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Ribosomal oxygenase 2 (60S ribosomal protein L27a histidine hydroxylase) (Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA) (EC 1.14.11.-) (Histone lysine demethylase MINA) (MYC-induced nuclear antigen) (Mineral dust-induced gene protein) (Nucleolar protein 52) (Ribosomal oxygenase MINA) (ROX)

 RIOX2_HUMAN             Reviewed;         465 AA.
Q8IUF8; D3DN35; Q6AHW4; Q6SKS0; Q8IU69; Q8IUF6; Q8IUF7; Q96C17;
Q96KB0;
23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
13-NOV-2019, entry version 144.
RecName: Full=Ribosomal oxygenase 2 {ECO:0000312|HGNC:HGNC:19441};
AltName: Full=60S ribosomal protein L27a histidine hydroxylase;
AltName: Full=Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA;
EC=1.14.11.-;
AltName: Full=Histone lysine demethylase MINA;
AltName: Full=MYC-induced nuclear antigen;
AltName: Full=Mineral dust-induced gene protein;
AltName: Full=Nucleolar protein 52;
AltName: Full=Ribosomal oxygenase MINA;
Short=ROX;
Name=RIOX2 {ECO:0000312|HGNC:HGNC:19441};
Synonyms=MDIG {ECO:0000312|EMBL:AAP59421.1}, MINA,
MINA53 {ECO:0000312|EMBL:BAC16537.1},
NO52 {ECO:0000312|EMBL:AAR27293.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:BAC16537.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), FUNCTION,
SUBCELLULAR LOCATION, AND INDUCTION.
TISSUE=Erythroleukemia {ECO:0000312|EMBL:BAC16537.1};
PubMed=12091391; DOI=10.1074/jbc.m204458200;
Tsuneoka M., Koda Y., Soejima M., Teye K., Kimura H.;
"A novel myc target gene, mina53, that is involved in cell
proliferation.";
J. Biol. Chem. 277:35450-35459(2002).
[2] {ECO:0000305, ECO:0000312|EMBL:AAR27293.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-386.
PubMed=14742713; DOI=10.1091/mbc.e03-08-0623;
Eilbracht J., Reichenzeller M., Hergt M., Schnoelzer M., Heid H.,
Stoehr M., Franke W.W., Schmidt-Zachmann M.S.;
"NO66, a highly conserved dual location protein in the nucleolus and
in a special type of synchronously replicating chromatin.";
Mol. Biol. Cell 15:1816-1832(2004).
[3] {ECO:0000305, ECO:0000312|EMBL:AAP59421.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, TISSUE
SPECIFICITY, AND INDUCTION.
TISSUE=Alveolar macrophage {ECO:0000312|EMBL:AAP59421.1}, and
Lung cancer {ECO:0000312|EMBL:AAR21572.1};
PubMed=15897898; DOI=10.1038/sj.onc.1208668;
Zhang Y., Lu Y., Yuan B.-Z., Castranova V., Shi X., Stauffer J.L.,
Demers L.M., Chen F.;
"The human mineral dust-induced gene, mdig, is a cell growth
regulating gene associated with lung cancer.";
Oncogene 24:4873-4882(2005).
[4] {ECO:0000305, ECO:0000312|EMBL:ABE28016.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lung {ECO:0000312|EMBL:ABE28016.1};
Chang Q., Castranova V., Chen F.;
"MDIG gene, a potential biomarker for human lung cancer.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000305, ECO:0000312|EMBL:BAB55024.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
THR-386.
TISSUE=Embryo {ECO:0000312|EMBL:BAB55024.1};
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[7] {ECO:0000305, ECO:0000312|EMBL:ABE28016.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000305, ECO:0000312|EMBL:AAH14928.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
THR-386.
TISSUE=Skin {ECO:0000312|EMBL:AAH14928.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-465 (ISOFORM 1), AND
VARIANT THR-386.
TISSUE=Melanoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[10] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14695334; DOI=10.1016/s0002-9440(10)63111-2;
Teye K., Tsuneoka M., Arima N., Koda Y., Nakamura Y., Ueta Y.,
Shirouzu K., Kimura H.;
"Increased expression of a Myc target gene Mina53 in human colon
cancer.";
Am. J. Pathol. 164:205-216(2004).
