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Database: UniProt
Entry: Q9Z148
LinkDB: Q9Z148
Original site: Q9Z148 
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   13-FEB-2019, entry version 181.
DE   RecName: Full=Histone-lysine N-methyltransferase EHMT2;
DE            EC=2.1.1.-;
DE            EC=2.1.1.43;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Fukuda M., Takeda N., Niida H., Kato H., Shinkai Y.;
RT   "G9a histone methyltransferase plays a dominant role in euchromatic
RT   histone H3 lysine 9 methylation and is essential for early
RT   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.,
RA   Campbell R.D., 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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
RT   class 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
RT   mammalian histone methyltransferase with hyperactivity and specific
RT   selectivity to 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
RP   EHMT1, 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
RT   are 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
RT   the 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
RP   SER-466, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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
RT   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.,
RA   Carey M.F., Grunstein M.;
RT   "Histone H3 lysine 56 methylation regulates DNA replication through
RT   its interaction with PCNA.";
RL   Mol. Cell 46:7-17(2012).
RN   [13]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-40, AND IDENTIFICATION BY
RP   MASS 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.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., 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).
CC   -!- FUNCTION: Histone methyltransferase that specifically mono- and
CC       dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2,
CC       respectively) in euchromatin. H3K9me represents a specific tag for
CC       epigenetic transcriptional repression by recruiting HP1 proteins
CC       to methylated histones. Also mediates monomethylation of 'Lys-56'
CC       of histone H3 (H3K56me1) in G1 phase, leading to promote
CC       interaction between histone H3 and PCNA and regulating DNA
CC       replication. Also weakly methylates 'Lys-27' of histone H3
CC       (H3K27me). Also required for DNA methylation, the histone
CC       methyltransferase activity is not required for DNA methylation,
CC       suggesting that these 2 activities function independently.
CC       Probably targeted to histone H3 by different DNA-binding proteins
CC       like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In
CC       addition to the histone methyltransferase activity, also
CC       methylates non-histone proteins: mediates dimethylation of 'Lys-
CC       373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1,
CC       ERCC6, KLF12 and itself. {ECO:0000269|PubMed:12130538,
CC       ECO:0000269|PubMed:15774718, ECO:0000269|PubMed:18818694,
CC       ECO:0000269|PubMed:22387026}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000269|PubMed:11316813,
CC         ECO:0000269|PubMed:15774718};
CC   -!- SUBUNIT: Part of the E2F6.com-1 complex in G0 phase composed of
CC       E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR,
CC       GFI1B, L3MBTL2 and YAF2 (By similarity). Heterodimer;
CC       heterodimerizes with EHMT1. Interacts with WIZ. {ECO:0000250,
CC       ECO:0000269|PubMed:15774718, ECO:0000269|PubMed:16702210,
CC       ECO:0000269|PubMed:19056828}.
CC   -!- INTERACTION:
CC       O88508-1:Dnmt3a; NbExp=3; IntAct=EBI-15737169, EBI-15650457;
CC       O88509:Dnmt3b; NbExp=3; IntAct=EBI-15737169, EBI-7987547;
CC       O70237:Gfi1b; NbExp=2; IntAct=EBI-444966, EBI-4287943;
CC       P09631:Hoxa9; NbExp=2; IntAct=EBI-444966, EBI-925334;
CC       Q07279:Nfe2; NbExp=4; IntAct=EBI-444981, EBI-6554737;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000305}.
CC       Note=Almost excluded form nucleoli. Associates with euchromatic
CC       regions. Does not associate with heterochromatin. Part of a
CC       complex composed of TRIM28, HDAC1, HDAC2 and EHMT2 (By
CC       similarity). Interacts with CDYL. Interacts with REST only in the
CC       presence of CDYL. Part of a complex containing at least CDYL,
CC       REST, WIZ, SETB1, EHMT1 and EHMT2 (By similarity). Interacts with
CC       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
CC       are arranged in a triangular cluster; some of these Cys residues
CC       contribute to the binding of two zinc ions within the cluster.
CC       {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),
CC       display severe developmental defects and die within E9.5-E12.5
CC       stages. {ECO:0000269|PubMed:12130538}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
CC       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=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=AAH58357.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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; CAM27791.1; -; 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   UniGene; Mm.35345; -.
DR   ProteinModelPortal; Q9Z148; -.
DR   SMR; Q9Z148; -.
DR   BioGrid; 225335; 52.
DR   CORUM; Q9Z148; -.
DR   DIP; DIP-31916N; -.
DR   IntAct; Q9Z148; 18.
DR   MINT; Q9Z148; -.
DR   STRING; 10090.ENSMUSP00000013931; -.
DR   BindingDB; Q9Z148; -.
DR   ChEMBL; CHEMBL2169718; -.
DR   iPTMnet; Q9Z148; -.
DR   PhosphoSitePlus; Q9Z148; -.
DR   jPOST; Q9Z148; -.
DR   PaxDb; Q9Z148; -.
DR   PeptideAtlas; Q9Z148; -.
DR   PRIDE; Q9Z148; -.
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   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG0666; LUCA.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000159459; -.
DR   HOGENOM; HOG000231216; -.
DR   HOVERGEN; HBG028394; -.
DR   InParanoid; Q9Z148; -.
DR   KO; K11420; -.
DR   OrthoDB; 753093at2759; -.
DR   PhylomeDB; Q9Z148; -.
DR   TreeFam; TF106443; -.
DR   BRENDA; 1.97.1.10; 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   ChiTaRS; Ehmt2; mouse.
DR   PRO; PR:Q9Z148; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   Bgee; ENSMUSG00000013787; Expressed in 314 organ(s), highest expression level in neocortex.
