KDM6B_HUMAN
ID KDM6B_HUMAN Reviewed; 1643 AA.
AC O15054; C9IZ40; Q96G33;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Lysine-specific demethylase 6B;
DE EC=1.14.11.68 {ECO:0000269|PubMed:17713478, ECO:0000269|PubMed:17825402, ECO:0000269|PubMed:17851529, ECO:0000269|PubMed:18003914};
DE AltName: Full=JmjC domain-containing protein 3;
DE AltName: Full=Jumonji domain-containing protein 3;
DE AltName: Full=Lysine demethylase 6B;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(27) demethylase 6B {ECO:0000305};
GN Name=KDM6B; Synonyms=JMJD3, KIAA0346;
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).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1000-1643 (ISOFORM 2).
RC TISSUE=Brain;
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 INDUCTION BY TPA.
RX PubMed=17193924; DOI=10.3727/000000006783991791;
RA Hu L.Y., Tepper C.G., Lo S.H., Lin W.C.;
RT "An efficient strategy to identify early TPA-responsive genes during
RT differentiation of HL-60 cells.";
RL Gene Expr. 13:179-189(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION IN THE MLL4 COMPLEX.
RX PubMed=17825402; DOI=10.1016/j.cell.2007.08.019;
RA De Santa F., Totaro M.G., Prosperini E., Notarbartolo S., Testa G.,
RA Natoli G.;
RT "The histone H3 lysine-27 demethylase Jmjd3 links inflammation to
RT inhibition of polycomb-mediated gene silencing.";
RL Cell 130:1083-1094(2007).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17851529; DOI=10.1038/nature06192;
RA Lan F., Bayliss P.E., Rinn J.L., Whetstine J.R., Wang J.K., Chen S.,
RA Iwase S., Alpatov R., Issaeva I., Canaani E., Roberts T.M., Chang H.Y.,
RA Shi Y.;
RT "A histone H3 lysine 27 demethylase regulates animal posterior
RT development.";
RL Nature 449:689-694(2007).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17713478; DOI=10.1038/nature06145;
RA Agger K., Cloos P.A., Christensen J., Pasini D., Rose S., Rappsilber J.,
RA Issaeva I., Canaani E., Salcini A.E., Helin K.;
RT "UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene
RT regulation and development.";
RL Nature 449:731-734(2007).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18003914; DOI=10.1073/pnas.0707292104;
RA Hong S., Cho Y.W., Yu L.-R., Yu H., Veenstra T.D., Ge K.;
RT "Identification of JmjC domain-containing UTX and JMJD3 as histone H3
RT lysine 27 demethylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18439-18444(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [11]
RP FUNCTION, AND MUTAGENESIS OF 1390-HIS--GLU-1392.
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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1109, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1176-1502 IN COMPLEX WITH NICKEL
RP IONS AND 8-HYDROXYQUINOLINE-5-CARBOXYLIC ACID.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the human JMJD3 Jumonji domain.";
RL Submitted (DEC-2010) to the PDB data bank.
RN [14]
RP INVOLVEMENT IN NEDCFSA, AND VARIANTS NEDCFSA 75-TYR--ARG-1643 DEL; ARG-149
RP DEL; 1244-GLU--ARG-1643 DEL; SER-1331 AND SER-1379.
RX PubMed=31124279; DOI=10.1002/ajmg.a.61173;
RA Stolerman E.S., Francisco E., Stallworth J.L., Jones J.R., Monaghan K.G.,
RA Keller-Ramey J., Person R., Wentzensen I.M., McWalter K., Keren B.,
RA Heron B., Nava C., Heron D., Kim K., Burton B., Al-Musafri F., O'Grady L.,
RA Sahai I., Escobar L.F., Meuwissen M., Reyniers E., Kooy F., Lacassie Y.,
RA Gunay-Aygun M., Schatz K.S., Hochstenbach R., Zwijnenburg P.J.G.,
RA Waisfisz Q., van Slegtenhorst M., Mancini G.M.S., Louie R.J.;
RT "Genetic variants in the KDM6B gene are associated with neurodevelopmental
RT delays and dysmorphic features.";
RL Am. J. Med. Genet. A 179:1276-1286(2019).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-27'
CC of histone H3, thereby playing a central role in histone code
CC (PubMed:17825402, PubMed:17851529, PubMed:17713478, PubMed:18003914).
CC Demethylates trimethylated and dimethylated H3 'Lys-27'
CC (PubMed:17825402, PubMed:17851529, PubMed:17713478, PubMed:18003914).