[11] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15534111; DOI=10.1158/1078-0432.ccr-03-0543;
Tsuneoka M., Fujita H., Arima N., Teye K., Okamura T., Inutsuka H.,
Koda Y., Shirouzu K., Kimura H.;
"Mina53 as a potential prognostic factor for esophageal squamous cell
carcinoma.";
Clin. Cancer Res. 10:7347-7356(2004).
[12] {ECO:0000305}
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15819408; DOI=10.1016/j.ejcb.2004.12.022;
Eilbracht J., Kneissel S., Hofmann A., Schmidt-Zachmann M.S.;
"Protein NO52 -- a constitutive nucleolar component sharing high
sequence homologies to protein NO66.";
Eur. J. Cell Biol. 84:279-294(2005).
[13] {ECO:0000305}
FUNCTION.
PubMed=17317935; DOI=10.2739/kurumemedj.53.71;
Kuratomi K., Yano H., Tsuneoka M., Sakamoto K., Kusukawa J.,
Kojiro M.;
"Immunohistochemical expression of Mina53 and Ki67 proteins in human
primary gingival squamous cell carcinoma.";
Kurume Med. J. 53:71-78(2006).
[14]
FUNCTION AS HISTONE DEMETHYLASE, TISSUE SPECIFICITY, AND MUTAGENESIS
OF HIS-179.
PubMed=19502796; DOI=10.4161/cc.8.13.8927;
Lu Y., Chang Q., Zhang Y., Beezhold K., Rojanasakul Y., Zhao H.,
Castranova V., Shi X., Chen F.;
"Lung cancer-associated JmjC domain protein mdig suppresses formation
of tri-methyl lysine 9 of histone H3.";
Cell Cycle 8:2101-2109(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
FUNCTION AS RPL27A HYDROXYLASE, AND CATALYTIC ACTIVITY.
PubMed=23103944; DOI=10.1038/nchembio.1093;
Ge W., Wolf A., Feng T., Ho C.H., Sekirnik R., Zayer A., Granatino N.,
Cockman M.E., Loenarz C., Loik N.D., Hardy A.P., Claridge T.D.,
Hamed R.B., Chowdhury R., Gong L., Robinson C.V., Trudgian D.C.,
Jiang M., Mackeen M.M., McCullagh J.S., Gordiyenko Y., Thalhammer A.,
Yamamoto A., Yang M., Liu-Yi P., Zhang Z., Schmidt-Zachmann M.,
Kessler B.M., Ratcliffe P.J., Preston G.M., Coleman M.L.,
Schofield C.J.;
"Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and
humans.";
Nat. Chem. Biol. 8:960-962(2012).
-!- FUNCTION: Oxygenase that can act as both a histone lysine
demethylase and a ribosomal histidine hydroxylase. Is involved in
the demethylation of trimethylated 'Lys-9' on histone H3
(H3K9me3), leading to an increase in ribosomal RNA expression.
Also catalyzes the hydroxylation of 60S ribosomal protein L27a on
'His-39'. May play an important role in cell growth and survival.
May be involved in ribosome biogenesis, most likely during the
assembly process of pre-ribosomal particles.
{ECO:0000269|PubMed:12091391, ECO:0000269|PubMed:14695334,
ECO:0000269|PubMed:15534111, ECO:0000269|PubMed:15819408,
ECO:0000269|PubMed:15897898, ECO:0000269|PubMed:17317935,
ECO:0000269|PubMed:19502796, ECO:0000269|PubMed:23103944}.
