ID   KDM4A_MOUSE             Reviewed;        1064 AA.
AC   Q8BW72; A2A8L8; Q3UKM5; Q3UM81; Q3UWV2; Q6ZQ72; Q8K137;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   24-JAN-2024, entry version 164.
DE   RecName: Full=Lysine-specific demethylase 4A;
DE            EC=1.14.11.66 {ECO:0000250|UniProtKB:O75164};
DE            EC=1.14.11.69 {ECO:0000250|UniProtKB:O75164};
DE   AltName: Full=JmjC domain-containing histone demethylation protein 3A;
DE   AltName: Full=Jumonji domain-containing protein 2A;
DE   AltName: Full=[histone H3]-trimethyl-L-lysine(36) demethylase 4A {ECO:0000305};
DE   AltName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase 4A {ECO:0000305};
GN   Name=Kdm4a; Synonyms=Jhdm3a, Jmjd2, Jmjd2a, Kiaa0677;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Mammary gland, Oviduct, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Colon;
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   PROTEIN SEQUENCE OF 499-505, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=16024779; DOI=10.1128/mcb.25.15.6404-6414.2005;
RA   Zhang D., Yoon H.-G., Wong J.;
RT   "JMJD2A is a novel N-CoR-interacting protein and is involved in repression
RT   of the human transcription factor achaete scute-like homologue 2
RT   (ASCL2/Hash2).";
RL   Mol. Cell. Biol. 25:6404-6414(2005).
RN   [7]
RP   FUNCTION.
RX   PubMed=24953653; DOI=10.1016/j.celrep.2014.05.041;
RA   Cardamone M.D., Tanasa B., Chan M., Cederquist C.T., Andricovich J.,
RA   Rosenfeld M.G., Perissi V.;
RT   "GPS2/KDM4A pioneering activity regulates promoter-specific recruitment of
RT   PPARgamma.";
RL   Cell Rep. 8:163-176(2014).
CC   -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-9'
CC       and 'Lys-36' residues of histone H3, thereby playing a central role in
CC       histone code (PubMed:24953653). Does not demethylate histone H3 'Lys-
CC       4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9'
CC       and H3 'Lys-36' residue, while it has no activity on mono- and
CC       dimethylated residues. Demethylation of Lys residue generates
CC       formaldehyde and succinate. Participates in transcriptional repression
CC       of ASCL2 and E2F-responsive promoters via the recruitment of histone
CC       deacetylases and NCOR1, respectively (By similarity).
CC       {ECO:0000250|UniProtKB:O75164, ECO:0000269|PubMed:24953653}.
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:0000250|UniProtKB:O75164};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-
CC         [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC         lysyl(36)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60236,
CC         Rhea:RHEA-COMP:9786, Rhea:RHEA-COMP:15536, 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=1.14.11.69; Evidence={ECO:0000250|UniProtKB:O75164};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:O75164};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:O75164};
CC   -!- SUBUNIT: Interacts with histone deacetylase proteins HDAC1, HDAC2 and
CC       HDAC3. Interacts with RB and NCOR1 (By similarity).
CC       {ECO:0000250|UniProtKB:O75164}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BW72-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BW72-2; Sequence=VSP_016144, VSP_016145;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16024779}.
CC   -!- DOMAIN: The 2 Tudor domains recognize and bind methylated histone H3
CC       'Lys-4' residue (H3K4me). Double Tudor domain has an interdigitated
CC       structure and the unusual fold is required for its ability to bind
CC       methylated histone tails. Trimethylated H3 'Lys-4' (H3K4me3) is bound
CC       in a cage of 3 aromatic residues, 2 of which are from the Tudor domain
CC       2, while the binding specificity is determined by side-chain
CC       interactions involving residues from the Tudor domain 1. The Tudor
CC       domains are also able to bind trimethylated histone H3 'Lys-9'
CC       (H3K9me3), di- and trimethylated H4 'Lys-20' (H4K20me2 and H4K20me3).
CC       Has high affinity for H4K20me2, blocking recruitment of proteins such
CC       as TP53BP1 (By similarity). {ECO:0000250|UniProtKB:O75164}.
CC   -!- PTM: Ubiquitinated by RNF8 and RNF168, leading to its degradation
CC       (PubMed:24953653). Degradation promotes accessibility of H4K20me2 mark
CC       for DNA repair protein TP53BP1, which is then recruited (By
CC       similarity). {ECO:0000250|UniProtKB:O75164,
CC       ECO:0000269|PubMed:24953653}.
CC   -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97997.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK129187; BAC97997.1; ALT_INIT; mRNA.
DR   EMBL; AK054095; BAC35653.1; -; mRNA.
DR   EMBL; AK136085; BAE22812.1; -; mRNA.
DR   EMBL; AK145066; BAE26217.1; -; mRNA.
DR   EMBL; AK145947; BAE26776.1; -; mRNA.
DR   EMBL; AL626764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC028866; AAH28866.1; -; mRNA.
DR   CCDS; CCDS51282.1; -. [Q8BW72-1]
DR   RefSeq; NP_001155295.1; NM_001161823.1. [Q8BW72-1]
DR   RefSeq; NP_759014.2; NM_172382.2.
DR   RefSeq; XP_006503073.1; XM_006503010.2. [Q8BW72-1]
DR   AlphaFoldDB; Q8BW72; -.
DR   SMR; Q8BW72; -.
DR   BioGRID; 230999; 4.
DR   IntAct; Q8BW72; 1.
DR   STRING; 10090.ENSMUSP00000102014; -.
DR   GlyGen; Q8BW72; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BW72; -.
DR   PhosphoSitePlus; Q8BW72; -.
DR   EPD; Q8BW72; -.
DR   jPOST; Q8BW72; -.
DR   MaxQB; Q8BW72; -.
DR   PaxDb; 10090-ENSMUSP00000102014; -.
DR   PeptideAtlas; Q8BW72; -.
DR   ProteomicsDB; 264987; -. [Q8BW72-1]
DR   ProteomicsDB; 264988; -. [Q8BW72-2]
DR   Pumba; Q8BW72; -.
DR   DNASU; 230674; -.
DR   Ensembl; ENSMUST00000097911.9; ENSMUSP00000095524.3; ENSMUSG00000033326.16. [Q8BW72-1]
DR   Ensembl; ENSMUST00000106403.8; ENSMUSP00000102011.2; ENSMUSG00000033326.16. [Q8BW72-1]
DR   Ensembl; ENSMUST00000106406.9; ENSMUSP00000102014.3; ENSMUSG00000033326.16. [Q8BW72-1]
DR   GeneID; 230674; -.
DR   KEGG; mmu:230674; -.
DR   UCSC; uc008ujn.2; mouse. [Q8BW72-1]
DR   AGR; MGI:2446210; -.
DR   CTD; 9682; -.
DR   MGI; MGI:2446210; Kdm4a.
DR   VEuPathDB; HostDB:ENSMUSG00000033326; -.
DR   eggNOG; KOG0958; Eukaryota.
DR   GeneTree; ENSGT00940000159643; -.
DR   HOGENOM; CLU_001442_0_1_1; -.
DR   InParanoid; Q8BW72; -.
DR   OMA; SGQYDMT; -.
DR   OrthoDB; 48111at2759; -.
DR   PhylomeDB; Q8BW72; -.
DR   TreeFam; TF106449; -.
DR   BRENDA; 1.14.11.66; 3474.
DR   BRENDA; 1.14.11.69; 3474.
DR   Reactome; R-MMU-3214842; HDMs demethylate histones.
DR   Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   BioGRID-ORCS; 230674; 8 hits in 82 CRISPR screens.
DR   ChiTaRS; Kdm4a; mouse.
DR   PRO; PR:Q8BW72; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8BW72; Protein.
DR   Bgee; ENSMUSG00000033326; Expressed in manus and 227 other cell types or tissues.
DR   ExpressionAtlas; Q8BW72; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005721; C:pericentric heterochromatin; IDA:MGI.
DR   GO; GO:0032452; F:histone demethylase activity; IDA:MGI.
DR   GO; GO:0051864; F:histone H3K36 demethylase activity; ISO:MGI.
DR   GO; GO:0140681; F:histone H3K36me2/H3K36me3 demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032454; F:histone H3K9 demethylase activity; IDA:MGI.
DR   GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; ISO:MGI.
DR   GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR   GO; GO:0030263; P:apoptotic chromosome condensation; ISO:MGI.
DR   GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IMP:MGI.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0048712; P:negative regulation of astrocyte differentiation; ISO:MGI.
DR   GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR   CDD; cd15713; ePHD_JMJD2A; 1.
DR   CDD; cd20463; Tudor_JMJD2A_rpt1; 1.
DR   CDD; cd20466; Tudor_JMJD2A_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; IPR047482; JMJD2A_ePHD.
DR   InterPro; IPR003349; JmjN.
DR   InterPro; IPR040477; KDM4-like_Tudor.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR047479; Tudor_KDM4A_rpt1.
DR   InterPro; IPR047481; Tudor_KDM4A_rpt2.
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:SF119; LYSINE-SPECIFIC DEMETHYLASE 4A; 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.
