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Reviewed, UniProtKB/Swiss-Prot Q15233 (NONO_HUMAN)

Last modified January 19, 2010. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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
    p54(nrb)
      Short name=p54nrb
    55 kDa nuclear protein
    NMT55
    DNA-binding p52/p100 complex, 52 kDa subunit
Gene names
Name: NONO
Synonyms: NRB54
OrganismHomo sapiens (Human) [Complete 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 By similarity. Involved in pre-mRNA splicing, probably as an 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/SF-1 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. Ref.11 Ref.12 Ref.13 Ref.15

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/SF-1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SPI1 By similarity. Interacts with RNF43. Ref.15 Ref.7 Ref.14 Ref.16 Ref.25

Subcellular location

Nucleus.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-350527,EBI-350527
PSPC1Q8WXF14EBI-350527,EBI-1392258
RxraP287001EBI-350527,EBI-346715From a different organism.
SFPQP23246-11EBI-350527,EBI-355463

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 residue51N6-acetyllysine Ref.29
Modified residue111N6-acetyllysine Ref.29
Modified residue961N6-acetyllysine Ref.29
Modified residue1471Phosphoserine Ref.22 Ref.24
Modified residue1981N6-acetyllysine Ref.29
Modified residue4281Phosphothreonine Ref.19 Ref.23 Ref.27 Ref.28
Modified residue4501Phosphothreonine Ref.22 Ref.24 Ref.19 Ref.23 Ref.27 Ref.28 Ref.17 Ref.18 Ref.20 Ref.21
Modified residue4671N6-acetyllysine Ref.29

Experimental info

Sequence conflict191H → K Ref.5
Sequence conflict1511T → H in AAC37578. Ref.1
Sequence conflict358 – 3592QQ → HE Ref.3
Sequence conflict358 – 3592QQ → HE Ref.4
Sequence conflict366 – 3672QQ → HE Ref.3
Sequence conflict366 – 3672QQ → HE Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q15233-1 [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

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: 8371983] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 9360842] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 9341872] [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].
[5]"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].
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cervix, Kidney, Muscle and Skin.
[7]"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: 8439294] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21 AND 133-153, BLOCKAGE OF N-TERMINUS, SUBUNIT.
[8]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.
[9]"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: 9393982] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION.
[10]"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: 9756848] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH SFPQ AND TOP1.
[11]"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: 10858305] [Abstract]
Cited for: FUNCTION IN DNA UNWINDING.
[12]"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: 11525732] [Abstract]
Cited for: FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, IDENTIFICATION IN A COMPLEX WITH NONO AND MATR3.
[13]"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: 11897684] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION IN TRANSCRIPTION REGULATION, IDENTIFICATION IN A COMPLEX WITH SFPQ AND NR5A1.
[14]"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: 12403470] [Abstract]
Cited for: INTERACTION WITH PSQF AND U5 SNRNA, IDENTIFICATION IN IN U5/4/6 SNRNP SND SPLICEOSOME COMPLEXES.
[15]"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: 15590677] [Abstract]
Cited for: FUNCTION IN DNA REPAIR, IDENTIFICATION BY MASS SPECTROMETRY, DNA-BINDING, SUBUNIT.
[16]"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: 16148043] [Abstract]
Cited for: INTERACTION WITH PSPC1.
[17]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, MASS SPECTROMETRY.
Tissue: Epithelium.
[18]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, MASS SPECTROMETRY.
Tissue: Epithelium.
[19]"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: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, MASS SPECTROMETRY.
Tissue: Epithelium.
[20]"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: 17693683] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, MASS SPECTROMETRY.
[21]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-450, MASS SPECTROMETRY.
[22]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND THR-450, MASS SPECTROMETRY.
[23]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, MASS SPECTROMETRY.
[24]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND THR-450, MASS SPECTROMETRY.
[25]"Proteomic identification of a PSF/p54nrb heterodimer as RNF43 oncoprotein-interacting proteins."
Miyamoto K., Sakurai H., Sugiura T.
Proteomics 8:2907-2910(2008) [PubMed: 18655028] [Abstract]
Cited for: INTERACTION WITH RNF43.
[26]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[27]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, MASS SPECTROMETRY.
[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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428 AND THR-450, MASS SPECTROMETRY.
Tissue: 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., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-11; LYS-96; LYS-198 AND LYS-467, MASS SPECTROMETRY.
+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.
CR456761 mRNA. Translation: CAG33042.1.
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.
IPIIPI00304596.
PIRG01211.
S29769.
S41768.
RefSeqNP_001138880.1.
NP_001138881.1.
NP_001138882.1.
NP_031389.3.
UniGeneHs.533282
Hs.700344

3D structure databases

SMRQ15233. Positions 67-151, 72-206.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29951N.
IntActQ15233. 23 interactions.
STRINGQ15233.

PTM databases

PhosphoSiteQ15233.

2-D gel databases

SWISS-2DPAGEQ15233.
REPRODUCTION-2DPAGEIPI00304596.

Proteomic databases

PeptideAtlasQ15233.
PRIDEQ15233.

Genome annotation databases

EnsemblENST00000276079; ENSP00000276079; ENSG00000147140; Homo sapiens. [Genome view]
ENST00000373841; ENSP00000362947; ENSG00000147140; Homo sapiens. [Genome view]
ENST00000373856; ENSP00000362963; ENSG00000147140; Homo sapiens. [Genome view]
GeneID4841.
KEGGhsa:4841.
NMPDRfig|9606.3.peg.32966.
UCSCuc004dzn.1. human.

Organism-specific databases

CTD4841.
GeneCardsGC0XP070420.
H-InvDBHIX0016862.
HIX0038889.
HGNCHGNC:7871. NONO.
HPACAB022069.
MIM300084. gene.
PharmGKBPA31680.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG18466.
HOGENOMHBG715412.
HOVERGENQ15233.
InParanoidQ15233.
OMAKQNHAPR.
OrthoDBEOG941SXM.
PhylomeDBQ15233.

Enzyme and pathway databases

Pathway_Interaction_DBcircadianpathway. Circadian rhythm pathway.

Gene expression databases

ArrayExpressQ15233.
BgeeQ15233.
CleanExHS_NONO.
GenevestigatorQ15233.
GermOnlineENSG00000147140. Homo sapiens.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR012975. NOPS.
IPR000504. RRM_RNP1.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
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 Resources

NextBio18654.
PMAP-CutDBQ15233.
SOURCESearch...

Entry information

Entry nameNONO_HUMAN
AccessionPrimary (citable) accession number: Q15233
Secondary accession number(s): O00201 expand/collapse secondary AC list , P30807, Q12786, Q9BQC5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 5, 2005
Last modified: January 19, 2010
This is version 111 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome X

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents