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Q15233 (NONO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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 avtivity. NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription. Plays a role in the control of circadians rhythms. Ref.14 Ref.15 Ref.16 Ref.18 Ref.35

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. 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. Ref.10 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.27

Subcellular location

Nucleus. Nucleusnucleolus. Nucleus speckle. Note: Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. Ref.34 Ref.35

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 processBiological rhythms
DNA damage
DNA recombination
DNA repair
mRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DomainCoiled coil
Repeat
   LigandDNA-binding
RNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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

circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA processing

Traceable author statement Ref.2. Source: ProtInc

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnuclear matrix

Inferred from direct assay PubMed 19874820. Source: BHF-UCL

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

paraspeckles

Inferred from direct assay PubMed 19217333. Source: MGI

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction Ref.19PubMed 16189514PubMed 21988832PubMed 23555304. Source: IntAct

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16417406. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself4EBI-350527,EBI-350527
PSPC1Q8WXF16EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 471471Non-POU domain-containing octamer-binding protein
PRO_0000081683

Regions

Domain74 – 14168RRM 1
Domain148 – 22982RRM 2
Region54 – 373320DBHS
Coiled coil268 – 372105 Potential
Compositional bias30 – 356Poly-Gln
Compositional bias36 – 427Poly-Pro
Compositional bias348 – 3514Poly-Arg

Sites

Site377 – 3782Breakpoint for translocation to form NONO-TFE3

Amino acid modifications

Modified residue11N-acetylmethionine Ref.30
Modified residue51N6-acetyllysine Ref.30
Modified residue111N6-acetyllysine Ref.30
Modified residue1471Phosphoserine Ref.31
Modified residue1981N6-acetyllysine Ref.30
Modified residue2951N6-acetyllysine By similarity
Modified residue3711N6-acetyllysine By similarity
Modified residue4281Phosphothreonine Ref.22 Ref.25 Ref.29
Modified residue4401Phosphothreonine Ref.31
Modified residue4501Phosphothreonine Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.29 Ref.31 Ref.33

Natural variations

Alternative sequence1 – 8989Missing in isoform 2.
VSP_045470

Experimental info

Mutagenesis2671Y → A: Abolishes interaction with PSPC1 and localization in nuclear paraspeckles; when associated with A-271. Ref.35
Mutagenesis2711W → A: Abolishes interaction with PSPC1 and localization in nuclear paraspeckles; when associated with A-267. Ref.35
Sequence conflict1511T → H in AAC37578. Ref.1
Sequence conflict358 – 3592QQ → HE in CAA72157. Ref.3
Sequence conflict358 – 3592QQ → HE in AAA03427. Ref.4
Sequence conflict366 – 3672QQ → HE in CAA72157. Ref.3
Sequence conflict366 – 3672QQ → HE in AAA03427. Ref.4
Sequence conflict3871M → I in BAH12508. Ref.5

Secondary structure

................................... 471
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2005. Version 4.
Checksum: 26BBD3828F5B9E49

FASTA47154,232
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 5B6CF35CAB8486D4
Show »

FASTA38243,866

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[30]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"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].
[33]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"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].
[35]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L14599 mRNA. Translation: AAC37578.1.
U89867 mRNA. Translation: AAC51852.1.
Y11289 expand/collapse EMBL AC list , 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.
CCDSCCDS14410.1. [Q15233-1]
CCDS55445.1. [Q15233-2]
PIRG01211.
S29769.
S41768.
RefSeqNP_001138880.1. NM_001145408.1. [Q15233-1]
NP_001138881.1. NM_001145409.1. [Q15233-1]
NP_001138882.1. NM_001145410.1. [Q15233-2]
NP_031389.3. NM_007363.4. [Q15233-1]
UniGeneHs.533282.
Hs.700344.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3SDEX-ray1.90B53-312[»]
ProteinModelPortalQ15233.
SMRQ15233. Positions 66-304.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110904. 126 interactions.
DIPDIP-29951N.
IntActQ15233. 38 interactions.
MINTMINT-1131452.
STRING9606.ENSP00000276079.

PTM databases

PhosphoSiteQ15233.

Polymorphism databases

DMDM67469924.

2D gel databases

REPRODUCTION-2DPAGEIPI00304596.
SWISS-2DPAGEQ15233.

Proteomic databases

MaxQBQ15233.
PaxDbQ15233.
PeptideAtlasQ15233.
PRIDEQ15233.

Protocols and materials databases

DNASU4841.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000276079; ENSP00000276079; ENSG00000147140. [Q15233-1]
ENST00000373841; ENSP00000362947; ENSG00000147140. [Q15233-1]
ENST00000373856; ENSP00000362963; ENSG00000147140. [Q15233-1]
ENST00000535149; ENSP00000441364; ENSG00000147140. [Q15233-2]
GeneID4841.
KEGGhsa:4841.
UCSCuc004dzn.3. human. [Q15233-1]

Organism-specific databases

CTD4841.
GeneCardsGC0XP070503.
HGNCHGNC:7871. NONO.
HPACAB022069.
HPA054094.
HPA054559.
MIM300084. gene.
neXtProtNX_Q15233.
Orphanet319308. Translocation renal cell carcinoma.
PharmGKBPA31680.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298586.
HOGENOMHOG000231095.
HOVERGENHBG009801.
InParanoidQ15233.
KOK13214.
OMANQQYHKE.
OrthoDBEOG7327P0.
PhylomeDBQ15233.
TreeFamTF315795.

Gene expression databases

ArrayExpressQ15233.
BgeeQ15233.
CleanExHS_NONO.
GenevestigatorQ15233.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012975. NOPS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF08075. NOPS. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNONO.
GenomeRNAi4841.
NextBio18654.
PMAP-CutDBQ15233.
PROQ15233.
SOURCESearch...

Entry information

Entry nameNONO_HUMAN
AccessionPrimary (citable) accession number: Q15233
Secondary accession number(s): B7Z4C2 expand/collapse secondary AC list , D3DVV4, F5GYZ3, O00201, P30807, Q12786, Q9BQC5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 5, 2005
Last modified: July 9, 2014
This is version 154 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM