ID EHMT2_HUMAN Reviewed; 1210 AA. AC Q96KQ7; B0UZY2; Q14349; Q5JP83; Q5JQ92; Q5JQA1; Q5JQG3; Q6PK06; Q96MH5; AC Q96QD0; Q9UQL8; Q9Y331; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 27-MAR-2024, entry version 225. DE RecName: Full=Histone-lysine N-methyltransferase EHMT2; DE EC=2.1.1.- {ECO:0000269|PubMed:11316813, ECO:0000269|PubMed:20084102}; DE EC=2.1.1.367 {ECO:0000269|PubMed:11316813, ECO:0000269|PubMed:20084102}; 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=Lysine N-methyltransferase 1C; DE AltName: Full=Protein G9a; GN Name=EHMT2; Synonyms=BAT8, C6orf30, G9A, KMT1C, NG36; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2), RP TISSUE SPECIFICITY, AND VARIANT ASN-55. RX PubMed=11707778; DOI=10.1007/s00335-001-3029-3; RA Brown S.E., Campbell R.D., Sanderson C.M.; RT "Novel NG36/G9a gene products encoded within the human and mouse MHC class RT III regions."; RL Mamm. Genome 12:916-924(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Salivary gland; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14656967; DOI=10.1101/gr.1736803; RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., RA Hood L.; RT "Analysis of the gene-dense major histocompatibility complex class III RT region and its comparison to mouse."; RL Genome Res. 13:2621-2636(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-55. RA Hirakawa M., Yamaguchi H., Imai K., Shimada J., Shiina S., Tamiya G., RA Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-55. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-1210 (ISOFORM 1), AND VARIANT RP ASN-55. RC TISSUE=Muscle, and Uterus; 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 195-1210, AND FUNCTION. RC TISSUE=Histiocytic lymphoma; RX PubMed=8457211; DOI=10.1042/bj2900811; RA Milner C.M., Campbell R.D.; RT "The G9a gene in the human major histocompatibility complex encodes a novel RT protein containing ankyrin-like repeats."; RL Biochem. J. 290:811-818(1993). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=11316813; DOI=10.1074/jbc.m101914200; RA Tachibana M., Sugimoto K., Fukushima T., Shinkai Y.; RT "Set domain-containing protein, G9a, is a novel lysine-preferring mammalian RT histone methyltransferase with hyperactivity and specific selectivity to RT lysines 9 and 27 of histone H3."; RL J. Biol. Chem. 276:25309-25317(2001). RN [10] RP IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EHMT1; CBX3; RING1; RP RNF2; MBLR; L3MBTL2 AND YAF2. RX PubMed=12004135; DOI=10.1126/science.1069861; RA Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.; RT "A complex with chromatin modifiers that occupies E2F- and Myc-responsive RT genes in G0 cells."; RL Science 296:1132-1136(2002). RN [11] RP INTERACTION WITH GFI1B. RX PubMed=16688220; DOI=10.1038/sj.emboj.7601124; RA Vassen L., Fiolka K., Moeroey T.; RT "Gfi1b alters histone methylation at target gene promoters and sites of RT gamma-satellite containing heterochromatin."; RL EMBO J. 25:2409-2419(2006). RN [12] RP INTERACTION WITH WIZ AND EHMT1. RX PubMed=16702210; DOI=10.1074/jbc.m603087200; RA Ueda J., Tachibana M., Ikura T., Shinkai Y.; RT "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the RT co-repressor molecule CtBP."; RL J. Biol. Chem. 281:20120-20128(2006). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [15] RP INTERACTION WITH CDYL AND REST, AND IDENTIFICATION IN A COMPLEX WITH REST; RP CDYL; SETB1; EHMT1 AND WIZ. RX PubMed=19061646; DOI=10.1016/j.molcel.2008.10.025; RA Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., RA Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.; RT "CDYL bridges REST and histone methyltransferases for gene repression and RT suppression of cellular transformation."; RL Mol. Cell 32:718-726(2008). RN [16] RP FUNCTION, METHYLATION AT LYS-185, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=18438403; DOI=10.1038/nchembio.88; RA Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R., Jurkowska R., RA Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.; RT "Protein lysine methyltransferase G9a acts on non-histone targets."; RL Nat. Chem. Biol. 4:344-346(2008). RN [17] RP DOMAIN ANK REPEATS, AND MUTAGENESIS OF