ID KDM4B_HUMAN Reviewed; 1096 AA.
AC O94953; B9EGN8; D6W631; O75274; Q6P3R5; Q9P1V1; Q9UF40;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 4.
DT 24-JAN-2024, entry version 192.
DE RecName: Full=Lysine-specific demethylase 4B;
DE EC=1.14.11.66 {ECO:0000269|PubMed:16603238};
DE AltName: Full=JmjC domain-containing histone demethylation protein 3B;
DE AltName: Full=Jumonji domain-containing protein 2B;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase 4B {ECO:0000305};
GN Name=KDM4B; Synonyms=JHDM3B, JMJD2B, KIAA0876;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-710.
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-710.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLU-710.
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 487-1096, AND VARIANT GLU-710.
RC TISSUE=Testis;
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15927959; DOI=10.1074/jbc.m413687200;
RA Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H.,
RA Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.;
RT "Functional characterization of JMJD2A, a histone deacetylase- and
RT retinoblastoma-binding protein.";
RL J. Biol. Chem. 280:28507-28518(2005).
RN [8]
RP FUNCTION, AND ENZYME ACTIVITY.
RX PubMed=16603238; DOI=10.1016/j.cell.2006.03.028;
RA Whetstine J.R., Nottke A., Lan F., Huarte M., Smolikov S., Chen Z.,
RA Spooner E., Li E., Zhang G., Colaiacovo M., Shi Y.;
RT "Reversal of histone lysine trimethylation by the JMJD2 family of histone
RT demethylases.";
RL Cell 125:467-481(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566 AND THR-1065, AND
RP IDENTIFICATION BY 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-602, AND IDENTIFICATION BY MASS
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566 AND THR-1065, AND
RP IDENTIFICATION BY 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).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF 189-HIS--GLU-191.
RX PubMed=28262558; DOI=10.1016/j.chembiol.2017.02.006;
RA Tumber A., Nuzzi A., Hookway E.S., Hatch S.B., Velupillai S., Johansson C.,
RA Kawamura A., Savitsky P., Yapp C., Szykowska A., Wu N., Bountra C.,
RA Strain-Damerell C., Burgess-Brown N.A., Ruda G.F., Fedorov O., Munro S.,
RA England K.S., Nowak R.P., Schofield C.J., La Thangue N.B., Pawlyn C.,
RA Davies F., Morgan G., Athanasou N., Muller S., Oppermann U., Brennan P.E.;
RT "Potent and Selective KDM5 Inhibitor Stops Cellular Demethylation of
RT H3K4me3 at Transcription Start Sites and Proliferation of MM1S Myeloma
RT Cells.";
RL Cell Chem. Biol. 24:371-380(2017).
RN [14]
RP INVOLVEMENT IN MRD65, AND VARIANTS MRD65 PRO-220; TRP-222; ARG-768 AND
RP LEU-1095.
RX PubMed=33232677; DOI=10.1016/j.ajhg.2020.11.001;
RA Duncan A.R., Vitobello A., Collins S.C., Vancollie V.E., Lelliott C.J.,
RA Rodan L., Shi J., Seman A.R., Agolini E., Novelli A., Prontera P.,
RA Guillen Sacoto M.J., Santiago-Sim T., Trimouille A., Goizet C., Nizon M.,
RA Bruel A.L., Philippe C., Grant P.E., Wojcik M.H., Stoler J., Genetti C.A.,
RA van Dooren M.F., Maas S.M., Alders M., Faivre L., Sorlin A., Yoon G.,
RA Yalcin B., Agrawal P.B.;
RT "Heterozygous variants in KDM4B lead to global developmental delay and
RT neuroanatomical defects.";
RL Am. J. Hum. Genet. 107:1170-1177(2020).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of
CC histone H3, thereby playing a role in histone code. Does not
CC demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-
CC 20'. Only able to demethylate trimethylated H3 'Lys-9', with a weaker
CC activity than KDM4A, KDM4C and KDM4D. Demethylation of Lys residue
CC generates formaldehyde and succinate (PubMed:16603238,
CC PubMed:28262558). Plays a critical role in the development of the
CC central nervous system (CNS). {ECO:0000250|UniProtKB:Q91VY5,
CC ECO:0000269|PubMed:16603238, ECO:0000269|PubMed:28262558}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.66; Evidence={ECO:0000269|PubMed:16603238};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537,
CC ECO:0000269|PubMed:15927959}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O94953-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94953-2; Sequence=VSP_018307, VSP_018308;
CC -!- DOMAIN: The 2 Tudor domains recognize and bind methylated histones.
