RIOX1_HUMAN
ID RIOX1_HUMAN Reviewed; 641 AA.
AC Q9H6W3; B4DT02;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ribosomal oxygenase 1 {ECO:0000312|HGNC:HGNC:20968};
DE AltName: Full=60S ribosomal protein L8 histidine hydroxylase;
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:23103944};
DE AltName: Full=Histone lysine demethylase NO66;
DE AltName: Full=Myc-associated protein with JmjC domain;
DE AltName: Full=Nucleolar protein 66;
DE Short=hsNO66;
DE AltName: Full=Ribosomal oxygenase NO66;
DE Short=ROX;
GN Name=RIOX1 {ECO:0000312|HGNC:HGNC:20968}; Synonyms=C14orf169, MAPJD, NO66;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND VARIANTS ARG-17 AND ALA-364.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP ARG-17 AND ALA-364.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ARG-17 AND
RP ALA-364.
RC TISSUE=Lymph, and Mammary gland;
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 [5]
RP FUNCTION, INTERACTION WITH MYC, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17308053; DOI=10.1158/1535-7163.mct-06-0659;
RA Suzuki C., Takahashi K., Hayama S., Ishikawa N., Kato T., Ito T.,
RA Tsuchiya E., Nakamura Y., Daigo Y.;
RT "Identification of Myc-associated protein with JmjC domain as a novel
RT therapeutic target oncogene for lung cancer.";
RL Mol. Cancer Ther. 6:542-551(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP INTERACTION WITH PHF19.
RX PubMed=23160351; DOI=10.1038/nsmb.2449;
RA Brien G.L., Gambero G., O'Connell D.J., Jerman E., Turner S.A., Egan C.M.,
RA Dunne E.J., Jurgens M.C., Wynne K., Piao L., Lohan A.J., Ferguson N.,
RA Shi X., Sinha K.M., Loftus B.J., Cagney G., Bracken A.P.;
RT "Polycomb PHF19 binds H3K36me3 and recruits PRC2 and demethylase NO66 to
RT embryonic stem cell genes during differentiation.";
RL Nat. Struct. Mol. Biol. 19:1273-1281(2012).
RN [9]
RP FUNCTION AS RPL8 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).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Oxygenase that can act as both a histone lysine demethylase
CC and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-
CC 4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a
CC central role in histone code. Preferentially demethylates trimethylated
CC H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues,
CC while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2).
CC Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-
CC 216'. Acts as a regulator of osteoblast differentiation via its
CC interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby
CC inhibiting SP7/OSX-mediated promoter activation (By similarity). May
CC also play a role in ribosome biogenesis and in the replication or
CC remodeling of certain heterochromatic region. Participates in MYC-
CC induced transcriptional activation. {ECO:0000250,
CC ECO:0000269|PubMed:14742713, ECO:0000269|PubMed:17308053,
CC ECO:0000269|PubMed:23103944}.
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: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;
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 -!- SUBUNIT: Interacts with SP7/OSX; the interaction is direct (By
CC similarity). Interacts with MYC. Interacts with PHF19; leading to its
CC recruitment to H3K36me3 sites. {ECO:0000250,
CC ECO:0000269|PubMed:17308053, ECO:0000269|PubMed:23160351}.
CC -!- INTERACTION:
CC Q9H6W3; Q8VI67: Sp7; Xeno; NbExp=6; IntAct=EBI-2513645, EBI-7608836;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm.
CC Note=Granular part of nucleoli. Nucleoplasm, nucleoplasmic foci, some
CC of them associated with nucleoli.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H6W3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H6W3-2; Sequence=VSP_038663;
CC -!- TISSUE SPECIFICITY: Widely expressed. Overexpressed in lung carcinomas.
CC {ECO:0000269|PubMed:14742713, ECO:0000269|PubMed:17308053}.
CC -!- SIMILARITY: Belongs to the ROX family. NO66 subfamily. {ECO:0000305}.
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; AY390535; AAR27292.1; -; mRNA.
DR EMBL; AK025455; BAB15138.1; -; mRNA.
DR EMBL; AK299994; BAG61814.1; -; mRNA.
DR EMBL; AC005280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011350; AAH11350.1; -; mRNA.
DR EMBL; BC071954; AAH71954.1; -; mRNA.
DR CCDS; CCDS73660.1; -. [Q9H6W3-1]
DR RefSeq; NP_078920.2; NM_024644.4. [Q9H6W3-1]
DR PDB; 4CCJ; X-ray; 2.15 A; A/B/C/D=183-641.
DR PDB; 4CCK; X-ray; 2.15 A; A/B/C/D=183-641.
DR PDB; 4CCM; X-ray; 2.51 A; A/B=183-641.
DR PDB; 4CCN; X-ray; 2.23 A; A/B=183-641.
DR PDB; 4CCO; X-ray; 2.30 A; A/B=183-641.
DR PDB; 4DIQ; X-ray; 2.40 A; A/B=167-641.
DR PDB; 4E4H; X-ray; 2.28 A; A/B/C/D=183-641.
DR PDB; 4Y33; X-ray; 2.70 A; A/B/C/D=176-641.
DR PDB; 4Y3O; X-ray; 2.20 A; A/B=176-641.
DR PDB; 4Y4R; X-ray; 3.30 A; A/B=176-525, A/B=541-641.
DR PDBsum; 4CCJ; -.
DR PDBsum; 4CCK; -.
DR PDBsum; 4CCM; -.
DR PDBsum; 4CCN; -.
DR PDBsum; 4CCO; -.
DR PDBsum; 4DIQ; -.
DR PDBsum; 4E4H; -.
DR PDBsum; 4Y33; -.
DR PDBsum; 4Y3O; -.
DR PDBsum; 4Y4R; -.
DR AlphaFoldDB; Q9H6W3; -.
DR SMR; Q9H6W3; -.
DR BioGRID; 122818; 60.
DR DIP; DIP-53768N; -.
DR IntAct; Q9H6W3; 30.
DR MINT; Q9H6W3; -.
DR STRING; 9606.ENSP00000477507; -.
DR BindingDB; Q9H6W3; -.
DR iPTMnet; Q9H6W3; -.
DR PhosphoSitePlus; Q9H6W3; -.
DR SwissPalm; Q9H6W3; -.
DR BioMuta; RIOX1; -.
DR DMDM; 284018103; -.
DR EPD; Q9H6W3; -.
DR jPOST; Q9H6W3; -.
DR MassIVE; Q9H6W3; -.
DR MaxQB; Q9H6W3; -.
DR PeptideAtlas; Q9H6W3; -.
DR PRIDE; Q9H6W3; -.
DR ProteomicsDB; 81046; -. [Q9H6W3-1]
DR ProteomicsDB; 81047; -. [Q9H6W3-2]
DR ABCD; Q9H6W3; 1 sequenced antibody.
DR Antibodypedia; 73399; 100 antibodies from 25 providers.
DR DNASU; 79697; -.
DR Ensembl; ENST00000304061.8; ENSP00000477507.1; ENSG00000170468.8. [Q9H6W3-1]
DR GeneID; 79697; -.
DR KEGG; hsa:79697; -.
DR MANE-Select; ENST00000304061.8; ENSP00000477507.1; NM_024644.5; NP_078920.2.
DR UCSC; uc032bfz.2; human. [Q9H6W3-1]
DR CTD; 79697; -.
DR DisGeNET; 79697; -.
DR GeneCards; RIOX1; -.
DR HGNC; HGNC:20968; RIOX1.
DR HPA; ENSG00000170468; Low tissue specificity.
DR MIM; 611919; gene.
DR neXtProt; NX_Q9H6W3; -.
DR OpenTargets; ENSG00000170468; -.
DR PharmGKB; PA134919088; -.
DR VEuPathDB; HostDB:ENSG00000170468; -.
DR eggNOG; KOG3706; Eukaryota.
DR GeneTree; ENSGT00390000000083; -.
DR HOGENOM; CLU_013645_4_1_1; -.
DR InParanoid; Q9H6W3; -.
DR OMA; EWGCMAG; -.
DR OrthoDB; 693909at2759; -.
DR PhylomeDB; Q9H6W3; -.
DR BioCyc; MetaCyc:ENSG00000170468-MON; -.
DR PathwayCommons; Q9H6W3; -.
DR SignaLink; Q9H6W3; -.
DR BioGRID-ORCS; 79697; 14 hits in 214 CRISPR screens.
DR GenomeRNAi; 79697; -.
DR Pharos; Q9H6W3; Tbio.
DR PRO; PR:Q9H6W3; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9H6W3; protein.
DR Bgee; ENSG00000170468; Expressed in oocyte and 184 other tissues.
DR Genevisible; Q9H6W3; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISS: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; ISS: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; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0070544; P:histone H3-K36 demethylation; ISS:UniProtKB.
DR GO; GO:0034720; P:histone H3-K4 demethylation; ISS:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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 PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..641
FT /note="Ribosomal oxygenase 1"
FT /id="PRO_0000264613"
FT DOMAIN 294..439
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 340
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 342
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 405
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZU57"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZU57"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..212
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038663"
FT VARIANT 17
FT /note="K -> R (in dbSNP:rs10144469)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:14742713, ECO:0000269|PubMed:15489334"
FT /id="VAR_062422"
FT VARIANT 218
FT /note="F -> S (in dbSNP:rs758109)"
FT /id="VAR_057819"
FT VARIANT 239
FT /note="Q -> H (in dbSNP:rs34970526)"
FT /id="VAR_060191"
FT VARIANT 364
FT /note="V -> A (in dbSNP:rs3813563)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:14742713, ECO:0000269|PubMed:15489334"
FT /id="VAR_062423"
FT CONFLICT 392
FT /note="E -> G (in Ref. 2; BAG61814)"
FT /evidence="ECO:0000305"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:4CCJ"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:4CCJ"
FT TURN 235..240
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:4CCJ"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:4Y3O"
FT STRAND 343..353
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:4CCJ"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 415..422
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 428..446
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 448..451
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 472..487
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 488..491
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 494..508
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 516..520
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 523..525
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:4E4H"
FT STRAND 532..536
FT /evidence="ECO:0007829|PDB:4Y3O"
FT STRAND 547..561
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 564..570
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 583..587
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:4CCJ"
FT HELIX 592..600
FT /evidence="ECO:0007829|PDB:4CCJ"
FT TURN 601..603
FT /evidence="ECO:0007829|PDB:4DIQ"
FT HELIX 608..610
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 612..615
FT /evidence="ECO:0007829|PDB:4CCM"
FT HELIX 616..628
FT /evidence="ECO:0007829|PDB:4CCJ"
FT STRAND 632..636
FT /evidence="ECO:0007829|PDB:4CCJ"
SQ SEQUENCE 641 AA; 71086 MW; E66A4342B1D1BFF2 CRC64;
MDGLQASAGP LRRGRPKRRR KPQPHSGSVL ALPLRSRKIR KQLRSVVSRM AALRTQTLPS
ENSEESRVES TADDLGDALP GGAAVAAVPD AARREPYGHL GPAELLEASP AARSLQTPSA
RLVPASAPPA RLVEVPAAPV RVVETSALLC TAQHLAAVQS SGAPATASGP QVDNTGGEPA
WDSPLRRVLA ELNRIPSSRR RAARLFEWLI APMPPDHFYR RLWEREAVLV RRQDHTYYQG
LFSTADLDSM LRNEEVQFGQ HLDAARYING RRETLNPPGR ALPAAAWSLY QAGCSLRLLC
PQAFSTTVWQ FLAVLQEQFG SMAGSNVYLT PPNSQGFAPH YDDIEAFVLQ LEGRKLWRVY
RPRVPTEELA LTSSPNFSQD DLGEPVLQTV LEPGDLLYFP RGFIHQAECQ DGVHSLHLTL
STYQRNTWGD FLEAILPLAV QAAMEENVEF RRGLPRDFMD YMGAQHSDSK DPRRTAFMEK
VRVLVARLGH FAPVDAVADQ RAKDFIHDSL PPVLTDRERA LSVYGLPIRW EAGEPVNVGA
QLTTETEVHM LQDGIARLVG EGGHLFLYYT VENSRVYHLE EPKCLEIYPQ QADAMELLLG
SYPEFVRVGD LPCDSVEDQL SLATTLYDKG LLLTKMPLAL N
