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Q99K48

- NONO_MOUSE

UniProt

Q99K48 - NONO_MOUSE

Protein

Non-POU domain-containing octamer-binding protein

Gene

Nono

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (05 Jul 2005)
      Previous versions | rss
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    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.3 Publications

    GO - Molecular functioni

    1. core promoter binding Source: UniProtKB
    2. nucleotide binding Source: InterPro
    3. protein binding Source: UniProtKB
    4. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. circadian rhythm Source: UniProtKB
    2. DNA recombination Source: UniProtKB-KW
    3. DNA repair Source: UniProtKB-KW
    4. mRNA processing Source: UniProtKB-KW
    5. negative regulation of transcription, DNA-templated Source: UniProtKB
    6. regulation of circadian rhythm Source: UniProtKB
    7. RNA splicing Source: UniProtKB-KW
    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
    Gene namesi
    Name:Nono
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1855692. Nono.

    Subcellular locationi

    Nucleus 1 Publication. Nucleusnucleolus By similarity. Nucleus speckle By similarity
    Note: Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles.By similarity

    GO - Cellular componenti

    1. nuclear matrix Source: Ensembl
    2. nuclear speck Source: UniProtKB-SubCell
    3. nucleolus Source: UniProtKB-SubCell
    4. nucleus Source: UniProtKB
    5. paraspeckles Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 473473Non-POU domain-containing octamer-binding proteinPRO_0000081684Add
    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 residuei149 – 1491PhosphoserineBy similarity
    Modified residuei200 – 2001N6-acetyllysine1 Publication
    Modified residuei297 – 2971N6-acetyllysine1 Publication
    Modified residuei373 – 3731N6-acetyllysine1 Publication
    Modified residuei430 – 4301PhosphothreonineBy similarity
    Modified residuei442 – 4421PhosphothreonineBy similarity
    Modified residuei452 – 4521Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ99K48.
    PaxDbiQ99K48.
    PRIDEiQ99K48.

    PTM databases

    PhosphoSiteiQ99K48.

    Expressioni

    Tissue specificityi

    Expressed in liver and suprachiasmatic nuclei, hippocampus and neocortex (at protein level). Detected in testis and kidney.2 Publications

    Gene expression databases

    ArrayExpressiQ99K48.
    BgeeiQ99K48.
    GenevestigatoriQ99K48.

    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 PER2.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Spi1P174333EBI-607499,EBI-607588

    Protein-protein interaction databases

    BioGridi207330. 15 interactions.
    IntActiQ99K48. 5 interactions.
    MINTiMINT-1751475.

    Structurei

    Secondary structure

    1
    473
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi77 – 826
    Helixi89 – 957
    Helixi97 – 993
    Beta strandi103 – 1086
    Turni109 – 1124
    Beta strandi113 – 1175
    Beta strandi119 – 1213
    Helixi122 – 13110
    Beta strandi142 – 1476

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CPJNMR-A68-153[»]
    2RS8NMR-A68-153[»]
    ProteinModelPortaliQ99K48.
    SMRiQ99K48. Positions 20-306.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99K48.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini76 – 14368RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini150 – 23182RRM 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni56 – 375320DBHSBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili270 – 374105Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi29 – 3810Poly-Gln
    Compositional biasi39 – 446Poly-Pro
    Compositional biasi350 – 3534Poly-Arg

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG298586.
    GeneTreeiENSGT00390000005004.
    HOVERGENiHBG009801.
    InParanoidiQ99K48.
    KOiK13214.
    OMAiNQQYHKE.
    TreeFamiTF315795.

    Family and domain databases

    Gene3Di3.30.70.330. 3 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: Q99K48-1) [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

    MQSNKAFNLE KQNHTPRKHH QHHHQQHHQQ QQQQQQQQPP PPIPANGQQA    50
    SSQNEGLTID LKNFRKPGEK TFTQRSRLFV GNLPPDITEE EMRKLFEKYG 100
    KAGEVFIHKD KGFGFIRLET RTLAEIAKVE LDNMPLRGKQ LRVRFACHSA 150
    SLTVRNLPQY VSNELLEEAF SVFGQVERAV VIVDDRGRPS GKGIVEFSGK 200
    PAARKALDRC SEGSFLLTTF PRPVTVEPMD QLDDEEGLPE KLVIKNQQFH 250
    KEREQPPRFA QPGSFEYEYA MRWKALIEME KQQQDQVDRN IKEAREKLEM 300
    EMEAARHEHQ VMLMRQDLMR RQEELRRMEE LHNQEVQKRK QLELRQEEER 350
    RRREEEMRRQ QEEMMRRQQE GFKGTFPDAR EQEIRMGQMA MGGAMGINNR 400
    GAMPPAPVPP GTPAPPGPAT MMPDGTLGLT PPTTERFGQA ATMEGIGAIG 450
    GTPPAFNRPA PGAEFAPNKR RRY 473
    Length:473
    Mass (Da):54,541
    Last modified:July 5, 2005 - v3
    Checksum:iF65E6AE25D471A38
    GO
    Isoform 2 (identifier: Q99K48-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         220-473: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:219
    Mass (Da):24,969
    Checksum:iCFF17042BD1E721E
    GO