-!- CATALYTIC ACTIVITY:
Reaction=2-oxoglutarate + L-histidyl-[ribosomal protein uL15] + O2
= (3S)-3-hydroxy-L-histidyl-[ribosomal protein uL15] + CO2 +
succinate; Xref=Rhea:RHEA:54024, Rhea:RHEA-COMP:13760,
Rhea:RHEA-COMP:13761, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
ChEBI:CHEBI:16810, ChEBI:CHEBI:29979, ChEBI:CHEBI:30031,
ChEBI:CHEBI:138021; Evidence={ECO:0000269|PubMed:23103944};
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-751580, EBI-751580;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12091391,
ECO:0000269|PubMed:15819408}. Nucleus, nucleolus
{ECO:0000269|PubMed:12091391, ECO:0000269|PubMed:15819408}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1 {ECO:0000269|PubMed:12091391, ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:14742713, ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15897898, ECO:0000269|Ref.4};
IsoId=Q8IUF8-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:12091391};
IsoId=Q8IUF8-2; Sequence=VSP_052589, VSP_052590;
Name=3 {ECO:0000269|PubMed:15897898};
IsoId=Q8IUF8-3; Sequence=VSP_052587, VSP_052588;
Name=4;
IsoId=Q8IUF8-4; Sequence=VSP_038373;
-!- TISSUE SPECIFICITY: Expressed in liver, skeletal muscle, heart,
pancreas, and placenta. Not detected in brain, lung or kidney.
Expressed in several lung cancer tissues, but is barely detected
in the adjacent non-cancerous tissues. Also highly expressed in
several esophageal squamous cell carcinoma (ESCC), and colon
cancer tissues, and in various cancer cell lines.
{ECO:0000269|PubMed:14695334, ECO:0000269|PubMed:15534111,
ECO:0000269|PubMed:15897898, ECO:0000269|PubMed:19502796}.
-!- INDUCTION: Up-regulated in response to MYC, in alveolar
macrophages from coal miners and in silica particle-treated A549
lung cancer cells. {ECO:0000269|PubMed:12091391,
ECO:0000269|PubMed:15897898}.
-!- SIMILARITY: Belongs to the ROX family. MINA53 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAH10679.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MINAID44409ch3q11.html";
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EMBL; AB083189; BAC16537.1; -; mRNA.
EMBL; AB083190; BAC16358.1; -; mRNA.
EMBL; AB083191; BAC16359.1; -; mRNA.
EMBL; AB083192; BAC16360.1; -; mRNA.
EMBL; AB083193; BAC16361.1; -; mRNA.
EMBL; AY390536; AAR27293.1; -; mRNA.
EMBL; AY302110; AAP59421.1; -; mRNA.
EMBL; AY456380; AAR21572.1; -; mRNA.
EMBL; DQ453796; ABE28016.1; -; mRNA.
EMBL; AK027299; BAB55024.1; -; mRNA.
EMBL; AC026100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC110491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW79872.1; -; Genomic_DNA.
EMBL; CH471052; EAW79873.1; -; Genomic_DNA.
EMBL; BC014928; AAH14928.1; -; mRNA.
EMBL; CR627479; CAH10679.1; ALT_TERM; mRNA.
CCDS; CCDS2929.1; -. [Q8IUF8-4]
CCDS; CCDS43114.1; -. [Q8IUF8-1]
RefSeq; NP_001035998.1; NM_001042533.2. [Q8IUF8-1]
RefSeq; NP_001248758.1; NM_001261829.1. [Q8IUF8-4]
RefSeq; NP_116167.3; NM_032778.5. [Q8IUF8-4]
RefSeq; NP_694822.2; NM_153182.3. [Q8IUF8-1]
RefSeq; XP_005247895.1; XM_005247838.4. [Q8IUF8-1]
PDB; 2XDV; X-ray; 2.57 A; A=26-465.
PDB; 4BU2; X-ray; 2.78 A; A=26-465.
PDB; 4BXF; X-ray; 2.05 A; A/B=26-465.
PDBsum; 2XDV; -.
PDBsum; 4BU2; -.
PDBsum; 4BXF; -.
SMR; Q8IUF8; -.
BioGrid; 124309; 38.
DIP; DIP-28141N; -.
IntAct; Q8IUF8; 26.
MINT; Q8IUF8; -.
STRING; 9606.ENSP00000328251; -.
BindingDB; Q8IUF8; -.
iPTMnet; Q8IUF8; -.
PhosphoSitePlus; Q8IUF8; -.
BioMuta; RIOX2; -.
DMDM; 74750624; -.
EPD; Q8IUF8; -.
jPOST; Q8IUF8; -.
MassIVE; Q8IUF8; -.
MaxQB; Q8IUF8; -.
PaxDb; Q8IUF8; -.
