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Q15233

- NONO_HUMAN

UniProt

Q15233 - NONO_HUMAN

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Protein

Non-POU domain-containing octamer-binding protein

Gene
NONO, NRB54
Organism
Homo sapiens (Human)
Status
Reviewed - 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.5 Publications

Sites

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

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. nucleotide binding Source: InterPro
  4. poly(A) RNA binding Source: UniProtKB
  5. protein binding Source: UniProtKB

GO - Biological processi

  1. circadian rhythm Source: UniProtKB
  2. DNA recombination Source: UniProtKB-KW
  3. DNA repair Source: UniProtKB-KW
  4. mRNA processing Source: ProtInc
  5. regulation of transcription, DNA-templated Source: UniProtKB-KW
  6. RNA splicing Source: ProtInc
  7. transcription, DNA-templated Source: UniProtKB-KW
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

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
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:7871. NONO.

Subcellular locationi

Nucleus. Nucleusnucleolus. Nucleus speckle
Note: Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles.2 Publications

GO - Cellular componenti

  1. nuclear matrix Source: BHF-UCL
  2. nuclear speck Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB
  4. paraspeckles Source: MGI
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.

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

Organism-specific databases

Orphaneti319308. Translocation renal cell carcinoma.
PharmGKBiPA31680.

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-acetylmethionine1 Publication
Modified residuei5 – 51N6-acetyllysine1 Publication
Modified residuei11 – 111N6-acetyllysine1 Publication
Modified residuei147 – 1471Phosphoserine1 Publication
Modified residuei198 – 1981N6-acetyllysine1 Publication
Modified residuei295 – 2951N6-acetyllysine By similarity
Modified residuei371 – 3711N6-acetyllysine By similarity
Modified residuei428 – 4281Phosphothreonine3 Publications
Modified residuei440 – 4401Phosphothreonine1 Publication
Modified residuei450 – 4501Phosphothreonine10 Publications

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15233.
PaxDbiQ15233.
PeptideAtlasiQ15233.
PRIDEiQ15233.

2D gel databases

REPRODUCTION-2DPAGEIPI00304596.
SWISS-2DPAGEQ15233.

PTM databases

PhosphoSiteiQ15233.

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

ArrayExpressiQ15233.
BgeeiQ15233.
CleanExiHS_NONO.
GenevestigatoriQ15233.

Organism-specific databases

HPAiCAB022069.
HPA054094.
HPA054559.

Interactioni

Subunit structurei

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 PER2.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-350527,EBI-350527
PSPC1Q8WXF16EBI-350527,EBI-1392258

Protein-protein interaction databases

BioGridi110904. 127 interactions.
DIPiDIP-29951N.
IntActiQ15233. 38 interactions.
MINTiMINT-1131452.
STRINGi9606.ENSP00000276079.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SDEX-ray1.90B53-312[»]
ProteinModelPortaliQ15233.
SMRiQ15233. Positions 66-304.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 14168RRM 1Add
BLAST
Domaini148 – 22982RRM 2Add
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili268 – 372105 Reviewed predictionAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG298586.
HOGENOMiHOG000231095.
HOVERGENiHBG009801.
InParanoidiQ15233.
KOiK13214.
OMAiNQQYHKE.
OrthoDBiEOG7327P0.
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]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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

