Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q99K48 (NONO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Non-POU domain-containing octamer-binding protein

Short name=NonO protein
Gene names
Name:Nono
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length473 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.1 Ref.5

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.4 Ref.6

Subcellular location

Nucleus. Nucleusnucleolus By similarity. Nucleus speckle By similarity. Note: Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles By similarity. Ref.7

Tissue specificity

Expressed in liver (at protein level). Detected in brain, testis and kidney. Ref.7

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Sequence caution

The sequence BAB23598.1 differs from that shown. Reason: Erroneous termination at position 258. Translated as Arg.

The sequence BAB28857.1 differs from that shown. Reason: Frameshift at position 187.

Ontologies

Keywords
   Biological processBiological rhythms
DNA damage
DNA recombination
DNA repair
mRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   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

Inferred from electronic annotation. Source: UniProtKB-KW

circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

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 electronic annotation. Source: Ensembl

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

paraspeckles

Inferred from sequence orthology PubMed 19217333. Source: MGI

   Molecular_functionDNA 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

protein binding

Inferred from physical interaction Ref.4. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Spi1P174333EBI-607499,EBI-607588

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99K48-1)

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: Q99K48-2)

The sequence of this isoform differs from the canonical sequence as follows:
     220-473: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Non-POU domain-containing octamer-binding protein
PRO_0000081684

Regions

Domain76 – 14368RRM 1
Domain150 – 23182RRM 2
Region56 – 375320DBHS By similarity
Coiled coil270 – 374105 Potential
Compositional bias29 – 3810Poly-Gln
Compositional bias39 – 446Poly-Pro
Compositional bias350 – 3534Poly-Arg

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9
Modified residue51N6-acetyllysine Ref.9
Modified residue111N6-acetyllysine Ref.9
Modified residue1491Phosphoserine By similarity
Modified residue2001N6-acetyllysine Ref.9
Modified residue2971N6-acetyllysine Ref.9
Modified residue3731N6-acetyllysine Ref.9
Modified residue4301Phosphothreonine By similarity
Modified residue4421Phosphothreonine By similarity
Modified residue4521Phosphothreonine Ref.8

Natural variations

Alternative sequence220 – 473254Missing in isoform 2.
VSP_013981

Experimental info

Sequence conflict761S → T in BAB28857. Ref.2
Sequence conflict1171R → N in BAB28857. Ref.2
Sequence conflict1271A → V in AAB27887. Ref.1
Sequence conflict1531T → K in BAB28857. Ref.2
Sequence conflict1671E → G in BAB28857. Ref.2
Sequence conflict1831V → E in BAB28857. Ref.2
Sequence conflict1881R → W in BAB28857. Ref.2
Sequence conflict203 – 2042AR → VL in BAB28857. Ref.2
Sequence conflict2221R → W in AAB27887. Ref.1

Secondary structure

................ 473
Helix Strand Turn

Details...

Sequences

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

Last modified July 5, 2005. Version 3.
Checksum: F65E6AE25D471A38

FASTA47354,541
        10         20         30         40         50         60 
MQSNKAFNLE KQNHTPRKHH QHHHQQHHQQ QQQQQQQQPP PPIPANGQQA SSQNEGLTID 

        70         80         90        100        110        120 
LKNFRKPGEK TFTQRSRLFV GNLPPDITEE EMRKLFEKYG KAGEVFIHKD KGFGFIRLET 

       130        140        150        160        170        180 
RTLAEIAKVE LDNMPLRGKQ LRVRFACHSA SLTVRNLPQY VSNELLEEAF SVFGQVERAV 

       190        200        210        220        230        240 
VIVDDRGRPS GKGIVEFSGK PAARKALDRC SEGSFLLTTF PRPVTVEPMD QLDDEEGLPE 

       250        260        270        280        290        300 
KLVIKNQQFH KEREQPPRFA QPGSFEYEYA MRWKALIEME KQQQDQVDRN IKEAREKLEM 

       310        320        330        340        350        360 
EMEAARHEHQ VMLMRQDLMR RQEELRRMEE LHNQEVQKRK QLELRQEEER RRREEEMRRQ 

       370        380        390        400        410        420 
QEEMMRRQQE GFKGTFPDAR EQEIRMGQMA MGGAMGINNR GAMPPAPVPP GTPAPPGPAT 

       430        440        450        460        470 
MMPDGTLGLT PPTTERFGQA ATMEGIGAIG GTPPAFNRPA PGAEFAPNKR RRY 

« Hide

Isoform 2 [UniParc].

