RIOX2_HUMAN
ID RIOX2_HUMAN Reviewed; 465 AA.
AC Q8IUF8; D3DN35; Q6AHW4; Q6SKS0; Q8IU69; Q8IUF6; Q8IUF7; Q96C17; Q96KB0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ribosomal oxygenase 2 {ECO:0000312|HGNC:HGNC:19441};
DE AltName: Full=60S ribosomal protein L27a histidine hydroxylase;
DE AltName: Full=Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA;
DE EC=1.14.11.-;
DE AltName: Full=Histone lysine demethylase MINA;
DE AltName: Full=MYC-induced nuclear antigen;
DE AltName: Full=Mineral dust-induced gene protein;
DE AltName: Full=Nucleolar protein 52;
DE AltName: Full=Ribosomal oxygenase MINA;
DE Short=ROX;
GN Name=RIOX2 {ECO:0000312|HGNC:HGNC:19441};
GN Synonyms=MDIG {ECO:0000312|EMBL:AAP59421.1}, MINA,
GN MINA53 {ECO:0000312|EMBL:BAC16537.1}, NO52 {ECO:0000312|EMBL:AAR27293.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC16537.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), FUNCTION, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RC TISSUE=Erythroleukemia {ECO:0000312|EMBL:BAC16537.1};
RX PubMed=12091391; DOI=10.1074/jbc.m204458200;
RA Tsuneoka M., Koda Y., Soejima M., Teye K., Kimura H.;
RT "A novel myc target gene, mina53, that is involved in cell proliferation.";
RL J. Biol. Chem. 277:35450-35459(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAR27293.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-386.
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAP59421.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Alveolar macrophage {ECO:0000312|EMBL:AAP59421.1}, and
RC Lung cancer {ECO:0000312|EMBL:AAR21572.1};
RX PubMed=15897898; DOI=10.1038/sj.onc.1208668;
RA Zhang Y., Lu Y., Yuan B.-Z., Castranova V., Shi X., Stauffer J.L.,
RA Demers L.M., Chen F.;
RT "The human mineral dust-induced gene, mdig, is a cell growth regulating
RT gene associated with lung cancer.";
RL Oncogene 24:4873-4882(2005).
RN [4] {ECO:0000305, ECO:0000312|EMBL:ABE28016.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung {ECO:0000312|EMBL:ABE28016.1};
RA Chang Q., Castranova V., Chen F.;
RT "MDIG gene, a potential biomarker for human lung cancer.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:BAB55024.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP THR-386.
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB55024.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7] {ECO:0000305, ECO:0000312|EMBL:ABE28016.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000305, ECO:0000312|EMBL:AAH14928.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-386.
RC TISSUE=Skin {ECO:0000312|EMBL:AAH14928.1};
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-465 (ISOFORM 1), AND VARIANT
RP THR-386.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14695334; DOI=10.1016/s0002-9440(10)63111-2;
RA Teye K., Tsuneoka M., Arima N., Koda Y., Nakamura Y., Ueta Y., Shirouzu K.,
RA Kimura H.;
RT "Increased expression of a Myc target gene Mina53 in human colon cancer.";
RL Am. J. Pathol. 164:205-216(2004).
RN [11] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15534111; DOI=10.1158/1078-0432.ccr-03-0543;
RA Tsuneoka M., Fujita H., Arima N., Teye K., Okamura T., Inutsuka H.,
RA Koda Y., Shirouzu K., Kimura H.;
RT "Mina53 as a potential prognostic factor for esophageal squamous cell
RT carcinoma.";
RL Clin. Cancer Res. 10:7347-7356(2004).
RN [12] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15819408; DOI=10.1016/j.ejcb.2004.12.022;
RA Eilbracht J., Kneissel S., Hofmann A., Schmidt-Zachmann M.S.;
RT "Protein NO52 -- a constitutive nucleolar component sharing high sequence
RT homologies to protein NO66.";
RL Eur. J. Cell Biol. 84:279-294(2005).
RN [13] {ECO:0000305}
RP FUNCTION.
RX PubMed=17317935; DOI=10.2739/kurumemedj.53.71;
RA Kuratomi K., Yano H., Tsuneoka M., Sakamoto K., Kusukawa J., Kojiro M.;
RT "Immunohistochemical expression of Mina53 and Ki67 proteins in human
RT primary gingival squamous cell carcinoma.";
RL Kurume Med. J. 53:71-78(2006).
RN [14]
RP FUNCTION AS HISTONE DEMETHYLASE, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP HIS-179.