CC Double Tudor domain has an interdigitated structure and the unusual
CC fold is required for its ability to bind methylated histone tails (By
CC similarity). {ECO:0000250}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 65
CC (MRD65) [MIM:619320]: An autosomal dominant form of intellectual
CC disability, a disorder characterized by significantly below average
CC general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRD65
CC is characterized by delayed motor and speech acquisition, variably
CC impaired intellectual development, behavioral abnormalities, and
CC dysmorphic facial features. Additional variable features include
CC feeding difficulties, hypotonia, and seizures.
CC {ECO:0000269|PubMed:33232677}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC33799.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA74899.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB020683; BAA74899.2; ALT_INIT; mRNA.
DR EMBL; AC005595; AAC33799.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC022517; AAF31271.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69181.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69183.1; -; Genomic_DNA.
DR EMBL; BC063889; AAH63889.1; -; mRNA.
DR EMBL; BC136611; AAI36612.1; -; mRNA.
DR EMBL; AL133622; CAB63748.2; -; mRNA.
DR CCDS; CCDS12138.1; -. [O94953-1]
DR CCDS; CCDS92493.1; -. [O94953-2]
DR PIR; T43460; T43460.
DR RefSeq; NP_055830.1; NM_015015.2.
DR PDB; 4LXL; X-ray; 1.87 A; A=1-348.
DR PDB; 4UC4; X-ray; 2.56 A; A/B=917-1031.
DR PDB; 7JM5; X-ray; 2.70 A; A/B=1-366.
DR PDBsum; 4LXL; -.
DR PDBsum; 4UC4; -.
DR PDBsum; 7JM5; -.
DR AlphaFoldDB; O94953; -.
DR SMR; O94953; -.
DR BioGRID; 116669; 62.
DR DIP; DIP-47283N; -.
DR IntAct; O94953; 18.
DR MINT; O94953; -.
DR STRING; 9606.ENSP00000159111; -.
DR BindingDB; O94953; -.
DR ChEMBL; CHEMBL3313832; -.
DR CarbonylDB; O94953; -.
DR GlyGen; O94953; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O94953; -.
DR PhosphoSitePlus; O94953; -.
DR BioMuta; KDM4B; -.
DR EPD; O94953; -.
DR jPOST; O94953; -.
DR MassIVE; O94953; -.
DR MaxQB; O94953; -.
DR PaxDb; 9606-ENSP00000159111; -.
DR PeptideAtlas; O94953; -.
DR ProteomicsDB; 50574; -. [O94953-1]
DR ProteomicsDB; 50575; -. [O94953-2]
DR Pumba; O94953; -.
DR ABCD; O94953; 1 sequenced antibody.
DR Antibodypedia; 11548; 601 antibodies from 36 providers.
DR DNASU; 23030; -.
DR Ensembl; ENST00000381759.8; ENSP00000371178.3; ENSG00000127663.15. [O94953-2]
DR GeneID; 23030; -.
DR KEGG; hsa:23030; -.
DR UCSC; uc002mbq.5; human. [O94953-1]
DR AGR; HGNC:29136; -.
DR CTD; 23030; -.
DR DisGeNET; 23030; -.
DR GeneCards; KDM4B; -.
DR HGNC; HGNC:29136; KDM4B.
DR HPA; ENSG00000127663; Low tissue specificity.
DR MalaCards; KDM4B; -.
DR MIM; 609765; gene.
DR MIM; 619320; phenotype.
DR neXtProt; NX_O94953; -.
DR OpenTargets; ENSG00000127663; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA164721452; -.
DR VEuPathDB; HostDB:ENSG00000127663; -.
DR eggNOG; KOG0958; Eukaryota.
