GenomeNet

Database: UniProt
Entry: Q5DW34
LinkDB: Q5DW34
Original site: Q5DW34 
ID   EHMT1_MOUSE             Reviewed;        1296 AA.
AC   Q5DW34; A2AIS3; A2AIS4; Q5EBR1; Q6PGM0;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   13-FEB-2019, entry version 134.
DE   RecName: Full=Histone-lysine N-methyltransferase EHMT1;
DE            EC=2.1.1.-;
DE            EC=2.1.1.43;
DE   AltName: Full=Euchromatic histone-lysine N-methyltransferase 1;
DE            Short=Eu-HMTase1;
DE   AltName: Full=G9a-like protein 1;
DE            Short=GLP;
DE            Short=GLP1;
DE   AltName: Full=Lysine N-methyltransferase 1D;
GN   Name=Ehmt1; Synonyms=Euhmtase1, Glp, Kmt1d;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH EHMT2,
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
RT   are both crucial for methylation of euchromatin at H3-K9.";
RL   Genes Dev. 19:815-826(2005).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-1296 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1296 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [4]
RP   FUNCTION, AND MUTAGENESIS OF TYR-1153; 1198-ASN--CYS-1201; CYS-1201
RP   AND TYR-1240.
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   [5]
RP   DOMAIN ANK REPEATS, AND INTERACTION WITH RELA.
RX   PubMed=21131967; DOI=10.1038/ni.1968;
RA   Levy D., Kuo A.J., Chang Y., Schaefer U., Kitson C., Cheung P.,
RA   Espejo A., Zee B.M., Liu C.L., Tangsombatvisit S., Tennen R.I.,
RA   Kuo A.Y., Tanjing S., Cheung R., Chua K.F., Utz P.J., Shi X.,
RA   Prinjha R.K., Lee K., Garcia B.A., Bedford M.T., Tarakhovsky A.,
RA   Cheng X., Gozani O.;
RT   "Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples
RT   activity of the histone methyltransferase GLP at chromatin to tonic
RT   repression of NF-kappaB signaling.";
RL   Nat. Immunol. 12:29-36(2011).
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 weakly methylates 'Lys-27' of histone
CC       H3 (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. During G0 phase, it probably
CC       contributes to silencing of MYC- and E2F-responsive genes,
CC       suggesting a role in G0/G1 transition in cell cycle. In addition
CC       to the histone methyltransferase activity, also methylates non-
CC       histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53.
CC       {ECO:0000269|PubMed:15774718, ECO:0000269|PubMed:18818694}.
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:15774718};
CC   -!- ACTIVITY REGULATION: Methyltransferase activity is inhibited by
CC       BIX-01294. Efficiently inhibited by compound E72, a BIX-01294
CC       derivative in which the diazepane ring and the benzyl are replaced
CC       with a 3-dimethylaminopropyl and a 5-aminopentyl group at sites B
CC       and C, respectively (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with WIZ. Part of the E2F6.com-1 complex in G0
CC       phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1,
CC       RNF2, MBLR, L3MBTL2 and YAF2. Interacts with MPHOSPH8 (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). Heterodimer;
CC       heterodimerizes with EHMT2. Interacts (via ANK repeats) with RELA
CC       (when monomethylated at 'Lys-310'). {ECO:0000250,
CC       ECO:0000269|PubMed:15774718, ECO:0000269|PubMed:21131967}.
CC   -!- INTERACTION:
CC       A2A935-3:Prdm16; NbExp=2; IntAct=EBI-16080518, EBI-16080455;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15774718}.
CC       Chromosome {ECO:0000269|PubMed:15774718}. Note=Associates with
CC       euchromatic regions.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5DW34-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5DW34-2; Sequence=VSP_040724, VSP_040725;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q5DW34-3; Sequence=VSP_040726;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15774718}.
CC   -!- DOMAIN: The ANK repeats specifically recognize and bind H3K9me1
CC       and H3K9me2 (By similarity). They also specifically recognize and
CC       bind RELA subunit of NF-kappa-B, when RELA is monomethylated at
CC       'Lys-310'. {ECO:0000250, ECO:0000269|PubMed:21131967}.