RX PubMed=19502796; DOI=10.4161/cc.8.13.8927;
RA Lu Y., Chang Q., Zhang Y., Beezhold K., Rojanasakul Y., Zhao H.,
RA Castranova V., Shi X., Chen F.;
RT "Lung cancer-associated JmjC domain protein mdig suppresses formation of
RT tri-methyl lysine 9 of histone H3.";
RL Cell Cycle 8:2101-2109(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP FUNCTION AS RPL27A HYDROXYLASE, AND CATALYTIC ACTIVITY.
RX PubMed=23103944; DOI=10.1038/nchembio.1093;
RA Ge W., Wolf A., Feng T., Ho C.H., Sekirnik R., Zayer A., Granatino N.,
RA Cockman M.E., Loenarz C., Loik N.D., Hardy A.P., Claridge T.D., Hamed R.B.,
RA Chowdhury R., Gong L., Robinson C.V., Trudgian D.C., Jiang M.,
RA Mackeen M.M., McCullagh J.S., Gordiyenko Y., Thalhammer A., Yamamoto A.,
RA Yang M., Liu-Yi P., Zhang Z., Schmidt-Zachmann M., Kessler B.M.,
RA Ratcliffe P.J., Preston G.M., Coleman M.L., Schofield C.J.;
RT "Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and
RT humans.";
RL Nat. Chem. Biol. 8:960-962(2012).
CC -!- FUNCTION: Oxygenase that can act as both a histone lysine demethylase
CC and a ribosomal histidine hydroxylase. Is involved in the demethylation
CC of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an
CC increase in ribosomal RNA expression. Also catalyzes the hydroxylation
CC of 60S ribosomal protein L27a on 'His-39'. May play an important role
CC in cell growth and survival. May be involved in ribosome biogenesis,
CC most likely during the assembly process of pre-ribosomal particles.
CC {ECO:0000269|PubMed:12091391, ECO:0000269|PubMed:14695334,
CC ECO:0000269|PubMed:15534111, ECO:0000269|PubMed:15819408,
CC ECO:0000269|PubMed:15897898, ECO:0000269|PubMed:17317935,
CC ECO:0000269|PubMed:19502796, ECO:0000269|PubMed:23103944}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-histidyl-[ribosomal protein uL15] + O2 =
CC (3S)-3-hydroxy-L-histidyl-[ribosomal protein uL15] + CO2 + succinate;
CC Xref=Rhea:RHEA:54024, Rhea:RHEA-COMP:13760, Rhea:RHEA-COMP:13761,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:30031, ChEBI:CHEBI:138021;
CC Evidence={ECO:0000269|PubMed:23103944};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC Q8IUF8; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-751580, EBI-739832;
CC Q8IUF8; Q8IUF8: RIOX2; NbExp=5; IntAct=EBI-751580, EBI-751580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12091391,
CC ECO:0000269|PubMed:15819408}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:12091391, ECO:0000269|PubMed:15819408}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:12091391, ECO:0000269|PubMed:14702039,
CC ECO:0000269|PubMed:14742713, ECO:0000269|PubMed:15489334,
CC ECO:0000269|PubMed:15897898, ECO:0000269|Ref.4};
CC IsoId=Q8IUF8-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12091391};
CC IsoId=Q8IUF8-2; Sequence=VSP_052589, VSP_052590;
CC Name=3 {ECO:0000269|PubMed:15897898};
CC IsoId=Q8IUF8-3; Sequence=VSP_052587, VSP_052588;
CC Name=4;
CC IsoId=Q8IUF8-4; Sequence=VSP_038373;
CC -!- TISSUE SPECIFICITY: Expressed in liver, skeletal muscle, heart,
CC pancreas, and placenta. Not detected in brain, lung or kidney.
CC Expressed in several lung cancer tissues, but is barely detected in the
CC adjacent non-cancerous tissues. Also highly expressed in several
CC esophageal squamous cell carcinoma (ESCC), and colon cancer tissues,
CC and in various cancer cell lines. {ECO:0000269|PubMed:14695334,
CC ECO:0000269|PubMed:15534111, ECO:0000269|PubMed:15897898,
CC ECO:0000269|PubMed:19502796}.
CC -!- INDUCTION: Up-regulated in response to MYC, in alveolar macrophages
CC from coal miners and in silica particle-treated A549 lung cancer cells.
CC {ECO:0000269|PubMed:12091391, ECO:0000269|PubMed:15897898}.
CC -!- SIMILARITY: Belongs to the ROX family. MINA53 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH10679.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MINAID44409ch3q11.html";
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DR EMBL; AB083189; BAC16537.1; -; mRNA.