DR GeneTree; ENSGT00940000159248; -.
DR HOGENOM; CLU_001442_6_1_1; -.
DR InParanoid; O94953; -.
DR OrthoDB; 48111at2759; -.
DR PhylomeDB; O94953; -.
DR TreeFam; TF106449; -.
DR BioCyc; MetaCyc:ENSG00000127663-MONOMER; -.
DR BRENDA; 1.14.11.27; 2681.
DR BRENDA; 1.14.11.66; 2681.
DR BRENDA; 1.14.11.69; 2681.
DR PathwayCommons; O94953; -.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; O94953; -.
DR SIGNOR; O94953; -.
DR BioGRID-ORCS; 23030; 25 hits in 1167 CRISPR screens.
DR ChiTaRS; KDM4B; human.
DR GeneWiki; JMJD2B; -.
DR GenomeRNAi; 23030; -.
DR Pharos; O94953; Tchem.
DR PRO; PR:O94953; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O94953; Protein.
DR Bgee; ENSG00000127663; Expressed in cervix squamous epithelium and 210 other cell types or tissues.
DR ExpressionAtlas; O94953; baseline and differential.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032452; F:histone demethylase activity; TAS:Reactome.
DR GO; GO:0051864; F:histone H3K36 demethylase activity; IDA:UniProtKB.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IMP:UniProtKB.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd15714; ePHD_JMJD2B; 1.
DR CDD; cd15576; PHD_JMJD2B; 1.
DR CDD; cd20464; Tudor_JMJD2B_rpt1; 1.
DR CDD; cd20467; Tudor_JMJD2B_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.10.330.70; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047483; Tudor_KDM4B_rpt1.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF30; LYSINE-SPECIFIC DEMETHYLASE 4B; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF18104; Tudor_2; 2.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW Dioxygenase; Disease variant; Intellectual disability; Iron; Metal-binding;
KW Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1096
FT /note="Lysine-specific demethylase 4B"
FT /id="PRO_0000183175"
FT DOMAIN 15..57
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 146..309
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT DOMAIN 917..974
FT /note="Tudor 1"
FT DOMAIN 975..1031
FT /note="Tudor 2"
FT ZN_FING 731..789
FT /note="PHD-type 1"
FT ZN_FING 794..827
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 850..907
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 369..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 191
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 199
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 207
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 277
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 602
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1065
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 373..448
FT /note="SHRKRSQPKKPKPEDPKFPGEGTAGAALLEEAGGSVKEEAGPEVDPEEEEEE
FT PQPLPHGREAEGAEEDGRGKLRPT -> TPPCVSPHRPSQPGIWCPPGGEAKASAASWL
FT LTTRGHGDTEAGPGLGGDPLHAQSEGQASCVSTSRLRMATQDPCR (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018307"
FT VAR_SEQ 449..1096
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018308"
FT VARIANT 29
FT /note="N -> T (in dbSNP:rs11667206)"
FT /id="VAR_026223"
FT VARIANT 220
FT /note="L -> P (in MRD65)"
FT /evidence="ECO:0000269|PubMed:33232677"
FT /id="VAR_085967"
FT VARIANT 222
FT /note="R -> W (in MRD65)"
FT /evidence="ECO:0000269|PubMed:33232677"
FT /id="VAR_085968"
FT VARIANT 710
FT /note="K -> E (in dbSNP:rs2620836)"
FT /evidence="ECO:0000269|PubMed:10048485,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.4"
FT /id="VAR_026224"
FT VARIANT 768
FT /note="H -> R (in MRD65)"
FT /evidence="ECO:0000269|PubMed:33232677"
FT /id="VAR_085969"
FT VARIANT 1095
FT /note="P -> L (in MRD65; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:33232677"
FT /id="VAR_085970"
FT MUTAGEN 189..191
FT /note="HTE->ATA: Abolishes lysine-specific histone
FT demethylase activity."
