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Q9H6W3

- NO66_HUMAN

UniProt

Q9H6W3 - NO66_HUMAN

Protein

Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66

Gene

NO66

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (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. 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). 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 By similarity. 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 similarity3 Publications

    Catalytic activityi

    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
    L-histidine-[60S ribosomal protein L8] + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-histidine-[60S ribosomal protein L8] + succinate + CO2.1 Publication

    Cofactori

    Binds 1 Fe2+ ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi340 – 3401Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi342 – 3421Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi405 – 4051Iron; catalyticPROSITE-ProRule annotation

    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. histone H3-K36 demethylation Source: UniProtKB
    2. histone H3-K4 demethylation Source: UniProtKB
    3. negative regulation of osteoblast differentiation Source: UniProtKB
    4. negative regulation of transcription, DNA-templated Source: UniProtKB
    5. 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):
    60S ribosomal protein L8 histidine hydroxylase
    Histone lysine demethylase NO66
    Myc-associated protein with JmjC domain
    Nucleolar protein 66
    Short name:
    hsNO66
    Ribosomal oxygenase NO66
    Short name:
    ROX
    Gene namesi
    Name:NO66
    Synonyms:C14orf169, MAPJD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:20968. C14orf169.

    Subcellular locationi

    Nucleusnucleolus. Nucleusnucleoplasm
    Note: Granular part of nucleoli. Nucleoplasm, nucleoplasmic foci, some of them associated with nucleoli.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134919088.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 641641Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66PRO_0000264613Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei109 – 1091Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H6W3.
    PeptideAtlasiQ9H6W3.
    PRIDEiQ9H6W3.

    PTM databases

    PhosphoSiteiQ9H6W3.

    Expressioni

    Tissue specificityi

    Widely expressed. Overexpressed in lung carcinomas.2 Publications

    Gene expression databases

    CleanExiHS_C14orf169.
    GenevestigatoriQ9H6W3.

    Interactioni

    Subunit structurei

    Interacts with SP7/OSX; the interaction is direct By similarity. Interacts with MYC. Interacts with PHF19; leading to its recruitment to H3K36me3 sites.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Sp7Q8VI676EBI-2513645,EBI-7608836From a different organism.

    Protein-protein interaction databases

    BioGridi122818. 4 interactions.
    DIPiDIP-53768N.
    IntActiQ9H6W3. 3 interactions.
    MINTiMINT-5009834.

    Structurei

    Secondary structure

    1
    641
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi184 – 19310
    Helixi198 – 21013
    Helixi215 – 2217
    Turni222 – 2254
    Beta strandi228 – 2303
    Turni235 – 2406
    Helixi244 – 25310
    Turni259 – 2613
    Beta strandi262 – 2687
    Beta strandi271 – 2744
    Beta strandi278 – 2803
    Helixi283 – 2919
    Beta strandi295 – 2995
    Helixi301 – 3033
    Helixi306 – 31914
    Beta strandi324 – 3307
    Beta strandi332 – 3343
    Beta strandi343 – 35311
    Beta strandi355 – 3595
    Helixi365 – 3673
    Turni379 – 3813
    Beta strandi386 – 3916
    Beta strandi396 – 3994
    Beta strandi405 – 4084
    Beta strandi415 – 4228
    Helixi428 – 44619
    Helixi448 – 4514
    Helixi458 – 4603
    Helixi464 – 4663
    Helixi472 – 48716
    Helixi488 – 4914
    Helixi494 – 50815
    Helixi516 – 5205
    Helixi523 – 5253
    Beta strandi529 – 5313
    Beta strandi535 – 5373
    Beta strandi547 – 56115
    Beta strandi564 – 5707
    Beta strandi583 – 5875
    Helixi589 – 5913
    Helixi592 – 6009
    Turni601 – 6033
    Helixi608 – 6103
    Beta strandi612 – 6154
    Helixi616 – 62813
    Beta strandi632 – 6365