DR EMBL; AB083190; BAC16358.1; -; mRNA.
DR EMBL; AB083191; BAC16359.1; -; mRNA.
DR EMBL; AB083192; BAC16360.1; -; mRNA.
DR EMBL; AB083193; BAC16361.1; -; mRNA.
DR EMBL; AY390536; AAR27293.1; -; mRNA.
DR EMBL; AY302110; AAP59421.1; -; mRNA.
DR EMBL; AY456380; AAR21572.1; -; mRNA.
DR EMBL; DQ453796; ABE28016.1; -; mRNA.
DR EMBL; AK027299; BAB55024.1; -; mRNA.
DR EMBL; AC026100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79872.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79873.1; -; Genomic_DNA.
DR EMBL; BC014928; AAH14928.1; -; mRNA.
DR EMBL; CR627479; CAH10679.1; ALT_TERM; mRNA.
DR CCDS; CCDS2929.1; -. [Q8IUF8-4]
DR CCDS; CCDS43114.1; -. [Q8IUF8-1]
DR RefSeq; NP_001035998.1; NM_001042533.2. [Q8IUF8-1]
DR RefSeq; NP_001248758.1; NM_001261829.1. [Q8IUF8-4]
DR RefSeq; NP_116167.3; NM_032778.5. [Q8IUF8-4]
DR RefSeq; NP_694822.2; NM_153182.3. [Q8IUF8-1]
DR RefSeq; XP_005247895.1; XM_005247838.4. [Q8IUF8-1]
DR PDB; 2XDV; X-ray; 2.57 A; A=26-465.
DR PDB; 4BU2; X-ray; 2.78 A; A=26-465.
DR PDB; 4BXF; X-ray; 2.05 A; A/B=26-465.
DR PDBsum; 2XDV; -.
DR PDBsum; 4BU2; -.
DR PDBsum; 4BXF; -.
DR AlphaFoldDB; Q8IUF8; -.
DR SMR; Q8IUF8; -.
DR BioGRID; 124309; 91.
DR DIP; DIP-28141N; -.
DR IntAct; Q8IUF8; 29.
DR MINT; Q8IUF8; -.
DR STRING; 9606.ENSP00000328251; -.
DR BindingDB; Q8IUF8; -.
DR iPTMnet; Q8IUF8; -.
DR PhosphoSitePlus; Q8IUF8; -.
DR BioMuta; RIOX2; -.
DR DMDM; 74750624; -.
DR EPD; Q8IUF8; -.
DR jPOST; Q8IUF8; -.
DR MassIVE; Q8IUF8; -.
DR MaxQB; Q8IUF8; -.
DR PaxDb; Q8IUF8; -.
DR PeptideAtlas; Q8IUF8; -.
DR PRIDE; Q8IUF8; -.
DR ProteomicsDB; 70558; -. [Q8IUF8-1]
DR ProteomicsDB; 70559; -. [Q8IUF8-2]
DR ProteomicsDB; 70560; -. [Q8IUF8-3]
DR ProteomicsDB; 70561; -. [Q8IUF8-4]
DR TopDownProteomics; Q8IUF8-2; -. [Q8IUF8-2]
DR Antibodypedia; 2005; 390 antibodies from 37 providers.
DR DNASU; 84864; -.
DR Ensembl; ENST00000333396.11; ENSP00000328251.6; ENSG00000170854.18. [Q8IUF8-1]
DR Ensembl; ENST00000360258.8; ENSP00000353395.4; ENSG00000170854.18. [Q8IUF8-4]
DR Ensembl; ENST00000394198.7; ENSP00000377748.2; ENSG00000170854.18. [Q8IUF8-1]
DR Ensembl; ENST00000514314.5; ENSP00000424955.1; ENSG00000170854.18. [Q8IUF8-2]
DR GeneID; 84864; -.
DR KEGG; hsa:84864; -.
DR MANE-Select; ENST00000394198.7; ENSP00000377748.2; NM_153182.4; NP_694822.2.
DR UCSC; uc003drz.3; human. [Q8IUF8-1]
DR CTD; 84864; -.
DR DisGeNET; 84864; -.
DR GeneCards; RIOX2; -.
DR HGNC; HGNC:19441; RIOX2.
DR HPA; ENSG00000170854; Low tissue specificity.
DR MIM; 612049; gene.
DR neXtProt; NX_Q8IUF8; -.
DR OpenTargets; ENSG00000170854; -.
DR PharmGKB; PA134991047; -.
DR VEuPathDB; HostDB:ENSG00000170854; -.
DR eggNOG; KOG3706; Eukaryota.