TRP-786; TRP-791; GLU-794; GLU-817; RP TRP-824 AND ASP-852. RX PubMed=18264113; DOI=10.1038/nsmb.1384; RA Collins R.E., Northrop J.P., Horton J.R., Lee D.Y., Zhang X., RA Stallcup M.R., Cheng X.; RT "The ankyrin repeats of G9a and GLP histone methyltransferases are RT mono- and dimethyllysine binding modules."; RL Nat. Struct. Mol. Biol. 15:245-250(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-173; SER-232; RP SER-246 AND THR-1210, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [20] 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 [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [22] RP FUNCTION. RX PubMed=20118233; DOI=10.1074/jbc.m109.062588; RA Huang J., Dorsey J., Chuikov S., Perez-Burgos L., Zhang X., Jenuwein T., RA Reinberg D., Berger S.L.; RT "G9a and Glp methylate lysine 373 in the tumor suppressor p53."; RL J. Biol. Chem. 285:9636-9641(2010). RN [23] RP ERRATUM OF PUBMED:20118233. RA Huang J., Dorsey J., Chuikov S., Perez-Burgos L., Zhang X., Jenuwein T., RA Reinberg D., Berger S.L.; RL J. Biol. Chem. 285:18122-18122(2010). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-232 AND SER-246, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [25] RP IDENTIFICATION IN A COMPLEX WITH TRIM28; HDAC1 AND HDAC2. RX PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036; RA Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., RA Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., RA Mermoud J.E.; RT "Maintenance of silent chromatin through replication requires SWI/SNF-like RT chromatin remodeler SMARCAD1."; RL Mol. Cell 42:285-296(2011). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-232; SER-246; RP SER-413 AND SER-1204, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [27] RP FUNCTION. RX PubMed=22387026; DOI=10.1016/j.molcel.2012.01.019; RA Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A., Carey M.F., RA Grunstein M.; RT "Histone H3 lysine 56 methylation regulates DNA replication through its RT interaction with PCNA."; RL Mol. Cell 46:7-17(2012). RN [28] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44; SER-47; SER-140; SER-232; RP SER-242; SER-350 AND THR-555, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [31] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219; LYS-229 AND LYS-634, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [32] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 913-1193 IN COMPLEX WITH RP S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20084102; DOI=10.1371/journal.pone.0008570; RA Wu H., Min J., Lunin V.V., Antoshenko T., Dombrovski L., Zeng H., RA Allali-Hassani A., Campagna-Slater V., Vedadi M., Arrowsmith C.H., RA Plotnikov A.N., Schapira M.; RT "Structural biology of human H3K9 methyltransferases."; RL PLoS ONE 5:E8570-E8570(2010). CC -!- FUNCTION: Histone methyltransferase that specifically mono- and CC dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) CC in euchromatin. H3K9me represents a specific tag for epigenetic CC transcriptional repression by recruiting HP1 proteins to methylated CC histones. Also mediates monomethylation of 'Lys-56' of histone H3 CC (H3K56me1) in G1 phase, leading to promote interaction between histone CC H3 and PCNA and regulating DNA replication. Also weakly methylates CC 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, CC the histone methyltransferase activity is not required for DNA CC methylation, suggesting that these 2 activities function independently. CC Probably targeted to histone H3 by different DNA-binding proteins like CC E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition CC to the histone methyltransferase activity, also methylates non-histone CC proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also CC methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself. CC Recruited to the promoters of target genes through interaction with CC transcriptional repressor MSX1, leading to the inhibition of myoblast CC differentiation via transcriptional repression of differentiation CC factors (By similarity). {ECO:0000250|UniProtKB:Q9Z148, CC ECO:0000269|PubMed:11316813, ECO:0000269|PubMed:18438403, CC ECO:0000269|PubMed:20084102, ECO:0000269|PubMed:20118233, CC ECO:0000269|PubMed:22387026, ECO:0000269|PubMed:8457211}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:60284, Rhea:RHEA-COMP:15541, Rhea:RHEA- CC COMP:15542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; CC Evidence={ECO:0000269|PubMed:11316813, ECO:0000269|PubMed:20084102}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + CC N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.367; CC Evidence={ECO:0000269|PubMed:11316813, ECO:0000269|PubMed:20084102}; CC -!