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Protein

Non-POU domain-containing octamer-binding protein

Gene

NONO

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Important for the functional organization of GABAergic synapses. Plays a specific and important role in the regulation of synaptic RNAs and GPHN/gephyrin scaffold structure, through the regulation of GABRA2 transcript.By similarity6 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Biological rhythms, DNA damage, DNA recombination, DNA repair, mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

SIGNORiQ15233.

Names & Taxonomyi

Protein namesi
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 namesi
Name:NONO
Synonyms:NRB54
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:7871. NONO.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • nuclear matrix Source: BHF-UCL
  • nuclear speck Source: UniProtKB-SubCell
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • paraspeckles Source: MGI
  • RNA polymerase II transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Mental retardation, X-linked, syndromic, 34 (MRXS34)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA mental retardation syndrome characterized by intellectual deficit, delayed psychomotor development, poor speech, and dysmorphic features. Mental retardation is defined by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
See also OMIM:300967

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi267 – 2671Y → A: Abolishes interaction with PSPC1 and localization in nuclear paraspeckles; when associated with A-271. 1 Publication
Mutagenesisi271 – 2711W → A: Abolishes interaction with PSPC1 and localization in nuclear paraspeckles; when associated with A-267. 1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei377 – 3782Breakpoint for translocation to form NONO-TFE3

Keywords - Diseasei

Mental retardation

Organism-specific databases

MalaCardsiNONO.
MIMi300967. phenotype.
Orphaneti319308. Translocation renal cell carcinoma.
PharmGKBiPA31680.

Polymorphism and mutation databases

BioMutaiNONO.
DMDMi67469924.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471Non-POU domain-containing octamer-binding proteinPRO_0000081683Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei5 – 51N6-acetyllysine; alternateCombined sources
Cross-linki5 – 5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei6 – 61PhosphothreonineCombined sources
Modified residuei11 – 111N6-acetyllysineCombined sources
Modified residuei147 – 1471PhosphoserineCombined sources
Modified residuei198 – 1981N6-acetyllysineCombined sources
Modified residuei262 – 2621PhosphoserineCombined sources
Modified residuei295 – 2951N6-acetyllysineBy similarity
Modified residuei371 – 3711N6-acetyllysine; alternateBy similarity
Cross-linki371 – 371Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei428 – 4281PhosphothreonineCombined sources
Modified residuei440 – 4401PhosphothreonineCombined sources
Modified residuei450 – 4501PhosphothreonineCombined sources

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ15233.
MaxQBiQ15233.
PaxDbiQ15233.
PeptideAtlasiQ15233.
PRIDEiQ15233.
TopDownProteomicsiQ15233-1. [Q15233-1]

2D gel databases

REPRODUCTION-2DPAGEIPI00304596.
SWISS-2DPAGEQ15233.

PTM databases

iPTMnetiQ15233.
PhosphoSiteiQ15233.
SwissPalmiQ15233.

Miscellaneous databases

PMAP-CutDBQ15233.

Expressioni

Tissue specificityi

Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Also found in a number of breast tumor cell lines.1 Publication

Gene expression databases

BgeeiENSG00000147140.
CleanExiHS_NONO.
ExpressionAtlasiQ15233. baseline and differential.
GenevisibleiQ15233. HS.

Organism-specific databases

HPAiCAB022069.
HPA054094.
HPA054559.

Interactioni

Subunit structurei

Interacts with CPNE4 (via VWFA domain) (By similarity). Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits. NONO is a component of spliceosome and U5.4/6 snRNP complexes. Forms heterodimers with PSPC1; this involves formation of a coiled coil domain by helices from both proteins. Interacts with PSPC1 and SNRPA/U1A. Part of complex consisting of SFPQ, NONO and MATR3. Part of a complex consisting of SFPQ, NONO and NR5A1. Part of a complex consisting of SFPQ, NONO and TOP1. Interacts with SPI1. Interacts with RNF43. Interacts with PER1 and PER2.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-350527,EBI-350527
C11orf68Q9H3H33EBI-350527,EBI-721765
DDX6P261963EBI-10203843,EBI-351257
EBNA-LPQ8AZK72EBI-350527,EBI-1185167From a different organism.
LMO4P619683EBI-10203843,EBI-2798728
PIN1Q135264EBI-350527,EBI-714158
PRKAA2P546463EBI-10203843,EBI-1383852
PSPC1Q8WXF111EBI-350527,EBI-1392258

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi110904. 166 interactions.
DIPiDIP-29951N.
IntActiQ15233. 51 interactions.
MINTiMINT-1131452.
STRINGi9606.ENSP00000276079.

