RIOX1_MOUSE
ID RIOX1_MOUSE Reviewed; 603 AA.
AC Q9JJF3; B2RQV2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Ribosomal oxygenase 1 {ECO:0000312|MGI:MGI:1919202};
DE AltName: Full=Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66;
DE EC=1.14.11.-;
DE EC=1.14.11.27 {ECO:0000269|PubMed:19927124};
DE AltName: Full=Histone lysine demethylase NO66;
GN Name=Riox1 {ECO:0000312|MGI:MGI:1919202}; Synonyms=Mapjd, No66;
GN ORFNames=MNCb-7109;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=14742713; DOI=10.1091/mbc.e03-08-0623;
RA Eilbracht J., Reichenzeller M., Hergt M., Schnoelzer M., Heid H.,
RA Stoehr M., Franke W.W., Schmidt-Zachmann M.S.;
RT "NO66, a highly conserved dual location protein in the nucleolus and in a
RT special type of synchronously replicating chromatin.";
RL Mol. Biol. Cell 15:1816-1832(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBCELLULAR LOCATION, INTERACTION WITH SP7, AND MUTAGENESIS OF
RP HIS-302 AND HIS-367.
RX PubMed=19927124; DOI=10.1038/emboj.2009.332;
RA Sinha K.M., Yasuda H., Coombes M.M., Dent S.Y., de Crombrugghe B.;
RT "Regulation of the osteoblast-specific transcription factor Osterix by
RT NO66, a Jumonji family histone demethylase.";
RL EMBO J. 29:68-79(2010).
CC -!- FUNCTION: Oxygenase that can act as both a histone lysine demethylase
CC and a ribosomal histidine hydroxylase. Also catalyzes the hydroxylation
CC of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of
CC osteoblast differentiation via its interaction with SP7/OSX by
CC demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated
CC promoter activation. May also play a role in ribosome biogenesis and in
CC the replication or remodeling of certain heterochromatic region.
CC Participates in MYC-induced transcriptional activation (By similarity).
CC Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of
CC histone H3, thereby playing a central role in histone code.
CC Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and
CC monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker
CC activity for dimethylated H3 'Lys-36' (H3K36me2). {ECO:0000250,
CC ECO:0000269|PubMed:19927124}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-histidyl-[protein] + O2 = (3S)-3-hydroxy-L-
CC histidyl-[protein] + CO2 + succinate; Xref=Rhea:RHEA:54256,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:13840, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:138021;
CC Evidence={ECO:0000269|PubMed:19927124};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.27;
CC Evidence={ECO:0000269|PubMed:19927124};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:19927124};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:19927124};
CC -!- SUBUNIT: Interacts with SP7/OSX; the interaction is direct. Interacts
CC with PHF19; leading to its recruitment to H3K36me3 sites. Interacts
CC with MYC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9JJF3; Q8VI67: Sp7; NbExp=3; IntAct=EBI-7608809, EBI-7608836;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:14742713, ECO:0000269|PubMed:19927124}.
CC -!- TISSUE SPECIFICITY: Present in developing bones (at protein level).
CC Widely but not ubiquitously expressed.
CC -!- SIMILARITY: Belongs to the ROX family. NO66 subfamily. {ECO:0000305}.
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DR EMBL; AB041553; BAA95038.1; -; mRNA.
DR EMBL; CH466590; EDL02754.1; -; Genomic_DNA.
DR EMBL; BC138094; AAI38095.1; -; mRNA.
DR CCDS; CCDS26033.1; -.
DR RefSeq; NP_076122.2; NM_023633.3.
DR AlphaFoldDB; Q9JJF3; -.
DR SMR; Q9JJF3; -.
DR BioGRID; 215052; 2.
DR IntAct; Q9JJF3; 2.
DR MINT; Q9JJF3; -.
DR STRING; 10090.ENSMUSP00000057984; -.
DR iPTMnet; Q9JJF3; -.
DR PhosphoSitePlus; Q9JJF3; -.
DR EPD; Q9JJF3; -.
DR jPOST; Q9JJF3; -.
DR MaxQB; Q9JJF3; -.
DR PaxDb; Q9JJF3; -.
DR PeptideAtlas; Q9JJF3; -.
DR PRIDE; Q9JJF3; -.
