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Q9JJF3

- NO66_MOUSE

UniProt

Q9JJF3 - NO66_MOUSE

Protein

Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66

Gene

No66

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (19 Jan 2010)
      Previous versions | rss
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    Functioni

    Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation. May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation By similarity. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2).By similarity1 Publication

    Catalytic activityi

    L-histidine-[60S ribosomal protein L8] + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-histidine-[60S ribosomal protein L8] + succinate + CO2.1 Publication
    Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2.1 Publication
    Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2.1 Publication

    Cofactori

    Binds 1 Fe2+ ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi302 – 3021Iron; catalyticCurated
    Metal bindingi304 – 3041Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi367 – 3671Iron; catalyticCurated

    GO - Molecular functioni

    1. histone demethylase activity (H3-K36 specific) Source: UniProtKB
    2. histone demethylase activity (H3-K4 specific) Source: UniProtKB
    3. iron ion binding Source: UniProtKB
    4. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors Source: UniProtKB
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. chromatin remodeling Source: MGI
    2. histone H3-K36 demethylation Source: UniProtKB
    3. histone H3-K4 demethylation Source: UniProtKB
    4. negative regulation of osteoblast differentiation Source: UniProtKB
    5. negative regulation of transcription, DNA-templated Source: UniProtKB
    6. ribosome biogenesis Source: MGI
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Dioxygenase, Oxidoreductase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66 (EC:1.14.11.-, EC:1.14.11.27)
    Alternative name(s):
    Histone lysine demethylase NO66
    Gene namesi
    Name:No66
    Synonyms:Mapjd
    ORF Names:MNCb-7109
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:1919202. 2410016O06Rik.

    Subcellular locationi

    Nucleusnucleolus By similarity. Nucleusnucleoplasm 2 Publications

    GO - Cellular componenti

    1. nucleolus Source: MGI
    2. nucleoplasm Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi302 – 3021H → A: Loss of demethylase activity. 1 Publication
    Mutagenesisi367 – 3671H → A: Loss of demethylase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 603603Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66PRO_0000264614Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei91 – 911PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ9JJF3.
    PRIDEiQ9JJF3.

    PTM databases

    PhosphoSiteiQ9JJF3.

    Expressioni

    Tissue specificityi

    Present in developing bones (at protein level). Widely but not ubiquitously expressed.

    Gene expression databases

    BgeeiQ9JJF3.
    CleanExiMM_2410016O06RIK.
    GenevestigatoriQ9JJF3.

    Interactioni

    Subunit structurei

    Interacts with SP7/OSX; the interaction is direct. Interacts with PHF19; leading to its recruitment to H3K36me3 sites. Interacts with MYC By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Sp7Q8VI673EBI-7608809,EBI-7608836

    Protein-protein interaction databases

    BioGridi215052. 1 interaction.
    IntActiQ9JJF3. 3 interactions.
    MINTiMINT-4130008.
    STRINGi10090.ENSMUSP00000057984.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JJF3.
    SMRiQ9JJF3. Positions 144-600.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini256 – 401146JmjCPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MINA53/NO66 family. NO66 subfamily.Curated
    Contains 1 JmjC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG83808.
    GeneTreeiENSGT00390000000083.
    HOGENOMiHOG000030688.
    HOVERGENiHBG060021.
    InParanoidiB2RQV2.
    KOiK16914.
    OMAiTVENSRV.
    OrthoDBiEOG74FF0N.
    PhylomeDBiQ9JJF3.
    TreeFamiTF318659.

