Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9JJF3 (NO66_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:No66
Synonyms:Mapjd
ORF Names:MNCb-7109
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.5

Catalytic activity

L-histidine-[60S ribosomal protein L8] + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-histidine-[60S ribosomal protein L8] + succinate + CO2. Ref.5

Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2. Ref.5

Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2. Ref.5

Cofactor

Binds 1 Fe2+ ion per subunit. Ref.5

Subunit structure

Interacts with SP7/OSX; the interaction is direct. Interacts with PHF19; leading to its recruitment to H3K36me3 sites. Interacts with MYC By similarity. Ref.5

Subcellular location

Nucleusnucleolus By similarity. Nucleusnucleoplasm Ref.4 Ref.5.

Tissue specificity

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

Sequence similarities

Belongs to the MINA53/NO66 family. NO66 subfamily.

Contains 1 JmjC domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   LigandIron
Metal-binding
   Molecular functionChromatin regulator
Dioxygenase
Oxidoreductase
Repressor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin remodeling

Traceable author statement Ref.4. Source: MGI

histone H3-K36 demethylation

Inferred from direct assay Ref.5. Source: UniProtKB

histone H3-K4 demethylation

Inferred from direct assay Ref.5. Source: UniProtKB

negative regulation of osteoblast differentiation

Inferred from mutant phenotype Ref.5. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.5. Source: UniProtKB

ribosome biogenesis

Traceable author statement Ref.4. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleolus

Inferred from direct assay Ref.4. Source: MGI

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.5. Source: UniProtKB

   Molecular_functionhistone demethylase activity (H3-K36 specific)

Inferred from direct assay Ref.5. Source: UniProtKB

histone demethylase activity (H3-K4 specific)

Inferred from direct assay Ref.5. Source: UniProtKB

iron ion binding

Inferred from mutant phenotype Ref.5. Source: UniProtKB

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

Inferred from mutant phenotype Ref.5. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sp7Q8VI673EBI-7608809,EBI-7608836

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 603603Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66
PRO_0000264614

Regions

Domain256 – 401146JmjC

Sites

Metal binding3021Iron; catalytic Probable
Metal binding3041Iron; catalytic By similarity
Metal binding3671Iron; catalytic Probable

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue911Phosphoserine By similarity

Experimental info

Mutagenesis3021H → A: Loss of demethylase activity. Ref.5
Mutagenesis3671H → A: Loss of demethylase activity. Ref.5
Sequence conflict4101V → E in BAA95038. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9JJF3 [UniParc].

Last modified January 19, 2010. Version 2.
Checksum: DAB901939874D538

FASTA60367,557
        10         20         30         40         50         60 
MDELPNGNGA ALLKRGRGRR RRHPQSQPRG ASVLALPLRP RKIRRHRKSA AASRVAALRA 

        70         80         90        100        110        120 
RALRSEDSDS KVAVASVRGK RKRPAELLEA SRSAEPRPVS ARPRSASATL PSRVEGWAAL 

       130        140        150        160        170        180 
SRNLGTAAPP PPGSHADEPG RPRASPLQQV LTELNGIPSS RRRAARLFEW LLAPLPPDHF 

       190        200        210        220        230        240 
YRRLWEREAV LVRRQDRSYY EGLFSTADLD SMLRYEDVQF GQHLDAARYV DGRRETLNPP 

       250        260        270        280        290        300 
GRALPAAAWS LYRAGCSLRL LCPQAFSPTV WQFLAVLQEQ FGSMAGSNVY LTPPDSQGFA 

       310        320        330        340        350        360 
PHYDDIEAFV LQLEGRKLWR VYRPRDPSEE LALTSSPNFS QEDLGEPVLQ TVLEPGDLLY 

       370        380        390        400        410        420 
FPRGFIHQAE CQDGVHSLHL TLSTYQRNTW GDFLEAVLPL AVQAAIEENV EFRRGLPRDF 

       430        440        450        460        470        480 
MDYMGAQHSD SKDPRRTAFM EKVRVLVARL GHFAPVDAVA DQRAKDFIHD SLPPVLTDRE 

       490        500        510        520        530        540 
RALSVHGLPV RWEAGEPVNV GAQLTTETQV HMLQDGVARL VGEGGRLFLY HTVENSRVYH 

       550        560        570        580        590        600 
LEEPKCLEIH PQQADAMELL LRSYPEFVRV GDLPCDSVED QLSLATMLYD KGLLLTKTPL 


VPS 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB041553 mRNA. Translation: BAA95038.1.
CH466590 Genomic DNA. Translation: EDL02754.1.
BC138094 mRNA. Translation: AAI38095.1.
RefSeqNP_076122.2. NM_023633.3.
UniGeneMm.251483.

3D structure databases

ProteinModelPortalQ9JJF3.
SMRQ9JJF3. Positions 144-600.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9JJF3. 3 interactions.
MINTMINT-4130008.
STRING10090.ENSMUSP00000057984.

PTM databases

PhosphoSiteQ9JJF3.

Proteomic databases

PaxDbQ9JJF3.
PRIDEQ9JJF3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000053744; ENSMUSP00000057984; ENSMUSG00000046791.
GeneID71952.
KEGGmmu:71952.
UCSCuc007odz.2. mouse.

Organism-specific databases

MGIMGI:1919202. 2410016O06Rik.

Phylogenomic databases

eggNOGNOG83808.
GeneTreeENSGT00390000000083.
HOGENOMHOG000030688.
HOVERGENHBG060021.
InParanoidB2RQV2.
KOK16914.
OMATVENSRV.
OrthoDBEOG74FF0N.
PhylomeDBQ9JJF3.
TreeFamTF318659.

Gene expression databases

BgeeQ9JJF3.
CleanExMM_2410016O06RIK.
GenevestigatorQ9JJF3.

Family and domain databases

InterProIPR003347. JmjC_dom.
IPR013109. NO66/MINA.
[Graphical view]
PANTHERPTHR13096:SF0. PTHR13096:SF0. 1 hit.
PfamPF08007. Cupin_4. 1 hit.
[Graphical view]
SMARTSM00558. JmjC. 1 hit.
[Graphical view]
PROSITEPS51184. JMJC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio335036.
PROQ9JJF3.
SOURCESearch...

Entry information

Entry nameNO66_MOUSE
AccessionPrimary (citable) accession number: Q9JJF3
Secondary accession number(s): B2RQV2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 19, 2010
Last modified: April 16, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot