KDM4A_MOUSE
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 03-AUG-2022, entry version 156.
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 iPTMnet; Q8BW72; -.
DR PhosphoSitePlus; Q8BW72; -.
DR EPD; Q8BW72; -.
DR jPOST; Q8BW72; -.
DR MaxQB; Q8BW72; -.
DR PaxDb; Q8BW72; -.
DR PeptideAtlas; Q8BW72; -.
DR PRIDE; Q8BW72; -.
DR ProteomicsDB; 264987; -. [Q8BW72-1]
DR ProteomicsDB; 264988; -. [Q8BW72-2]
DR DNASU; 230674; -.
DR Ensembl; ENSMUST00000097911; ENSMUSP00000095524; ENSMUSG00000033326. [Q8BW72-1]
DR Ensembl; ENSMUST00000106403; ENSMUSP00000102011; ENSMUSG00000033326. [Q8BW72-1]
DR Ensembl; ENSMUST00000106406; ENSMUSP00000102014; ENSMUSG00000033326. [Q8BW72-1]
DR GeneID; 230674; -.
DR KEGG; mmu:230674; -.
DR UCSC; uc008ujn.2; mouse. [Q8BW72-1]
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; AQQPPYC; -.
DR OrthoDB; 1186832at2759; -.
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 76 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 226 other tissues.
DR ExpressionAtlas; Q8BW72; baseline and differential.
DR Genevisible; Q8BW72; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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 H3-methyl-lysine-36 demethylase activity; ISO:MGI.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; ISO:MGI.
DR GO; GO:0140681; F:histone H3-tri/dimethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0140684; F:histone H3-tri/dimethyl-lysine-9 demethylase activity; IEA:UniProtKB-EC.
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:0014898; P:cardiac muscle hypertrophy in response to stress; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0016577; P:histone demethylation; ISO:MGI.
DR GO; GO:0070544; P:histone H3-K36 demethylation; ISO:MGI.
DR GO; GO:0033169; P:histone H3-K9 demethylation; ISO:MGI.
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:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:1900113; P:negative regulation of histone H3-K9 trimethylation; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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:0031667; P:response to nutrient levels; IEA:Ensembl.
DR CDD; cd04508; TUDOR; 2.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR040477; KDM4_Tudor_2.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF18104; Tudor_2; 2.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
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