CC   -!- DOMAIN: The SET domain mediates interaction with WIZ.
CC       {ECO:0000250}.
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   -!- DISRUPTION PHENOTYPE: Embryos die around E9.5. Levels of H3K9me1
CC       and H3K9me2 are drastically reduced.
CC       {ECO:0000269|PubMed:15774718}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM22112.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; AB205007; BAD90007.1; -; mRNA.
DR   EMBL; AL732525; CAM22112.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL732525; CAM22113.1; -; Genomic_DNA.
DR   EMBL; AL732525; CAM22114.1; -; Genomic_DNA.
DR   EMBL; BC056938; AAH56938.1; -; mRNA.
DR   EMBL; BC089302; AAH89302.1; -; mRNA.
DR   CCDS; CCDS15740.1; -. [Q5DW34-1]
DR   CCDS; CCDS59634.1; -. [Q5DW34-2]
DR   CCDS; CCDS59636.1; -. [Q5DW34-3]
DR   RefSeq; NP_001012536.2; NM_001012518.3. [Q5DW34-1]
DR   RefSeq; NP_001103156.1; NM_001109686.2. [Q5DW34-2]
DR   RefSeq; NP_001103157.1; NM_001109687.2. [Q5DW34-3]
DR   UniGene; Mm.24176; -.
DR   ProteinModelPortal; Q5DW34; -.
DR   SMR; Q5DW34; -.
DR   BioGrid; 218847; 12.
DR   DIP; DIP-49000N; -.
DR   DIP; DIP-59572N; -.
DR   IntAct; Q5DW34; 10.
DR   MINT; Q5DW34; -.
DR   STRING; 10090.ENSMUSP00000100002; -.
DR   iPTMnet; Q5DW34; -.
DR   PhosphoSitePlus; Q5DW34; -.
DR   SwissPalm; Q5DW34; -.
DR   jPOST; Q5DW34; -.
DR   PaxDb; Q5DW34; -.
DR   PeptideAtlas; Q5DW34; -.
DR   PRIDE; Q5DW34; -.
DR   Ensembl; ENSMUST00000046227; ENSMUSP00000046077; ENSMUSG00000036893. [Q5DW34-3]
DR   Ensembl; ENSMUST00000114432; ENSMUSP00000110075; ENSMUSG00000036893. [Q5DW34-2]
DR   Ensembl; ENSMUST00000147147; ENSMUSP00000119057; ENSMUSG00000036893. [Q5DW34-1]
DR   GeneID; 77683; -.
DR   KEGG; mmu:77683; -.
DR   UCSC; uc008iph.4; mouse. [Q5DW34-3]
DR   UCSC; uc008ipi.4; mouse. [Q5DW34-1]
DR   UCSC; uc012brr.3; mouse. [Q5DW34-2]
DR   CTD; 79813; -.
DR   MGI; MGI:1924933; Ehmt1.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG0666; LUCA.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000156002; -.
DR   HOGENOM; HOG000231216; -.
DR   HOVERGEN; HBG028394; -.
DR   InParanoid; Q5DW34; -.
DR   KO; K11420; -.
DR   OMA; YRTQNMG; -.
DR   OrthoDB; 753093at2759; -.
DR   PhylomeDB; Q5DW34; -.
DR   TreeFam; TF106443; -.
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-8953750; Transcriptional Regulation by E2F6.
DR   ChiTaRS; Ehmt1; mouse.
DR   PRO; PR:Q5DW34; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000036893; Expressed in 242 organ(s), highest expression level in pes.
DR   ExpressionAtlas; Q5DW34; baseline and differential.
DR   Genevisible; Q5DW34; MM.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016604; C:nuclear body; 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; ISO:MGI.
DR   GO; GO:0008168; F:methyltransferase activity; ISO:MGI.
DR   GO; GO:0002039; F:p53 binding; ISO:MGI.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; ISO:MGI.
DR   GO; GO:0006306; P:DNA methylation; IDA:UniProtKB.
DR   GO; GO:0016571; P:histone methylation; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IMP:UniProtKB.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; IMP:UniProtKB.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:0045995; P:regulation of embryonic development; IMP:UniProtKB.
DR   GO; GO:0060992; P:response to fungicide; IEA:Ensembl.
DR   CDD; cd00204; ANK; 1.
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; IPR038035; EHMT1.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   PANTHER; PTHR22884:SF364; PTHR22884:SF364; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 7.
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   Acetylation; Alternative splicing; ANK repeat; Chromatin regulator;
KW   Chromosome; Complete proteome; Isopeptide bond; Metal-binding;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; S-adenosyl-L-methionine; Transferase; Ubl conjugation; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q9H9B1}.
FT   CHAIN         2   1296       Histone-lysine N-methyltransferase EHMT1.
FT                                /FTId=PRO_0000405844.
FT   REPEAT      735    764       ANK 1.
FT   REPEAT      770    799       ANK 2.
FT   REPEAT      803    832       ANK 3.
FT   REPEAT      836    866       ANK 4.
FT   REPEAT      870    899       ANK 5.
FT   REPEAT      903    932       ANK 6.
FT   REPEAT      936    965       ANK 7.
FT   REPEAT      969   1002       ANK 8.
FT   DOMAIN     1058   1121       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN     1124   1241       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      903    905       Histone H3K9me binding. {ECO:0000250}.
FT   REGION     1134   1136       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION     1160   1179       Interaction with histone H3.
FT                                {ECO:0000250}.
FT   REGION     1198   1199       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION     1240   1243       Interaction with histone H3.
FT                                {ECO:0000250}.
FT   COMPBIAS    440    447       Poly-Arg.
FT   COMPBIAS   1290   1293       Poly-Ala.
FT   METAL      1060   1060       Zinc 1. {ECO:0000250}.
FT   METAL      1060   1060       Zinc 2. {ECO:0000250}.
FT   METAL      1062   1062       Zinc 1. {ECO:0000250}.
FT   METAL      1066   1066       Zinc 1. {ECO:0000250}.
FT   METAL      1066   1066       Zinc 3. {ECO:0000250}.
FT   METAL      1071   1071       Zinc 1. {ECO:0000250}.
FT   METAL      1073   1073       Zinc 2. {ECO:0000250}.
FT   METAL      1103   1103       Zinc 2. {ECO:0000250}.
FT   METAL      1103   1103       Zinc 3. {ECO:0000250}.
FT   METAL      1107   1107       Zinc 2. {ECO:0000250}.
FT   METAL      1109   1109       Zinc 3. {ECO:0000250}.
FT   METAL      1113   1113       Zinc 3. {ECO:0000250}.
FT   METAL      1201   1201       Zinc 4. {ECO:0000250}.
FT   METAL      1254   1254       Zinc 4. {ECO:0000250}.
FT   METAL      1256   1256       Zinc 4. {ECO:0000250}.
FT   METAL      1261   1261       Zinc 4. {ECO:0000250}.
FT   BINDING    1153   1153       Histone H3K9me. {ECO:0000250}.
FT   BINDING    1171   1171       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING    1255   1255       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   MOD_RES     433    433       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   MOD_RES     481    481       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   MOD_RES    1046   1046       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   CROSSLNK     23     23       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   CROSSLNK     23     23       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   CROSSLNK    191    191       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   CROSSLNK    229    229       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   CROSSLNK    232    232       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   CROSSLNK    315    315       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   CROSSLNK    325    325       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   CROSSLNK    430    430       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   CROSSLNK    559    559       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   CROSSLNK    644    644       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   CROSSLNK    659    659       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   CROSSLNK    729    729       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9H9B1}.
FT   VAR_SEQ     273    279       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_040724.
FT   VAR_SEQ     455    500       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_040725.
FT   VAR_SEQ     550    597       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_040726.
FT   MUTAGEN    1153   1153       Y->V: In LM7; does not prevent
FT                                methyltransferase activity; when
FT                                associated with F-1240.
FT                                {ECO:0000269|PubMed:18818694}.
FT   MUTAGEN    1198   1201       Missing: In LM3; does not form
FT                                heterodimer with EHMT2 and is defective
FT                                in mediating both H3K9me and DNA
FT                                methylation.
FT                                {ECO:0000269|PubMed:18818694}.
FT   MUTAGEN    1201   1201       C->A: In LM4; does not prevent
FT                                methyltransferase activity.
FT                                {ECO:0000269|PubMed:18818694}.
FT   MUTAGEN    1240   1240       Y->F: In LM7; does not prevent
FT                                methyltransferase activity; when
FT                                associated with V-1153.
FT                                {ECO:0000269|PubMed:18818694}.
FT   CONFLICT    411    411       E -> D (in Ref. 1; BAD90007).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1296 AA;  141999 MW;  B7783B6F38D3C7CB CRC64;
     MAAADAEQAV LAKQETKQDC CMKTELLRED TPMAADEGST EKQEGETPMA ADGETNGSCE
     KSGDPSHLNA PKHTQENTRA SPQEGTNRVS RVAENGVSER DTEVGKQNHV TADDFMQTSV
     IGSNGYFLNK PALQGQPLRT PNILTSSLPG HAAKTLPGGA SKCRTLSALP QTPTTAPTVP
     GEGSADTEDR KPTASGTDVR VHRARKTMPK SILGLHAASK DHREVQDHKE PKEDINRNIS
     ECGRQQLLPT FPALHQSLPQ NQCYMATTKS QTACLPFVLA AAVSRKKKRR MGTYSLVPKK
     KTKVLKQRTV IEMFKSITHS TVGAKGEKAL DDSALHVNGE SLEMDSEDED SDELEDDEDH
     GAEQAAAFPT EDSRTSKESM SETDRAAKMD GDSEEEQESP DTGEDEDGGD ESDLSSESSI
     KKKFLKRRGK TDSPWIKPAR KRRRRSRKKP SSMLGSEACK SSPGSMEQAA LGDSAGYMEV
     SLDSLDLRVR GILSSQTENE GLASGPDVLG TDGLQEVPLC SCRMETPKSR EISTLANNQC
     MATESVDHEL GRCTNSVVKY ELMRPSNKAP LLVLCEDHRG RMVKHQCCPG CGYFCTAGNF
     MECQPESSIS HRFHKDCASR VNNASYCPHC GEEASKAKEV TIAKADTTST VTLAPGQEKS
     LAAEGRADTT TGSIAGAPED ERSQSTAPQA PECFDPAGPA GLVRPTSGLS QGPGKETLES
     ALIALDSEKP KKLRFHPKQL YFSARQGELQ KVLLMLVDGI DPNFKMEHQS KRSPLHAAAE
     AGHVDICHML VQAGANIDTC SEDQRTPLME AAENNHLDAV KYLIKAGAQV DPKDAEGSTC
     LHLAAKKGHY DVVQYLLSNG QMDVNCQDDG GWTPMIWATE YKHVELVKLL LSKGSDINIR
     DNEENICLHW AAFSGCVDIA EILLAAKCDL HAVNIHGDSP LHIAARENRY DCVVLFLSRD
     SDVTLKNKEG ETPLQCASLS SQVWSALQMS KALRDSAPDK PVAVEKTVSR DIARGYERIP
     IPCVNAVDSE LCPTNYKYVS QNCVTSPMNI DRNITHLQYC VCVDDCSSST CMCGQLSMRC
     WYDKDGRLLP EFNMAEPPLI FECNHACSCW RNCRNRVVQN GLRARLQLYR TQDMGWGVRS
     LQDIPLGTFV CEYVGELISD SEADVREEDS YLFDLDNKDG EVYCIDARFY GNVSRFINHH
     CEPNLVPVRV FMSHQDLRFP RIAFFSTRLI QAGEQLGFDY GERFWDVKGK LFSCRCGSSK
     CRHSSAALAQ RQASAAQEPQ ENGLPDTSSA AAADPL
//
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