -; mRNA.
EMBL; BC003129; AAH03129.1; -; mRNA.
EMBL; BC012141; AAH12141.1; -; mRNA.
EMBL; BC028299; AAH28299.1; -; mRNA.
EMBL; BC069616; AAH69616.1; -; mRNA.
EMBL; BC069639; AAH69639.1; -; mRNA.
CCDS; CCDS14410.1; -. [Q15233-1]
CCDS; CCDS55445.1; -. [Q15233-2]
PIR; G01211; G01211.
PIR; S29769; S29769.
PIR; S41768; S41768.
RefSeq; NP_001138880.1; NM_001145408.1. [Q15233-1]
RefSeq; NP_001138881.1; NM_001145409.1. [Q15233-1]
RefSeq; NP_001138882.1; NM_001145410.1. [Q15233-2]
RefSeq; NP_031389.3; NM_007363.4. [Q15233-1]
UniGene; Hs.533282; -.
UniGene; Hs.700344; -.
PDB; 3SDE; X-ray; 1.90 A; B=53-312.
PDB; 5IFM; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=53-312.
PDBsum; 3SDE; -.
PDBsum; 5IFM; -.
ProteinModelPortal; Q15233; -.
SMR; Q15233; -.
BioGrid; 110904; 252.
CORUM; Q15233; -.
DIP; DIP-29951N; -.
IntAct; Q15233; 61.
MINT; Q15233; -.
STRING; 9606.ENSP00000276079; -.
iPTMnet; Q15233; -.
PhosphoSitePlus; Q15233; -.
SwissPalm; Q15233; -.
BioMuta; NONO; -.
DMDM; 67469924; -.
REPRODUCTION-2DPAGE; IPI00304596; -.
SWISS-2DPAGE; Q15233; -.
EPD; Q15233; -.
MaxQB; Q15233; -.
PaxDb; Q15233; -.
PeptideAtlas; Q15233; -.
PRIDE; Q15233; -.
ProteomicsDB; 60494; -.
TopDownProteomics; Q15233-1; -. [Q15233-1]
DNASU; 4841; -.
Ensembl; ENST00000276079; ENSP00000276079; ENSG00000147140. [Q15233-1]
Ensembl; ENST00000373841; ENSP00000362947; ENSG00000147140. [Q15233-1]
Ensembl; ENST00000373856; ENSP00000362963; ENSG00000147140. [Q15233-1]
Ensembl; ENST00000535149; ENSP00000441364; ENSG00000147140. [Q15233-2]
GeneID; 4841; -.
KEGG; hsa:4841; -.
UCSC; uc004dzn.5; human. [Q15233-1]
CTD; 4841; -.
DisGeNET; 4841; -.
EuPathDB; HostDB:ENSG00000147140.15; -.
GeneCards; NONO; -.
HGNC; HGNC:7871; NONO.
HPA; CAB022069; -.
HPA; HPA054094; -.
HPA; HPA054559; -.
MalaCards; NONO; -.
MIM; 300084; gene.
MIM; 300967; phenotype.
neXtProt; NX_Q15233; -.
OpenTargets; ENSG00000147140; -.
Orphanet; 319308; Translocation renal cell carcinoma.
PharmGKB; PA31680; -.
eggNOG; KOG0115; Eukaryota.
eggNOG; ENOG410XQA0; LUCA.
GeneTree; ENSGT00390000005004; -.
HOGENOM; HOG000231095; -.
HOVERGEN; HBG009801; -.
InParanoid; Q15233; -.
KO; K13214; -.
OMA; NQQYHKE; -.
OrthoDB; EOG091G09T7; -.
PhylomeDB; Q15233; -.
TreeFam; TF315795; -.
SIGNOR; Q15233; -.
ChiTaRS; NONO; human.
GeneWiki; NONO; -.
GenomeRNAi; 4841; -.
PMAP-CutDB; Q15233; -.
PRO; PR:Q15233; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000147140; Expressed in 111 organ(s), highest expression level in endometrium epithelium.
CleanEx; HS_NONO; -.
ExpressionAtlas; Q15233; baseline and differential.
Genevisible; Q15233; HS.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IDA:BHF-UCL.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0042382; C:paraspeckles; IDA:MGI.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISS:BHF-UCL.
GO; GO:0003682; F:chromatin binding; ISS:BHF-UCL.
GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; ISS:BHF-UCL.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd12588; RRM1_p54nrb; 1.
CDD; cd12591; RRM2_p54nrb; 1.
Gene3D; 3.30.70.330; -; 2.
InterPro; IPR012975; NOPS.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR034552; p54nrb_RRM1.
InterPro; IPR034558; p54nrb_RRM2.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF08075; NOPS; 1.
Pfam; PF00076; RRM_1; 2.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Biological rhythms; Chromosomal rearrangement; Coiled coil;
Complete proteome; Direct protein sequencing; DNA damage;
DNA recombination; DNA repair; DNA-binding; Immunity; Innate immunity;
Isopeptide bond; Mental retardation; Methylation; mRNA processing;
mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Repressor; RNA-binding; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 471 Non-POU domain-containing octamer-binding
protein.
/FTId=PRO_0000081683.
DOMAIN 74 141 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 148 229 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 54 373 DBHS.
COILED 268 372 {ECO:0000255}.
COMPBIAS 30 35 Poly-Gln.
COMPBIAS 36 42 Poly-Pro.
COMPBIAS 348 351 Poly-Arg.
SITE 377 378 Breakpoint for translocation to form
NONO-TFE3.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q99K48}.
MOD_RES 5 5 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 6 6 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 11 11 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 147 147 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 198 198 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 262 262 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 295 295 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99K48}.
MOD_RES 371 371 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99K48}.
MOD_RES 428 428 Phosphothreonine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332}.
MOD_RES 440 440 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 450 450 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17693683,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 456 456 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
CROSSLNK 5 5 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 60 60 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 96 96 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 99 99 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 126 126 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 190 190 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 198 198 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 243 243 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 249 249 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 371 371 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 467 467 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 89 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_045470.
MUTAGEN 267 267 Y->A: Abolishes interaction with PSPC1
and localization in nuclear paraspeckles;
when associated with A-271.
{ECO:0000269|PubMed:22416126}.
MUTAGEN 271 271 W->A: Abolishes interaction with PSPC1
and localization in nuclear paraspeckles;
when associated with A-267.
{ECO:0000269|PubMed:22416126}.
CONFLICT 151 151 T -> H (in Ref. 1; AAC37578).
{ECO:0000305}.
CONFLICT 358 359 QQ -> HE (in Ref. 3; CAA72157 and 4;
AAA03427). {ECO:0000305}.
CONFLICT 366 367 QQ -> HE (in Ref. 3; CAA72157 and 4;
AAA03427). {ECO:0000305}.
CONFLICT 387 387 M -> I (in Ref. 5; BAH12508).
{ECO:0000305}.
STRAND 55 60 {ECO:0000244|PDB:5IFM}.
HELIX 72 74 {ECO:0000244|PDB:3SDE}.
STRAND 75 80 {ECO:0000244|PDB:3SDE}.
HELIX 87 94 {ECO:0000244|PDB:3SDE}.
HELIX 95 97 {ECO:0000244|PDB:3SDE}.
STRAND 100 106 {ECO:0000244|PDB:3SDE}.
TURN 107 110 {ECO:0000244|PDB:3SDE}.
STRAND 111 118 {ECO:0000244|PDB:3SDE}.
HELIX 119 129 {ECO:0000244|PDB:3SDE}.
STRAND 140 143 {ECO:0000244|PDB:3SDE}.
STRAND 149 154 {ECO:0000244|PDB:3SDE}.
HELIX 161 168 {ECO:0000244|PDB:3SDE}.
TURN 169 171 {ECO:0000244|PDB:5IFM}.
STRAND 174 182 {ECO:0000244|PDB:3SDE}.
STRAND 187 197 {ECO:0000244|PDB:3SDE}.
HELIX 198 210 {ECO:0000244|PDB:3SDE}.
STRAND 213 218 {ECO:0000244|PDB:3SDE}.
STRAND 223 226 {ECO:0000244|PDB:3SDE}.
STRAND 230 234 {ECO:0000244|PDB:5IFM}.
HELIX 238 240 {ECO:0000244|PDB:3SDE}.
HELIX 245 250 {ECO:0000244|PDB:3SDE}.
STRAND 255 257 {ECO:0000244|PDB:3SDE}.
HELIX 263 303 {ECO:0000244|PDB:3SDE}.
HELIX 308 311 {ECO:0000244|PDB:5IFM}.
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


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