ID EHMT1_HUMAN Reviewed; 1298 AA. AC Q9H9B1; B1AQ58; B1AQ59; Q86X08; Q8TCN7; Q96F53; Q96JF1; Q96KH4; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 08-MAR-2011, sequence version 4. DT 27-MAR-2024, entry version 222. DE RecName: Full=Histone-lysine N-methyltransferase EHMT1; DE EC=2.1.1.- {ECO:0000269|PubMed:12004135}; DE EC=2.1.1.367 {ECO:0000269|PubMed:12004135}; 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=Histone H3-K9 methyltransferase 5; DE Short=H3-K9-HMTase 5; DE AltName: Full=Lysine N-methyltransferase 1D; GN Name=EHMT1; Synonyms=EUHMTASE1, GLP, KIAA1876, KMT1D; 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 [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Teratocarcinoma; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 583-1298 (ISOFORM 1). RC TISSUE=Brain, and Testis; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 32-1298 (ISOFORM 1), FUNCTION, CATALYTIC RP ACTIVITY, AND IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; BAT8; RP CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2. RC TISSUE=Cervix carcinoma; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 382-1298 (ISOFORM 1). RC TISSUE=Brain; RA Tsuritani K., Ukai Y., Yajima Y., Amemiya C., Yoshimoto M.; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 382-1298 (ISOFORM 3), AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX PubMed=11347906; DOI=10.1093/dnares/8.2.85; RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XX. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 8:85-95(2001). RN [7] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1089-1298 (ISOFORM 1). RC TISSUE=Lymph node; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [9] RP INVOLVEMENT IN KLEFS1. RX PubMed=16826528; DOI=10.1086/505693; RA Kleefstra T., Brunner H.G., Amiel J., Oudakker A.R., Nillesen W.M., RA Magee A., Genevieve D., Cormier-Daire V., van Esch H., Fryns J.-P., RA Hamel B.C.J., Sistermans E.A., de Vries B.B.A., van Bokhoven H.; RT "Loss-of-function mutations in euchromatin histone methyl transferase 1 RT (EHMT1) cause the 9q34 subtelomeric deletion syndrome."; RL Am. J. Hum. Genet. 79:370-377(2006). RN [10] RP INTERACTION WITH WIZ AND EHMT2. 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 [11] RP IDENTIFICATION BY 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 [12] RP INTERACTION WITH CDYL AND REST, AND IDENTIFICATION IN A COMPLEX WITH REST; RP CDYL; SETB1; EHMT2 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [14] RP INTERACTION WITH MPHOSPH8. RX PubMed=20871592; DOI=10.1038/emboj.2010.239; RA Kokura K., Sun L., Bedford M.T., Fang J.; RT "Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing and RT promotes tumour cell motility and invasion."; RL EMBO J. 29:3673-3687(2010). RN [15] RP FUNCTION, AND INTERACTION WITH TP53. 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 [16] 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 [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP INTERACTION WITH RELA, AND MUTAGENESIS OF TRP-874; GLU-882 AND TRP-912. RX PubMed=21515635; DOI=10.1093/nar/gkr256; RA Chang Y., Levy D., Horton J.R., Peng J., Zhang X., Gozani O., Cheng X.; RT "Structural basis of SETD6-mediated regulation of the NF-kB network via RT methyl-lysine signaling."; RL Nucleic Acids Res. 39:6380-6389(2011). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-1004 AND SER-1048, RP AND IDENTIFICATION BY MASS SPECTROMETRY [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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, 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 [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-432, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-234, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [25] RP ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE. RX PubMed=25489052; DOI=10.1093/hmg/ddu611; RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A., RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H., RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.; RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt- RT acetylation defects."; RL Hum. Mol. Genet. 24:1956-1976(2015). RN [26] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-234 AND LYS-731, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [27] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-190; LYS-199; LYS-231; RP LYS-234; LYS-317; LYS-327; LYS-432; LYS-492; LYS-559; LYS-644; LYS-659; RP LYS-684 AND LYS-731, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [28] RP X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 765-999 IN COMPLEX WITH HISTONE RP H3, DOMAIN ANK REPEATS, AND MUTAGENESIS OF GLU-905. 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 [29] RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 982-1266 IN COMPLEX WITH RP S-ADENOSYL-L-HOMOCYSTEINE; ZINC ION AND E72 INHIBITOR, AND ACTIVITY RP REGULATION. RX PubMed=20434463; DOI=10.1016/j.jmb.2010.04.048; RA Chang Y., Ganesh T., Horton J.R., Spannhoff A., Liu J., Sun A., Zhang X., RA Bedford M.T., Shinkai Y., Snyder J.P., Cheng X.; RT "Adding a lysine mimic in the design of potent inhibitors of histone lysine RT methyltransferases."; RL J. Mol. Biol. 400:1-7(2010). RN [30] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 982-1266 IN COMPLEX WITH HISTONE RP H3; S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS. 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). RN [31] RP VARIANTS [LARGE SCALE ANALYSIS] VAL-43 AND PHE-1173. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [32] RP VARIANT KLEFS1 TYR-1075. RX PubMed=19264732; DOI=10.1136/jmg.2008.062950; RA Kleefstra T., van Zelst-Stams W.A., Nillesen W.M., Cormier-Daire V., RA Houge G., Foulds N., van Dooren M., Willemsen M.H., Pfundt R., Turner A., RA Wilson M., McGaughran J., Rauch A., Zenker M., Adam M.P., Innes M., RA Davies C., Lopez A.G., Casalone R., Weber A., Brueton L.A., Navarro A.D., RA Bralo M.P., Venselaar H., Stegmann S.P., Yntema H.G., van Bokhoven H., RA Brunner H.G.; RT "Further clinical and molecular delineation of the 9q subtelomeric deletion RT syndrome supports a major contribution of EHMT1 haploinsufficiency to the RT core phenotype."; RL J. Med. Genet. 46:598-606(2009). 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 (By similarity). {ECO:0000250|UniProtKB:Q5DW34, CC ECO:0000269|PubMed:12004135, ECO:0000269|PubMed:20118233}. 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:12004135}; 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:12004135}; 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. {ECO:0000269|PubMed:20434463}. CC -!- SUBUNIT: Heterodimer; heterodimerizes with EHMT2. Interacts with WIZ CC and EHMT2. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, CC MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR, L3MBTL2 and CC YAF2. Interacts (via ANK repeats) with RELA (when monomethylated at CC 'Lys-310') (PubMed:21515635). Interacts with MPHOSPH8. Interacts with CC CDYL. Interacts with REST only in the presence of CDYL. Part of a CC complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2. CC Interacts with BAZ2B (By similarity). Interacts with MSX1 (By CC similarity). {ECO:0000250|UniProtKB:Q5DW34, CC ECO:0000269|PubMed:12004135, ECO:0000269|PubMed:16702210, CC ECO:0000269|PubMed:18264113, ECO:0000269|PubMed:19061646, CC ECO:0000269|PubMed:20084102, ECO:0000269|PubMed:20118233, CC ECO:0000269|PubMed:20434463, ECO:0000269|PubMed:20871592, CC ECO:0000269|PubMed:21515635}. CC -!