- SUBUNIT: Heterodimer; heterodimerizes with EHMT1/GLP (PubMed:16702210). CC Interacts with GFI1B and WIZ (PubMed:16688220, PubMed:16702210). Part CC of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, CC TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR, L3MBTL2 and YAF2 CC (PubMed:12004135). Part of a complex composed of TRIM28, HDAC1, HDAC2 CC and EHMT2 (PubMed:21549307). Interacts with UHRF1 (PubMed:19056828). CC Interacts with CDYL (PubMed:19061646). Interacts with REST only in the CC presence of CDYL (PubMed:19061646). Part of a complex containing at CC least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2 (PubMed:19061646). CC Interacts with PRDM9 and CDYL; interaction only takes place when PRDM9 CC is bound to hotspot DNA (By similarity). Interacts with SMYD5 (By CC similarity). Interacts with MSX1 (via homeobox domain) (By similarity). CC {ECO:0000250|UniProtKB:Q9Z148, ECO:0000269|PubMed:12004135, CC ECO:0000269|PubMed:16688220, ECO:0000269|PubMed:16702210, CC ECO:0000269|PubMed:19056828, ECO:0000269|PubMed:19061646, CC ECO:0000269|PubMed:21549307}. CC -!- INTERACTION: CC Q96KQ7; Q6VMQ6-2: ATF7IP; NbExp=3; IntAct=EBI-744366, EBI-12070560; CC Q96KQ7; Q6P1J9: CDC73; NbExp=3; IntAct=EBI-744366, EBI-930143; CC Q96KQ7; Q9UBC3: DNMT3B; NbExp=2; IntAct=EBI-744366, EBI-80125; CC Q96KQ7; P38919: EIF4A3; NbExp=3; IntAct=EBI-744366, EBI-299104; CC Q96KQ7; Q9UM22: EPDR1; NbExp=3; IntAct=EBI-744366, EBI-946972; CC Q96KQ7; P23771: GATA3; NbExp=20; IntAct=EBI-744366, EBI-6664760; CC Q96KQ7; Q99684: GFI1; NbExp=2; IntAct=EBI-744366, EBI-949368; CC Q96KQ7; Q13547: HDAC1; NbExp=7; IntAct=EBI-744366, EBI-301834; CC Q96KQ7; Q96JB3: HIC2; NbExp=3; IntAct=EBI-744366, EBI-726282; CC Q96KQ7; Q92831: KAT2B; NbExp=3; IntAct=EBI-744366, EBI-477430; CC Q96KQ7; O60341-1: KDM1A; NbExp=2; IntAct=EBI-744366, EBI-15599570; CC Q96KQ7; Q9Y4X4: KLF12; NbExp=5; IntAct=EBI-744366, EBI-750750; CC Q96KQ7; P57682: KLF3; NbExp=4; IntAct=EBI-744366, EBI-8472267; CC Q96KQ7; Q13330: MTA1; NbExp=9; IntAct=EBI-744366, EBI-714236; CC Q96KQ7; O94776: MTA2; NbExp=7; IntAct=EBI-744366, EBI-1783035; CC Q96KQ7; Q9BTC8: MTA3; NbExp=18; IntAct=EBI-744366, EBI-2461787; CC Q96KQ7; P20592: MX2; NbExp=3; IntAct=EBI-744366, EBI-10200618; CC Q96KQ7; Q9BSU3: NAA11; NbExp=3; IntAct=EBI-744366, EBI-2585120; CC Q96KQ7; Q99801-1: NKX3-1; NbExp=3; IntAct=EBI-744366, EBI-16208773; CC Q96KQ7; O60568: PLOD3; NbExp=8; IntAct=EBI-744366, EBI-741582; CC Q96KQ7; Q9NQX1: PRDM5; NbExp=3; IntAct=EBI-744366, EBI-4292031; CC Q96KQ7; Q5JSZ5: PRRC2B; NbExp=2; IntAct=EBI-744366, EBI-744891; CC Q96KQ7; Q7Z3Z2: RD3; NbExp=3; IntAct=EBI-744366, EBI-10257497; CC Q96KQ7; Q9P2R6: RERE; NbExp=3; IntAct=EBI-744366, EBI-948076; CC Q96KQ7; Q14119: VEZF1; NbExp=3; IntAct=EBI-744366, EBI-11980193; CC Q96KQ7; O60315: ZEB2; NbExp=6; IntAct=EBI-744366, EBI-717614; CC Q96KQ7; Q9NWS9-2: ZNF446; NbExp=3; IntAct=EBI-744366, EBI-740232; CC Q96KQ7; Q96JM2: ZNF462; NbExp=4; IntAct=EBI-744366, EBI-1210359; CC Q96KQ7; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-744366, EBI-16429014; CC Q96KQ7; Q96BV0: ZNF775; NbExp=3; IntAct=EBI-744366, EBI-7149881; CC Q96KQ7; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-744366, EBI-11962574; CC Q96KQ7; Q07120: Gfi1; Xeno; NbExp=3; IntAct=EBI-744366, EBI-4289236; CC Q96KQ7-1; O60341-1: KDM1A; NbExp=3; IntAct=EBI-15737402, EBI-15599570; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11316813}. Chromosome CC {ECO:0000269|PubMed:11316813}. Note=Associates with euchromatic regions CC (PubMed:11316813). Does not associate with heterochromatin CC (PubMed:11316813). {ECO:0000269|PubMed:11316813}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=Q96KQ7-1; Sequence=Displayed; CC Name=2; Synonyms=NG36G9a-SPI; CC IsoId=Q96KQ7-2; Sequence=VSP_002211; CC Name=3; Synonyms=NG36; CC IsoId=Q96KQ7-3; Sequence=VSP_002212, VSP_002213; CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined, with high levels CC in fetal liver, thymus, lymph node, spleen and peripheral blood CC leukocytes and lower level in bone marrow. CC {ECO:0000269|PubMed:11707778}. CC -!