FT /evidence="ECO:0000269|PubMed:28262558"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:4LXL"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:4LXL"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7JM5"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:4LXL"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:4LXL"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:4LXL"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:4LXL"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:4LXL"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:7JM5"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:4LXL"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:4LXL"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:4LXL"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:4LXL"
FT STRAND 196..205
FT /evidence="ECO:0007829|PDB:4LXL"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:4LXL"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:4LXL"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:4LXL"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:4LXL"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:4LXL"
FT STRAND 283..292
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 319..325
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:4LXL"
FT HELIX 353..360
FT /evidence="ECO:0007829|PDB:7JM5"
FT STRAND 924..928
FT /evidence="ECO:0007829|PDB:4UC4"
FT STRAND 934..951
FT /evidence="ECO:0007829|PDB:4UC4"
FT STRAND 957..961
FT /evidence="ECO:0007829|PDB:4UC4"
FT HELIX 963..965
FT /evidence="ECO:0007829|PDB:4UC4"
FT STRAND 966..969
FT /evidence="ECO:0007829|PDB:4UC4"
FT HELIX 971..974
FT /evidence="ECO:0007829|PDB:4UC4"
FT STRAND 982..986
FT /evidence="ECO:0007829|PDB:4UC4"
FT STRAND 992..1010
FT /evidence="ECO:0007829|PDB:4UC4"
FT STRAND 1015..1019
FT /evidence="ECO:0007829|PDB:4UC4"
FT HELIX 1020..1022
FT /evidence="ECO:0007829|PDB:4UC4"
SQ SEQUENCE 1096 AA; 121897 MW; 300D5CD6F2DD4330 CRC64;
MGSEDHGAQN PSCKIMTFRP TMEEFKDFNK YVAYIESQGA HRAGLAKIIP PKEWKPRQTY
DDIDDVVIPA PIQQVVTGQS GLFTQYNIQK KAMTVGEYRR LANSEKYCTP RHQDFDDLER
KYWKNLTFVS PIYGADISGS LYDDDVAQWN IGSLRTILDM VERECGTIIE GVNTPYLYFG
MWKTTFAWHT EDMDLYSINY LHFGEPKSWY AIPPEHGKRL ERLAIGFFPG SSQGCDAFLR
HKMTLISPII LKKYGIPFSR ITQEAGEFMI TFPYGYHAGF NHGFNCAEST NFATLRWIDY
GKVATQCTCR KDMVKISMDV FVRILQPERY ELWKQGKDLT VLDHTRPTAL TSPELSSWSA
SRASLKAKLL RRSHRKRSQP KKPKPEDPKF PGEGTAGAAL LEEAGGSVKE EAGPEVDPEE
EEEEPQPLPH GREAEGAEED GRGKLRPTKA KSERKKKSFG LLPPQLPPPP AHFPSEEALW
LPSPLEPPVL GPGPAAMEES PLPAPLNVVP PEVPSEELEA KPRPIIPMLY VVPRPGKAAF
NQEHVSCQQA FEHFAQKGPT WKEPVSPMEL TGPEDGAASS GAGRMETKAR AGEGQAPSTF
SKLKMEIKKS RRHPLGRPPT RSPLSVVKQE ASSDEEASPF SGEEDVSDPD ALRPLLSLQW
KNRAASFQAE RKFNAAAART EPYCAICTLF YPYCQALQTE KEAPIASLGK GCPATLPSKS
RQKTRPLIPE MCFTSGGENT EPLPANSYIG DDGTSPLIAC GKCCLQVHAS CYGIRPELVN
EGWTCSRCAA HAWTAECCLC NLRGGALQMT TDRRWIHVIC AIAVPEARFL NVIERHPVDI
SAIPEQRWKL KCVYCRKRMK KVSGACIQCS YEHCSTSFHV TCAHAAGVLM EPDDWPYVVS
ITCLKHKSGG HAVQLLRAVS LGQVVITKNR NGLYYRCRVI GAASQTCYEV NFDDGSYSDN
LYPESITSRD CVQLGPPSEG ELVELRWTDG NLYKAKFISS VTSHIYQVEF EDGSQLTVKR
GDIFTLEEEL PKRVRSRLSL STGAPQEPAF SGEEAKAAKR PRVGTPLATE DSGRSQDYVA
FVESLLQVQG RPGAPF
//