- INTERACTION: CC Q9H9B1; Q99549: MPHOSPH8; NbExp=3; IntAct=EBI-766087, EBI-2653928; CC Q9H9B1; Q04206: RELA; NbExp=3; IntAct=EBI-766087, EBI-73886; CC Q9H9B1; Q04207: Rela; Xeno; NbExp=5; IntAct=EBI-766087, EBI-644400; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates with CC euchromatic regions. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Experimental confirmation may be lacking for some isoforms.; CC Name=1; CC IsoId=Q9H9B1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H9B1-2; Sequence=VSP_002222, VSP_002223; CC Name=3; CC IsoId=Q9H9B1-3; Sequence=VSP_002224, VSP_002225; CC Name=4; CC IsoId=Q9H9B1-4; Sequence=VSP_040717, VSP_040718; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11347906}. CC -!- DOMAIN: The ANK repeats recognize and bind RELA subunit of NF-kappa-B, CC when RELA is monomethylated at 'Lys-310' (By similarity). They also CC specifically recognize and bind H3K9me1 and H3K9me2. {ECO:0000250, CC ECO:0000269|PubMed:18264113}. CC -!- DOMAIN: The SET domain mediates interaction with WIZ. 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 -!- DISEASE: Kleefstra syndrome 1 (KLEFS1) [MIM:610253]: A form of CC Kleefstra syndrome, an autosomal dominant disease characterized by CC variable intellectual disability, psychomotor developmental delay, CC seizures, behavioral abnormalities, and facial dysmorphisms. KLEFS1 CC patients additionally manifest brachy(micro)cephaly, congenital heart CC defects, and urogenital defects. {ECO:0000269|PubMed:16826528, CC ECO:0000269|PubMed:19264732}. Note=The disease is caused by variants CC affecting the gene represented in this entry. The syndrome can be CC either caused by intragenic EHMT1 mutations leading to CC haploinsufficiency of the EHMT1 gene or by a submicroscopic 9q34.3 CC deletion. Although it is not known if and to what extent other genes in CC the 9q34.3 region contribute to the syndrome observed in deletion CC cases, EHMT1 seems to be the major determinant of the core disease CC phenotype (PubMed:19264732). {ECO:0000269|PubMed:16826528, CC ECO:0000269|PubMed:19264732}. CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB14321.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305}; CC Sequence=CAD28534.1; Type=Miscellaneous discrepancy; Note=Intron retention.; 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; AK022941; BAB14321.1; ALT_SEQ; mRNA. DR EMBL; AL590627; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL611925; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC011608; AAH11608.2; -; mRNA. DR EMBL; BC047504; AAH47504.1; -; mRNA. DR EMBL; AY083210; AAM09024.1; -; mRNA. DR EMBL; AB028932; BAB56104.1; -; mRNA. DR EMBL; AB058779; BAB47505.2; -; mRNA. DR EMBL; AL713772; CAD28534.1; ALT_SEQ; mRNA. DR CCDS; CCDS56595.1; -. [Q9H9B1-4] DR CCDS; CCDS7050.2; -. [Q9H9B1-1] DR RefSeq; NP_001138999.1; NM_001145527.1. [Q9H9B1-4] DR RefSeq; NP_079033.4; NM_024757.4. [Q9H9B1-1] DR PDB; 2IGQ; X-ray; 2.00 A; A/B=982-1266. DR PDB; 2RFI; X-ray; 1.59 A; A/B=982-1266. DR PDB; 3B7B; X-ray; 2.99 A; A/B=765-999. DR PDB; 3B95; X-ray; 2.99 A; A/B=765-999. DR PDB; 3FPD; X-ray; 2.40 A; A/B=1006-1266. DR PDB; 3HNA; X-ray; 1.50 A; A/B=982-1266. DR PDB; 3MO0; X-ray; 2.78 A; A/B=982-1266. DR PDB; 3MO2; X-ray; 2.49 A; A/B/C/D=982-1266. DR PDB; 3MO5; X-ray; 2.14 A; A/B/C/D=982-1266. DR PDB; 3SW9; X-ray; 3.05 A; A/B=982-1266. DR PDB; 3SWC; X-ray; 2.33 A; A/B=982-1266. DR PDB; 4I51; X-ray; 1.90 A; A/B=982-1266. DR PDB; 5TTG; X-ray; 1.66 A; A/B=982-1266. DR PDB; 5TUZ; X-ray; 1.95 A; A/B=1006-1266. DR PDB; 5V9J; X-ray; 1.74 A; A/B=982-1266. DR PDB; 5VSD; X-ray; 1.85 A; A/B=1006-1266. DR PDB; 5VSF; X-ray; 1.70 A; A/B=1006-1266. DR PDB; 6BY9; X-ray; 2.30 A; A=672-999. DR PDB; 6MBO; X-ray; 1.59 A; A/B=1006-1266. DR PDB; 6MBP; X-ray; 1.95 A; A/B=1006-1266. DR PDB; 7T7M; X-ray; 2.85 A; A/B/C/D=982-1266. DR PDBsum; 2IGQ; -. DR PDBsum; 2RFI; -. DR PDBsum; 3B7B; -. DR PDBsum; 3B95; -. DR PDBsum; 3FPD; -. DR PDBsum; 3HNA; -. DR