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Protein

Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66

Gene

No66

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

Fe2+1 PublicationNote: Binds 1 Fe2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi302Iron; catalyticCurated1
Metal bindingi304Iron; catalyticPROSITE-ProRule annotation1
Metal bindingi367Iron; catalyticCurated1

GO - Molecular functioni

  • histone demethylase activity (H3-K36 specific) Source: UniProtKB
  • histone demethylase activity (H3-K4 specific) Source: UniProtKB
  • iron ion binding 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 Source: UniProtKB

GO - Biological processi

  • chromatin remodeling Source: MGI
  • histone H3-K36 demethylation Source: UniProtKB
  • histone H3-K4 demethylation Source: UniProtKB
  • negative regulation of osteoblast differentiation Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • peptidyl-amino acid modification Source: GO_Central
  • post-translational protein modification Source: GO_Central
  • ribosome biogenesis Source: MGI
  • 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
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1919202. 2410016O06Rik.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: MGI
  • nucleoplasm Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi302H → A: Loss of demethylase activity. 1 Publication1
Mutagenesisi367H → A: Loss of demethylase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002646141 – 603Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66Add BLAST603

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei65PhosphoserineBy similarity1
Modified residuei68PhosphoserineBy similarity1
Modified residuei91PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9JJF3.
MaxQBiQ9JJF3.
PaxDbiQ9JJF3.
PeptideAtlasiQ9JJF3.
PRIDEiQ9JJF3.

PTM databases

iPTMnetiQ9JJF3.
PhosphoSitePlusiQ9JJF3.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000046791.
CleanExiMM_2410016O06RIK.
GenevisibleiQ9JJF3. MM.

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 interactor.
IntActiQ9JJF3. 3 interactors.
MINTiMINT-4130008.
STRINGi10090.ENSMUSP00000057984.

Structurei

3D structure databases

ProteinModelPortaliQ9JJF3.
SMRiQ9JJF3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini256 – 401JmjCPROSITE-ProRule annotationAdd BLAST146

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3706. Eukaryota.
ENOG410YNEJ. LUCA.
GeneTreeiENSGT00390000000083.
HOGENOMiHOG000030688.
HOVERGENiHBG060021.
InParanoidiQ9JJF3.
KOiK16914.
OMAiFEWLIAP.
OrthoDBiEOG091G04K2.
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

        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)DescriptionActionsGraphical viewLength
Sequence conflicti410V → E in BAA95038 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9JJF3.
SMRiQ9JJF3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215052. 1 interactor.
IntActiQ9JJF3. 3 interactors.
MINTiMINT-4130008.
STRINGi10090.ENSMUSP00000057984.

PTM databases

iPTMnetiQ9JJF3.
PhosphoSitePlusiQ9JJF3.

Proteomic databases

EPDiQ9JJF3.
MaxQBiQ9JJF3.
PaxDbiQ9JJF3.
PeptideAtlasiQ9JJF3.
PRIDEiQ9JJF3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

MGIiMGI:1919202. 2410016O06Rik.

Phylogenomic databases

eggNOGiKOG3706. Eukaryota.
ENOG410YNEJ. LUCA.
GeneTreeiENSGT00390000000083.
HOGENOMiHOG000030688.
HOVERGENiHBG060021.
InParanoidiQ9JJF3.
KOiK16914.
OMAiFEWLIAP.
OrthoDBiEOG091G04K2.
PhylomeDBiQ9JJF3.
TreeFamiTF318659.

Miscellaneous databases

PROiQ9JJF3.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000046791.
CleanExiMM_2410016O06RIK.
GenevisibleiQ9JJF3. MM.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 106 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.