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Histone-lysine N-methyltransferase EHMT2 (EC 2.1.1.-) (EC 2.1.1.43) (Euchromatic histone-lysine N-methyltransferase 2) (HLA-B-associated transcript 8) (Histone H3-K9 methyltransferase 3) (H3-K9-HMTase 3) (Protein G9a)

 EHMT2_MOUSE             Reviewed;        1263 AA.
Q9Z148; A2CG75; Q6PE08; Q8K4R6; Q8K4R7; Q9Z149;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
15-NOV-2002, sequence version 2.
25-OCT-2017, entry version 170.
RecName: Full=Histone-lysine N-methyltransferase EHMT2;
EC=2.1.1.-;
EC=2.1.1.43;
AltName: Full=Euchromatic histone-lysine N-methyltransferase 2;
AltName: Full=HLA-B-associated transcript 8;
AltName: Full=Histone H3-K9 methyltransferase 3;
Short=H3-K9-HMTase 3;
AltName: Full=Protein G9a;
Name=Ehmt2; Synonyms=Bat8, G9a, Ng36;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF
1165-ASN--CYS-1168, DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=12130538; DOI=10.1101/gad.989402;
Tachibana M., Sugimoto K., Nozaki M., Ueda J., Ohta T., Ohki M.,
Fukuda M., Takeda N., Niida H., Kato H., Shinkai Y.;
"G9a histone methyltransferase plays a dominant role in euchromatic
histone H3 lysine 9 methylation and is essential for early
embryogenesis.";
Genes Dev. 16:1779-1791(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=129;
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
ALTERNATIVE SPLICING (ISOFORM 2).
PubMed=11707778; DOI=10.1007/s00335-001-3029-3;
Brown S.E., Campbell R.D., Sanderson C.M.;
"Novel NG36/G9a gene products encoded within the human and mouse MHC
class III regions.";
Mamm. Genome 12:916-924(2001).
[6]
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-1162.
PubMed=11316813; DOI=10.1074/jbc.M101914200;
Tachibana M., Sugimoto K., Fukushima T., Shinkai Y.;
"Set domain-containing protein, G9a, is a novel lysine-preferring
mammalian histone methyltransferase with hyperactivity and specific
selectivity to lysines 9 and 27 of histone H3.";
J. Biol. Chem. 276:25309-25317(2001).
[7]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH
EHMT1, AND TISSUE SPECIFICITY.
PubMed=15774718; DOI=10.1101/gad.1284005;
Tachibana M., Ueda J., Fukuda M., Takeda N., Ohta T., Iwanari H.,
Sakihama T., Kodama T., Hamakubo T., Shinkai Y.;
"Histone methyltransferases G9a and GLP form heteromeric complexes and
are both crucial for methylation of euchromatin at H3-K9.";
Genes Dev. 19:815-826(2005).
[8]
INTERACTION WITH WIZ AND EHMT1.
PubMed=16702210; DOI=10.1074/jbc.M603087200;
Ueda J., Tachibana M., Ikura T., Shinkai Y.;
"Zinc finger protein Wiz links G9a/GLP histone methyltransferases to
the co-repressor molecule CtBP.";
J. Biol. Chem. 281:20120-20128(2006).
[9]
FUNCTION, AND MUTAGENESIS OF TYR-1120; 1165-ASN--CYS-1168;
1165-ASN-HIS-1166; CYS-1168 AND TYR-1207.
PubMed=18818694; DOI=10.1038/emboj.2008.192;
Tachibana M., Matsumura Y., Fukuda M., Kimura H., Shinkai Y.;
"G9a/GLP complexes independently mediate H3K9 and DNA methylation to
silence transcription.";
EMBO J. 27:2681-2690(2008).
[10]
INTERACTION WITH UHRF1.
PubMed=19056828; DOI=10.1093/nar/gkn961;
Kim J.K., Esteve P.O., Jacobsen S.E., Pradhan S.;
"UHRF1 binds G9a and participates in p21 transcriptional regulation in
mammalian cells.";
Nucleic Acids Res. 37:493-505(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193; SER-465 AND
SER-466, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
FUNCTION.
PubMed=22387026; DOI=10.1016/j.molcel.2012.01.019;
Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A.,
Carey M.F., Grunstein M.;
"Histone H3 lysine 56 methylation regulates DNA replication through
its interaction with PCNA.";
Mol. Cell 46:7-17(2012).
[13]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-40, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Histone methyltransferase that specifically mono- and
dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2,
respectively) in euchromatin. H3K9me represents a specific tag for
epigenetic transcriptional repression by recruiting HP1 proteins
to methylated histones. Also mediates monomethylation of 'Lys-56'
of histone H3 (H3K56me1) in G1 phase, leading to promote
interaction between histone H3 and PCNA and regulating DNA
replication. Also weakly methylates 'Lys-27' of histone H3
(H3K27me). Also required for DNA methylation, the histone
methyltransferase activity is not required for DNA methylation,
suggesting that these 2 activities function independently.
Probably targeted to histone H3 by different DNA-binding proteins
like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In
addition to the histone methyltransferase activity, also
methylates non-histone proteins: mediates dimethylation of 'Lys-
373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1,
ERCC6, KLF12 and itself. {ECO:0000269|PubMed:12130538,
ECO:0000269|PubMed:15774718, ECO:0000269|PubMed:18818694,
ECO:0000269|PubMed:22387026}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:11316813, ECO:0000269|PubMed:15774718}.
-!- SUBUNIT: Part of the E2F6.com-1 complex in G0 phase composed of
E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR,
GFI1B, L3MBTL2 and YAF2 (By similarity). Heterodimer;
heterodimerizes with EHMT1. Interacts with WIZ. {ECO:0000250,
ECO:0000269|PubMed:15774718, ECO:0000269|PubMed:16702210,
ECO:0000269|PubMed:19056828}.
-!- INTERACTION:
O88508-1:Dnmt3a; NbExp=3; IntAct=EBI-15737169, EBI-15650457;
O88509:Dnmt3b; NbExp=3; IntAct=EBI-15737169, EBI-7987547;
O70237:Gfi1b; NbExp=2; IntAct=EBI-444966, EBI-4287943;
Q07279:Nfe2; NbExp=4; IntAct=EBI-444981, EBI-6554737;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000305}.
Note=Almost excluded form nucleoli. Associates with euchromatic
regions. Does not associate with heterochromatin. Part of a
complex composed of TRIM28, HDAC1, HDAC2 and EHMT2 (By
similarity). Interacts with CDYL. Interacts with REST only in the
presence of CDYL. Part of a complex containing at least CDYL,
REST, WIZ, SETB1, EHMT1 and EHMT2 (By similarity). Interacts with
UHRF1. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=G9a-L;
IsoId=Q9Z148-1; Sequence=Displayed;
Name=2; Synonyms=G9a-S;
IsoId=Q9Z148-2; Sequence=VSP_002214, VSP_002215, VSP_002216;
Name=3;
IsoId=Q9Z148-3; Sequence=VSP_002214, VSP_002215;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15774718}.
-!- DOMAIN: The ANK repeats bind H3K9me1 and H3K9me2. {ECO:0000250}.
-!- DOMAIN: The SET domain mediates interaction with WIZ.
-!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
are arranged in a triangular cluster; some of these Cys residues
contribute to the binding of two zinc ions within the cluster.
{ECO:0000250}.
-!- PTM: Methylated at Lys-239; automethylated. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice show a higher level of histone H3 with
acetylated 'Lys-9' (H3K9ac) and/or methylated 'Lys-4' (H3K4me),
display severe developmental defects and die within E9.5-E12.5
stages. {ECO:0000269|PubMed:12130538}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
-!- CAUTION: NG36 and G9a were originally thought to derive from two
separate genes. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC84164.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAC84165.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAH25539.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH58357.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF109906; AAC84164.1; ALT_SEQ; Genomic_DNA.
EMBL; AF109906; AAC84165.1; ALT_SEQ; Genomic_DNA.
EMBL; AB077209; BAC05482.1; -; mRNA.
EMBL; AB077210; BAC05483.1; -; mRNA.
EMBL; CT025759; CAM27791.1; -; Genomic_DNA.
EMBL; BC025539; AAH25539.1; ALT_INIT; mRNA.
EMBL; BC058357; AAH58357.1; ALT_INIT; mRNA.
CCDS; CCDS28666.1; -. [Q9Z148-2]
CCDS; CCDS28667.1; -. [Q9Z148-1]
CCDS; CCDS70797.1; -. [Q9Z148-3]
RefSeq; NP_001273502.1; NM_001286573.1.
RefSeq; NP_001273504.1; NM_001286575.1. [Q9Z148-3]
RefSeq; NP_665829.1; NM_145830.2. [Q9Z148-1]
RefSeq; NP_671493.1; NM_147151.2. [Q9Z148-2]
UniGene; Mm.35345; -.
ProteinModelPortal; Q9Z148; -.
SMR; Q9Z148; -.
BioGrid; 225335; 8.
DIP; DIP-31916N; -.
IntAct; Q9Z148; 15.