PDBsum; 3MO0; -. DR PDBsum; 3MO2; -. DR PDBsum; 3MO5; -. DR PDBsum; 3SW9; -. DR PDBsum; 3SWC; -. DR PDBsum; 4I51; -. DR PDBsum; 5TTG; -. DR PDBsum; 5TUZ; -. DR PDBsum; 5V9J; -. DR PDBsum; 5VSD; -. DR PDBsum; 5VSF; -. DR PDBsum; 6BY9; -. DR PDBsum; 6MBO; -. DR PDBsum; 6MBP; -. DR PDBsum; 7T7M; -. DR AlphaFoldDB; Q9H9B1; -. DR SMR; Q9H9B1; -. DR BioGRID; 122908; 174. DR CORUM; Q9H9B1; -. DR DIP; DIP-34585N; -. DR IntAct; Q9H9B1; 80. DR MINT; Q9H9B1; -. DR STRING; 9606.ENSP00000417980; -. DR BindingDB; Q9H9B1; -. DR ChEMBL; CHEMBL6031; -. DR GuidetoPHARMACOLOGY; 2651; -. DR GlyCosmos; Q9H9B1; 1 site, 3 glycans. DR GlyGen; Q9H9B1; 2 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q9H9B1; -. DR PhosphoSitePlus; Q9H9B1; -. DR SwissPalm; Q9H9B1; -. DR BioMuta; EHMT1; -. DR DMDM; 325511404; -. DR EPD; Q9H9B1; -. DR jPOST; Q9H9B1; -. DR MassIVE; Q9H9B1; -. DR MaxQB; Q9H9B1; -. DR PaxDb; 9606-ENSP00000417980; -. DR PeptideAtlas; Q9H9B1; -. DR ProteomicsDB; 81307; -. [Q9H9B1-1] DR ProteomicsDB; 81308; -. [Q9H9B1-2] DR ProteomicsDB; 81309; -. [Q9H9B1-3] DR ProteomicsDB; 81310; -. [Q9H9B1-4] DR Pumba; Q9H9B1; -. DR ABCD; Q9H9B1; 1 sequenced antibody. DR Antibodypedia; 32511; 559 antibodies from 31 providers. DR DNASU; 79813; -. DR Ensembl; ENST00000371394.6; ENSP00000485945.1; ENSG00000181090.21. [Q9H9B1-2] DR Ensembl; ENST00000460843.6; ENSP00000417980.1; ENSG00000181090.21. [Q9H9B1-1] DR Ensembl; ENST00000462484.5; ENSP00000417328.1; ENSG00000181090.21. [Q9H9B1-4] DR GeneID; 79813; -. DR KEGG; hsa:79813; -. DR MANE-Select; ENST00000460843.6; ENSP00000417980.1; NM_024757.5; NP_079033.4. DR UCSC; uc004coa.3; human. [Q9H9B1-1] DR AGR; HGNC:24650; -. DR CTD; 79813; -. DR DisGeNET; 79813; -. DR GeneCards; EHMT1; -. DR GeneReviews; EHMT1; -. DR HGNC; HGNC:24650; EHMT1. DR HPA; ENSG00000181090; Low tissue specificity. DR MalaCards; EHMT1; -. DR MIM; 607001; gene. DR MIM; 610253; phenotype. DR neXtProt; NX_Q9H9B1; -. DR OpenTargets; ENSG00000181090; -. DR Orphanet; 96147; Kleefstra syndrome due to 9q34 microdeletion. DR Orphanet; 261652; Kleefstra syndrome due to a point mutation. DR PharmGKB; PA134941393; -. DR VEuPathDB; HostDB:ENSG00000181090; -. DR eggNOG; KOG1082; Eukaryota. DR GeneTree; ENSGT00940000156002; -. DR HOGENOM; CLU_005790_3_0_1; -. DR InParanoid; Q9H9B1; -. DR OMA; MPKSIMG; -. DR OrthoDB; 5481936at2759; -. DR PhylomeDB; Q9H9B1; -. DR TreeFam; TF106443; -. DR BioCyc; MetaCyc:HS17627-MONOMER; -. DR BRENDA; 2.1.1.367; 2681. DR BRENDA; 2.1.1.368; 2681. DR PathwayCommons; Q9H9B1; -. DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP). DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines. DR Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation. DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX. DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6. DR SignaLink; Q9H9B1; -. DR SIGNOR; Q9H9B1; -. DR BioGRID-ORCS; 79813; 76 hits in 1180 CRISPR screens. DR ChiTaRS; EHMT1; human. DR EvolutionaryTrace; Q9H9B1; -. DR GeneWiki; EHMT1; -. DR GenomeRNAi; 79813; -. DR Pharos; Q9H9B1; Tchem. DR PRO; PR:Q9H9B1; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9H9B1; Protein. DR Bgee; ENSG00000181090; Expressed in sural nerve and 172 other cell types or tissues. DR ExpressionAtlas; Q9H9B1; baseline and differential. DR GO; GO:0000785; C:chromatin; IBA:GO_Central. DR GO; GO:0016604; C:nuclear body; 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; IEA:Ensembl. DR GO; GO:0046976; F:histone H3K27 methyltransferase activity; ISS:UniProtKB. DR GO; GO:0046974; F:histone H3K9 methyltransferase activity; IDA:UniProtKB. DR GO; GO:0140947; F:histone H3K9me2 methyltransferase activity; IEA:RHEA. DR GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB. DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB. DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB. DR GO; GO:0001222; F:transcription corepressor binding; IPI:ARUK-UCL. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006325; P:chromatin organization; IDA:UniProtKB. DR GO; GO:0006306; P:DNA methylation; ISS:UniProtKB. DR GO; GO:0140718; P:facultative heterochromatin formation; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0018027; P:peptidyl-lysine dimethylation; IDA:UniProtKB. DR GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab. DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB. DR GO; GO:0060992; P:response to fungicide; IEA:Ensembl. DR CDD; cd20905; EHMT_ZBD; 1. DR CDD; cd10535; SET_EHMT1; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR Gene3D; 2.170.270.10; SET domain; 1. DR IDEAL; IID00500; -. 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; IPR038035; SET_EHMT1. DR PANTHER; PTHR46307; G9A, ISOFORM B; 1. DR PANTHER; PTHR46307:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE EHMT1; 1. DR Pfam; PF12796; Ank_2; 2. DR Pfam; PF13637; Ank_4; 1. 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; 7. 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; Q9H9B1; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ANK repeat; KW Chromatin regulator; Chromosome; Disease variant; Intellectual disability; KW Isopeptide bond; Metal-binding; 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:0000269|PubMed:25489052" FT CHAIN 2..1298 FT /note="Histone-lysine N-methyltransferase EHMT1" FT /id="PRO_0000186067" FT REPEAT 737..766 FT /note="ANK 1" FT REPEAT 772..801 FT /note="ANK 2" FT REPEAT 805..834 FT /note="ANK 3" FT REPEAT 838..868 FT /note="ANK 4" FT REPEAT 872..901 FT /note="ANK 5" FT REPEAT 905..934 FT /note="ANK 6" FT REPEAT 938..967 FT /note="ANK 7" FT REPEAT 971..1004 FT /note="ANK 8" FT DOMAIN 1060..1123 FT /note="Pre-SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157" FT DOMAIN 1126..1243 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 144..192 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 211..234 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 339..479 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 644..717 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 905..907 FT /note="Histone H3K9me binding" FT REGION 1162..1181 FT /note="Interaction with histone H3" FT REGION 1242..1245 FT /note="Interaction with histone H3" FT REGION 1274..1298 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 54..94 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 216..234 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 345..361 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 377..395 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 396..415 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 457..477 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1062 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 1062 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 1064 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 1068 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 1068 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT BINDING 1073 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 1075 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 1105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 1105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT BINDING 1109 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 1111 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT BINDING 1115 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT BINDING 1136..1138 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 1173 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 1200..1201 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 1203 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT BINDING 1256 