DR ProteomicsDB; 255152; -.
DR Antibodypedia; 73399; 100 antibodies from 25 providers.
DR DNASU; 71952; -.
DR Ensembl; ENSMUST00000053744; ENSMUSP00000057984; ENSMUSG00000046791.
DR GeneID; 71952; -.
DR KEGG; mmu:71952; -.
DR UCSC; uc007odz.2; mouse.
DR CTD; 79697; -.
DR MGI; MGI:1919202; Riox1.
DR VEuPathDB; HostDB:ENSMUSG00000046791; -.
DR eggNOG; KOG3706; Eukaryota.
DR GeneTree; ENSGT00390000000083; -.
DR HOGENOM; CLU_013645_4_1_1; -.
DR InParanoid; Q9JJF3; -.
DR OMA; EWGCMAG; -.
DR OrthoDB; 693909at2759; -.
DR PhylomeDB; Q9JJF3; -.
DR TreeFam; TF318659; -.
DR BioGRID-ORCS; 71952; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Riox1; mouse.
DR PRO; PR:Q9JJF3; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9JJF3; protein.
DR Bgee; ENSMUSG00000046791; Expressed in cleaving embryo and 227 other tissues.
DR Genevisible; Q9JJF3; MM.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IMP:UniProtKB.
DR GO; GO:0140680; F:histone H3-di/monomethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; IDA:UniProtKB.
DR GO; GO:0032453; F:histone H3-methyl-lysine-4 demethylase activity; IBA:GO_Central.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; TAS:MGI.
DR GO; GO:0070544; P:histone H3-K36 demethylation; IDA:UniProtKB.
DR GO; GO:0034720; P:histone H3-K4 demethylation; IDA:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; TAS:MGI.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR039994; JmjC_protein.
DR InterPro; IPR013109; NO66.
DR PANTHER; PTHR13096; PTHR13096; 1.
DR PANTHER; PTHR13096:SF4; PTHR13096:SF4; 1.
DR Pfam; PF08007; Cupin_4; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromatin regulator; Dioxygenase; Iron; Metal-binding;
KW Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..603
FT /note="Ribosomal oxygenase 1"
FT /id="PRO_0000264614"
FT DOMAIN 256..401
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 302
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 304
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 367
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6W3"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZU57"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZU57"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6W3"
FT MUTAGEN 302
FT /note="H->A: Loss of demethylase activity."
FT /evidence="ECO:0000269|PubMed:19927124"
FT MUTAGEN 367
FT /note="H->A: Loss of demethylase activity."
FT /evidence="ECO:0000269|PubMed:19927124"
FT CONFLICT 410
FT /note="V -> E (in Ref. 1; BAA95038)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 603 AA; 67557 MW; DAB901939874D538 CRC64;
MDELPNGNGA ALLKRGRGRR RRHPQSQPRG ASVLALPLRP RKIRRHRKSA AASRVAALRA
RALRSEDSDS KVAVASVRGK RKRPAELLEA SRSAEPRPVS ARPRSASATL PSRVEGWAAL
SRNLGTAAPP PPGSHADEPG RPRASPLQQV LTELNGIPSS RRRAARLFEW LLAPLPPDHF
YRRLWEREAV LVRRQDRSYY EGLFSTADLD SMLRYEDVQF GQHLDAARYV DGRRETLNPP
GRALPAAAWS LYRAGCSLRL LCPQAFSPTV WQFLAVLQEQ FGSMAGSNVY LTPPDSQGFA
PHYDDIEAFV LQLEGRKLWR VYRPRDPSEE LALTSSPNFS QEDLGEPVLQ TVLEPGDLLY
FPRGFIHQAE CQDGVHSLHL TLSTYQRNTW GDFLEAVLPL AVQAAIEENV EFRRGLPRDF
MDYMGAQHSD SKDPRRTAFM EKVRVLVARL GHFAPVDAVA DQRAKDFIHD SLPPVLTDRE
RALSVHGLPV RWEAGEPVNV GAQLTTETQV HMLQDGVARL VGEGGRLFLY HTVENSRVYH
LEEPKCLEIH PQQADAMELL LRSYPEFVRV GDLPCDSVED QLSLATMLYD KGLLLTKTPL
VPS
