EHMT2_HUMAN
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 03-AUG-2022, entry version 216.
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 CATALYTIC ACTIVITY, FUNCTION, 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 {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). {ECO:0000250|UniProtKB:Q9Z148,
CC ECO:0000269|PubMed:12004135, ECO:0000269|PubMed:16688220,
CC ECO:0000269|PubMed:16702210, ECO:0000269|PubMed:19056828,
CC ECO:0000269|PubMed:19061646, 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
CC regions. Does not associate with heterochromatin.
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};
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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 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 AlphaFoldDB; Q96KQ7; -.
DR SMR; Q96KQ7; -.
DR BioGRID; 116123; 283.
DR CORUM; Q96KQ7; -.
DR DIP; DIP-34461N; -.
DR IntAct; Q96KQ7; 155.
DR MINT; Q96KQ7; -.
DR STRING; 9606.ENSP00000364678; -.
DR BindingDB; Q96KQ7; -.
DR ChEMBL; CHEMBL6032; -.
DR GuidetoPHARMACOLOGY; 2652; -.
DR iPTMnet; Q96KQ7; -.
DR MetOSite; Q96KQ7; -.
DR PhosphoSitePlus; Q96KQ7; -.
DR BioMuta; EHMT2; -.
DR DMDM; 116241348; -.
DR EPD; Q96KQ7; -.
DR jPOST; Q96KQ7; -.
DR MassIVE; Q96KQ7; -.
DR MaxQB; Q96KQ7; -.
DR PaxDb; Q96KQ7; -.
DR PeptideAtlas; Q96KQ7; -.
DR PRIDE; Q96KQ7; -.
DR ProteomicsDB; 77102; -. [Q96KQ7-1]
DR ProteomicsDB; 77103; -. [Q96KQ7-2]
DR ProteomicsDB; 77104; -. [Q96KQ7-3]
DR ABCD; Q96KQ7; 2 sequenced antibodies.
DR Antibodypedia; 27888; 371 antibodies from 39 providers.
DR DNASU; 10919; -.
DR Ensembl; ENST00000375530.8; ENSP00000364680.4; ENSG00000204371.11. [Q96KQ7-2]
DR Ensembl; ENST00000375537.8; ENSP00000364687.4; ENSG00000204371.11. [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 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; 753093at2759; -.
DR PhylomeDB; Q96KQ7; -.
DR TreeFam; TF106443; -.
DR BioCyc; MetaCyc:HS06313-MON; -.
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; 101 hits in 1100 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 97 other tissues.
DR ExpressionAtlas; Q96KQ7; baseline and differential.
DR Genevisible; Q96KQ7; HS.
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 methyltransferase activity (H3-K27 specific); ISS:UniProtKB.
DR GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); ISS:UniProtKB.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:MGI.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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:0070734; P:histone H3-K27 methylation; IEA:Ensembl.
DR GO; GO:0051567; P:histone H3-K9 methylation; IBA:GO_Central.
DR GO; GO:0034968; P:histone lysine methylation; IDA:MGI.
DR GO; GO:0016571; P:histone methylation; IMP:UniProtKB.
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:0051569; P:regulation of histone H3-K4 methylation; IEA:Ensembl.
DR GO; GO:0051570; P:regulation of histone H3-K9 methylation; IBA:GO_Central.
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 Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR IDEAL; IID00250; -.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR043550; EHMT1/EHMT2.
DR InterPro; IPR038034; EHMT2.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR46307; PTHR46307; 1.
DR PANTHER; PTHR46307:SF1; PTHR46307:SF1; 1.
DR Pfam; PF12796; Ank_2; 3.
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; SSF48403; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW 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 1008..1010
FT /evidence="ECO:0007829|PDB:5VSC"
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..1095
FT /evidence="ECO:0007829|PDB:5JIY"
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