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4CCJX-ray2.15A/B/C/D183-641[»]
    4CCKX-ray2.15A/B/C/D183-641[»]
    4CCMX-ray2.51A/B183-641[»]
    4CCNX-ray2.23A/B183-641[»]
    4CCOX-ray2.30A/B183-641[»]
    4DIQX-ray2.40A/B167-641[»]
    4E4HX-ray2.28A/B/C/D183-641[»]
    ProteinModelPortaliQ9H6W3.
    SMRiQ9H6W3. Positions 183-638.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini294 – 439146JmjCPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    HOVERGENiHBG060021.
    KOiK16914.
    PhylomeDBiQ9H6W3.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H6W3-1) [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

    MDGLQASAGP LRRGRPKRRR KPQPHSGSVL ALPLRSRKIR KQLRSVVSRM    50
    AALRTQTLPS ENSEESRVES TADDLGDALP GGAAVAAVPD AARREPYGHL 100
    GPAELLEASP AARSLQTPSA RLVPASAPPA RLVEVPAAPV RVVETSALLC 150
    TAQHLAAVQS SGAPATASGP QVDNTGGEPA WDSPLRRVLA ELNRIPSSRR 200
    RAARLFEWLI APMPPDHFYR RLWEREAVLV RRQDHTYYQG LFSTADLDSM 250
    LRNEEVQFGQ HLDAARYING RRETLNPPGR ALPAAAWSLY QAGCSLRLLC 300
    PQAFSTTVWQ FLAVLQEQFG SMAGSNVYLT PPNSQGFAPH YDDIEAFVLQ 350
    LEGRKLWRVY RPRVPTEELA LTSSPNFSQD DLGEPVLQTV LEPGDLLYFP 400
    RGFIHQAECQ DGVHSLHLTL STYQRNTWGD FLEAILPLAV QAAMEENVEF 450
    RRGLPRDFMD YMGAQHSDSK DPRRTAFMEK VRVLVARLGH FAPVDAVADQ 500
    RAKDFIHDSL PPVLTDRERA LSVYGLPIRW EAGEPVNVGA QLTTETEVHM 550
    LQDGIARLVG EGGHLFLYYT VENSRVYHLE EPKCLEIYPQ QADAMELLLG 600
    SYPEFVRVGD LPCDSVEDQL SLATTLYDKG LLLTKMPLAL N 641
    Length:641
    Mass (Da):71,086
    Last modified:January 19, 2010 - v2
    Checksum:iE66A4342B1D1BFF2
    GO
    Isoform 2 (identifier: Q9H6W3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-212: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:429
    Mass (Da):48,687
    Checksum:iF07631F3A3F8CDB7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti392 – 3921E → G in BAG61814. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171K → R.3 Publications
    Corresponds to variant rs10144469 [ dbSNP | Ensembl ].
    VAR_062422
    Natural varianti218 – 2181F → S.
    Corresponds to variant rs758109 [ dbSNP | Ensembl ].
    VAR_057819
    Natural varianti239 – 2391Q → H.
    Corresponds to variant rs34970526 [ dbSNP | Ensembl ].
    VAR_060191
    Natural varianti364 – 3641V → A.3 Publications
    Corresponds to variant rs3813563 [ dbSNP | Ensembl ].
    VAR_062423

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 212212Missing in isoform 2. 1 PublicationVSP_038663Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY390535 mRNA. Translation: AAR27292.1.
    AK025455 mRNA. Translation: BAB15138.1.
    AK299994 mRNA. Translation: BAG61814.1.
    AC005280 Genomic DNA. No translation available.
    BC011350 mRNA. Translation: AAH11350.1.
    BC071954 mRNA. Translation: AAH71954.1.
    RefSeqiNP_078920.2. NM_024644.4. [Q9H6W3-1]
    UniGeneiHs.509916.

