Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66

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Q9JJF3 (NO66_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 79. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	No66
Synonyms:	Mapjd
ORF Names:	MNCb-7109

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	603 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleolus By similarity. Nucleus › nucleoplasm 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	Iron Metal-binding
Molecular function	Chromatin regulator Dioxygenase Oxidoreductase Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin remodeling Traceable author statement Ref.4. Source: MGI negative regulation of osteoblast differentiation Inferred from mutant phenotype Ref.5. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.5. Source: UniProtKB ribosome biogenesis Traceable author statement Ref.4. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleolus Inferred from direct assay Ref.4. Source: MGI nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	histone 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 single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 603

603

Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66

PRO_0000264614

Regions

Domain

256 – 401

146

JmjC

Sites

Metal binding

302

Iron; catalytic Probable

Metal binding

304

Iron; catalytic By similarity

Metal binding

367

Iron; catalytic Probable

Amino acid modifications

Modified residue

Phosphoserine By similarity

Experimental info

Mutagenesis

302

H → A: Loss of demethylase activity. Ref.5

Mutagenesis

367

H → A: Loss of demethylase activity. Ref.5

Sequence conflict

410

V → E in BAA95038. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9JJF3 [UniParc].

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

FASTA

603

67,557

        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' referencesShow '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.
IPI	IPI00121767.
RefSeq	NP_076122.2. NM_023633.3.
UniGene	Mm.251483.
3D structure databases
ProteinModelPortal	Q9JJF3.
SMR	Q9JJF3. Positions 145-600.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000057984.
PTM databases
PhosphoSite	Q9JJF3.
Proteomic databases
PaxDb	Q9JJF3.
PRIDE	Q9JJF3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000053744; ENSMUSP00000057984; ENSMUSG00000046791.
GeneID	71952.
KEGG	mmu:71952.
UCSC	uc007odz.2. mouse.
Organism-specific databases
MGI	MGI:1919202. 2410016O06Rik.
Phylogenomic databases
eggNOG	NOG83808.
GeneTree	ENSGT00390000000083.
HOGENOM	HOG000030688.
HOVERGEN	HBG060021.
InParanoid	B2RQV2.
OMA	TVENSRV.
OrthoDB	EOG4ZCT4H.
Gene expression databases
Bgee	Q9JJF3.
CleanEx	MM_2410016O06RIK.
Genevestigator	Q9JJF3.
GermOnline	ENSMUSG00000046791. Mus musculus.
Family and domain databases
InterPro	IPR003347. JmjC_dom. IPR013109. NO66/MINA. [Graphical view]
PANTHER	PTHR13096. PTHR13096. 1 hit.
Pfam	PF08007. Cupin_4. 1 hit. [Graphical view]
SMART	SM00558. JmjC. 1 hit. [Graphical view]
PROSITE	PS51184. JMJC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	335036.
SOURCE	Search...

Entry information

Entry name

NO66_MOUSE

Accession

Primary (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 3, 2013
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents