EHMT2_MOUSE
ID EHMT2_MOUSE Reviewed; 1263 AA.
AC Q9Z148; A2CG75; Q6PE08; Q8K4R6; Q8K4R7; Q9Z149;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Histone-lysine N-methyltransferase EHMT2;
DE EC=2.1.1.- {ECO:0000269|PubMed:11316813, ECO:0000269|PubMed:15774718};
DE EC=2.1.1.367 {ECO:0000269|PubMed:11316813, ECO:0000269|PubMed:15774718};
DE AltName: Full=Euchromatic histone-lysine N-methyltransferase 2;
DE AltName: Full=HLA-B-associated transcript 8;
DE AltName: Full=Histone H3-K9 methyltransferase 3;
DE Short=H3-K9-HMTase 3;
DE AltName: Full=Protein G9a;
GN Name=Ehmt2; Synonyms=Bat8, G9a, Ng36;
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 [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF
RP 1165-ASN--CYS-1168, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12130538; DOI=10.1101/gad.989402;
RA Tachibana M., Sugimoto K., Nozaki M., Ueda J., Ohta T., Ohki M., Fukuda M.,
RA Takeda N., Niida H., Kato H., Shinkai Y.;
RT "G9a histone methyltransferase plays a dominant role in euchromatic histone
RT H3 lysine 9 methylation and is essential for early embryogenesis.";
RL Genes Dev. 16:1779-1791(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
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 3).
RC TISSUE=Mammary tumor;
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 ALTERNATIVE SPLICING (ISOFORM 2).
RX PubMed=11707778; DOI=10.1007/s00335-001-3029-3;
RA Brown S.E., Campbell R.D., Sanderson C.M.;
RT "Novel NG36/G9a gene products encoded within the human and mouse MHC class
RT III regions.";
RL Mamm. Genome 12:916-924(2001).
RN [6]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-1162.
RX PubMed=11316813; DOI=10.1074/jbc.m101914200;
RA Tachibana M., Sugimoto K., Fukushima T., Shinkai Y.;
RT "Set domain-containing protein, G9a, is a novel lysine-preferring mammalian
RT histone methyltransferase with hyperactivity and specific selectivity to
RT lysines 9 and 27 of histone H3.";
RL J. Biol. Chem. 276:25309-25317(2001).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH EHMT1,
RP AND TISSUE SPECIFICITY.
RX PubMed=15774718; DOI=10.1101/gad.1284005;
RA Tachibana M., Ueda J., Fukuda M., Takeda N., Ohta T., Iwanari H.,
RA Sakihama T., Kodama T., Hamakubo T., Shinkai Y.;
RT "Histone methyltransferases G9a and GLP form heteromeric complexes and are
RT both crucial for methylation of euchromatin at H3-K9.";
RL Genes Dev. 19:815-826(2005).
RN [8]
RP INTERACTION WITH WIZ AND EHMT1.
RX PubMed=16702210; DOI=10.1074/jbc.m603087200;
RA Ueda J., Tachibana M., Ikura T., Shinkai Y.;
RT "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the
RT co-repressor molecule CtBP.";
RL J. Biol. Chem. 281:20120-20128(2006).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF TYR-1120; 1165-ASN--CYS-1168;
RP 1165-ASN-HIS-1166; CYS-1168 AND TYR-1207.
RX PubMed=18818694; DOI=10.1038/emboj.2008.192;
RA Tachibana M., Matsumura Y., Fukuda M., Kimura H., Shinkai Y.;
RT "G9a/GLP complexes independently mediate H3K9 and DNA methylation to
RT silence transcription.";
RL EMBO J. 27:2681-2690(2008).
RN [10]
RP INTERACTION WITH UHRF1.
RX PubMed=19056828; DOI=10.1093/nar/gkn961;
RA Kim J.K., Esteve P.O., Jacobsen S.E., Pradhan S.;
RT "UHRF1 binds G9a and participates in p21 transcriptional regulation in
RT mammalian cells.";
RL Nucleic Acids Res. 37:493-505(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193; SER-465 AND SER-466, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP FUNCTION.
RX PubMed=22387026; DOI=10.1016/j.molcel.2012.01.019;
RA Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A., Carey M.F.,
RA Grunstein M.;
RT "Histone H3 lysine 56 methylation regulates DNA replication through its
RT interaction with PCNA.";
RL Mol. Cell 46:7-17(2012).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-40, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [14]
RP INTERACTION WITH SMYD5.
RX PubMed=28250819; DOI=10.1186/s13072-017-0115-7;
RA Kidder B.L., Hu G., Cui K., Zhao K.;
RT "SMYD5 regulates H4K20me3-marked heterochromatin to safeguard ES cell self-
RT renewal and prevent spurious differentiation.";
RL Epigenetics Chromatin 10:8-8(2017).
RN [15]
RP INTERACTION WITH PRDM9 AND CDYL.
RX PubMed=27932493; DOI=10.1091/mbc.e16-09-0686;
RA Parvanov E.D., Tian H., Billings T., Saxl R.L., Spruce C., Aithal R.,
RA Krejci L., Paigen K., Petkov P.M.;
RT "PRDM9 interactions with other proteins provide a link between
RT recombination hotspots and the chromosomal axis in meiosis.";
RL Mol. Biol. Cell 28:488-499(2017).
CC -!- FUNCTION: Histone methyltransferase that specifically mono- and
CC dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively)
CC in euchromatin. H3K9me represents a specific tag for epigenetic
CC transcriptional repression by recruiting HP1 proteins to methylated
CC histones. Also mediates monomethylation of 'Lys-56' of histone H3
CC (H3K56me1) in G1 phase, leading to promote interaction between histone
CC H3 and PCNA and regulating DNA replication. Also weakly methylates
CC 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation,
CC the histone methyltransferase activity is not required for DNA
CC methylation, suggesting that these 2 activities function independently.
CC Probably targeted to histone H3 by different DNA-binding proteins like
CC E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition
CC to the histone methyltransferase activity, also methylates non-histone
CC proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also
CC methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself.
CC {ECO:0000269|PubMed:12130538, ECO:0000269|PubMed:15774718,
CC ECO:0000269|PubMed:18818694, ECO:0000269|PubMed:22387026}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60284, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000269|PubMed:11316813, ECO:0000269|PubMed:15774718};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.367;
CC Evidence={ECO:0000269|PubMed:11316813, ECO:0000269|PubMed:15774718};
CC -!- SUBUNIT: Heterodimer; heterodimerizes with EHMT1/GLP (PubMed:15774718,
CC PubMed:16702210). Interacts with GFI1B and WIZ (PubMed:16702210). Part
CC of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX,
CC TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR, L3MBTL2 and YAF2 (By
CC similarity). Part of a complex composed of TRIM28, HDAC1, HDAC2 and
CC EHMT2. Interacts with UHRF1 (PubMed:19056828). Interacts with CDYL.
CC Interacts with REST only in the presence of CDYL. Part of a complex
CC containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2 (By
CC similarity). Interacts with PRDM9 and CDYL; interaction only takes
CC place when PRDM9 is bound to hotspot DNA (PubMed:27932493). Interacts
CC with SMYD5 (PubMed:28250819). {ECO:0000250|UniProtKB:Q96KQ7,
CC ECO:0000269|PubMed:15774718, ECO:0000269|PubMed:16702210,
CC ECO:0000269|PubMed:19056828, ECO:0000269|PubMed:27932493,
CC ECO:0000269|PubMed:28250819}.
CC -!- INTERACTION:
CC Q9Z148; O70237: Gfi1b; NbExp=2; IntAct=EBI-444966, EBI-4287943;
CC Q9Z148; P09631: Hoxa9; NbExp=2; IntAct=EBI-444966, EBI-925334;
CC Q9Z148-1; Q07279: Nfe2; NbExp=4; IntAct=EBI-444981, EBI-6554737;
CC Q9Z148-2; O88508-1: Dnmt3a; NbExp=3; IntAct=EBI-15737169, EBI-15650457;
CC Q9Z148-2; O88509: Dnmt3b; NbExp=3; IntAct=EBI-15737169, EBI-7987547;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000305}. Note=Almost
CC excluded form nucleoli. Associates with euchromatic regions. Does not
CC associate with heterochromatin. Part of a complex composed of TRIM28,
CC HDAC1, HDAC2 and EHMT2 (By similarity). Interacts with CDYL. Interacts
CC with REST only in the presence of CDYL. Part of a complex containing at
CC least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2 (By similarity).
CC Interacts with UHRF1. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=G9a-L;
CC IsoId=Q9Z148-1; Sequence=Displayed;
CC Name=2; Synonyms=G9a-S;
CC IsoId=Q9Z148-2; Sequence=VSP_002214, VSP_002215, VSP_002216;
CC Name=3;
CC IsoId=Q9Z148-3; Sequence=VSP_002214, VSP_002215;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15774718}.
CC -!- DOMAIN: The ANK repeats bind H3K9me1 and H3K9me2. {ECO:0000250}.
CC -!- DOMAIN: The SET domain mediates interaction with WIZ.
CC -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are
CC arranged in a triangular cluster; some of these Cys residues contribute
CC to the binding of two zinc ions within the cluster. {ECO:0000250}.
CC -!- PTM: Methylated at Lys-239; automethylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice show a higher level of histone H3 with
CC acetylated 'Lys-9' (H3K9ac) and/or methylated 'Lys-4' (H3K4me), display
CC severe developmental defects and die within E9.5-E12.5 stages.
CC {ECO:0000269|PubMed:12130538}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- CAUTION: NG36 and G9a were originally thought to derive from two
CC separate genes. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC84164.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC84165.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAH25539.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH58357.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF109906; AAC84164.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF109906; AAC84165.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB077209; BAC05482.1; -; mRNA.
DR EMBL; AB077210; BAC05483.1; -; mRNA.
DR EMBL; CT025759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025539; AAH25539.1; ALT_INIT; mRNA.
DR EMBL; BC058357; AAH58357.1; ALT_INIT; mRNA.
DR CCDS; CCDS28666.1; -. [Q9Z148-2]
DR CCDS; CCDS28667.1; -. [Q9Z148-1]
DR CCDS; CCDS70797.1; -. [Q9Z148-3]
DR RefSeq; NP_001273502.1; NM_001286573.1.
DR RefSeq; NP_001273504.1; NM_001286575.1. [Q9Z148-3]
DR RefSeq; NP_665829.1; NM_145830.2. [Q9Z148-1]
DR RefSeq; NP_671493.1; NM_147151.2. [Q9Z148-2]
DR AlphaFoldDB; Q9Z148; -.
DR SMR; Q9Z148; -.
DR BioGRID; 225335; 60.
DR CORUM; Q9Z148; -.
DR DIP; DIP-31916N; -.
DR IntAct; Q9Z148; 16.
DR MINT; Q9Z148; -.
DR STRING; 10090.ENSMUSP00000013931; -.
DR BindingDB; Q9Z148; -.
DR ChEMBL; CHEMBL2169718; -.
DR iPTMnet; Q9Z148; -.
DR PhosphoSitePlus; Q9Z148; -.
DR EPD; Q9Z148; -.
DR jPOST; Q9Z148; -.
DR MaxQB; Q9Z148; -.
DR PaxDb; Q9Z148; -.
DR PeptideAtlas; Q9Z148; -.
DR PRIDE; Q9Z148; -.
DR ProteomicsDB; 277573; -. [Q9Z148-1]
DR ProteomicsDB; 277574; -. [Q9Z148-2]
DR ProteomicsDB; 277575; -. [Q9Z148-3]
DR Antibodypedia; 27888; 371 antibodies from 39 providers.
DR DNASU; 110147; -.
DR Ensembl; ENSMUST00000013931; ENSMUSP00000013931; ENSMUSG00000013787. [Q9Z148-1]
DR Ensembl; ENSMUST00000078061; ENSMUSP00000077208; ENSMUSG00000013787. [Q9Z148-2]
DR Ensembl; ENSMUST00000114033; ENSMUSP00000109667; ENSMUSG00000013787. [Q9Z148-3]
DR GeneID; 110147; -.
DR KEGG; mmu:110147; -.
DR UCSC; uc008ceb.3; mouse. [Q9Z148-2]
DR UCSC; uc008cec.3; mouse. [Q9Z148-3]
DR UCSC; uc008ced.3; mouse. [Q9Z148-1]
DR CTD; 10919; -.
DR MGI; MGI:2148922; Ehmt2.
DR VEuPathDB; HostDB:ENSMUSG00000013787; -.
DR eggNOG; KOG1082; Eukaryota.
DR GeneTree; ENSGT00940000159459; -.
DR HOGENOM; CLU_005790_0_0_1; -.
DR InParanoid; Q9Z148; -.
DR OMA; DSWLEDA; -.
DR OrthoDB; 753093at2759; -.
