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 27-MAR-2024, entry version 167. 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=1.14.11.79 {ECO:0000269|PubMed:23103944}; 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, MINA53 GN {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 Lung RC 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-[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; EC=1.14.11.79; CC Evidence={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="https://atlasgeneticsoncology.org/gene/44409/MINA"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 104. DR DIP; DIP-28141N; -. DR IntAct; Q8IUF8; 29. DR MINT; Q8IUF8; -. DR STRING; 9606.ENSP00000328251; -. DR BindingDB; Q8IUF8; -. DR GlyGen; Q8IUF8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8IUF8; -. DR PhosphoSitePlus; Q8IUF8; -. DR SwissPalm; Q8IUF8; -. DR BioMuta; RIOX2; -. DR DMDM; 74750624; -. DR EPD; Q8IUF8; -. DR jPOST; Q8IUF8; -. DR MassIVE; Q8IUF8; -. DR MaxQB; Q8IUF8; -. DR PaxDb; 9606-ENSP00000328251; -. DR PeptideAtlas; Q8IUF8; -. DR ProteomicsDB; 70558; -. [Q8IUF8-1] DR ProteomicsDB; 70559; -. [Q8IUF8-2] DR ProteomicsDB; 70560; -. [Q8IUF8-3] DR ProteomicsDB; 70561; -. [Q8IUF8-4] DR Pumba; Q8IUF8; -. DR TopDownProteomics; Q8IUF8-2; -. [Q8IUF8-2] DR Antibodypedia; 2005; 426 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 AGR; HGNC:19441; -. 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; IRREMVY; -. DR OrthoDB; 5491189at2759; -. DR PhylomeDB; Q8IUF8; -. DR TreeFam; TF318659; -. DR BioCyc; MetaCyc:ENSG00000170854-MONOMER; -. DR PathwayCommons; Q8IUF8; -. DR Reactome; R-HSA-3214842; HDMs demethylate histones. DR Reactome; R-HSA-9629569; Protein hydroxylation. DR SignaLink; Q8IUF8; -. DR BioGRID-ORCS; 84864; 12 hits in 1165 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 209 other cell types or tissues. DR ExpressionAtlas; Q8IUF8; baseline and differential. 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:0032452; F:histone demethylase activity; TAS:Reactome. DR GO; GO:0051864; F:histone H3K36 demethylase activity; IBA:GO_Central. DR GO; GO:0032453; F:histone H3K4 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:0036139; F:peptidyl-histidine dioxygenase activity; IDA:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW. DR Gene3D; 3.90.930.40; -; 1. DR Gene3D; 2.60.120.650; Cupin; 1. DR Gene3D; 1.10.10.1500; JmjC domain-containing ribosomal oxygenase (ROX), dimer domain; 1. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR039994; NO66-like. DR InterPro; IPR046799; ROXA-like_wH. DR PANTHER; PTHR13096; MINA53 MYC INDUCED NUCLEAR ANTIGEN; 1. DR PANTHER; PTHR13096:SF10; RIBOSOMAL OXYGENASE 1-RELATED; 1. DR Pfam; PF08007; JmjC_2; 1. DR Pfam; PF20514; ROXA-like_wH; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR PROSITE; PS51184; JMJC; 1. DR Genevisible; Q8IUF8; HS. 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 //