    Genome annotation databases

    GeneIDi79697.
    KEGGihsa:79697.
    UCSCiuc001xok.1. human. [Q9H6W3-1]

    Polymorphism databases

    DMDMi284018103.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY390535 mRNA. Translation: AAR27292.1 .
    AK025455 mRNA. Translation: BAB15138.1 .
    AK299994 mRNA. Translation: BAG61814.1 .
    AC005280 Genomic DNA. No translation available.
    BC011350 mRNA. Translation: AAH11350.1 .
    BC071954 mRNA. Translation: AAH71954.1 .
    RefSeqi NP_078920.2. NM_024644.4. [Q9H6W3-1 ]
    UniGenei Hs.509916.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4CCJ X-ray 2.15 A/B/C/D 183-641 [» ]
    4CCK X-ray 2.15 A/B/C/D 183-641 [» ]
    4CCM X-ray 2.51 A/B 183-641 [» ]
    4CCN X-ray 2.23 A/B 183-641 [» ]
    4CCO X-ray 2.30 A/B 183-641 [» ]
    4DIQ X-ray 2.40 A/B 167-641 [» ]
    4E4H X-ray 2.28 A/B/C/D 183-641 [» ]
    ProteinModelPortali Q9H6W3.
    SMRi Q9H6W3. Positions 183-638.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122818. 4 interactions.
    DIPi DIP-53768N.
    IntActi Q9H6W3. 3 interactions.
    MINTi MINT-5009834.

    PTM databases

    PhosphoSitei Q9H6W3.

    Polymorphism databases

    DMDMi 284018103.

    Proteomic databases

    MaxQBi Q9H6W3.
    PeptideAtlasi Q9H6W3.
    PRIDEi Q9H6W3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 79697.
    KEGGi hsa:79697.
    UCSCi uc001xok.1. human. [Q9H6W3-1 ]

    Organism-specific databases

    CTDi 79697.
    GeneCardsi GC14P073958.
    H-InvDB HIX0011794.
    HGNCi HGNC:20968. C14orf169.
    MIMi 611919. gene.
    neXtProti NX_Q9H6W3.
    PharmGKBi PA134919088.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG060021.
    KOi K16914.
    PhylomeDBi Q9H6W3.

    Miscellaneous databases

    GenomeRNAii 79697.
    NextBioi 68992.
    PROi Q9H6W3.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_C14orf169.
    Genevestigatori Q9H6W3.

    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. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS ARG-17 AND ALA-364.
    2. "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] (ISOFORMS 1 AND 2), VARIANTS ARG-17 AND ALA-364.
    3. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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), VARIANTS ARG-17 AND ALA-364.
      Tissue: Lymph and Mammary gland.
    5. "Identification of Myc-associated protein with JmjC domain as a novel therapeutic target oncogene for lung cancer."
      Suzuki C., Takahashi K., Hayama S., Ishikawa N., Kato T., Ito T., Tsuchiya E., Nakamura Y., Daigo Y.
      Mol. Cancer Ther. 6:542-551(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MYC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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 SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "Polycomb PHF19 binds H3K36me3 and recruits PRC2 and demethylase NO66 to embryonic stem cell genes during differentiation."
      Brien G.L., Gambero G., O'Connell D.J., Jerman E., Turner S.A., Egan C.M., Dunne E.J., Jurgens M.C., Wynne K., Piao L., Lohan A.J., Ferguson N., Shi X., Sinha K.M., Loftus B.J., Cagney G., Bracken A.P.
      Nat. Struct. Mol. Biol. 19:1273-1281(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHF19.
    9. Cited for: FUNCTION AS RPL8 HYDROXYLASE, CATALYTIC ACTIVITY.
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNO66_HUMAN
    AccessioniPrimary (citable) accession number: Q9H6W3
    Secondary accession number(s): B4DT02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: January 19, 2010
    Last modified: October 1, 2014
    This is version 101 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3