DR PhylomeDB; Q9Z148; -.
DR TreeFam; TF106443; -.
DR BRENDA; 1.21.99.4; 3474.
DR BRENDA; 2.1.1.355; 3474.
DR BRENDA; 2.1.1.368; 3474.
DR Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR BioGRID-ORCS; 110147; 9 hits in 77 CRISPR screens.
DR ChiTaRS; Ehmt2; mouse.
DR PRO; PR:Q9Z148; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9Z148; protein.
DR Bgee; ENSMUSG00000013787; Expressed in gonadal ridge and 261 other tissues.
DR ExpressionAtlas; Q9Z148; baseline and differential.
DR Genevisible; Q9Z148; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB.
DR GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IDA:UniProtKB.
DR GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:UniProtKB.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:MGI.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
DR GO; GO:0071314; P:cellular response to cocaine; IDA:MGI.
DR GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006306; P:DNA methylation; IDA:UniProtKB.
DR GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IMP:MGI.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0070734; P:histone H3-K27 methylation; IMP:MGI.
DR GO; GO:0051567; P:histone H3-K9 methylation; IMP:MGI.
DR GO; GO:0034968; P:histone lysine methylation; ISO:MGI.
DR GO; GO:0016571; P:histone methylation; IMP:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISO:MGI.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0048665; P:neuron fate specification; IMP:MGI.
DR GO; GO:0048599; P:oocyte development; IMP:MGI.
DR GO; GO:0035265; P:organ growth; IMP:MGI.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; ISS:UniProtKB.
DR GO; GO:0036166; P:phenotypic switching; IMP:MGI.
DR GO; GO:0044030; P:regulation of DNA methylation; ISO:MGI.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; ISO:MGI.
DR GO; GO:0051570; P:regulation of histone H3-K9 methylation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0060992; P:response to fungicide; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR043550; EHMT1/EHMT2.
DR InterPro; IPR038034; EHMT2.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR46307; PTHR46307; 1.
DR PANTHER; PTHR46307:SF1; PTHR46307:SF1; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Chromatin regulator; Chromosome;
KW Isopeptide bond; Metal-binding; Methylation; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW Transferase; Ubl conjugation; Zinc.
FT CHAIN 1..1263
FT /note="Histone-lysine N-methyltransferase EHMT2"
FT /id="PRO_0000186069"
FT REPEAT 702..731
FT /note="ANK 1"
FT REPEAT 737..766
FT /note="ANK 2"
FT REPEAT 770..799
FT /note="ANK 3"
FT REPEAT 803..833
FT /note="ANK 4"
FT REPEAT 837..866
FT /note="ANK 5"
FT REPEAT 870..899
FT /note="ANK 6"
FT REPEAT 903..932
FT /note="ANK 7"
FT DOMAIN 1025..1088
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 1091..1208
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1217..1233
FT /note="Post-SET"
FT REGION 1..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..872
FT /note="Histone H3K9me binding"
FT /evidence="ECO:0000250"
FT REGION 1127..1146
FT /note="Interaction with histone H3"
FT /evidence="ECO:0000250"
FT REGION 1207..1210
FT /note="Interaction with histone H3"
FT /evidence="ECO:0000250"
FT COMPBIAS 256..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..381
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..418
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1027
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1027
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1029
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1033
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1033
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1038
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1040
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1070
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1070
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1074
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1076
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1080
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1101..1103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 1138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 1165..1166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 1168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 1221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 1223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 1228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT SITE 1120
FT /note="Histone H3K9me binding"
FT /evidence="ECO:0000250"
FT MOD_RES 40
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 239
FT /note="N6,N6,N6-trimethyllysine; by EHMT2; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT MOD_RES 239
FT /note="N6,N6-dimethyllysine; by EHMT2; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 608
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT MOD_RES 1257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT MOD_RES 1263
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT CROSSLNK 272
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT CROSSLNK 282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT CROSSLNK 687
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96KQ7"
FT VAR_SEQ 1..57
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12130538,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_002214"
FT VAR_SEQ 58..71
FT /note="AGLTGPPVPCLPSQ -> MAAAAGAAAAAAAE (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:12130538,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_002215"
FT VAR_SEQ 426..459
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12130538"
FT /id="VSP_002216"
FT MUTAGEN 1120
FT /note="Y->V: In GM7; defective in methyltransferase
FT activity without affecting DNA methylation; when associated
FT with F-1207."