Checksum: CFF17042BD1E721E
Show »

FASTA21924,969

References

« Hide 'large scale' references
[1]"NonO, a non-POU-domain-containing, octamer-binding protein, is the mammalian homolog of Drosophila nonAdiss."
Yang Y.-S., Hanke J.H., Carayannopoulos L., Craft C.M., Capra J.D., Tucker P.W.
Mol. Cell. Biol. 13:5593-5603(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 195-201; 260-274; 300-306; 387-400 AND 438-445, FUNCTION.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Embryo and Lung.
[3]"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).
Strain: C57BL/6 and FVB/N.
Tissue: Mammary tumor and Olfactory epithelium.
[4]"The transcription factor Spi-1/PU.1 binds RNA and interferes with the RNA-binding protein p54nrb."
Hallier M., Tavitian A., Moreau-Gachelin F.
J. Biol. Chem. 271:11177-11181(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 298-312, INTERACTION WITH SPI1.
[5]"The intracisternal A-particle proximal enhancer-binding protein activates transcription and is identical to the RNA- and DNA-binding protein p54nrb/NonO."
Basu A., Dong B., Krainer A.R., Howe C.C.
Mol. Cell. Biol. 17:677-686(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTIONAL REGULATION, DNA-BINDING.
[6]"Expression and functional significance of mouse paraspeckle protein 1 on spermatogenesis."
Myojin R., Kuwahara S., Yasaki T., Matsunaga T., Sakurai T., Kimura M., Uesugi S., Kurihara Y.
Biol. Reprod. 71:926-932(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSPC1.
[7]"PERIOD1-associated proteins modulate the negative limb of the mammalian circadian oscillator."
Brown S.A., Ripperger J., Kadener S., Fleury-Olela F., Vilbois F., Rosbash M., Schibler U.
Science 308:693-696(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[8]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-5; LYS-11; LYS-200; LYS-297 AND LYS-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[10]"Solution structure of the N-terminal RNA recognition motif of NonO."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 68-153.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S64860 mRNA. Translation: AAB27887.1.
AK004830 mRNA. Translation: BAB23598.1. Sequence problems.
AK013444 mRNA. Translation: BAB28857.1. Sequence problems.
AK028338 mRNA. Translation: BAC25890.1.
BC005465 mRNA. Translation: AAH05465.1.
BC083074 mRNA. Translation: AAH83074.1.
CCDSCCDS30316.1. [Q99K48-1]
RefSeqNP_001239447.1. NM_001252518.1. [Q99K48-1]
NP_075633.2. NM_023144.2. [Q99K48-1]
UniGeneMm.280069.
Mm.475350.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CPJNMR-A68-153[»]
2RS8NMR-A68-153[»]
ProteinModelPortalQ99K48.
SMRQ99K48. Positions 20-306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207330. 15 interactions.
IntActQ99K48. 5 interactions.
MINTMINT-1751475.

PTM databases

PhosphoSiteQ99K48.

Proteomic databases

MaxQBQ99K48.
PaxDbQ99K48.
PRIDEQ99K48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033673; ENSMUSP00000033673; ENSMUSG00000031311. [Q99K48-1]
GeneID53610.
KEGGmmu:53610.
UCSCuc009txr.2. mouse. [Q99K48-2]
uc009txs.2. mouse. [Q99K48-1]

Organism-specific databases

CTD4841.
MGIMGI:1855692. Nono.

Phylogenomic databases

eggNOGNOG298586.
GeneTreeENSGT00390000005004.
HOVERGENHBG009801.
InParanoidQ99K48.
KOK13214.
OMANQQYHKE.
TreeFamTF315795.

Gene expression databases

ArrayExpressQ99K48.
BgeeQ99K48.
GenevestigatorQ99K48.

Family and domain databases

Gene3D3.30.70.330. 3 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

ChiTaRSNONO. mouse.
EvolutionaryTraceQ99K48.
NextBio310319.
PROQ99K48.
SOURCESearch...

Entry information

Entry nameNONO_MOUSE
AccessionPrimary (citable) accession number: Q99K48
Secondary accession number(s): Q63887, Q9CYQ4, Q9DBP2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2005
Last modified: July 9, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot