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Database: UniProt
Entry: Q96KQ7
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Original site: Q96KQ7 
ID   EHMT2_HUMAN             Reviewed;        1210 AA.
AC   Q96KQ7; B0UZY2; Q14349; Q5JP83; Q5JQ92; Q5JQA1; Q5JQG3; Q6PK06;
AC   Q96MH5; Q96QD0; Q9UQL8; Q9Y331;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   10-APR-2019, entry version 196.
DE   RecName: Full=Histone-lysine N-methyltransferase EHMT2;
DE            EC=2.1.1.-;
DE            EC=2.1.1.43;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM
RP   2), 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
RT   class 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Campbell R.D., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   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.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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
RP   VARIANT 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
RT   project: 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
RT   novel 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
RT   mammalian histone methyltransferase with hyperactivity and specific
RT   selectivity to 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;
RP   RING1; 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-
RT   responsive 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
RT   of 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
RT   the co-repressor molecule CtBP.";
RL   J. Biol. Chem. 281:20120-20128(2006).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION
RP   BY 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
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND IDENTIFICATION
RP   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,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., 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
RP   REST; 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.,
RA   Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J.,
RA   Shi Y.;
RT   "CDYL bridges REST and histone methyltransferases for gene repression
RT   and suppression of cellular transformation.";
RL   Mol. Cell 32:718-726(2008).
RN   [16]
RP   FUNCTION, METHYLATION AT LYS-185, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=18438403; DOI=10.1038/nchembio.88;
RA   Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R.,
RA   Jurkowska R., 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;
RP   GLU-817; 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
RP   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   [19]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a 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, 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.,
RA   Jenuwein T., 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.
RA   Huang J., Dorsey J., Chuikov S., Perez-Burgos L., Zhang X.,
RA   Jenuwein T., 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
RP   SER-246, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [25]
RP   INTERACTION WITH SMARCAD1.
RX   PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036;
RA   Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W.,
RA   Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M.,
RA   Varga-Weisz P., Mermoud J.E.;
RT   "Maintenance of silent chromatin through replication requires SWI/SNF-
RT   like 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
RP   SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome 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.,
RA   Carey M.F., Grunstein M.;
RT   "Histone H3 lysine 56 methylation regulates DNA replication through
RT   its 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
RP   SPECTROMETRY [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.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal 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;
RP   SER-232; SER-242; SER-350 AND THR-555, AND IDENTIFICATION BY MASS
RP   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   [30]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION
RP   BY 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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [31]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219; LYS-229 AND LYS-634,
RP   AND 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-
RT   modification 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
RP   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,
CC       respectively) in euchromatin. H3K9me represents a specific tag for
CC       epigenetic transcriptional repression by recruiting HP1 proteins
CC       to methylated histones. Also mediates monomethylation of 'Lys-56'
CC       of histone H3 (H3K56me1) in G1 phase, leading to promote
CC       interaction between histone H3 and PCNA and regulating DNA
CC       replication. Also weakly methylates 'Lys-27' of histone H3
CC       (H3K27me). Also required for DNA methylation, the histone
CC       methyltransferase activity is not required for DNA methylation,
CC       suggesting that these 2 activities function independently.
CC       Probably targeted to histone H3 by different DNA-binding proteins
CC       like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In
CC       addition to the histone methyltransferase activity, also
CC       methylates non-histone proteins: mediates dimethylation of 'Lys-
CC       373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1,
CC       ERCC6, KLF12 and itself. {ECO:0000269|PubMed:11316813,
CC       ECO:0000269|PubMed:18438403, ECO:0000269|PubMed:20084102,
CC       ECO:0000269|PubMed:20118233, ECO:0000269|PubMed:22387026,
CC       ECO:0000269|PubMed:8457211}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000269|PubMed:11316813,
CC         ECO:0000269|PubMed:20084102};
CC   -!- SUBUNIT: Heterodimer; heterodimerizes with EHMT1/GLP. Interacts
CC       with GFI1B and WIZ. Part of the E2F6.com-1 complex in G0 phase
CC       composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2,
CC       MBLR, L3MBTL2 and YAF2. Part of a complex composed of TRIM28,
CC       HDAC1, HDAC2 and EHMT2. Interacts with UHRF1. Interacts with CDYL.
CC       Interacts with REST only in the presence of CDYL. Part of a
CC       complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and
CC       EHMT2. {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:20084102,
CC       ECO:0000269|PubMed:20118233, ECO:0000269|PubMed:21549307}.