CC Plays a central role in regulation of posterior development, by
CC regulating HOX gene expression (PubMed:17851529). Involved in
CC inflammatory response by participating in macrophage differentiation in
CC case of inflammation by regulating gene expression and macrophage
CC differentiation (PubMed:17825402). Plays a demethylase-independent role
CC in chromatin remodeling to regulate T-box family member-dependent gene
CC expression by acting as a link between T-box factors and the SMARCA4-
CC containing SWI/SNF remodeling complex (By similarity).
CC {ECO:0000250|UniProtKB:Q5NCY0, ECO:0000269|PubMed:17713478,
CC ECO:0000269|PubMed:17825402, ECO:0000269|PubMed:17851529,
CC ECO:0000269|PubMed:18003914, ECO:0000269|PubMed:28262558}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224,
CC Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, 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=1.14.11.68; Evidence={ECO:0000269|PubMed:17713478,
CC ECO:0000269|PubMed:17825402, ECO:0000269|PubMed:17851529,
CC ECO:0000269|PubMed:18003914};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:17825402};
CC -!- SUBUNIT: Interacts with TLE1 (By similarity). Component of the MLL4
CC complex, at least composed of KMT2B/MLL4, ASH2L, RBBP5, WDR5, and KDM6B
CC (PubMed:17825402). Interacts with TBX21, SMARCA4, SMARCC1 and SMARCC2
CC (By similarity). {ECO:0000250|UniProtKB:Q5NCY0,
CC ECO:0000269|PubMed:17825402}.
CC -!- INTERACTION:
CC O15054; P03372: ESR1; NbExp=2; IntAct=EBI-2831260, EBI-78473;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:17825402}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=O15054-2; Sequence=Displayed;
CC Name=1;
CC IsoId=O15054-1; Sequence=VSP_040102;
CC -!- INDUCTION: By 12-O-tetradecanoylphorbol-13-acetate (TPA) in myeloid
CC leukemia cells. {ECO:0000269|PubMed:17193924}.
CC -!- DISEASE: Neurodevelopmental disorder with coarse facies and mild distal
CC skeletal abnormalities (NEDCFSA) [MIM:618505]: An autosomal dominant
CC disorder characterized by global developmental delay, variable
CC intellectual disability, poor language acquisition, and dysmorphic
CC facial features including a prominent nasal bridge and coarse features.
CC Some patients manifest autism spectrum disorder. Musculoskeletal
CC features may be present and include widened and thickened hands and
CC fingers, joint hypermobility, clinodactyly of the fifth fingers, and
CC toe syndactyly. {ECO:0000269|PubMed:31124279}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA21572.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB002344; BAA21572.2; ALT_INIT; mRNA.
DR EMBL; AC104581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009994; AAH09994.1; -; mRNA.
DR CCDS; CCDS32552.1; -. [O15054-1]
DR CCDS; CCDS86569.1; -. [O15054-2]
DR RefSeq; NP_001073893.1; NM_001080424.2. [O15054-1]
DR RefSeq; NP_001335645.1; NM_001348716.1. [O15054-2]
DR RefSeq; XP_005256606.1; XM_005256549.3. [O15054-1]
DR RefSeq; XP_005256607.1; XM_005256550.4. [O15054-1]
DR RefSeq; XP_005256608.1; XM_005256551.3. [O15054-1]
DR RefSeq; XP_005256609.1; XM_005256552.4. [O15054-1]
DR RefSeq; XP_006721546.1; XM_006721483.3. [O15054-1]
DR RefSeq; XP_011522052.1; XM_011523750.2. [O15054-1]
DR RefSeq; XP_011522054.1; XM_011523752.2. [O15054-1]
DR PDB; 2XUE; X-ray; 2.00 A; A/B=1141-1643.
DR PDB; 2XXZ; X-ray; 1.80 A; A/B=1176-1505.
DR PDB; 4ASK; X-ray; 1.86 A; A/B=1141-1643.
DR PDB; 5FP3; X-ray; 2.05 A; A/B=1141-1643.
DR PDB; 5OY3; X-ray; 2.14 A; A=1141-1643.
DR PDB; 6F6D; X-ray; 1.82 A; A=1141-1643.
DR PDBsum; 2XUE; -.
DR PDBsum; 2XXZ; -.
DR PDBsum; 4ASK; -.
DR PDBsum; 5FP3; -.
DR PDBsum; 5OY3; -.
DR PDBsum; 6F6D; -.
DR AlphaFoldDB; O15054; -.
DR SMR; O15054; -.
DR BioGRID; 116752; 95.