    Sequence cautioni

    The sequence BAB28857.1 differs from that shown. Reason: Frameshift at position 187.
    The sequence BAB23598.1 differs from that shown. Reason: Erroneous termination at position 258. Translated as Arg.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761S → T in BAB28857. (PubMed:16141072)Curated
    Sequence conflicti117 – 1171R → N in BAB28857. (PubMed:16141072)Curated
    Sequence conflicti127 – 1271A → V in AAB27887. (PubMed:8355702)Curated
    Sequence conflicti153 – 1531T → K in BAB28857. (PubMed:16141072)Curated
    Sequence conflicti167 – 1671E → G in BAB28857. (PubMed:16141072)Curated
    Sequence conflicti183 – 1831V → E in BAB28857. (PubMed:16141072)Curated
    Sequence conflicti188 – 1881R → W in BAB28857. (PubMed:16141072)Curated
    Sequence conflicti203 – 2042AR → VL in BAB28857. (PubMed:16141072)Curated
    Sequence conflicti222 – 2221R → W in AAB27887. (PubMed:8355702)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei220 – 473254Missing in isoform 2. 1 PublicationVSP_013981Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS30316.1. [Q99K48-1]
    RefSeqiNP_001239447.1. NM_001252518.1. [Q99K48-1]
    NP_075633.2. NM_023144.2. [Q99K48-1]
    UniGeneiMm.280069.
    Mm.475350.

    Genome annotation databases

    EnsembliENSMUST00000033673; ENSMUSP00000033673; ENSMUSG00000031311. [Q99K48-1]
    GeneIDi53610.
    KEGGimmu:53610.
    UCSCiuc009txr.2. mouse. [Q99K48-2]
    uc009txs.2. mouse. [Q99K48-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS30316.1. [Q99K48-1 ]
    RefSeqi NP_001239447.1. NM_001252518.1. [Q99K48-1 ]
    NP_075633.2. NM_023144.2. [Q99K48-1 ]
    UniGenei Mm.280069.
    Mm.475350.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CPJ NMR - A 68-153 [» ]
    2RS8 NMR - A 68-153 [» ]
    ProteinModelPortali Q99K48.
    SMRi Q99K48. Positions 20-306.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207330. 15 interactions.
    IntActi Q99K48. 5 interactions.
    MINTi MINT-1751475.

    PTM databases

    PhosphoSitei Q99K48.

    Proteomic databases

    MaxQBi Q99K48.
    PaxDbi Q99K48.
    PRIDEi Q99K48.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033673 ; ENSMUSP00000033673 ; ENSMUSG00000031311 . [Q99K48-1 ]
    GeneIDi 53610.
    KEGGi mmu:53610.
    UCSCi uc009txr.2. mouse. [Q99K48-2 ]
    uc009txs.2. mouse. [Q99K48-1 ]

    Organism-specific databases

    CTDi 4841.
    MGIi MGI:1855692. Nono.

    Phylogenomic databases

    eggNOGi NOG298586.
    GeneTreei ENSGT00390000005004.
    HOVERGENi HBG009801.
    InParanoidi Q99K48.
    KOi K13214.
    OMAi NQQYHKE.
    TreeFami TF315795.

    Miscellaneous databases

    ChiTaRSi NONO. mouse.
    EvolutionaryTracei Q99K48.
    NextBioi 310319.
    PROi Q99K48.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99K48.
    Bgeei Q99K48.
    Genevestigatori Q99K48.

    Family and domain databases

    Gene3Di 3.30.70.330. 3 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. "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.
      , 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. "Distinct roles of DBHS family members in the circadian transcriptional feedback loop."
      Kowalska E., Ripperger J.A., Muheim C., Maier B., Kurihara Y., Fox A.H., Kramer A., Brown S.A.
      Mol. Cell. Biol. 32:4585-4594(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PER1 AND PER2.
    10. "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.
    11. "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.

    Entry informationi

    Entry nameiNONO_MOUSE
    AccessioniPrimary (citable) accession number: Q99K48
    Secondary accession number(s): Q63887, Q9CYQ4, Q9DBP2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3