    Family and domain databases

    InterProiIPR003347. JmjC_dom.
    [Graphical view]
    PfamiPF08007. Cupin_4. 1 hit.
    [Graphical view]
    SMARTiSM00558. JmjC. 1 hit.
    [Graphical view]
    PROSITEiPS51184. JMJC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9JJF3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDELPNGNGA ALLKRGRGRR RRHPQSQPRG ASVLALPLRP RKIRRHRKSA    50
    AASRVAALRA RALRSEDSDS KVAVASVRGK RKRPAELLEA SRSAEPRPVS 100
    ARPRSASATL PSRVEGWAAL SRNLGTAAPP PPGSHADEPG RPRASPLQQV 150
    LTELNGIPSS RRRAARLFEW LLAPLPPDHF YRRLWEREAV LVRRQDRSYY 200
    EGLFSTADLD SMLRYEDVQF GQHLDAARYV DGRRETLNPP GRALPAAAWS 250
    LYRAGCSLRL LCPQAFSPTV WQFLAVLQEQ FGSMAGSNVY LTPPDSQGFA 300
    PHYDDIEAFV LQLEGRKLWR VYRPRDPSEE LALTSSPNFS QEDLGEPVLQ 350
    TVLEPGDLLY FPRGFIHQAE CQDGVHSLHL TLSTYQRNTW GDFLEAVLPL 400
    AVQAAIEENV EFRRGLPRDF MDYMGAQHSD SKDPRRTAFM EKVRVLVARL 450
    GHFAPVDAVA DQRAKDFIHD SLPPVLTDRE RALSVHGLPV RWEAGEPVNV 500
    GAQLTTETQV HMLQDGVARL VGEGGRLFLY HTVENSRVYH LEEPKCLEIH 550
    PQQADAMELL LRSYPEFVRV GDLPCDSVED QLSLATMLYD KGLLLTKTPL 600
    VPS 603
    Length:603
    Mass (Da):67,557
    Last modified:January 19, 2010 - v2
    Checksum:iDAB901939874D538
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti410 – 4101V → E in BAA95038. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB041553 mRNA. Translation: BAA95038.1.
    CH466590 Genomic DNA. Translation: EDL02754.1.
    BC138094 mRNA. Translation: AAI38095.1.
    CCDSiCCDS26033.1.
    RefSeqiNP_076122.2. NM_023633.3.
    UniGeneiMm.251483.

    Genome annotation databases

    EnsembliENSMUST00000053744; ENSMUSP00000057984; ENSMUSG00000046791.
    GeneIDi71952.
    KEGGimmu:71952.
    UCSCiuc007odz.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB041553 mRNA. Translation: BAA95038.1 .
    CH466590 Genomic DNA. Translation: EDL02754.1 .
    BC138094 mRNA. Translation: AAI38095.1 .
    CCDSi CCDS26033.1.
    RefSeqi NP_076122.2. NM_023633.3.
    UniGenei Mm.251483.

    3D structure databases

    ProteinModelPortali Q9JJF3.
    SMRi Q9JJF3. Positions 144-600.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 215052. 1 interaction.
    IntActi Q9JJF3. 3 interactions.
    MINTi MINT-4130008.
    STRINGi 10090.ENSMUSP00000057984.

    PTM databases

    PhosphoSitei Q9JJF3.

    Proteomic databases

    PaxDbi Q9JJF3.
    PRIDEi Q9JJF3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000053744 ; ENSMUSP00000057984 ; ENSMUSG00000046791 .
    GeneIDi 71952.
    KEGGi mmu:71952.
    UCSCi uc007odz.2. mouse.

    Organism-specific databases

    MGIi MGI:1919202. 2410016O06Rik.

    Phylogenomic databases

    eggNOGi NOG83808.
    GeneTreei ENSGT00390000000083.
    HOGENOMi HOG000030688.
    HOVERGENi HBG060021.
    InParanoidi B2RQV2.
    KOi K16914.
    OMAi TVENSRV.
    OrthoDBi EOG74FF0N.
    PhylomeDBi Q9JJF3.
    TreeFami TF318659.

    Miscellaneous databases

    NextBioi 335036.
    PROi Q9JJF3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9JJF3.
    CleanExi MM_2410016O06RIK.
    Genevestigatori Q9JJF3.

    Family and domain databases

    InterProi IPR003347. JmjC_dom.
    [Graphical view ]
    Pfami PF08007. Cupin_4. 1 hit.
    [Graphical view ]
    SMARTi SM00558. JmjC. 1 hit.
    [Graphical view ]
    PROSITEi PS51184. JMJC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
      Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Brain.
    4. "NO66, a highly conserved dual location protein in the nucleolus and in a special type of synchronously replicating chromatin."
      Eilbracht J., Reichenzeller M., Hergt M., Schnoelzer M., Heid H., Stoehr M., Franke W.W., Schmidt-Zachmann M.S.
      Mol. Biol. Cell 15:1816-1832(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    5. "Regulation of the osteoblast-specific transcription factor Osterix by NO66, a Jumonji family histone demethylase."
      Sinha K.M., Yasuda H., Coombes M.M., Dent S.Y., de Crombrugghe B.
      EMBO J. 29:68-79(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, INTERACTION WITH SP7, MUTAGENESIS OF HIS-302 AND HIS-367.

    Entry informationi

    Entry nameiNO66_MOUSE
    AccessioniPrimary (citable) accession number: Q9JJF3
    Secondary accession number(s): B2RQV2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: January 19, 2010
    Last modified: October 1, 2014
    This is version 92 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3