Structurei

Secondary structure

1
471
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi72 – 743Combined sources
Beta strandi75 – 806Combined sources
Helixi87 – 948Combined sources
Helixi95 – 973Combined sources
Beta strandi100 – 1067Combined sources
Turni107 – 1104Combined sources
Beta strandi111 – 1188Combined sources
Helixi119 – 12911Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi149 – 1546Combined sources
Helixi161 – 1688Combined sources
Beta strandi174 – 1829Combined sources
Beta strandi187 – 19711Combined sources
Helixi198 – 21013Combined sources
Beta strandi213 – 2186Combined sources
Beta strandi223 – 2264Combined sources
Helixi238 – 2403Combined sources
Helixi245 – 2506Combined sources
Beta strandi255 – 2573Combined sources
Helixi263 – 30341Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SDEX-ray1.90B53-312[»]
ProteinModelPortaliQ15233.
SMRiQ15233. Positions 66-368.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 14168RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini148 – 22982RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 373320DBHSAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili268 – 372105Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi30 – 356Poly-Gln
Compositional biasi36 – 427Poly-Pro
Compositional biasi348 – 3514Poly-Arg

Sequence similaritiesi

Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG0115. Eukaryota.
ENOG410XQA0. LUCA.
GeneTreeiENSGT00390000005004.
HOGENOMiHOG000231095.
HOVERGENiHBG009801.
InParanoidiQ15233.
KOiK13214.
OMAiNQQYHKE.
OrthoDBiEOG091G09T7.
PhylomeDBiQ15233.
TreeFamiTF315795.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012975. NOPS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF08075. NOPS. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15233-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MQSNKTFNLE KQNHTPRKHH QHHHQQQHHQ QQQQQPPPPP IPANGQQASS
60 70 80 90 100
QNEGLTIDLK NFRKPGEKTF TQRSRLFVGN LPPDITEEEM RKLFEKYGKA
110 120 130 140 150
GEVFIHKDKG FGFIRLETRT LAEIAKVELD NMPLRGKQLR VRFACHSASL
160 170 180 190 200
TVRNLPQYVS NELLEEAFSV FGQVERAVVI VDDRGRPSGK GIVEFSGKPA
210 220 230 240 250
ARKALDRCSE GSFLLTTFPR PVTVEPMDQL DDEEGLPEKL VIKNQQFHKE
260 270 280 290 300
REQPPRFAQP GSFEYEYAMR WKALIEMEKQ QQDQVDRNIK EAREKLEMEM
310 320 330 340 350
EAARHEHQVM LMRQDLMRRQ EELRRMEELH NQEVQKRKQL ELRQEEERRR
360 370 380 390 400
REEEMRRQQE EMMRRQQEGF KGTFPDAREQ EIRMGQMAMG GAMGINNRGA
410 420 430 440 450
MPPAPVPAGT PAPPGPATMM PDGTLGLTPP TTERFGQAAT MEGIGAIGGT
460 470
PPAFNRAAPG AEFAPNKRRR Y
Length:471
Mass (Da):54,232
Last modified:July 5, 2005 - v4
Checksum:i26BBD3828F5B9E49
GO
Isoform 2 (identifier: Q15233-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:382
Mass (Da):43,866
Checksum:i5B6CF35CAB8486D4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti151 – 1511T → H in AAC37578 (PubMed:8371983).Curated
Sequence conflicti358 – 3592QQ → HE in CAA72157 (PubMed:9341872).Curated
Sequence conflicti358 – 3592QQ → HE in AAA03427 (Ref. 4) Curated
Sequence conflicti366 – 3672QQ → HE in CAA72157 (PubMed:9341872).Curated
Sequence conflicti366 – 3672QQ → HE in AAA03427 (Ref. 4) Curated
Sequence conflicti387 – 3871M → I in BAH12508 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8989Missing in isoform 2. CuratedVSP_045470Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14410.1. [Q15233-1]
CCDS55445.1. [Q15233-2]
PIRiG01211.
S29769.
S41768.
RefSeqiNP_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]
UniGeneiHs.533282.
Hs.700344.

Genome annotation databases

EnsembliENST00000276079; ENSP00000276079; ENSG00000147140. [Q15233-1]
ENST00000373841; ENSP00000362947; ENSG00000147140. [Q15233-1]
ENST00000373856; ENSP00000362963; ENSG00000147140. [Q15233-1]
ENST00000535149; ENSP00000441364; ENSG00000147140. [Q15233-2]
GeneIDi4841.
KEGGihsa:4841.
UCSCiuc004dzn.5. human. [Q15233-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14410.1. [Q15233-1]
CCDS55445.1. [Q15233-2]
PIRiG01211.
S29769.
S41768.
RefSeqiNP_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]
UniGeneiHs.533282.
Hs.700344.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SDEX-ray1.90B53-312[»]
ProteinModelPortaliQ15233.
SMRiQ15233. Positions 66-368.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110904. 166 interactions.
DIPiDIP-29951N.
IntActiQ15233. 51 interactions.
MINTiMINT-1131452.
STRINGi9606.ENSP00000276079.

PTM databases

iPTMnetiQ15233.
PhosphoSiteiQ15233.
SwissPalmiQ15233.

Polymorphism and mutation databases

BioMutaiNONO.
DMDMi67469924.

2D gel databases

REPRODUCTION-2DPAGEIPI00304596.
SWISS-2DPAGEQ15233.

Proteomic databases

EPDiQ15233.
MaxQBiQ15233.
PaxDbiQ15233.
PeptideAtlasiQ15233.
PRIDEiQ15233.
TopDownProteomicsiQ15233-1. [Q15233-1]

Protocols and materials databases

DNASUi4841.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000276079; ENSP00000276079; ENSG00000147140. [Q15233-1]
ENST00000373841; ENSP00000362947; ENSG00000147140. [Q15233-1]
ENST00000373856; ENSP00000362963; ENSG00000147140. [Q15233-1]
ENST00000535149; ENSP00000441364; ENSG00000147140. [Q15233-2]
GeneIDi4841.
KEGGihsa:4841.
UCSCiuc004dzn.5. human. [Q15233-1]

Organism-specific databases

CTDi4841.
GeneCardsiNONO.
HGNCiHGNC:7871. NONO.
HPAiCAB022069.
HPA054094.
HPA054559.
MalaCardsiNONO.
MIMi300084. gene.
300967. phenotype.
neXtProtiNX_Q15233.
Orphaneti319308. Translocation renal cell carcinoma.
PharmGKBiPA31680.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0115. Eukaryota.
ENOG410XQA0. LUCA.
GeneTreeiENSGT00390000005004.
HOGENOMiHOG000231095.
HOVERGENiHBG009801.
InParanoidiQ15233.
KOiK13214.
OMAiNQQYHKE.
OrthoDBiEOG091G09T7.
PhylomeDBiQ15233.
TreeFamiTF315795.

Enzyme and pathway databases

SIGNORiQ15233.

Miscellaneous databases

GeneWikiiNONO.
GenomeRNAii4841.
PMAP-CutDBQ15233.
PROiQ15233.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000147140.
CleanExiHS_NONO.
ExpressionAtlasiQ15233. baseline and differential.
GenevisibleiQ15233. HS.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012975. NOPS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF08075. NOPS. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNONO_HUMAN
AccessioniPrimary (citable) accession number: Q15233
Secondary accession number(s): B7Z4C2
, D3DVV4, F5GYZ3, O00201, P30807, Q12786, Q9BQC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 5, 2005
Last modified: September 7, 2016
This is version 178 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.