- DOMAIN: The SET domain mediates interaction with WIZ. CC {ECO:0000269|PubMed:18264113}. CC -!- DOMAIN: The ANK repeats bind H3K9me1 and H3K9me2. CC {ECO:0000269|PubMed:18264113}. 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. CC {ECO:0000269|PubMed:18264113}. CC -!- PTM: Methylated at Lys-185; automethylated. CC {ECO:0000269|PubMed:18438403}. CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. Suvar3-9 CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}. CC -!- CAUTION: While NG36 and G9a were originally thought to derive from 2 CC separate genes, all G9A transcripts also contain the in frame coding CC sequence of NG36. {ECO:0000305|PubMed:11707778}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-21 is the initiator CC methionine. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD21811.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=AAD21812.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=AAH02686.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH09351.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH18718.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH20970.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB63294.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=BAB63295.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAA49491.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ315532; CAC86666.1; -; mRNA. DR EMBL; AK056936; BAB71314.1; -; mRNA. DR EMBL; AF134726; AAD21811.1; ALT_SEQ; Genomic_DNA. DR EMBL; AF134726; AAD21812.1; ALT_SEQ; Genomic_DNA. DR EMBL; BA000025; BAB63294.1; ALT_SEQ; Genomic_DNA. DR EMBL; BA000025; BAB63295.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL662834; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL671762; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL844853; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR388202; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR388219; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759784; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936237; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03542.1; -; Genomic_DNA. DR EMBL; BC002686; AAH02686.2; ALT_INIT; mRNA. DR EMBL; BC009351; AAH09351.1; ALT_INIT; mRNA. DR EMBL; BC018718; AAH18718.1; ALT_INIT; mRNA. DR EMBL; BC020970; AAH20970.2; ALT_INIT; mRNA. DR EMBL; X69838; CAA49491.1; ALT_INIT; mRNA. DR CCDS; CCDS4725.1; -. [Q96KQ7-1] DR CCDS; CCDS4726.1; -. [Q96KQ7-2] DR RefSeq; NP_001276342.1; NM_001289413.1. DR RefSeq; NP_001305762.1; NM_001318833.1. DR RefSeq; NP_006700.3; NM_006709.4. [Q96KQ7-1] DR RefSeq; NP_079532.5; NM_025256.6. [Q96KQ7-2] DR PDB; 2O8J; X-ray; 1.80 A; A/B/C/D=913-1193. DR PDB; 3DM1; X-ray; 2.40 A; B/D/F/H=179-190. DR PDB; 3K5K; X-ray; 1.70 A; A/B=913-1193. DR PDB; 3RJW; X-ray; 2.56 A; A/B=913-1193. DR PDB; 4NVQ; X-ray; 2.03 A; A/B=913-1193. DR PDB; 5JHN; X-ray; 1.67 A; A/B=916-1189. DR PDB; 5JIN; X-ray; 1.85 A; A/B=916-1189. DR PDB; 5JIY; X-ray; 1.48 A; A/B=916-1189. DR PDB; 5JJ0; X-ray; 1.72 A; A/B=916-1189. DR PDB; 5T0K; X-ray; 1.70 A; A/B=913-1193. DR PDB; 5T0M; X-ray; 1.90 A; A/B=913-1193. DR PDB; 5TTF; X-ray; 1.72 A; A/B/C/D=913-1193. DR PDB; 5TUY; X-ray; 2.60 A; A/B=921-1187. DR PDB; 5V9I; X-ray; 1.74 A; A/B/C/D=913-1193. DR PDB; 5VSC; X-ray; 1.40 A; A/B=916-1190. DR PDB; 5VSE; X-ray; 1.60 A; A/B=917-1190. DR PDB; 6MM1; X-ray; 1.90 A; A/B/C/D=419-552. DR PDB; 7BTV; X-ray; 2.00 A; A/B=913-1193. DR PDB; 7BUC; X-ray; 2.60 A; A/B=913-1193. DR PDB; 7DCF; X-ray; 1.80 A; A/B=913-1193. DR PDB; 7T7L; X-ray; 2.20 A; A/B/C/D=913-1193. DR PDB; 7X73; X-ray; 1.49 A; A/B=913-1193. DR PDB; 7XUA; X-ray; 1.87 A; A/B=913-1193. DR PDB; 7XUB; X-ray; 2.00 A; A/B=913-1193. DR PDB; 7XUC; X-ray; 1.67 A; A/B=913-1193. DR PDB; 7XUD; X-ray; 1.45 A; A/B=913-1193. DR PDBsum; 2O8J; -. DR PDBsum; 3DM1; -. DR PDBsum; 3K5K; -. DR PDBsum; 3RJW; -. DR PDBsum; 4NVQ; -. DR PDBsum; 5JHN; -. DR PDBsum; 5JIN; -. DR PDBsum; 5JIY; -. DR PDBsum; 5JJ0; -. DR PDBsum; 5T0K; -. DR PDBsum; 5T0M; -. DR PDBsum; 5TTF; -. DR PDBsum; 5TUY; -. DR PDBsum; 5V9I; -. DR PDBsum; 5VSC; -. DR PDBsum; 5VSE; -. DR PDBsum; 6MM1; -. DR PDBsum; 7BTV; -. DR PDBsum; 7BUC; -. DR PDBsum; 7DCF; -. DR PDBsum; 7T7L; -. DR PDBsum; 7X73; -. DR PDBsum; 7XUA; -. DR PDBsum; 7XUB; -. DR PDBsum; 7XUC; -. DR PDBsum; 7XUD; -. DR AlphaFoldDB; Q96KQ7; -. DR SMR; Q96KQ7; -. DR BioGRID; 116123; 306. DR CORUM; Q96KQ7; -. DR DIP; DIP-34461N; -. DR IntAct; Q96KQ7; 156. DR MINT; Q96KQ7; -. DR STRING; 9606.ENSP00000379078; -. DR BindingDB; Q96KQ7; -. DR ChEMBL; CHEMBL6032; -. DR GuidetoPHARMACOLOGY; 2652; -. DR GlyGen; Q96KQ7; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96KQ7; -. DR MetOSite; Q96KQ7; -. DR PhosphoSitePlus; Q96KQ7; -. DR SwissPalm; Q96KQ7; -. DR BioMuta; EHMT2; -. DR DMDM; 116241348; -. DR EPD; Q96KQ7; -. DR jPOST; Q96KQ7; -. DR MassIVE; Q96KQ7; -. DR MaxQB; Q96KQ7; -. DR PaxDb; 9606-ENSP00000364678; -. DR PeptideAtlas; Q96KQ7; -. DR ProteomicsDB; 77102; -. [Q96KQ7-1] DR ProteomicsDB; 77103; -. [Q96KQ7-2] DR ProteomicsDB; 77104; -. [Q96KQ7-3] DR Pumba; Q96KQ7; -. DR ABCD; Q96KQ7; 2 sequenced antibodies. DR Antibodypedia; 27888; 415 antibodies from 39 providers. DR DNASU; 10919; -. DR Ensembl; ENST00000375530.8; ENSP00000364680.4; ENSG00000204371.12. [Q96KQ7-2] DR Ensembl; ENST00000375537.9; ENSP00000364687.4; ENSG00000204371.12. [Q96KQ7-1] DR Ensembl; ENST00000383372.6; ENSP00000372863.2; ENSG00000206376.9. [Q96KQ7-2] DR Ensembl; ENST00000383373.8; ENSP00000372864.4; ENSG00000206376.9. [Q96KQ7-1] DR Ensembl; ENST00000420336.6; ENSP00000396119.2; ENSG00000238134.8. DR Ensembl; ENST00000420874.5; ENSP00000411035.1; ENSG00000236759.7. [Q96KQ7-2] DR Ensembl; ENST00000421926.6; ENSP00000416957.2; ENSG00000232045.7. DR Ensembl; ENST00000429506.6; ENSP00000406110.2; ENSG00000227333.8. [Q96KQ7-1] DR Ensembl; ENST00000450075.6; ENSP00000392305.2; ENSG00000236759.7. [Q96KQ7-1] DR Ensembl; ENST00000450229.5; ENSP00000400838.1; ENSG00000227333.8. [Q96KQ7-2] DR GeneID; 10919; -. DR KEGG; hsa:10919; -. DR MANE-Select; ENST00000375537.9; ENSP00000364687.4; NM_006709.5; NP_006700.3. DR UCSC; uc003nxz.3; human. [Q96KQ7-1] DR AGR; HGNC:14129; -. DR CTD; 10919; -. DR DisGeNET; 10919; -. DR GeneCards; EHMT2; -. DR HGNC; HGNC:14129; EHMT2. DR HPA; ENSG00000204371; Low tissue specificity. DR MIM; 604599; gene. DR neXtProt; NX_Q96KQ7; -. DR OpenTargets; ENSG00000204371; -. DR PharmGKB; PA25267; -. DR VEuPathDB; HostDB:ENSG00000204371; -. DR eggNOG; KOG1082; Eukaryota. DR GeneTree; ENSGT00940000159459; -. DR InParanoid; Q96KQ7; -. DR OrthoDB; 5481936at2759; -. DR PhylomeDB; Q96KQ7; -. DR TreeFam; TF106443; -. DR BioCyc; MetaCyc:HS06313-MONOMER; -. DR BRENDA; 2.1.1.355; 2681. DR BRENDA; 2.1.1.356; 2681. DR BRENDA; 2.1.1.367; 2681. DR BRENDA; 2.1.1.368; 2681. DR PathwayCommons; Q96KQ7; -. DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP). DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines. DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression. DR Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation. DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation. DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX. DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6. DR SignaLink; Q96KQ7; -. DR SIGNOR; Q96KQ7; -. DR BioGRID-ORCS; 10919; 106 hits in 1179 CRISPR screens. DR ChiTaRS; EHMT2; human. DR EvolutionaryTrace; Q96KQ7; -. DR GeneWiki; EHMT2; -. DR GenomeRNAi; 10919; -. DR Pharos; Q96KQ7; Tchem. DR PRO; PR:Q96KQ7; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q96KQ7; Protein. DR Bgee; ENSG00000204371; Expressed in nucleus accumbens and 99 other cell types or tissues. DR ExpressionAtlas; Q96KQ7; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:MGI. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB. DR GO; GO:0046976; F:histone H3K27 methyltransferase activity; ISS:UniProtKB. DR GO; GO:0140759; F:histone H3K56 methyltransferase activity; IMP:UniProtKB. DR GO; GO:0046974; F:histone H3K9 methyltransferase activity; ISS:UniProtKB. DR GO; GO:0140947; F:histone H3K9me2 methyltransferase activity; IEA:RHEA. DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB. DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI. DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0001222; F:transcription corepressor binding; IPI:ARUK-UCL. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl. DR GO; GO:0071314; P:cellular response to cocaine; IEA:Ensembl. DR GO; GO:0009267; P:cellular response to starvation; IDA:MGI. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0006306; P:DNA methylation; ISS:UniProtKB. DR GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IEA:Ensembl. DR GO; GO:0009566; P:fertilization; IEA:Ensembl. DR GO; GO:0034968; P:histone lysine methylation; IDA:MGI. DR GO; GO:0007616; P:long-term memory; IEA:Ensembl. DR GO; GO:1902902; P:negative regulation of autophagosome assembly; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0048665; P:neuron fate specification; IEA:Ensembl. DR GO; GO:0048599; P:oocyte development; IEA:Ensembl. DR GO; GO:0035265; P:organ growth; IEA:Ensembl. DR GO; GO:0018027; P:peptidyl-lysine dimethylation; IDA:UniProtKB. DR GO; GO:0036166; P:phenotypic switching; IEA:Ensembl. DR GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl. DR GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB. DR GO; GO:0031399; P:regulation of protein modification process; IEA:Ensembl. 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; IEA:Ensembl. DR GO; GO:0007130; P:synaptonemal complex assembly; IEA:Ensembl. DR CDD; cd20905; EHMT_ZBD; 1. DR CDD; cd10533; SET_EHMT2; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR Gene3D; 2.170.270.10; SET domain; 1. DR IDEAL; IID00250; -. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR043550; EHMT1/EHMT2. DR InterPro; IPR047762; EHMT_CRR. DR InterPro; IPR007728; Pre-SET_dom. DR InterPro; IPR001214; SET_dom. DR InterPro; IPR046341; SET_dom_sf. DR InterPro; IPR038034; SET_EHMT2. DR PANTHER; PTHR46307; G9A, ISOFORM B; 1. DR PANTHER; PTHR46307:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE EHMT2; 1. DR Pfam; PF00023; Ank; 1. DR Pfam; PF12796; Ank_2; 2. DR Pfam; PF21533; EHMT1-2_CRR; 1. 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; Ankyrin repeat; 1. DR SUPFAM; SSF82199; SET domain; 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. DR Genevisible; Q96KQ7; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ANK repeat; KW Chromatin regulator; Chromosome; Isopeptide bond; Metal-binding; KW Methylation; Methyltransferase; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; KW Ubl conjugation; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..1210 FT /note="Histone-lysine N-methyltransferase EHMT2" FT /id="PRO_0000186068" FT REPEAT 649..678 FT /note="ANK 1" FT REPEAT 684..713 FT /note="ANK 2" FT REPEAT 717..746 FT /note="ANK 3" FT REPEAT 750..780 FT /note="ANK 4" FT REPEAT 784..813 FT /note="ANK 5" FT REPEAT 817..846 FT /note="ANK 6" FT REPEAT 850..879 FT /note="ANK 7" FT DOMAIN 972..1035 FT /note="Pre-SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157" FT DOMAIN 1038..1155 FT /note="SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT DOMAIN 1164..1180 FT /note="Post-SET" FT REGION 1..262 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 280..386 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 548..608 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 817..819 FT /note="Histone H3K9me binding" FT /evidence="ECO:0000250" FT REGION 1074..1093 FT /note="Interaction with histone H3" FT /evidence="ECO:0000250" FT REGION 1154..1157 FT /note="Interaction with histone H3" FT /evidence="ECO:0000250" FT COMPBIAS 114..128 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 202..226 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 280..295 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 296..328 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 338..365 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 974 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 