MINT; MINT-2736375; -.
STRING; 10090.ENSMUSP00000013931; -.
BindingDB; Q9Z148; -.
ChEMBL; CHEMBL2169718; -.
iPTMnet; Q9Z148; -.
PhosphoSitePlus; Q9Z148; -.
PaxDb; Q9Z148; -.
PeptideAtlas; Q9Z148; -.
PRIDE; Q9Z148; -.
Ensembl; ENSMUST00000013931; ENSMUSP00000013931; ENSMUSG00000013787. [Q9Z148-1]
Ensembl; ENSMUST00000078061; ENSMUSP00000077208; ENSMUSG00000013787. [Q9Z148-2]
Ensembl; ENSMUST00000114033; ENSMUSP00000109667; ENSMUSG00000013787. [Q9Z148-3]
GeneID; 110147; -.
KEGG; mmu:110147; -.
UCSC; uc008ceb.3; mouse. [Q9Z148-2]
UCSC; uc008cec.3; mouse. [Q9Z148-3]
UCSC; uc008ced.3; mouse. [Q9Z148-1]
CTD; 10919; -.
MGI; MGI:2148922; Ehmt2.
eggNOG; KOG1082; Eukaryota.
eggNOG; COG0666; LUCA.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00780000121845; -.
HOGENOM; HOG000231216; -.
HOVERGEN; HBG028394; -.
InParanoid; Q9Z148; -.
KO; K11420; -.
OMA; RTEKIIC; -.
OrthoDB; EOG091G00U6; -.
PhylomeDB; Q9Z148; -.
TreeFam; TF106443; -.
BRENDA; 1.97.1.10; 3474.
Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation.
PRO; PR:Q9Z148; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000013787; -.
CleanEx; MM_EHMT2; -.
ExpressionAtlas; Q9Z148; baseline and differential.
Genevisible; Q9Z148; MM.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB.
GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IDA:UniProtKB.
GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:UniProtKB.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:MGI.
GO; GO:0002039; F:p53 binding; ISO:MGI.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
GO; GO:0071314; P:cellular response to cocaine; IDA:MGI.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
GO; GO:0006306; P:DNA methylation; IDA:UniProtKB.
GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IMP:MGI.
GO; GO:0009566; P:fertilization; IMP:MGI.
GO; GO:0007281; P:germ cell development; IMP:MGI.
GO; GO:0070734; P:histone H3-K27 methylation; IMP:MGI.
GO; GO:0051567; P:histone H3-K9 methylation; IMP:MGI.
GO; GO:0034968; P:histone lysine methylation; ISO:MGI.
GO; GO:0016571; P:histone methylation; IMP:UniProtKB.
GO; GO:0007616; P:long-term memory; IEA:Ensembl.
GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0048665; P:neuron fate specification; IMP:MGI.
GO; GO:0035265; P:organ growth; IMP:MGI.
GO; GO:0018027; P:peptidyl-lysine dimethylation; ISS:UniProtKB.
GO; GO:0036166; P:phenotypic switching; IMP:MGI.
GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
GO; GO:0051569; P:regulation of histone H3-K4 methylation; IEA:Ensembl.
GO; GO:0051570; P:regulation of histone H3-K9 methylation; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0060992; P:response to fungicide; IEA:Ensembl.
GO; GO:0007286; P:spermatid development; IMP:MGI.
GO; GO:0007130; P:synaptonemal complex assembly; IMP:MGI.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 3.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR007728; Pre-SET_dom.
InterPro; IPR001214; SET_dom.
Pfam; PF12796; Ank_2; 3.
Pfam; PF05033; Pre-SET; 1.
Pfam; PF00856; SET; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 6.
SMART; SM00468; PreSET; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 5.
PROSITE; PS50867; PRE_SET; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Chromatin regulator; Chromosome;
Complete proteome; Isopeptide bond; Metal-binding; Methylation;
Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
Repeat; S-adenosyl-L-methionine; Transferase; Ubl conjugation; Zinc.
CHAIN 1 1263 Histone-lysine N-methyltransferase EHMT2.
/FTId=PRO_0000186069.
REPEAT 702 731 ANK 1.
REPEAT 737 766 ANK 2.
REPEAT 770 799 ANK 3.
REPEAT 803 833 ANK 4.
REPEAT 837 866 ANK 5.
REPEAT 870 899 ANK 6.
REPEAT 903 932 ANK 7.
DOMAIN 1025 1088 Pre-SET. {ECO:0000255|PROSITE-
ProRule:PRU00157}.
DOMAIN 1091 1208 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 1217 1233 Post-SET.
REGION 870 872 Histone H3K9me binding. {ECO:0000250}.
REGION 1101 1103 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 1127 1146 Interaction with histone H3.
{ECO:0000250}.
REGION 1165 1166 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 1207 1210 Interaction with histone H3.
{ECO:0000250}.
COMPBIAS 352 379 Poly-Glu.
METAL 1027 1027 Zinc 1. {ECO:0000250}.
METAL 1027 1027 Zinc 2. {ECO:0000250}.
METAL 1029 1029 Zinc 1. {ECO:0000250}.
METAL 1033 1033 Zinc 1. {ECO:0000250}.
METAL 1033 1033 Zinc 3. {ECO:0000250}.
METAL 1038 1038 Zinc 1. {ECO:0000250}.
METAL 1040 1040 Zinc 2. {ECO:0000250}.
METAL 1070 1070 Zinc 2. {ECO:0000250}.
METAL 1070 1070 Zinc 3. {ECO:0000250}.
METAL 1074 1074 Zinc 2. {ECO:0000250}.
METAL 1076 1076 Zinc 3. {ECO:0000250}.
METAL 1080 1080 Zinc 3. {ECO:0000250}.
METAL 1168 1168 Zinc 4. {ECO:0000250}.
METAL 1221 1221 Zinc 4. {ECO:0000250}.
METAL 1223 1223 Zinc 4. {ECO:0000250}.
METAL 1228 1228 Zinc 4. {ECO:0000250}.
BINDING 1120 1120 Histone H3K9me. {ECO:0000250}.
BINDING 1138 1138 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
MOD_RES 40 40 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000250|UniProtKB:Q96KQ7}.
MOD_RES 101 101 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96KQ7}.
MOD_RES 104 104 Phosphoserine.
{ECO:0000250|UniProtKB:Q96KQ7}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 239 239 N6,N6,N6-trimethyllysine; by EHMT2;
alternate.
{ECO:0000250|UniProtKB:Q96KQ7}.
MOD_RES 239 239 N6,N6-dimethyllysine; by EHMT2;
alternate.
{ECO:0000250|UniProtKB:Q96KQ7}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000250|UniProtKB:Q96KQ7}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000250|UniProtKB:Q96KQ7}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000250|UniProtKB:Q96KQ7}.
MOD_RES 403 403 Phosphoserine.
{ECO:0000250|UniProtKB:Q96KQ7}.
MOD_RES 465 465 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 466 466 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 608 608 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96KQ7}.
MOD_RES 1257 1257 Phosphoserine.
{ECO:0000250|UniProtKB:Q96KQ7}.
MOD_RES 1263 1263 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96KQ7}.
CROSSLNK 272 272 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96KQ7}.
CROSSLNK 282 282 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96KQ7}.
CROSSLNK 687 687 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96KQ7}.
VAR_SEQ 1 57 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:12130538,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_002214.
VAR_SEQ 58 71 AGLTGPPVPCLPSQ -> MAAAAGAAAAAAAE (in
isoform 2 and isoform 3).
{ECO:0000303|PubMed:12130538,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_002215.
VAR_SEQ 426 459 Missing (in isoform 2).
{ECO:0000303|PubMed:12130538}.
/FTId=VSP_002216.
MUTAGEN 1120 1120 Y->V: In GM7; defective in
methyltransferase activity without
affecting DNA methylation; when
associated with F-1207.
{ECO:0000269|PubMed:18818694}.
MUTAGEN 1162 1162 R->H: Strongly reduces histone
methyltransferase activity.
{ECO:0000269|PubMed:11316813}.
MUTAGEN 1165 1168 Missing: Abolishes histone
methyltransferase activity and subsequent
repression. {ECO:0000269|PubMed:12130538,
ECO:0000269|PubMed:18818694}.
MUTAGEN 1165 1168 Missing: In GM3; does not form
heterodimer with EHMT1 and is defective
in mediating both H3K9me and DNA
methylation.
{ECO:0000269|PubMed:12130538,
ECO:0000269|PubMed:18818694}.
MUTAGEN 1165 1166 NH->LE: In GM6; does not form heterodimer
with EHMT1 and is defective in mediating
H3K9me. {ECO:0000269|PubMed:18818694}.
MUTAGEN 1168 1168 C->A: In GM4; defective in
methyltransferase activity without
affecting DNA methylation.
{ECO:0000269|PubMed:18818694}.
MUTAGEN 1207 1207 Y->F: In GM7; defective in
methyltransferase activity without
affecting DNA methylation; when
associated with V-1120.
{ECO:0000269|PubMed:18818694}.
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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