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT BINDING 1257 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 1258 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT BINDING 1263 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT SITE 1155 FT /note="Histone H3K9me binding" FT /evidence="ECO:0000269|PubMed:18264113, FT ECO:0000269|PubMed:20084102" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:25489052" FT MOD_RES 435 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 483 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1004 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1048 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 22 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 22 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 190 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 199 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 231 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 234 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 317 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 327 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 432 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 492 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 559 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 644 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 659 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 684 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 731 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 8..66 FT /note="AVPARGEPQQDCCVKTELLGEETPMAADEGSAEKQAGEAHMAADGETNGSCE FT NSDASSH -> RHLWLPMKAQQRNRQERPTWLRTVRPMGLVKTAMPAVMQMLQSTLRTA FT QGSTPRMAPTH (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_002222" FT VAR_SEQ 67..1298 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_002223" FT VAR_SEQ 795..808 FT /note="AGANIDTCSEDQRT -> FCRLGSPRSRGCLW (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040717" FT VAR_SEQ 809..1298 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040718" FT VAR_SEQ 1181..1184 FT /note="DGEV -> ISSA (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11347906" FT /id="VSP_002224" FT VAR_SEQ 1185..1298 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11347906" FT /id="VSP_002225" FT VARIANT 43 FT /note="A -> V (in a breast cancer sample; somatic mutation; FT dbSNP:rs79514677)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036345" FT VARIANT 388 FT /note="A -> T (in dbSNP:rs11137198)" FT /id="VAR_027642" FT VARIANT 1075 FT /note="C -> Y (in KLEFS1)" FT /evidence="ECO:0000269|PubMed:19264732" FT /id="VAR_069183" FT VARIANT 1173 FT /note="Y -> F (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036346" FT MUTAGEN 874 FT /note="W->A: Abolishes binding to methylated RELAK310me1, FT histone H3K9me1 and H3K9me2." FT /evidence="ECO:0000269|PubMed:21515635" FT MUTAGEN 882 FT /note="E->A: Abolishes binding to methylated RELAK310me1, FT histone H3K9me1 and H3K9me2." FT /evidence="ECO:0000269|PubMed:21515635" FT MUTAGEN 905 FT /note="E->A: Abolishes binding to histone H3K9me." FT /evidence="ECO:0000269|PubMed:18264113" FT MUTAGEN 912 FT /note="W->A: Abolishes binding to methylated RELAK310me1, FT histone H3K9me1 and H3K9me2." FT /evidence="ECO:0000269|PubMed:21515635" FT CONFLICT 555 FT /note="N -> D (in Ref. 3; AAH47504)" FT /evidence="ECO:0000305" FT CONFLICT 561 FT /note="E -> G (in Ref. 1; AAM09024 and 2; BAB14321)" FT /evidence="ECO:0000305" FT HELIX 739..748 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 751..759 FT /evidence="ECO:0007829|PDB:6BY9" FT TURN 769..773 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 776..783 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 786..795 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 809..815 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 