Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q15233

- NONO_HUMAN

UniProt

Q15233 - NONO_HUMAN

Protein

Non-POU domain-containing octamer-binding protein

Gene

NONO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 4 (05 Jul 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. core promoter binding Source: UniProtKB
    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. negative regulation of transcription, DNA-templated Source: UniProtKB
    6. regulation of circadian rhythm Source: UniProtKB
    7. RNA splicing Source: ProtInc
    8. transcription, DNA-templated Source: UniProtKB-KW

    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.

    GO - Cellular componenti

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

    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-acetyllysineBy similarity
    Modified residuei371 – 3711N6-acetyllysineBy 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 PER2.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-350527,EBI-350527
    EBNA-LPQ8AZK72EBI-350527,EBI-1185167From a different organism.
    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.
    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

    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

    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. 1 PublicationCurated
    Sequence conflicti366 – 3672QQ → HE in CAA72157. (PubMed:9341872)Curated
    Sequence conflicti366 – 3672QQ → HE in AAA03427. 1 PublicationCurated
    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:
    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

    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: October 1, 2014
    This is version 156 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