974 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 976 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 980 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 980 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT BINDING 985 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 987 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 1017 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 1017 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT BINDING 1021 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 1023 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT BINDING 1027 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT BINDING 1048..1050 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 1085 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 1112..1113 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 1115 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT BINDING 1168 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT BINDING 1169 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 1170 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT BINDING 1175 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT SITE 1067 FT /note="Histone H3K9me binding" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 40 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 44 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 47 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 140 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 173 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 185 FT /note="N6,N6,N6-trimethyllysine; by EHMT2; alternate" FT /evidence="ECO:0000269|PubMed:18438403" FT MOD_RES 185 FT /note="N6,N6-dimethyllysine; by EHMT2; alternate" FT /evidence="ECO:0000269|PubMed:18438403" FT MOD_RES 232 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 242 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 246 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 350 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 412 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z148" FT MOD_RES 413 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 555 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 569 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 1204 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1210 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT CROSSLNK 219 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 229 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 634 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 195..202 FT /note="PPVPEKRP -> VSGMGEMG (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_002212" FT VAR_SEQ 203..1210 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_002213" FT VAR_SEQ 373..406 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_002211" FT VARIANT 55 FT /note="T -> N (in dbSNP:rs7887)" FT /evidence="ECO:0000269|PubMed:11707778, FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.5" FT /id="VAR_027973" FT VARIANT 1165 FT /note="Y -> F (in dbSNP:rs13919)" FT /id="VAR_027974" FT MUTAGEN 786 FT /note="W->A: Abolishes binding to histone H3K9me without FT affecting the histone methyltransferase activity." FT /evidence="ECO:0000269|PubMed:18264113" FT MUTAGEN 791 FT /note="W->A: Abolishes binding to histone H3K9me without FT affecting the histone methyltransferase activity." FT /evidence="ECO:0000269|PubMed:18264113" FT MUTAGEN 794 FT /note="E->A: Abolishes binding to histone H3K9me without FT affecting the histone methyltransferase activity." FT /evidence="ECO:0000269|PubMed:18264113" FT MUTAGEN 817 FT /note="E->R: Impairs binding to histone H3K9me." FT /evidence="ECO:0000269|PubMed:18264113" FT MUTAGEN 824 FT /note="W->A: Abolishes binding to histone H3K9me without FT affecting the histone methyltransferase activity." FT /evidence="ECO:0000269|PubMed:18264113" FT MUTAGEN 852 FT /note="D->R: Impairs binding to histone H3K9me." FT /evidence="ECO:0000269|PubMed:18264113" FT CONFLICT 178 FT /note="P -> S (in Ref. 2; CAC86666)" FT /evidence="ECO:0000305" FT CONFLICT 985 FT /note="C -> R (in Ref. 2; CAC86666)" FT /evidence="ECO:0000305" FT