Q15233 (NONO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Non-POU domain-containing octamer-binding protein
Short name=NonO protein

Alternative name(s):
54 kDa nuclear RNA- and DNA-binding protein
55 kDa nuclear protein
DNA-binding p52/p100 complex, 52 kDa subunit
NMT55
p54(nrb)
Short name=p54nrb

Gene names

Name:	NONO
Synonyms:	NRB54

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 By similarity. 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. 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 nonhomologous 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 avtivity. NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription By similarity. Together with PSPC1, required for the formation of nuclear paraspeckles. Ref.14 Ref.15 Ref.16 Ref.18 Ref.34
Subunit structure	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. 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 By similarity. Interacts with RNF43. Forms heterodimers with PSPC1; this involves formation of a coiled coil domain by helices from both proteins. Ref.10 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.27
Subcellular location	Nucleus. Nucleus › nucleolus. Nucleus speckle. Note: Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. Ref.33 Ref.34
Tissue specificity	Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Also found in a number of breast tumor cell lines. Ref.3
Post-translational modification	The N-terminus is blocked.
Involvement in disease	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.
Sequence similarities	Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Domain	Coiled coil Repeat
Ligand	DNA-binding RNA-binding
Molecular function	Activator
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA repair Inferred from electronic annotation. Source: UniProtKB-KW RNA splicing Traceable author statement Ref.1. Source: ProtInc mRNA processing Traceable author statement Ref.2. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nuclear matrix Inferred from direct assay PubMed 19874820. Source: BHF-UCL nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell paraspeckles Inferred from direct assay PubMed 19217333. Source: MGI
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-350527,EBI-350527
PSPC1	Q8WXF1	6	EBI-350527,EBI-1392258

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15233-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q15233-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 471

471

Non-POU domain-containing octamer-binding protein

PRO_0000081683

Regions

Domain

74 – 141

68

RRM 1

Domain

148 – 229

82

RRM 2

Region

54 – 373

320

DBHS

Coiled coil

268 – 372

105

Potential

Compositional bias

30 – 35

6

Poly-Gln

Compositional bias

36 – 42

7

Poly-Pro

Compositional bias

348 – 351

4

Poly-Arg

Sites

Site

377 – 378

2

Breakpoint for translocation to form NONO-TFE3

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.29

Modified residue

5

1

N6-acetyllysine Ref.29

Modified residue

11

1

N6-acetyllysine Ref.29

Modified residue

147

1

Phosphoserine Ref.30

Modified residue

198

1

N6-acetyllysine Ref.29

Modified residue

428

1

Phosphothreonine Ref.22 Ref.25 Ref.28

Modified residue

440

1

Phosphothreonine Ref.30

Modified residue

450

1

Phosphothreonine Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.30 Ref.32

Natural variations

Alternative sequence

1 – 89

89

Missing in isoform 2.

VSP_045470

Experimental info

Mutagenesis

267

1

Y → A: Abolishes interaction with PSPC1 and localization in nuclear paraspeckles; when associated with A-271. Ref.34

Mutagenesis

271

1

W → A: Abolishes interaction with PSPC1 and localization in nuclear paraspeckles; when associated with A-267. Ref.34

Sequence conflict

151

1

T → H in AAC37578. Ref.1

Sequence conflict

358 – 359

2

QQ → HE in CAA72157. Ref.3

Sequence conflict

358 – 359

2

QQ → HE in AAA03427. Ref.4

Sequence conflict

366 – 367

2

QQ → HE in CAA72157. Ref.3

Sequence conflict

366 – 367

2

QQ → HE in AAA03427. Ref.4

Sequence conflict

387

1

M → I in BAH12508. Ref.5

Secondary structure

1

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471

Helix Strand Turn

Details...