DR CORUM; O15054; -.
DR DIP; DIP-59912N; -.
DR IntAct; O15054; 12.
DR MINT; O15054; -.
DR STRING; 9606.ENSP00000254846; -.
DR BindingDB; O15054; -.
DR ChEMBL; CHEMBL1938211; -.
DR GuidetoPHARMACOLOGY; 2685; -.
DR GlyGen; O15054; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; O15054; -.
DR PhosphoSitePlus; O15054; -.
DR BioMuta; KDM6B; -.
DR EPD; O15054; -.
DR jPOST; O15054; -.
DR MassIVE; O15054; -.
DR MaxQB; O15054; -.
DR PaxDb; O15054; -.
DR PeptideAtlas; O15054; -.
DR PRIDE; O15054; -.
DR ProteomicsDB; 48403; -. [O15054-2]
DR ProteomicsDB; 48404; -. [O15054-1]
DR ABCD; O15054; 1 sequenced antibody.
DR Antibodypedia; 24405; 370 antibodies from 33 providers.
DR DNASU; 23135; -.
DR Ensembl; ENST00000254846.9; ENSP00000254846.5; ENSG00000132510.11. [O15054-1]
DR Ensembl; ENST00000448097.7; ENSP00000412513.2; ENSG00000132510.11. [O15054-2]
DR GeneID; 23135; -.
DR KEGG; hsa:23135; -.
DR MANE-Select; ENST00000448097.7; ENSP00000412513.2; NM_001348716.2; NP_001335645.1.
DR UCSC; uc002giw.2; human. [O15054-2]
DR CTD; 23135; -.
DR DisGeNET; 23135; -.
DR GeneCards; KDM6B; -.
DR HGNC; HGNC:29012; KDM6B.
DR HPA; ENSG00000132510; Low tissue specificity.
DR MalaCards; KDM6B; -.
DR MIM; 611577; gene.
DR MIM; 618505; phenotype.
DR neXtProt; NX_O15054; -.
DR OpenTargets; ENSG00000132510; -.
DR VEuPathDB; HostDB:ENSG00000132510; -.
DR eggNOG; KOG1124; Eukaryota.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000160414; -.
DR HOGENOM; CLU_001909_0_0_1; -.
DR InParanoid; O15054; -.
DR OMA; LHGDVWG; -.
DR OrthoDB; 268901at2759; -.
DR PhylomeDB; O15054; -.
DR TreeFam; TF317405; -.
DR BioCyc; MetaCyc:ENSG00000132510-MON; -.
DR BRENDA; 1.14.11.68; 2681.
DR BRENDA; 1.14.18.B1; 2681.
DR PathwayCommons; O15054; -.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR SignaLink; O15054; -.
DR SIGNOR; O15054; -.
DR BioGRID-ORCS; 23135; 20 hits in 1098 CRISPR screens.
DR ChiTaRS; KDM6B; human.
DR EvolutionaryTrace; O15054; -.
DR GenomeRNAi; 23135; -.
DR Pharos; O15054; Tchem.
DR PRO; PR:O15054; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O15054; protein.
DR Bgee; ENSG00000132510; Expressed in blood and 182 other tissues.
DR ExpressionAtlas; O15054; baseline and differential.
DR Genevisible; O15054; HS.
DR GO; GO:0044666; C:MLL3/4 complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0032452; F:histone demethylase activity; TAS:Reactome.
DR GO; GO:0071558; F:histone H3-tri/di-methyl-lysine-27 demethylase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISS:BHF-UCL.
DR GO; GO:0045165; P:cell fate commitment; IEA:Ensembl.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0045446; P:endothelial cell differentiation; ISS:BHF-UCL.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0071557; P:histone H3-K27 demethylation; IMP:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0048333; P:mesodermal cell differentiation; ISS:BHF-UCL.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR029518; KDM6B.
DR PANTHER; PTHR14017:SF5; PTHR14017:SF5; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Dioxygenase;
KW Disease variant; Inflammatory response; Intellectual disability; Iron;
KW Isopeptide bond; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc.
FT CHAIN 1..1643
FT /note="Lysine-specific demethylase 6B"
FT /id="PRO_0000292007"
FT DOMAIN 1339..1502
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 52..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..344
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..487
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..608
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..662
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..802
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..848
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..906
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..992
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1065
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1390
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 1392
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 1470
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1578
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1602
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1605
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 1109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1636
FT /note="L -> LVRARRARGQRRRALGQAAGTGFGSPAAPFPEPPPAFSPQ (in
FT isoform 1)"
FT /evidence="ECO:0000303|PubMed:9205841"
FT /id="VSP_040102"
FT VARIANT 75..1643
FT /note="Missing (in NEDCFSA)"
FT /evidence="ECO:0000269|PubMed:31124279"
FT /id="VAR_083120"
FT VARIANT 149..1643
FT /note="Missing (in NEDCFSA)"
FT /evidence="ECO:0000269|PubMed:31124279"
FT /id="VAR_083121"
FT VARIANT 203
FT /note="P -> A (in dbSNP:rs60738318)"
FT /id="VAR_061670"
FT VARIANT 308
FT /note="S -> L (in dbSNP:rs2270516)"
FT /id="VAR_032927"
FT VARIANT 1244..1643
FT /note="Missing (in NEDCFSA)"
FT /evidence="ECO:0000269|PubMed:31124279"
FT /id="VAR_083122"
FT VARIANT 1331
FT /note="N -> S (in NEDCFSA; dbSNP:rs1567802147)"
FT /evidence="ECO:0000269|PubMed:31124279"
FT /id="VAR_083123"
FT VARIANT 1379
FT /note="Y -> S (in NEDCFSA; dbSNP:rs1567802439)"
FT /evidence="ECO:0000269|PubMed:31124279"
FT /id="VAR_083124"
FT MUTAGEN 1390..1392
FT /note="HQE->AQA: Abolishes lysine-specific histone
FT demethylase activity."
FT /evidence="ECO:0000269|PubMed:28262558"
FT CONFLICT 252..254
FT /note="Missing (in Ref. 1; BAA21572 and 3; AAH09994)"
FT /evidence="ECO:0000305"
FT HELIX 1162..1164
FT /evidence="ECO:0007829|PDB:6F6D"
FT STRAND 1172..1174
FT /evidence="ECO:0007829|PDB:5OY3"
FT HELIX 1178..1181
FT /evidence="ECO:0007829|PDB:6F6D"
FT STRAND 1187..1189
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1193..1195
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1199..1206
FT /evidence="ECO:0007829|PDB:2XXZ"
FT STRAND 1211..1217
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1218..1222
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1226..1229
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1231..1238
FT /evidence="ECO:0007829|PDB:2XXZ"
FT STRAND 1242..1249
FT /evidence="ECO:0007829|PDB:2XXZ"
FT STRAND 1261..1264
FT /evidence="ECO:0007829|PDB:2XXZ"
FT STRAND 1271..1276
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1277..1289
FT /evidence="ECO:0007829|PDB:2XXZ"
FT STRAND 1325..1333
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1337..1347
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1352..1354
FT /evidence="ECO:0007829|PDB:2XXZ"
FT TURN 1356..1359
FT /evidence="ECO:0007829|PDB:2XXZ"
FT STRAND 1363..1365
FT /evidence="ECO:0007829|PDB:2XXZ"