CONFLICT 994 FT /note="C -> R (in Ref. 8; CAA49491)" FT /evidence="ECO:0000305" FT HELIX 420..422 FT /evidence="ECO:0007829|PDB:6MM1" FT HELIX 438..441 FT /evidence="ECO:0007829|PDB:6MM1" FT TURN 442..444 FT /evidence="ECO:0007829|PDB:6MM1" FT STRAND 449..452 FT /evidence="ECO:0007829|PDB:6MM1" FT STRAND 455..458 FT /evidence="ECO:0007829|PDB:6MM1" FT HELIX 482..489 FT /evidence="ECO:0007829|PDB:6MM1" FT TURN 495..497 FT /evidence="ECO:0007829|PDB:6MM1" FT STRAND 500..512 FT /evidence="ECO:0007829|PDB:6MM1" FT STRAND 515..519 FT /evidence="ECO:0007829|PDB:6MM1" FT HELIX 521..523 FT /evidence="ECO:0007829|PDB:6MM1" FT STRAND 525..527 FT /evidence="ECO:0007829|PDB:6MM1" FT STRAND 530..532 FT /evidence="ECO:0007829|PDB:6MM1" FT TURN 534..536 FT /evidence="ECO:0007829|PDB:6MM1" FT HELIX 540..542 FT /evidence="ECO:0007829|PDB:6MM1" FT STRAND 544..548 FT /evidence="ECO:0007829|PDB:6MM1" FT STRAND 920..924 FT /evidence="ECO:0007829|PDB:5VSC" FT TURN 926..929 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 931..933 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 937..943 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 949..952 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 957..960 FT /evidence="ECO:0007829|PDB:5VSC" FT HELIX 968..970 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 977..980 FT /evidence="ECO:0007829|PDB:3K5K" FT HELIX 986..989 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 991..993 FT /evidence="ECO:0007829|PDB:7XUD" FT STRAND 1004..1006 FT /evidence="ECO:0007829|PDB:7X73" FT STRAND 1008..1010 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 1013..1015 FT /evidence="ECO:0007829|PDB:7XUD" FT STRAND 1021..1023 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 1027..1029 FT /evidence="ECO:0007829|PDB:5VSC" FT HELIX 1032..1034 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 1040..1044 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 1046..1056 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 1063..1067 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 1069..1073 FT /evidence="ECO:0007829|PDB:5VSC" FT HELIX 1074..1077 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 1086..1089 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 1092..1094 FT /evidence="ECO:0007829|PDB:7XUD" FT STRAND 1097..1105 FT /evidence="ECO:0007829|PDB:5VSC" FT HELIX 1107..1110 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 1118..1127 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 1135..1142 FT /evidence="ECO:0007829|PDB:5VSC" FT HELIX 1156..1162 FT /evidence="ECO:0007829|PDB:5VSC" FT TURN 1163..1165 FT /evidence="ECO:0007829|PDB:5VSC" FT STRAND 1176..1178 FT /evidence="ECO:0007829|PDB:5VSC" FT HELIX 1179..1189 FT /evidence="ECO:0007829|PDB:5VSC" SQ SEQUENCE 1210 AA; 132370 MW; A6C5DC6B72801520 CRC64; MAAAAGAAAA AAAEGEAPAE MGALLLEKET RGATERVHGS LGDTPRSEET LPKATPDSLE PAGPSSPASV TVTVGDEGAD TPVGATPLIG DESENLEGDG DLRGGRILLG HATKSFPSSP SKGGSCPSRA KMSMTGAGKS PPSVQSLAMR LLSMPGAQGA AAAGSEPPPA TTSPEGQPKV HRARKTMSKP GNGQPPVPEK RPPEIQHFRM SDDVHSLGKV TSDLAKRRKL NSGGGLSEEL GSARRSGEVT LTKGDPGSLE EWETVVGDDF SLYYDSYSVD ERVDSDSKSE VEALTEQLSE EEEEEEEEEE EEEEEEEEEE EEEDEESGNQ SDRSGSSGRR KAKKKWRKDS PWVKPSRKRR KREPPRAKEP RGVNGVGSSG PSEYMEVPLG SLELPSEGTL SPNHAGVSND TSSLETERGF EELPLCSCRM EAPKIDRISE RAGHKCMATE SVDGELSGCN AAILKRETMR PSSRVALMVL CETHRARMVK HHCCPGCGYF CTAGTFLECH PDFRVAHRFH KACVSQLNGM VFCPHCGEDA SEAQEVTIPR GDGVTPPAGT AAPAPPPLSQ DVPGRADTSQ PSARMRGHGE PRRPPCDPLA DTIDSSGPSL TLPNGGCLSA VGLPLGPGRE ALEKALVIQE SERRKKLRFH PRQLYLSVKQ GELQKVILML LDNLDPNFQS DQQSKRTPLH AAAQKGSVEI CHVLLQAGAN INAVDKQQRT PLMEAVVNNH LEVARYMVQR GGCVYSKEED GSTCLHHAAK IGNLEMVSLL LSTGQVDVNA QDSGGWTPII WAAEHKHIEV IRMLLTRGAD VTLTDNEENI CLHWASFTGS AAIAEVLLNA RCDLHAVNYH GDTPLHIAAR ESYHDCVLLF LSRGANPELR NKEGDTAWDL TPERSDVWFA LQLNRKLRLG VGNRAIRTEK IICRDVARGY ENVPIPCVNG VDGEPCPEDY KYISENCETS TMNIDRNITH LQHCTCVDDC SSSNCLCGQL SIRCWYDKDG RLLQEFNKIE PPLIFECNQA CSCWRNCKNR VVQSGIKVRL QLYRTAKMGW GVRALQTIPQ GTFICEYVGE LISDAEADVR EDDSYLFDLD NKDGEVYCID ARYYGNISRF INHLCDPNII PVRVFMLHQD LRFPRIAFFS SRDIRTGEEL GFDYGDRFWD IKSKYFTCQC GSEKCKHSAE AIALEQSRLA RLDPHPELLP ELGSLPPVNT //