EHMT1_MOUSE
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 03-AUG-2022, entry version 151.
DE RecName: Full=Histone-lysine N-methyltransferase EHMT1;
DE EC=2.1.1.- {ECO:0000269|PubMed:15774718};
DE EC=2.1.1.367 {ECO:0000269|PubMed:15774718};
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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, AND
RP 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 [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., 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 [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 project:
RT 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 AND
RP 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., Espejo A.,
RA Zee B.M., Liu C.L., Tangsombatvisit S., Tennen R.I., Kuo A.Y., Tanjing S.,
RA Cheung R., Chua K.F., Utz P.J., Shi X., Prinjha R.K., Lee K., Garcia B.A.,
RA Bedford M.T., Tarakhovsky A., Cheng X., Gozani O.;
RT "Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples activity
RT of the histone methyltransferase GLP at chromatin to tonic repression of
RT NF-kappaB signaling.";
RL Nat. Immunol. 12:29-36(2011).
RN [6] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH BAZ2B.
RX PubMed=32103178; DOI=10.1038/s41586-020-2037-y;
RA Yuan J., Chang S.Y., Yin S.G., Liu Z.Y., Cheng X., Liu X.J., Jiang Q.,
RA Gao G., Lin D.Y., Kang X.L., Ye S.W., Chen Z., Yin J.A., Hao P., Jiang L.,
RA Cai S.Q.;
RT "Two conserved epigenetic regulators prevent healthy ageing.";
RL Nature 579:118-122(2020).
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 weakly methylates 'Lys-27' of histone H3 (H3K27me). Also
CC required for DNA methylation, the histone methyltransferase activity is
CC not required for DNA methylation, suggesting that these 2 activities
CC function independently. Probably targeted to histone H3 by different
CC DNA-binding proteins like E2F6, MGA, MAX and/or DP1. During G0 phase,
CC it probably contributes to silencing of MYC- and E2F-responsive genes,
CC suggesting a role in G0/G1 transition in cell cycle. In addition to the
CC histone methyltransferase activity, also methylates non-histone
CC proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Represses
CC the expression of mitochondrial function-related genes, perhaps by
CC occupying their promoter regions, working in concert with probable
CC chromatin reader Baz2b (PubMed:32103178). {ECO:0000269|PubMed:15774718,
CC ECO:0000269|PubMed:18818694, ECO:0000269|PubMed:32103178}.
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: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:15774718};
CC -!- ACTIVITY REGULATION: Methyltransferase activity is inhibited by BIX-
CC 01294. Efficiently inhibited by compound E72, a BIX-01294 derivative in
CC which the diazepane ring and the benzyl are replaced with a 3-
CC dimethylaminopropyl and a 5-aminopentyl group at sites B and C,
CC respectively (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with WIZ. Part of the E2F6.com-1 complex in G0 phase
CC composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2,
CC MBLR, L3MBTL2 and YAF2. Interacts with MPHOSPH8 (By similarity).
CC Interacts with CDYL. Interacts with REST only in the presence of CDYL.
CC Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and
CC EHMT2 (By similarity). Heterodimer; heterodimerizes with EHMT2.
CC Interacts (via ANK repeats) with RELA (when monomethylated at 'Lys-
CC 310'). Interacts with Baz2b (PubMed:32103178). {ECO:0000250,
CC ECO:0000269|PubMed:15774718, ECO:0000269|PubMed:21131967,
CC ECO:0000269|PubMed:32103178}.
CC -!- INTERACTION:
CC Q5DW34-1; A2A935-3: Prdm16; NbExp=2; IntAct=EBI-16080518, EBI-16080455;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15774718}. Chromosome
CC {ECO:0000269|PubMed:15774718}. Note=Associates with euchromatic
CC 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 Name=3;
CC IsoId=Q5DW34-3; Sequence=VSP_040726;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15774718}.
CC -!- DOMAIN: The ANK repeats specifically recognize and bind H3K9me1 and
CC H3K9me2 (By similarity). They also specifically recognize and bind RELA
CC subunit of NF-kappa-B, when RELA is monomethylated at 'Lys-310'.
CC {ECO:0000250, ECO:0000269|PubMed:21131967}.
CC -!- DOMAIN: The SET domain mediates interaction with WIZ. {ECO:0000250}.
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 -!- DISRUPTION PHENOTYPE: Embryos die around E9.5. Levels of H3K9me1 and
CC H3K9me2 are drastically reduced. {ECO:0000269|PubMed:15774718}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM22112.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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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 AlphaFoldDB; Q5DW34; -.
DR SMR; Q5DW34; -.
DR BioGRID; 218847; 20.
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 EPD; Q5DW34; -.
DR jPOST; Q5DW34; -.
DR MaxQB; Q5DW34; -.
DR PaxDb; Q5DW34; -.
DR PeptideAtlas; Q5DW34; -.
DR PRIDE; Q5DW34; -.
DR ProteomicsDB; 277570; -. [Q5DW34-1]
DR ProteomicsDB; 277571; -. [Q5DW34-2]
DR ProteomicsDB; 277572; -. [Q5DW34-3]
DR Antibodypedia; 32511; 524 antibodies from 31 providers.
DR DNASU; 77683; -.
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 VEuPathDB; HostDB:ENSMUSG00000036893; -.
DR eggNOG; KOG1082; Eukaryota.
DR GeneTree; ENSGT00940000156002; -.
DR HOGENOM; CLU_005790_3_0_1; -.
DR InParanoid; Q5DW34; -.
DR OMA; LHAHKRE; -.
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 BioGRID-ORCS; 77683; 20 hits in 80 CRISPR screens.
DR ChiTaRS; Ehmt1; mouse.
DR PRO; PR:Q5DW34; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q5DW34; protein.
DR Bgee; ENSMUSG00000036893; Expressed in manus and 227 other tissues.
DR ExpressionAtlas; Q5DW34; baseline and differential.
DR Genevisible; Q5DW34; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
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:0001222; F:transcription corepressor binding; 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:0051567; P:histone H3-K9 methylation; IBA:GO_Central.
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:0051570; P:regulation of histone H3-K9 methylation; IBA:GO_Central.
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; IPR038035; EHMT1.
DR InterPro; IPR043550; EHMT1/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:SF2; PTHR46307:SF2; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
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 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 Acetylation; Alternative splicing; ANK repeat; Chromatin regulator;
KW Chromosome; Isopeptide bond; Metal-binding; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW Transferase; Ubl conjugation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT CHAIN 2..1296
FT /note="Histone-lysine N-methyltransferase EHMT1"
FT /id="PRO_0000405844"
FT REPEAT 735..764
FT /note="ANK 1"
FT REPEAT 770..799
FT /note="ANK 2"
FT REPEAT 803..832
FT /note="ANK 3"
FT REPEAT 836..866
FT /note="ANK 4"
FT REPEAT 870..899
FT /note="ANK 5"
FT REPEAT 903..932
FT /note="ANK 6"
FT REPEAT 936..965
FT /note="ANK 7"
FT REPEAT 969..1002
FT /note="ANK 8"
FT DOMAIN 1058..1121
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 1124..1241
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..905
FT /note="Histone H3K9me binding"
FT /evidence="ECO:0000250"
FT REGION 1160..1179
FT /note="Interaction with histone H3"
FT /evidence="ECO:0000250"
FT REGION 1240..1243
FT /note="Interaction with histone H3"
FT /evidence="ECO:0000250"
FT REGION 1271..1296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..360
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..413
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1060
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1060
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1062
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1066
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1066
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1071
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 1073
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1134..1136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 1171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 1198..1199
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 1201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 1254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 1255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 1256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 1261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT SITE 1153
FT /note="Histone H3K9me binding"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT MOD_RES 1046
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT CROSSLNK 23
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT CROSSLNK 23
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT CROSSLNK 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT CROSSLNK 232
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT CROSSLNK 315
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT CROSSLNK 559
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT CROSSLNK 644
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT CROSSLNK 659
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT CROSSLNK 729
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9B1"
FT VAR_SEQ 273..279
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040724"
FT VAR_SEQ 455..500
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040725"
FT VAR_SEQ 550..597
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040726"
FT MUTAGEN 1153
FT /note="Y->V: In LM7; does not prevent methyltransferase
FT activity; when associated with F-1240."
FT /evidence="ECO:0000269|PubMed:18818694"
FT MUTAGEN 1198..1201
FT /note="Missing: In LM3; does not form heterodimer with
FT EHMT2 and is defective in mediating both H3K9me and DNA
FT methylation."
FT /evidence="ECO:0000269|PubMed:18818694"
FT MUTAGEN 1201
FT /note="C->A: In LM4; does not prevent methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:18818694"
FT MUTAGEN 1240
FT /note="Y->F: In LM7; does not prevent methyltransferase
FT activity; when associated with V-1153."
FT /evidence="ECO:0000269|PubMed:18818694"
FT CONFLICT 411
FT /note="E -> D (in Ref. 1; BAD90007)"
FT /evidence="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