DR   Genevisible; Q8BW72; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromatin regulator; Dioxygenase;
KW   Direct protein sequencing; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O75164"
FT   CHAIN           2..1064
FT                   /note="Lysine-specific demethylase 4A"
FT                   /id="PRO_0000183173"
FT   DOMAIN          14..56
FT                   /note="JmjN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT   DOMAIN          142..308
FT                   /note="JmjC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   DOMAIN          897..954
FT                   /note="Tudor 1"
FT   DOMAIN          955..1011
FT                   /note="Tudor 2"
FT   ZN_FING         709..767
FT                   /note="PHD-type 1"
FT   ZN_FING         772..805
FT                   /note="C2HC pre-PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT   ZN_FING         828..885
FT                   /note="PHD-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT   REGION          354..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          597..638
FT                   /note="Interaction with NCOR1"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        503..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..571
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         132
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:O75164"
FT   BINDING         188
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         190
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         198
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:O75164"
FT   BINDING         206
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:O75164"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O75164"
FT   BINDING         240
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O75164"
FT   BINDING         241
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT   BINDING         276
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O75164"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O75164"
FT   SITE            945
FT                   /note="Histone H3K4me3 binding"
FT                   /evidence="ECO:0000250"
FT   SITE            967
FT                   /note="Histone H3K4me3 binding"
FT                   /evidence="ECO:0000250"
FT   SITE            973
FT                   /note="Histone H3K4me3 binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O75164"
FT   MOD_RES         523
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75164"
FT   VAR_SEQ         948..1033
FT                   /note="SQDCLQLGPPAEGEVVQVRWTDGQVYGAKFVASHPIQMYQVEFEDGSQLVVK
FT                   RDDVYTLDEELPKRVKSRLSVASDMRFNEIFTEK -> MSESGFWQHFGSSGTSSCYCR
FT                   LDDCGLFACPWSVSKQKEPLFPGSLSRKSGHAGALSFPEEFRGVSVPCSPLKYAYISDQ
FT                   IISNSI (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016144"
FT   VAR_SEQ         1034..1064
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016145"
FT   CONFLICT        339
FT                   /note="M -> T (in Ref. 1; BAC97997, 2; BAE26217 and 4;
FT                   AAH28866)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1007
FT                   /note="D -> G (in Ref. 2; BAE26776)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1064 AA;  120334 MW;  92FB3E363FDF9E7D CRC64;
     MASESETLNP SARIMTFYPT MEEFRNFSRY IAYIESQGAH RAGLAKVVPP KEWKPRTSYD
     DIDDLVIPAP IQQLVTGQSG LFTQYNIQKK AMTVREFRKI ANSDKYCTPR YSEFEELERK
     YWKNLTFNPP IYGADVNGTL YEQHVDEWNI GRLKTILDLV EKESGITIEG VNTPYLYFGM
     WKTSFAWHTE DMDLYSINYL HFGEPKSWYS VPPEHGKRLE RLAKGFFPGS AQSCEAFLRH
     KMTLISPLML KKYGIPFDKV TQEAGEFMIT FPYGYHAGFN HGFNCAESTN FATRRWIEYG
     KQAVLCSCRK DMVKISMDVF VRRFQPERYK LWKAGKDSMV IDHTLPTPEA AEFLKDSGGL
     TPRAGSEECP EEDVEAADQG EEGDVKRSLA KHRIGTKRHR VCLEIPQEVS QSELFPKEEL
     SSGQYEMTEC PATLAPVRPT HSSVRQVEDS LPFPDYSDPT EVKFEELKNV KLEEEDEEDE
     PEAAALDLSV NPASVGGRLV FSGSKKKSSS SLGSTSSQDS VSSDSETAES VSCQGQEKTG
     VLTVHSYARG DGKAATGEPS VKKKRSAPRS ISEQELAEVA DEYMLSLEEN KKTKGRRQPL
     SKLPRHHPLV LQECGSDDET SEQLTPEEEA EETEAWAKPL SQLWQNRPPN FEAEKEFNEI
     MAQQAPHCAV CMIFQTYHQV EFGAFSQSCG DASEPAAQTQ RTKPLIPEMC FTTTGCSTDI
     NLSTPYLEED GTSMLVSCKK CSVRVHASCY GVPPAKASEE WMCSRCSANA LEEDCCLCSL
     RGGALQRAND DRWVHVSCAV AILEARFVNI AERSPVDVSK IPLPRFKLKC VFCKKRRKRN
     AGCCVQCSHG RCPTAFHVSC AQAAGVMMQP DDWPFVVFIT CFRHKIPNLE RAKGALLSIT
     AGQKVISKHK NGRFYQCEVV RLTTETFYEV NFDDGSFSDN LYPEDIVSQD CLQLGPPAEG
     EVVQVRWTDG QVYGAKFVAS HPIQMYQVEF EDGSQLVVKR DDVYTLDEEL PKRVKSRLSV
     ASDMRFNEIF TEKEVKQEKK RQRVINSRYR EDYIEPALYR AIME
//