Helix

72 – 74

3

Beta strand

75 – 80

6

Helix

87 – 94

8

Helix

95 – 97

3

Beta strand

100 – 106

7

Turn

107 – 110

4

Beta strand

111 – 118

8

Helix

119 – 129

11

Beta strand

140 – 143

4

Beta strand

149 – 154

6

Helix

161 – 168

8

Beta strand

174 – 182

9

Beta strand

187 – 197

11

Helix

198 – 210

13

Beta strand

213 – 218

6

Beta strand

223 – 226

4

Helix

238 – 240

3

Helix

245 – 250

6

Beta strand

255 – 257

3

Helix

263 – 303

41

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2005. Version 4. Checksum: 26BBD3828F5B9E49	FASTA	471	54,232
	10 20 30 40 50 60 MQSNKTFNLE KQNHTPRKHH QHHHQQQHHQ QQQQQPPPPP IPANGQQASS QNEGLTIDLK 70 80 90 100 110 120 NFRKPGEKTF TQRSRLFVGN LPPDITEEEM RKLFEKYGKA GEVFIHKDKG FGFIRLETRT 130 140 150 160 170 180 LAEIAKVELD NMPLRGKQLR VRFACHSASL TVRNLPQYVS NELLEEAFSV FGQVERAVVI 190 200 210 220 230 240 VDDRGRPSGK GIVEFSGKPA ARKALDRCSE GSFLLTTFPR PVTVEPMDQL DDEEGLPEKL 250 260 270 280 290 300 VIKNQQFHKE REQPPRFAQP GSFEYEYAMR WKALIEMEKQ QQDQVDRNIK EAREKLEMEM 310 320 330 340 350 360 EAARHEHQVM LMRQDLMRRQ EELRRMEELH NQEVQKRKQL ELRQEEERRR REEEMRRQQE 370 380 390 400 410 420 EMMRRQQEGF KGTFPDAREQ EIRMGQMAMG GAMGINNRGA MPPAPVPAGT PAPPGPATMM 430 440 450 460 470 PDGTLGLTPP TTERFGQAAT MEGIGAIGGT PPAFNRAAPG AEFAPNKRRR Y
	Isoform 2 [UniParc]. Checksum: 5B6CF35CAB8486D4	FASTA	382	43,866
	10 20 30 40 50 60 MRKLFEKYGK AGEVFIHKDK GFGFIRLETR TLAEIAKVEL DNMPLRGKQL RVRFACHSAS 70 80 90 100 110 120 LTVRNLPQYV SNELLEEAFS VFGQVERAVV IVDDRGRPSG KGIVEFSGKP AARKALDRCS 130 140 150 160 170 180 EGSFLLTTFP RPVTVEPMDQ LDDEEGLPEK LVIKNQQFHK EREQPPRFAQ PGSFEYEYAM 190 200 210 220 230 240 RWKALIEMEK QQQDQVDRNI KEAREKLEME MEAARHEHQV MLMRQDLMRR QEELRRMEEL 250 260 270 280 290 300 HNQEVQKRKQ LELRQEEERR RREEEMRRQQ EEMMRRQQEG FKGTFPDARE QEIRMGQMAM 310 320 330 340 350 360 GGAMGINNRG AMPPAPVPAG TPAPPGPATM MPDGTLGLTP PTTERFGQAA TMEGIGAIGG 370 380 TPPAFNRAAP GAEFAPNKRR RY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Dong B., Horowitz D.S., Kobayashi R., Krainer A.R. Nucleic Acids Res. 21:4085-4092(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 252-267; 273-279 AND 283-289.
[2]	"Loss of expression of a 55 kDa nuclear protein (nmt55) in estrogen receptor-negative human breast cancer." Traish A.M., Huang Y.-H., Ashba J., Pronovost M., Pavao M., McAneny D.B., Moreland R.B. Diagn. Mol. Pathol. 6:209-221(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Mammary carcinoma.
[3]	"AFX1 and p54nrb: fine mapping, genomic structure, and exclusion as candidate genes of X-linked dystonia parkinsonism." Peters U., Haberhausen G., Kostrzewa M., Nolte D., Mueller U. Hum. Genet. 100:569-572(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY. Tissue: Blood.
[4]	"54 kDa human protein." Honore B., Rasmussen H.H., Celis J.E. Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"The DNA sequence of the human X chromosome." 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. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Cervix, Kidney, Muscle and Skin.
[10]	"Purification and characterization of a DNA-binding heterodimer of 52 and 100 kDa from HeLa cells." Zhang W.-W., Zhang L.-X., Busch R.K., Farres J., Busch H. Biochem. J. 290:267-272(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21 AND 133-153, BLOCKAGE OF N-TERMINUS, SUBUNIT.
[11]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 76-91; 127-135; 177-184; 257-270 AND 435-456, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[12]	"Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3 gene in papillary renal cell carcinoma." Clark J., Lu Y.-J., Sidhar S.K., Parker C., Gill S., Smedley D., Hamoudi R., Linehan W.M., Shipley J., Cooper C.S. Oncogene 15:2233-2239(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION.
[13]	"The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I activity by a direct interaction." Straub T., Grue P., Uhse A., Lisby M., Knudsen B.R., Tange T.O., Westergaard O., Boege F. J. Biol. Chem. 273:26261-26264(1998) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH SFPQ AND TOP1.
[14]	"PSF/p54(nrb) stimulates 'jumping' of DNA topoisomerase I between separate DNA helices." Straub T., Knudsen B.R., Boege F. Biochemistry 39:7552-7558(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DNA UNWINDING.
[15]	"The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs." Zhang Z., Carmichael G.G. Cell 106:465-475(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, IDENTIFICATION IN A COMPLEX WITH NONO AND MATR3.
[16]	"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." Sewer M.B., Nguyen V.Q., Huang C.J., Tucker P.W., Kagawa N., Waterman M.R. Endocrinology 143:1280-1290(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION IN TRANSCRIPTION REGULATION, IDENTIFICATION IN A COMPLEX WITH SFPQ AND NR5A1.
[17]	"PSF and p54nrb bind a conserved stem in U5 snRNA." Peng R., Dye B.T., Perez I., Barnard D.C., Thompson A.B., Patton J.G. RNA 8:1334-1347(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PSQF AND U5 SNRNA, IDENTIFICATION IN IN U5/4/6 SNRNP SND SPLICEOSOME COMPLEXES.
[18]	"Identification of the polypyrimidine tract binding protein-associated splicing factor.p54(nrb) complex as a candidate DNA double-strand break rejoining factor." Bladen C.L., Udayakumar D., Takeda Y., Dynan W.S. J. Biol. Chem. 280:5205-5210(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DNA REPAIR, IDENTIFICATION BY MASS SPECTROMETRY, DNA-BINDING, SUBUNIT.
[19]	"P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles in an RNA-dependent manner." Fox A.H., Bond C.S., Lamond A.I. Mol. Biol. Cell 16:5304-5315(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PSPC1.
[20]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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." 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. Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[24]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"Proteomic identification of a PSF/p54nrb heterodimer as RNF43 oncoprotein-interacting proteins." Miyamoto K., Sakurai H., Sugiura T. Proteomics 8:2907-2910(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RNF43.
[28]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[29]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-5; LYS-11 AND LYS-198, MASS SPECTROMETRY.
[30]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; THR-440 AND THR-450, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[31]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, MASS SPECTROMETRY.
[33]	"Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization." Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I. Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[34]	"Structure of the heterodimer of human NONO and paraspeckle protein component 1 and analysis of its role in subnuclear body formation." Passon D.M., Lee M., Rackham O., Stanley W.A., Sadowska A., Filipovska A., Fox A.H., Bond C.S. Proc. Natl. Acad. Sci. U.S.A. 109:4846-4850(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 53-312 IN COMPLEX WITH PSPC1, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-267 AND TRP-271.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L14599 mRNA. Translation: AAC37578.1.
U89867 mRNA. Translation: AAC51852.1.
Y11289 , Y11290, Y11291, Y11292, Y11293, Y11294, Y11295, Y11296, Y11297, Y11298 Genomic DNA. Translation: CAA72157.1.
U02493 mRNA. Translation: AAA03427.1.
AK297144 mRNA. Translation: BAH12508.1.
CR456761 mRNA. Translation: CAG33042.1.
AL590762 Genomic DNA. No translation available.
CH471132 Genomic DNA. Translation: EAX05298.1.
CH471132 Genomic DNA. Translation: EAX05299.1.
CH471132 Genomic DNA. Translation: EAX05300.1.
BC002364 mRNA. Translation: AAH02364.1.
BC003129 mRNA. Translation: AAH03129.1.
BC012141 mRNA. Translation: AAH12141.1.
BC028299 mRNA. Translation: AAH28299.1.
BC069616 mRNA. Translation: AAH69616.1.
BC069639 mRNA. Translation: AAH69639.1.

IPI

IPI00304596.
IPI00922367.

PIR

G01211.
S29769.
S41768.

RefSeq

NP_001138880.1. NM_001145408.1.
NP_001138881.1. NM_001145409.1.
NP_001138882.1. NM_001145410.1.
NP_031389.3. NM_007363.4.

UniGene

Hs.533282.
Hs.700344.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3SDE	X-ray	1.90	B	53-312	[»]

ProteinModelPortal

Q15233.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29951N.

IntAct

Q15233. 35 interactions.

MINT

MINT-1131452.

STRING

9606.ENSP00000276079.

PTM databases

PhosphoSite

Q15233.

Polymorphism databases

DMDM

67469924.

2D gel databases

REPRODUCTION-2DPAGE

IPI00304596.

SWISS-2DPAGE

Q15233.

Proteomic databases

PaxDb

Q15233.

PeptideAtlas

Q15233.

PRIDE

Q15233.

Protocols and materials databases

DNASU

4841.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000276079; ENSP00000276079; ENSG00000147140.
ENST00000373841; ENSP00000362947; ENSG00000147140.
ENST00000373856; ENSP00000362963; ENSG00000147140.
ENST00000535149; ENSP00000441364; ENSG00000147140.

GeneID

4841.

KEGG

hsa:4841.

UCSC

uc004dzn.3. human.

Organism-specific databases

CTD

4841.

GeneCards

GC0XP070503.

HGNC

HGNC:7871. NONO.

HPA

CAB022069.

MIM

300084. gene.

neXtProt

NX_Q15233.

PharmGKB

PA31680.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG298586.

HOGENOM

HOG000231095.

HOVERGEN

HBG009801.

InParanoid

Q15233.

KO

K13214.

OMA

NQQYHKE.

OrthoDB

EOG4ZCT50.

PhylomeDB

Q15233.

Enzyme and pathway databases

Pathway_Interaction_DB

circadianpathway. Circadian rhythm pathway.

Gene expression databases

ArrayExpress

Q15233.

Bgee

Q15233.

CleanEx

HS_NONO.

Genevestigator

Q15233.

GermOnline

ENSG00000147140. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 2 hits.

InterPro

IPR012975. NOPS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF08075. NOPS. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]

SMART

SM00360. RRM. 2 hits.
[Graphical view]

PROSITE

PS50102. RRM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

4841.

NextBio

18654.

PMAP-CutDB

Q15233.

SOURCE

Search...

Entry information

Entry name

NONO_HUMAN

Accession

Primary (citable) accession number: Q15233
Secondary accession number(s): B7Z4C2 , D3DVV4, F5GYZ3, O00201, P30807, Q12786, Q9BQC5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 5, 2005
Last modified:	May 1, 2013
This is version 142 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.