819..828 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 842..848 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 852..860 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 876..882 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 886..894 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 909..916 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 919..927 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 942..948 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 952..960 FT /evidence="ECO:0007829|PDB:6BY9" FT STRAND 970..972 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 975..978 FT /evidence="ECO:0007829|PDB:6BY9" FT HELIX 983..994 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1008..1012 FT /evidence="ECO:0007829|PDB:3HNA" FT TURN 1014..1017 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1019..1021 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1025..1031 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1037..1040 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1045..1048 FT /evidence="ECO:0007829|PDB:3HNA" FT HELIX 1056..1058 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1065..1068 FT /evidence="ECO:0007829|PDB:3HNA" FT HELIX 1074..1078 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1096..1098 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1109..1111 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1115..1117 FT /evidence="ECO:0007829|PDB:5TTG" FT HELIX 1120..1122 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1128..1132 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1134..1144 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1151..1155 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1157..1161 FT /evidence="ECO:0007829|PDB:3HNA" FT HELIX 1162..1166 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1174..1177 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1180..1183 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1185..1193 FT /evidence="ECO:0007829|PDB:3HNA" FT HELIX 1195..1198 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1206..1215 FT /evidence="ECO:0007829|PDB:3HNA" FT STRAND 1223..1230 FT /evidence="ECO:0007829|PDB:3HNA" FT HELIX 1244..1250 FT /evidence="ECO:0007829|PDB:3HNA" FT TURN 1251..1253 FT /evidence="ECO:0007829|PDB:3HNA" SQ SEQUENCE 1298 AA; 141466 MW; 071574F3FB3D371E CRC64; MAAADAEAVP ARGEPQQDCC VKTELLGEET PMAADEGSAE KQAGEAHMAA DGETNGSCEN SDASSHANAA KHTQDSARVN PQDGTNTLTR IAENGVSERD SEAAKQNHVT ADDFVQTSVI GSNGYILNKP ALQAQPLRTT STLASSLPGH AAKTLPGGAG KGRTPSAFPQ TPAAPPATLG EGSADTEDRK LPAPGADVKV HRARKTMPKS VVGLHAASKD PREVREARDH KEPKEEINKN ISDFGRQQLL PPFPSLHQSL PQNQCYMATT KSQTACLPFV LAAAVSRKKK RRMGTYSLVP KKKTKVLKQR TVIEMFKSIT HSTVGSKGEK DLGASSLHVN GESLEMDSDE DDSEELEEDD GHGAEQAAAF PTEDSRTSKE SMSEADRAQK MDGESEEEQE SVDTGEEEEG GDESDLSSES SIKKKFLKRK GKTDSPWIKP ARKRRRRSRK KPSGALGSES YKSSAGSAEQ TAPGDSTGYM EVSLDSLDLR VKGILSSQAE GLANGPDVLE TDGLQEVPLC SCRMETPKSR EITTLANNQC MATESVDHEL GRCTNSVVKY ELMRPSNKAP LLVLCEDHRG RMVKHQCCPG CGYFCTAGNF MECQPESSIS HRFHKDCASR VNNASYCPHC GEESSKAKEV TIAKADTTST VTPVPGQEKG SALEGRADTT TGSAAGPPLS EDDKLQGAAS HVPEGFDPTG PAGLGRPTPG LSQGPGKETL ESALIALDSE KPKKLRFHPK QLYFSARQGE LQKVLLMLVD GIDPNFKMEH QNKRSPLHAA AEAGHVDICH MLVQAGANID TCSEDQRTPL MEAAENNHLE AVKYLIKAGA LVDPKDAEGS TCLHLAAKKG HYEVVQYLLS NGQMDVNCQD DGGWTPMIWA TEYKHVDLVK LLLSKGSDIN IRDNEENICL HWAAFSGCVD IAEILLAAKC DLHAVNIHGD SPLHIAAREN RYDCVVLFLS RDSDVTLKNK EGETPLQCAS LNSQVWSALQ MSKALQDSAP DRPSPVERIV SRDIARGYER IPIPCVNAVD SEPCPSNYKY VSQNCVTSPM NIDRNITHLQ YCVCIDDCSS SNCMCGQLSM RCWYDKDGRL LPEFNMAEPP LIFECNHACS CWRNCRNRVV QNGLRARLQL YRTRDMGWGV RSLQDIPPGT FVCEYVGELI SDSEADVREE DSYLFDLDNK DGEVYCIDAR FYGNVSRFIN HHCEPNLVPV RVFMAHQDLR FPRIAFFSTR LIEAGEQLGF DYGERFWDIK GKLFSCRCGS PKCRHSSAAL AQRQASAAQE AQEDGLPDTS SAAAADPL //