PeptideAtlas; Q8IUF8; -.
PRIDE; Q8IUF8; -.
ProteomicsDB; 70558; -. [Q8IUF8-1]
ProteomicsDB; 70559; -. [Q8IUF8-2]
ProteomicsDB; 70560; -. [Q8IUF8-3]
ProteomicsDB; 70561; -. [Q8IUF8-4]
TopDownProteomics; Q8IUF8-2; -. [Q8IUF8-2]
DNASU; 84864; -.
Ensembl; ENST00000333396; ENSP00000328251; ENSG00000170854. [Q8IUF8-1]
Ensembl; ENST00000360258; ENSP00000353395; ENSG00000170854. [Q8IUF8-4]
Ensembl; ENST00000394198; ENSP00000377748; ENSG00000170854. [Q8IUF8-1]
Ensembl; ENST00000514314; ENSP00000424955; ENSG00000170854. [Q8IUF8-2]
GeneID; 84864; -.
KEGG; hsa:84864; -.
UCSC; uc003drz.3; human. [Q8IUF8-1]
CTD; 84864; -.
DisGeNET; 84864; -.
GeneCards; RIOX2; -.
HGNC; HGNC:19441; RIOX2.
HPA; CAB013458; -.
HPA; HPA007603; -.
HPA; HPA008080; -.
MIM; 612049; gene.
neXtProt; NX_Q8IUF8; -.
OpenTargets; ENSG00000170854; -.
PharmGKB; PA134991047; -.
eggNOG; KOG3706; Eukaryota.
eggNOG; ENOG410YNEJ; LUCA.
GeneTree; ENSGT00390000000083; -.
InParanoid; Q8IUF8; -.
KO; K21760; -.
OMA; RPTHEFT; -.
OrthoDB; 693909at2759; -.
PhylomeDB; Q8IUF8; -.
TreeFam; TF318659; -.
Reactome; R-HSA-3214842; HDMs demethylate histones.
ChiTaRS; MINA; human.
EvolutionaryTrace; Q8IUF8; -.
GeneWiki; MINA; -.
GeneWiki; MYC-induced_nuclear_antigen; -.
GenomeRNAi; 84864; -.
Pharos; Q8IUF8; -.
PRO; PR:Q8IUF8; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000170854; Expressed in 231 organ(s), highest expression level in amniotic fluid.
ExpressionAtlas; Q8IUF8; baseline and differential.
Genevisible; Q8IUF8; HS.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); IBA:GO_Central.
GO; GO:0032453; F:histone demethylase activity (H3-K4 specific); IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
InterPro; IPR003347; JmjC_dom.
InterPro; IPR039994; JmjC_protein.
PANTHER; PTHR13096; PTHR13096; 1.
Pfam; PF08007; Cupin_4; 1.
PROSITE; PS51184; JMJC; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Dioxygenase;
Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein;
Polymorphism; Reference proteome; Ribosome biogenesis; Transcription;
Transcription regulation.
CHAIN 1 465 Ribosomal oxygenase 2.
/FTId=PRO_0000308377.
DOMAIN 139 271 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 179 179 Iron; catalytic. {ECO:0000305}.
METAL 181 181 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 240 240 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 1 254 Missing (in isoform 3).
{ECO:0000303|PubMed:15897898}.
/FTId=VSP_052587.
VAR_SEQ 255 261 TISTYQN -> MLLQVPC (in isoform 3).
{ECO:0000303|PubMed:15897898}.
/FTId=VSP_052588.
VAR_SEQ 263 280 SWGDFLLDTISGLVFDTA -> DAGARMRRCDLRAIAPQK
(in isoform 2).
{ECO:0000303|PubMed:12091391}.
/FTId=VSP_052589.
VAR_SEQ 281 465 Missing (in isoform 2).
{ECO:0000303|PubMed:12091391}.
/FTId=VSP_052590.
VAR_SEQ 297 297 Missing (in isoform 4).
{ECO:0000303|PubMed:12091391,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_038373.
VARIANT 17 17 A -> P (in dbSNP:rs35391656).
/FTId=VAR_054079.
VARIANT 201 201 P -> L (in dbSNP:rs56183666).
/FTId=VAR_062241.