FT /evidence="ECO:0000269|PubMed:18818694"
FT MUTAGEN 1162
FT /note="R->H: Strongly reduces histone methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:11316813"
FT MUTAGEN 1165..1168
FT /note="Missing: Abolishes histone methyltransferase
FT activity and subsequent repression. In GM3; does not form
FT heterodimer with EHMT1 and is defective in mediating both
FT H3K9me and DNA methylation."
FT /evidence="ECO:0000269|PubMed:12130538,
FT ECO:0000269|PubMed:18818694"
FT MUTAGEN 1165..1166
FT /note="NH->LE: In GM6; does not form heterodimer with EHMT1
FT and is defective in mediating H3K9me."
FT /evidence="ECO:0000269|PubMed:18818694"
FT MUTAGEN 1168
FT /note="C->A: In GM4; defective in methyltransferase
FT activity without affecting DNA methylation."
FT /evidence="ECO:0000269|PubMed:18818694"
FT MUTAGEN 1207
FT /note="Y->F: In GM7; defective in methyltransferase
FT activity without affecting DNA methylation; when associated
FT with V-1120."
FT /evidence="ECO:0000269|PubMed:18818694"
SQ SEQUENCE 1263 AA; 138039 MW; 74DBFF9A36769589 CRC64;
MRGLPRGRGL MRARGRGRAA PTGGRGRGRG GAHRGRGRPR SLLSLPRAQA SWAPQLPAGL
TGPPVPCLPS QGEAPAEMGA LLLEKEPRGA AERVHSSLGD TPQSEETLPK ANPDSLEPAG
PSSPASVTVT VGDEGADTPV GAASLIGDEP ESLEGDGGRI VLGHATKSFP SSPSKGGACP
SRAKMSMTGA GKSPPSVQSL AMRLLSMPGA QGAATAGPEP SPATTAAQEG QPKVHRARKT
MSKPSNGQPP IPEKRPPEVQ HFRMSDDMHL GKVTSDVAKR RKLNSGSLSE DLGSAGGSGD
IILEKGEPRP LEEWETVVGD DFSLYYDAYS VDERVDSDSK SEVEALAEQL SEEEEEEEEE
EEEEEEEEEE EEEEEEDEES GNQSDRSGSS GRRKAKKKWR KDSPWVKPSR KRRKREPPRA
KEPRGVNGVG SSGPSEYMEV PLGSLELPSE GTLSPNHAGV SNDTSSLETE RGFEELPLCS
CRMEAPKIDR ISERAGHKCM ATESVDGELL GCNAAILKRE TMRPSSRVAL MVLCEAHRAR
MVKHHCCPGC GYFCTAGTFL ECHPDFRVAH RFHKACVSQL NGMVFCPHCG EDASEAQEVT
IPRGDGGTPP IGTAAPALPP LAHDAPGRAD TSQPSARMRG HGEPRRPPCD PLADTIDSSG
PSLTLPNGGC LSAVGLPPGP GREALEKALV IQESERRKKL RFHPRQLYLS VKQGELQKVI
LMLLDNLDPN FQSDQQSKRT PLHAAAQKGS VEICHVLLQA GANINAVDKQ QRTPLMEAVV
NNHLEVARYM VQLGGCVYSK EEDGSTCLHH AAKIGNLEMV SLLLSTGQVD VNAQDSGGWT
PIIWAAEHKH IDVIRMLLTR GADVTLTDNE ENICLHWASF TGSAAIAEVL LNAQCDLHAV
NYHGDTPLHI AARESYHDCV LLFLSRGANP ELRNKEGDTA WDLTPERSDV WFALQLNRKL
RLGVGNRAVR TEKIICRDVA RGYENVPIPC VNGVDGEPCP EDYKYISENC ETSTMNIDRN
ITHLQHCTCV DDCSSSNCLC GQLSIRCWYD KDGRLLQEFN KIEPPLIFEC NQACSCWRSC
KNRVVQSGIK VRLQLYRTAK MGWGVRALQT IPQGTFICEY VGELISDAEA DVREDDSYLF
DLDNKDGEVY CIDARYYGNI SRFINHLCDP NIIPVRVFML HQDLRFPRIA FFSSRDIRTG
EELGFDYGDR FWDIKSKYFT CQCGSEKCKH SAEAIALEQS RLARLDPHPE LLPDLSSLPP
INT