DR GeneTree; ENSGT00390000000083; -.
DR HOGENOM; CLU_013645_0_1_1; -.
DR InParanoid; Q8IUF8; -.
DR OMA; GSPTHEF; -.
DR OrthoDB; 693909at2759; -.
DR PhylomeDB; Q8IUF8; -.
DR TreeFam; TF318659; -.
DR BioCyc; MetaCyc:ENSG00000170854-MON; -.
DR PathwayCommons; Q8IUF8; -.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR SignaLink; Q8IUF8; -.
DR BioGRID-ORCS; 84864; 12 hits in 1086 CRISPR screens.
DR ChiTaRS; MINA; human.
DR EvolutionaryTrace; Q8IUF8; -.
DR GeneWiki; MINA; -.
DR GeneWiki; MYC-induced_nuclear_antigen; -.
DR GenomeRNAi; 84864; -.
DR Pharos; Q8IUF8; Tbio.
DR PRO; PR:Q8IUF8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8IUF8; protein.
DR Bgee; ENSG00000170854; Expressed in secondary oocyte and 207 other tissues.
DR ExpressionAtlas; Q8IUF8; baseline and differential.
DR Genevisible; Q8IUF8; HS.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR GO; GO:0032452; F:histone demethylase activity; TAS:Reactome.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; IBA:GO_Central.
DR GO; GO:0032453; F:histone H3-methyl-lysine-4 demethylase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0070544; P:histone H3-K36 demethylation; IBA:GO_Central.
DR GO; GO:0034720; P:histone H3-K4 demethylation; IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR039994; JmjC_protein.
DR PANTHER; PTHR13096; PTHR13096; 1.
DR Pfam; PF08007; Cupin_4; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Dioxygenase; Iron; Metal-binding;
KW Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; Transcription; Transcription regulation.
FT CHAIN 1..465
FT /note="Ribosomal oxygenase 2"
FT /id="PRO_0000308377"
FT DOMAIN 139..271
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 179
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 240
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..254
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15897898"
FT /id="VSP_052587"
FT VAR_SEQ 255..261
FT /note="TISTYQN -> MLLQVPC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15897898"
FT /id="VSP_052588"
FT VAR_SEQ 263..280
FT /note="SWGDFLLDTISGLVFDTA -> DAGARMRRCDLRAIAPQK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12091391"
FT /id="VSP_052589"
FT VAR_SEQ 281..465
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12091391"
FT /id="VSP_052590"
FT VAR_SEQ 297
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12091391,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_038373"
FT VARIANT 17
FT /note="A -> P (in dbSNP:rs35391656)"
FT /id="VAR_054079"
FT VARIANT 201
FT /note="P -> L (in dbSNP:rs56183666)"
FT /id="VAR_062241"
FT VARIANT 386
FT /note="A -> T (in dbSNP:rs2172257)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:14742713, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_036811"
FT MUTAGEN 179
FT /note="H->Y: Abolishes demethylase activity."
FT /evidence="ECO:0000269|PubMed:19502796"
FT CONFLICT 87
FT /note="K -> E (in Ref. 1; BAC16359)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="N -> S (in Ref. 1; BAC16359)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="G -> S (in Ref. 5; BAB55024)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="V -> A (in Ref. 1; BAC16359)"
FT /evidence="ECO:0000305"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:4BXF"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:4BXF"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:4BXF"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 182..192
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 302..321
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:4BXF"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 390..395
FT /evidence="ECO:0007829|PDB:4BXF"
FT TURN 402..405
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 424..431
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:4BXF"
FT HELIX 446..458
FT /evidence="ECO:0007829|PDB:4BXF"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:4BXF"
SQ SEQUENCE 465 AA; 52800 MW; B59F8AE9C802FEB0 CRC64;
MPKKAKPTGS GKEEGPAPCK QMKLEAAGGP SALNFDSPSS LFESLISPIK TETFFKEFWE
QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV NVCRCVNGKK KVLNKDGKAH
FLQLRKDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGSQGLPPHY
DDVEVFILQL EGEKHWRLYH PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH
QADTPAGLAH STHVTISTYQ NNSWGDFLLD TISGLVFDTA KEDVELRTGI PRQLLLQVES
TTVATRRLSG FLRTLADRLE GTKELLSSDM KKDFIMHRLP PYSAGDGAEL STPGGKLPRL
DSVVRLQFKD HIVLTVLPDQ DQSDEAQEKM VYIYHSLKNS RETHMMGNEE ETEFHGLRFP
LSHLDALKQI WNSPAISVKD LKLTTDEEKE SLVLSLWTEC LIQVV