VARIANT 386 386 A -> T (in dbSNP:rs2172257).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:14742713,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_036811.
MUTAGEN 179 179 H->Y: Abolishes demethylase activity.
{ECO:0000269|PubMed:19502796}.
CONFLICT 87 87 K -> E (in Ref. 1; BAC16359).
{ECO:0000305}.
CONFLICT 107 107 N -> S (in Ref. 1; BAC16359).
{ECO:0000305}.
CONFLICT 159 159 G -> S (in Ref. 5; BAB55024).
{ECO:0000305}.
CONFLICT 221 221 V -> A (in Ref. 1; BAC16359).
{ECO:0000305}.
HELIX 38 45 {ECO:0000244|PDB:4BXF}.
TURN 46 48 {ECO:0000244|PDB:4BXF}.
HELIX 51 57 {ECO:0000244|PDB:4BXF}.
TURN 58 61 {ECO:0000244|PDB:4BXF}.
STRAND 64 66 {ECO:0000244|PDB:4BXF}.
HELIX 71 80 {ECO:0000244|PDB:4BXF}.
HELIX 85 90 {ECO:0000244|PDB:4BXF}.
STRAND 94 96 {ECO:0000244|PDB:4BXF}.
TURN 97 99 {ECO:0000244|PDB:4BXF}.
STRAND 100 106 {ECO:0000244|PDB:4BXF}.
STRAND 109 112 {ECO:0000244|PDB:4BXF}.
STRAND 116 119 {ECO:0000244|PDB:4BXF}.
HELIX 121 129 {ECO:0000244|PDB:4BXF}.
STRAND 134 138 {ECO:0000244|PDB:4BXF}.
HELIX 140 142 {ECO:0000244|PDB:4BXF}.
HELIX 145 158 {ECO:0000244|PDB:4BXF}.
STRAND 162 169 {ECO:0000244|PDB:4BXF}.
STRAND 178 180 {ECO:0000244|PDB:4BXF}.
STRAND 182 192 {ECO:0000244|PDB:4BXF}.
STRAND 194 199 {ECO:0000244|PDB:4BXF}.
HELIX 214 216 {ECO:0000244|PDB:4BXF}.
STRAND 221 226 {ECO:0000244|PDB:4BXF}.
STRAND 231 234 {ECO:0000244|PDB:4BXF}.
STRAND 239 243 {ECO:0000244|PDB:4BXF}.
STRAND 246 248 {ECO:0000244|PDB:4BXF}.
STRAND 251 258 {ECO:0000244|PDB:4BXF}.
HELIX 264 276 {ECO:0000244|PDB:4BXF}.
HELIX 284 287 {ECO:0000244|PDB:4BXF}.
HELIX 294 296 {ECO:0000244|PDB:4BXF}.
HELIX 302 321 {ECO:0000244|PDB:4BXF}.
HELIX 329 337 {ECO:0000244|PDB:4BXF}.
STRAND 344 348 {ECO:0000244|PDB:4BXF}.
TURN 349 351 {ECO:0000244|PDB:4BXF}.
STRAND 363 366 {ECO:0000244|PDB:4BXF}.
HELIX 369 371 {ECO:0000244|PDB:4BXF}.
STRAND 372 375 {ECO:0000244|PDB:4BXF}.
STRAND 390 395 {ECO:0000244|PDB:4BXF}.
TURN 402 405 {ECO:0000244|PDB:4BXF}.
STRAND 417 420 {ECO:0000244|PDB:4BXF}.
HELIX 421 423 {ECO:0000244|PDB:4BXF}.
HELIX 424 431 {ECO:0000244|PDB:4BXF}.
STRAND 434 437 {ECO:0000244|PDB:4BXF}.
HELIX 438 440 {ECO:0000244|PDB:4BXF}.
HELIX 446 458 {ECO:0000244|PDB:4BXF}.
STRAND 462 464 {ECO:0000244|PDB:4BXF}.