FT STRAND 1366..1368
FT /evidence="ECO:0007829|PDB:4ASK"
FT TURN 1371..1373
FT /evidence="ECO:0007829|PDB:4ASK"
FT STRAND 1375..1381
FT /evidence="ECO:0007829|PDB:2XXZ"
FT STRAND 1386..1390
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1393..1395
FT /evidence="ECO:0007829|PDB:2XXZ"
FT STRAND 1397..1406
FT /evidence="ECO:0007829|PDB:2XXZ"
FT STRAND 1408..1413
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1415..1417
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1418..1427
FT /evidence="ECO:0007829|PDB:2XXZ"
FT TURN 1432..1434
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1441..1446
FT /evidence="ECO:0007829|PDB:2XXZ"
FT STRAND 1452..1456
FT /evidence="ECO:0007829|PDB:2XXZ"
FT STRAND 1461..1464
FT /evidence="ECO:0007829|PDB:2XXZ"
FT STRAND 1469..1487
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1491..1495
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1497..1501
FT /evidence="ECO:0007829|PDB:2XXZ"
FT HELIX 1514..1524
FT /evidence="ECO:0007829|PDB:6F6D"
FT HELIX 1530..1556
FT /evidence="ECO:0007829|PDB:6F6D"
FT STRAND 1561..1563
FT /evidence="ECO:0007829|PDB:4ASK"
FT TURN 1576..1578
FT /evidence="ECO:0007829|PDB:6F6D"
FT STRAND 1584..1589
FT /evidence="ECO:0007829|PDB:6F6D"
FT STRAND 1592..1596
FT /evidence="ECO:0007829|PDB:5FP3"
FT STRAND 1597..1601
FT /evidence="ECO:0007829|PDB:6F6D"
FT HELIX 1603..1609
FT /evidence="ECO:0007829|PDB:6F6D"
FT TURN 1610..1615
FT /evidence="ECO:0007829|PDB:4ASK"
FT STRAND 1617..1622
FT /evidence="ECO:0007829|PDB:6F6D"
FT HELIX 1624..1633
FT /evidence="ECO:0007829|PDB:6F6D"
SQ SEQUENCE 1643 AA; 176632 MW; 8CE32AE602683BA3 CRC64;
MHRAVDPPGA RAAREAFALG GLSCAGAWSS CPPHPPPRSA WLPGGRCSAS IGQPPLPAPL
PPSHGSSSGH PSKPYYAPGA PTPRPLHGKL ESLHGCVQAL LREPAQPGLW EQLGQLYESE
HDSEEATRCY HSALRYGGSF AELGPRIGRL QQAQLWNFHT GSCQHRAKVL PPLEQVWNLL
HLEHKRNYGA KRGGPPVKRA AEPPVVQPVP PAALSGPSGE EGLSPGGKRR RGCNSEQTGL
PPGLPLPPPP LPPPPPPPPP PPPPLPGLAT SPPFQLTKPG LWSTLHGDAW GPERKGSAPP
ERQEQRHSLP HPYPYPAPAY TAHPPGHRLV PAAPPGPGPR PPGAESHGCL PATRPPGSDL
RESRVQRSRM DSSVSPAATT ACVPYAPSRP PGLPGTTTSS SSSSSSNTGL RGVEPNPGIP
GADHYQTPAL EVSHHGRLGP SAHSSRKPFL GAPAATPHLS LPPGPSSPPP PPCPRLLRPP
PPPAWLKGPA CRAAREDGEI LEELFFGTEG PPRPAPPPLP HREGFLGPPA SRFSVGTQDS
HTPPTPPTPT TSSSNSNSGS HSSSPAGPVS FPPPPYLARS IDPLPRPPSP AQNPQDPPLV
PLTLALPPAP PSSCHQNTSG SFRRPESPRP RVSFPKTPEV GPGPPPGPLS KAPQPVPPGV
GELPARGPRL FDFPPTPLED QFEEPAEFKI LPDGLANIMK MLDESIRKEE EQQQHEAGVA
PQPPLKEPFA SLQSPFPTDT APTTTAPAVA VTTTTTTTTT TTATQEEEKK PPPALPPPPP
LAKFPPPSQP QPPPPPPPSP ASLLKSLASV LEGQKYCYRG TGAAVSTRPG PLPTTQYSPG
PPSGATALPP TSAAPSAQGS PQPSASSSSQ FSTSGGPWAR ERRAGEEPVP GPMTPTQPPP
PLSLPPARSE SEVLEEISRA CETLVERVGR SATDPADPVD TAEPADSGTE RLLPPAQAKE
EAGGVAAVSG SCKRRQKEHQ KEHRRHRRAC KDSVGRRPRE GRAKAKAKVP KEKSRRVLGN
LDLQSEEIQG REKSRPDLGG ASKAKPPTAP APPSAPAPSA QPTPPSASVP GKKAREEAPG
PPGVSRADML KLRSLSEGPP KELKIRLIKV ESGDKETFIA SEVEERRLRM ADLTISHCAA
DVVRASRNAK VKGKFRESYL SPAQSVKPKI NTEEKLPREK LNPPTPSIYL ESKRDAFSPV
LLQFCTDPRN PITVIRGLAG SLRLNLGLFS TKTLVEASGE HTVEVRTQVQ QPSDENWDLT
GTRQIWPCES SRSHTTIAKY AQYQASSFQE SLQEEKESED EESEEPDSTT GTPPSSAPDP
KNHHIIKFGT NIDLSDAKRW KPQLQELLKL PAFMRVTSTG NMLSHVGHTI LGMNTVQLYM
KVPGSRTPGH QENNNFCSVN INIGPGDCEW FAVHEHYWET ISAFCDRHGV DYLTGSWWPI
LDDLYASNIP VYRFVQRPGD LVWINAGTVH WVQATGWCNN IAWNVGPLTA YQYQLALERY
EWNEVKNVKS IVPMIHVSWN VARTVKISDP DLFKMIKFCL LQSMKHCQVQ RESLVRAGKK
IAYQGRVKDE PAYYCNECDV EVFNILFVTS ENGSRNTYLV HCEGCARRRS AGLQGVVVLE
QYRTEELAQA YDAFTLAPAS TSR
