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Q9JJF3

- NO66_MOUSE

UniProt

Q9JJF3 - NO66_MOUSE

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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

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

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
Complete GO annotation...

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. nucleus Source: UniProtKB
Complete GO annotation...

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

MaxQBiQ9JJF3.
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 145-600.
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.
InParanoidiQ9JJF3.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDELPNGNGA ALLKRGRGRR RRHPQSQPRG ASVLALPLRP RKIRRHRKSA
60 70 80 90 100
AASRVAALRA RALRSEDSDS KVAVASVRGK RKRPAELLEA SRSAEPRPVS
110 120 130 140 150
ARPRSASATL PSRVEGWAAL SRNLGTAAPP PPGSHADEPG RPRASPLQQV
160 170 180 190 200
LTELNGIPSS RRRAARLFEW LLAPLPPDHF YRRLWEREAV LVRRQDRSYY
210 220 230 240 250
EGLFSTADLD SMLRYEDVQF GQHLDAARYV DGRRETLNPP GRALPAAAWS
260 270 280 290 300
LYRAGCSLRL LCPQAFSPTV WQFLAVLQEQ FGSMAGSNVY LTPPDSQGFA
310 320 330 340 350
PHYDDIEAFV LQLEGRKLWR VYRPRDPSEE LALTSSPNFS QEDLGEPVLQ
360 370 380 390 400
TVLEPGDLLY FPRGFIHQAE CQDGVHSLHL TLSTYQRNTW GDFLEAVLPL
410 420 430 440 450
AVQAAIEENV EFRRGLPRDF MDYMGAQHSD SKDPRRTAFM EKVRVLVARL
460 470 480 490 500
GHFAPVDAVA DQRAKDFIHD SLPPVLTDRE RALSVHGLPV RWEAGEPVNV
510 520 530 540 550
GAQLTTETQV HMLQDGVARL VGEGGRLFLY HTVENSRVYH LEEPKCLEIH
560 570 580 590 600
PQQADAMELL LRSYPEFVRV GDLPCDSVED QLSLATMLYD KGLLLTKTPL

VPS
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 145-600.
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

MaxQBi Q9JJF3.
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 Q9JJF3.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 93 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