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


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[RIOX2 MDIG MINA MINA53 NO52] Ribosomal oxygenase 2 (60S ribosomal protein L27a histidine hydroxylase) (Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA) (EC 1.14.11.-) (Histone lysine demethylase MINA) (MYC-induced nuclear antigen) (Mineral dust-induced gene protein) (Nucleolar protein 52) (Ribosomal oxygenase MINA) (ROX)
[RIOX1 C14orf169 MAPJD NO66] Ribosomal oxygenase 1 (60S ribosomal protein L8 histidine hydroxylase) (Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66) (EC 1.14.11.-) (EC 1.14.11.27) (Histone lysine demethylase NO66) (Myc-associated protein with JmjC domain) (Nucleolar protein 66) (hsNO66) (Ribosomal oxygenase NO66) (ROX)
[Riox1 Mapjd No66 MNCb-7109] Ribosomal oxygenase 1 (Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66) (EC 1.14.11.-) (EC 1.14.11.27) (Histone lysine demethylase NO66)
[RIOX1 MAPJD NO66] Ribosomal oxygenase 1 (Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66) (EC 1.14.11.-) (EC 1.14.11.27) (Histone lysine demethylase NO66)
[Riox1 Mapjd No66] Ribosomal oxygenase 1 (Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66) (EC 1.14.11.-) (EC 1.14.11.27) (Histone lysine demethylase NO66)
[JMJD6 KIAA0585 PSR PTDSR] Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC 1.14.11.-) (Histone arginine demethylase JMJD6) (JmjC domain-containing protein 6) (Jumonji domain-containing protein 6) (Lysyl-hydroxylase JMJD6) (Peptide-lysine 5-dioxygenase JMJD6) (Phosphatidylserine receptor) (Protein PTDSR)
[Jmjd6 Kiaa0585 Ptdsr] Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC 1.14.11.-) (Histone arginine demethylase JMJD6) (JmjC domain-containing protein 6) (Jumonji domain-containing protein 6) (Lysyl-hydroxylase JMJD6) (Peptide-lysine 5-dioxygenase JMJD6) (Phosphatidylserine receptor) (Protein PTDSR)
[KDM5B JARID1B PLU1 RBBP2H1] Lysine-specific demethylase 5B (EC 1.14.11.-) (Cancer/testis antigen 31) (CT31) (Histone demethylase JARID1B) (Jumonji/ARID domain-containing protein 1B) (PLU-1) (Retinoblastoma-binding protein 2 homolog 1) (RBP2-H1)
[RIOX1 NO66 RCJMB04_1k4] Ribosomal oxygenase 1 (Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66) (EC 1.14.11.-) (EC 1.14.11.27) (Histone lysine demethylase NO66)
[riox1 no66 zgc:162967] Ribosomal oxygenase 1 (Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66) (EC 1.14.11.-) (EC 1.14.11.27) (Histone lysine demethylase NO66)
[roxA ycfD b1128 JW1114] 50S ribosomal protein L16 3-hydroxylase (EC 1.14.11.47) (Ribosomal oxygenase RoxA) (ROX)
[Kdm8 Jmjd5] Bifunctional peptidase and arginyl-hydroxylase JMJD5 (EC 1.14.11.-) (EC 3.4.-.-) (JmjC domain-containing protein 5) (Jumonji C domain-containing protein 5) (L-arginine (3R)-hydroxylase KDM8) (Lysine-specific demethylase 8)
[KDM5A JARID1A RBBP2 RBP2] Lysine-specific demethylase 5A (EC 1.14.11.-) (Histone demethylase JARID1A) (Jumonji/ARID domain-containing protein 1A) (Retinoblastoma-binding protein 2) (RBBP-2)
[KDM2B CXXC2 FBL10 FBXL10 JHDM1B NDY1 PCCX2] Lysine-specific demethylase 2B (EC 1.14.11.27) (CXXC-type zinc finger protein 2) (F-box and leucine-rich repeat protein 10) (F-box protein FBL10) (F-box/LRR-repeat protein 10) (JmjC domain-containing histone demethylation protein 1B) (Jumonji domain-containing EMSY-interactor methyltransferase motif protein) (Protein JEMMA) (Protein-containing CXXC domain 2) ([Histone-H3]-lysine-36 demethylase 1B)