MQSNKTFNLE KQNHTPRKHH QHHHQQQHHQ QQQQQPPPPP IPANGQQASS    50
QNEGLTIDLK NFRKPGEKTF TQRSRLFVGN LPPDITEEEM RKLFEKYGKA 100
GEVFIHKDKG FGFIRLETRT LAEIAKVELD NMPLRGKQLR VRFACHSASL 150
TVRNLPQYVS NELLEEAFSV FGQVERAVVI VDDRGRPSGK GIVEFSGKPA 200
ARKALDRCSE GSFLLTTFPR PVTVEPMDQL DDEEGLPEKL VIKNQQFHKE 250
REQPPRFAQP GSFEYEYAMR WKALIEMEKQ QQDQVDRNIK EAREKLEMEM 300
EAARHEHQVM LMRQDLMRRQ EELRRMEELH NQEVQKRKQL ELRQEEERRR 350
REEEMRRQQE EMMRRQQEGF KGTFPDAREQ EIRMGQMAMG GAMGINNRGA 400
MPPAPVPAGT PAPPGPATMM PDGTLGLTPP TTERFGQAAT MEGIGAIGGT 450
PPAFNRAAPG AEFAPNKRRR Y 471
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8989Missing in isoform 2. VSP_045470Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti151 – 1511T → H in AAC37578. 1 Publication
Sequence conflicti358 – 3592QQ → HE in CAA72157. 1 Publication
Sequence conflicti358 – 3592QQ → HE in AAA03427. 1 Publication
Sequence conflicti366 – 3672QQ → HE in CAA72157. 1 Publication
Sequence conflicti366 – 3672QQ → HE in AAA03427. 1 Publication
Sequence conflicti387 – 3871M → I in BAH12508. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human. [Q15233-1]

Polymorphism databases

DMDMi67469924.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14410.1. [Q15233-1 ]
CCDS55445.1. [Q15233-2 ]
PIRi G01211.
S29769.
S41768.
RefSeqi NP_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 ]
UniGenei Hs.533282.
Hs.700344.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3SDE X-ray 1.90 B 53-312 [» ]
ProteinModelPortali Q15233.
SMRi Q15233. Positions 66-304.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110904. 127 interactions.
DIPi DIP-29951N.
IntActi Q15233. 38 interactions.
MINTi MINT-1131452.
STRINGi 9606.ENSP00000276079.

PTM databases

PhosphoSitei Q15233.

Polymorphism databases

DMDMi 67469924.

2D gel databases

REPRODUCTION-2DPAGE IPI00304596.
SWISS-2DPAGE Q15233.

Proteomic databases

MaxQBi Q15233.
PaxDbi Q15233.
PeptideAtlasi Q15233.
PRIDEi Q15233.

Protocols and materials databases

DNASUi 4841.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000276079 ; ENSP00000276079 ; ENSG00000147140 . [Q15233-1 ]
ENST00000373841 ; ENSP00000362947 ; ENSG00000147140 . [Q15233-1 ]
ENST00000373856 ; ENSP00000362963 ; ENSG00000147140 . [Q15233-1 ]
ENST00000535149 ; ENSP00000441364 ; ENSG00000147140 . [Q15233-2 ]
GeneIDi 4841.
KEGGi hsa:4841.
UCSCi uc004dzn.3. human. [Q15233-1 ]

Organism-specific databases

CTDi 4841.
GeneCardsi GC0XP070503.
HGNCi HGNC:7871. NONO.
HPAi CAB022069.
HPA054094.
HPA054559.
MIMi 300084. gene.
neXtProti NX_Q15233.
Orphaneti 319308. Translocation renal cell carcinoma.
PharmGKBi PA31680.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG298586.
HOGENOMi HOG000231095.
HOVERGENi HBG009801.
InParanoidi Q15233.
KOi K13214.
OMAi NQQYHKE.
OrthoDBi EOG7327P0.
PhylomeDBi Q15233.
TreeFami TF315795.

Miscellaneous databases

GeneWikii NONO.
GenomeRNAii 4841.
NextBioi 18654.
PMAP-CutDB Q15233.
PROi Q15233.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15233.
Bgeei Q15233.
CleanExi HS_NONO.
Genevestigatori Q15233.

Family and domain databases

Gene3Di 3.30.70.330. 2 hits.
InterProi IPR012975. NOPS.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF08075. NOPS. 1 hit.
PF00076. RRM_1. 2 hits.
[Graphical view ]
SMARTi SM00360. RRM. 2 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

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 3, 2014
This is version 155 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

External Data

Dasty 3

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