DR   ExpressionAtlas; Q9Z148; baseline and differential.
DR   Genevisible; Q9Z148; MM.
DR   GO; GO:0000790; C:nuclear 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 regulatory region sequence-specific DNA binding; IDA: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:0035690; P:cellular response to drug; ISO:MGI.
DR   GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
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:0007281; P:germ cell development; 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: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   CDD; cd00204; ANK; 2.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR038034; EHMT2.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   PANTHER; PTHR22884:SF361; PTHR22884:SF361; 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   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   Complete proteome; Isopeptide bond; Metal-binding; Methylation;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; S-adenosyl-L-methionine; Transferase; Ubl conjugation; Zinc.
FT   CHAIN         1   1263       Histone-lysine N-methyltransferase EHMT2.
FT                                /FTId=PRO_0000186069.
FT   REPEAT      702    731       ANK 1.
FT   REPEAT      737    766       ANK 2.
FT   REPEAT      770    799       ANK 3.
FT   REPEAT      803    833       ANK 4.
FT   REPEAT      837    866       ANK 5.
FT   REPEAT      870    899       ANK 6.
FT   REPEAT      903    932       ANK 7.
FT   DOMAIN     1025   1088       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN     1091   1208       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1217   1233       Post-SET.
FT   REGION      870    872       Histone H3K9me binding. {ECO:0000250}.
FT   REGION     1101   1103       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION     1127   1146       Interaction with histone H3.
FT                                {ECO:0000250}.
FT   REGION     1165   1166       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION     1207   1210       Interaction with histone H3.
FT                                {ECO:0000250}.
FT   COMPBIAS    352    379       Poly-Glu.
FT   METAL      1027   1027       Zinc 1. {ECO:0000250}.
FT   METAL      1027   1027       Zinc 2. {ECO:0000250}.
FT   METAL      1029   1029       Zinc 1. {ECO:0000250}.
FT   METAL      1033   1033       Zinc 1. {ECO:0000250}.
FT   METAL      1033   1033       Zinc 3. {ECO:0000250}.
FT   METAL      1038   1038       Zinc 1. {ECO:0000250}.
FT   METAL      1040   1040       Zinc 2. {ECO:0000250}.
FT   METAL      1070   1070       Zinc 2. {ECO:0000250}.
FT   METAL      1070   1070       Zinc 3. {ECO:0000250}.
FT   METAL      1074   1074       Zinc 2. {ECO:0000250}.
FT   METAL      1076   1076       Zinc 3. {ECO:0000250}.
FT   METAL      1080   1080       Zinc 3. {ECO:0000250}.
FT   METAL      1168   1168       Zinc 4. {ECO:0000250}.
FT   METAL      1221   1221       Zinc 4. {ECO:0000250}.
FT   METAL      1223   1223       Zinc 4. {ECO:0000250}.
FT   METAL      1228   1228       Zinc 4. {ECO:0000250}.
FT   BINDING    1120   1120       Histone H3K9me. {ECO:0000250}.
FT   BINDING    1138   1138       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   MOD_RES      40     40       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES      97     97       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   MOD_RES     101    101       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   MOD_RES     104    104       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   MOD_RES     193    193       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     239    239       N6,N6,N6-trimethyllysine; by EHMT2;
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   MOD_RES     239    239       N6,N6-dimethyllysine; by EHMT2;
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   MOD_RES     285    285       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   MOD_RES     294    294       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   MOD_RES     298    298       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   MOD_RES     403    403       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   MOD_RES     465    465       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     466    466       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     608    608       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   MOD_RES    1257   1257       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   MOD_RES    1263   1263       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   CROSSLNK    272    272       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   CROSSLNK    282    282       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   CROSSLNK    687    687       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q96KQ7}.
FT   VAR_SEQ       1     57       Missing (in isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:12130538,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_002214.
FT   VAR_SEQ      58     71       AGLTGPPVPCLPSQ -> MAAAAGAAAAAAAE (in
FT                                isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:12130538,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_002215.
FT   VAR_SEQ     426    459       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:12130538}.
FT                                /FTId=VSP_002216.
FT   MUTAGEN    1120   1120       Y->V: In GM7; defective in
FT                                methyltransferase activity without
FT                                affecting DNA methylation; when
FT                                associated with F-1207.
FT                                {ECO:0000269|PubMed:18818694}.
FT   MUTAGEN    1162   1162       R->H: Strongly reduces histone
FT                                methyltransferase activity.
FT                                {ECO:0000269|PubMed:11316813}.
FT   MUTAGEN    1165   1168       Missing: Abolishes histone
FT                                methyltransferase activity and subsequent
FT                                repression. {ECO:0000269|PubMed:12130538,
FT                                ECO:0000269|PubMed:18818694}.
FT   MUTAGEN    1165   1168       Missing: In GM3; does not form
FT                                heterodimer with EHMT1 and is defective
FT                                in mediating both H3K9me and DNA
FT                                methylation.
FT                                {ECO:0000269|PubMed:12130538,
FT                                ECO:0000269|PubMed:18818694}.
FT   MUTAGEN    1165   1166       NH->LE: In GM6; does not form heterodimer
FT                                with EHMT1 and is defective in mediating
FT                                H3K9me. {ECO:0000269|PubMed:18818694}.
FT   MUTAGEN    1168   1168       C->A: In GM4; defective in
FT                                methyltransferase activity without
FT                                affecting DNA methylation.
FT                                {ECO:0000269|PubMed:18818694}.
FT   MUTAGEN    1207   1207       Y->F: In GM7; defective in
FT                                methyltransferase activity without
FT                                affecting DNA methylation; when
FT                                associated with V-1120.
FT                                {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
//
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