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[lid CG9088] Lysine-specific demethylase lid (EC 1.14.11.-) (Histone demethylase lid) (Jumonji/ARID domain-containing protein lid) (Protein little imaginal disks) (Retinoblastoma-binding protein 2 homolog)
[Kdm5a Jarid1a Rbp2] Lysine-specific demethylase 5A (EC 1.14.11.-) (Histone demethylase JARID1A) (Jumonji/ARID domain-containing protein 1A) (Retinoblastoma-binding protein 2) (RBBP-2)
[Kdm5b Jarid1b Kiaa4034 Plu1] Lysine-specific demethylase 5B (EC 1.14.11.-) (Histone demethylase JARID1B) (Jumonji/ARID domain-containing protein 1B) (PLU-1)
[Kdm3a Jhdm2a Jmjd1a Kiaa0742] Lysine-specific demethylase 3A (EC 1.14.11.-) (JmjC domain-containing histone demethylation protein 2A) (Jumonji domain-containing protein 1A)
[Kdm2a Fbl11 Fbxl11 Jhdm1a Kiaa1004] Lysine-specific demethylase 2A (EC 1.14.11.27) (F-box and leucine-rich repeat protein 11) (F-box/LRR-repeat protein 11) (JmjC domain-containing histone demethylation protein 1A) ([Histone-H3]-lysine-36 demethylase 1A)
[KDM2A CXXC8 FBL11 FBL7 FBXL11 JHDM1A KIAA1004] Lysine-specific demethylase 2A (EC 1.14.11.27) (CXXC-type zinc finger protein 8) (F-box and leucine-rich repeat protein 11) (F-box protein FBL7) (F-box protein Lilina) (F-box/LRR-repeat protein 11) (JmjC domain-containing histone demethylation protein 1A) ([Histone-H3]-lysine-36 demethylase 1A)
[KDM3A JHDM2A JMJD1 JMJD1A KIAA0742 TSGA] Lysine-specific demethylase 3A (EC 1.14.11.-) (JmjC domain-containing histone demethylation protein 2A) (Jumonji domain-containing protein 1A)
[KDM5D HY HYA JARID1D KIAA0234 SMCY] Lysine-specific demethylase 5D (EC 1.14.11.-) (Histocompatibility Y antigen) (H-Y) (Histone demethylase JARID1D) (Jumonji/ARID domain-containing protein 1D) (Protein SmcY)
[UBA52 UBCEP2] Ubiquitin-60S ribosomal protein L40 (CEP52) (Ubiquitin A-52 residue ribosomal protein fusion product 1) [Cleaved into: Ubiquitin; 60S ribosomal protein L40 (Large ribosomal subunit protein eL40)]
[Kdm5d Hya Jarid1d Smcy] Lysine-specific demethylase 5D (EC 1.14.11.-) (Histocompatibility Y antigen) (H-Y) (Histone demethylase JARID1D) (Jumonji/ARID domain-containing protein 1D) (Protein SmcY)
[Kdm3a Jhdm2a Jmjd1a Tsga] Lysine-specific demethylase 3A (EC 1.14.11.-) (JmjC domain-containing histone demethylation protein 2A) (Jumonji domain-containing protein 1A) (Testis-specific gene A protein) (Zinc finger protein TSGA)
[Kdm5c Jarid1c Kiaa0234 Smcx Xe169] Lysine-specific demethylase 5C (EC 1.14.11.-) (Histone demethylase JARID1C) (Jumonji/ARID domain-containing protein 1C) (Protein SmcX) (Protein Xe169)
[KDM6A UTX] Lysine-specific demethylase 6A (EC 1.14.11.-) (Histone demethylase UTX) (Ubiquitously-transcribed TPR protein on the X chromosome) (Ubiquitously-transcribed X chromosome tetratricopeptide repeat protein)
[KDM1A AOF2 KDM1 KIAA0601 LSD1] Lysine-specific histone demethylase 1A (EC 1.-.-.-) (BRAF35-HDAC complex protein BHC110) (Flavin-containing amine oxidase domain-containing protein 2)
[ELF6 JMJ11 PKDM9B At5g04240 F21E1.160] Probable lysine-specific demethylase ELF6 (EC 1.14.11.-) (Early flowering 6) (Jumonji domain-containing protein 11) (Probable lysine-specific histone demethylase ELF6)

Bibliography :