CC   -!- INTERACTION:
CC       Q6P1J9:CDC73; NbExp=3; IntAct=EBI-744366, EBI-930143;
CC       Q9UBC3:DNMT3B; NbExp=2; IntAct=EBI-744366, EBI-80125;
CC       P23771:GATA3; NbExp=20; IntAct=EBI-744366, EBI-6664760;
CC       Q99684:GFI1; NbExp=2; IntAct=EBI-744366, EBI-949368;
CC       Q07120:Gfi1 (xeno); NbExp=3; IntAct=EBI-744366, EBI-4289236;
CC       Q13547:HDAC1; NbExp=7; IntAct=EBI-744366, EBI-301834;
CC       Q92831:KAT2B; NbExp=3; IntAct=EBI-744366, EBI-477430;
CC       O60341-1:KDM1A; NbExp=3; IntAct=EBI-15737402, EBI-15599570;
CC       Q9Y4X4:KLF12; NbExp=3; IntAct=EBI-744366, EBI-750750;
CC       Q13330:MTA1; NbExp=9; IntAct=EBI-744366, EBI-714236;
CC       O94776:MTA2; NbExp=7; IntAct=EBI-744366, EBI-1783035;
CC       Q9BTC8:MTA3; NbExp=18; IntAct=EBI-744366, EBI-2461787;
CC       Q99801-1:NKX3-1; NbExp=3; IntAct=EBI-744366, EBI-16208773;
CC       O60568:PLOD3; NbExp=7; IntAct=EBI-744366, EBI-741582;
CC       Q9NQX1:PRDM5; NbExp=3; IntAct=EBI-744366, EBI-4292031;
CC       Q5JSZ5:PRRC2B; NbExp=2; IntAct=EBI-744366, EBI-744891;
CC       Q9P2R6:RERE; NbExp=3; IntAct=EBI-744366, EBI-948076;
CC       O60315:ZEB2; NbExp=6; IntAct=EBI-744366, EBI-717614;
CC       Q96JM2:ZNF462; NbExp=3; IntAct=EBI-744366, EBI-1210359;
CC       A0A0S2Z5X4:ZNF688; NbExp=3; IntAct=EBI-744366, EBI-16429014;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11316813}.
CC       Chromosome {ECO:0000269|PubMed:11316813}. Note=Associates with
CC       euchromatic 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
CC       levels in fetal liver, thymus, lymph node, spleen and peripheral
CC       blood 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
CC       are arranged in a triangular cluster; some of these Cys residues
CC       contribute to the binding of two zinc ions within the cluster.
CC       {ECO: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
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- CAUTION: While NG36 and G9a were originally thought to derive from
CC       2 separate genes, all G9A transcripts also contain the in frame
CC       coding 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=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=AAH09351.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=AAH18718.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAH20970.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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=Translation N-terminally extended.; Evidence={ECO:0000305};
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   UniGene; Hs.709218; -.
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   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   ProteinModelPortal; Q96KQ7; -.
DR   SMR; Q96KQ7; -.
DR   BioGrid; 116123; 141.
DR   CORUM; Q96KQ7; -.
DR   DIP; DIP-34461N; -.
DR   IntAct; Q96KQ7; 103.
DR   MINT; Q96KQ7; -.
DR   STRING; 9606.ENSP00000364678; -.
DR   BindingDB; Q96KQ7; -.
DR   ChEMBL; CHEMBL6032; -.
DR   GuidetoPHARMACOLOGY; 2652; -.
DR   iPTMnet; Q96KQ7; -.
DR   PhosphoSitePlus; Q96KQ7; -.
DR   BioMuta; EHMT2; -.
DR   DMDM; 116241348; -.
DR   EPD; Q96KQ7; -.
DR   jPOST; Q96KQ7; -.
DR   MaxQB; Q96KQ7; -.
DR   PaxDb; Q96KQ7; -.
DR   PeptideAtlas; Q96KQ7; -.
DR   PRIDE; Q96KQ7; -.
DR   ProteomicsDB; 77102; -.
DR   ProteomicsDB; 77103; -. [Q96KQ7-2]
DR   ProteomicsDB; 77104; -. [Q96KQ7-3]
DR   Ensembl; ENST00000375530; ENSP00000364680; ENSG00000204371. [Q96KQ7-2]
DR   Ensembl; ENST00000375537; ENSP00000364687; ENSG00000204371. [Q96KQ7-1]
DR   Ensembl; ENST00000383372; ENSP00000372863; ENSG00000206376. [Q96KQ7-2]
DR   Ensembl; ENST00000383373; ENSP00000372864; ENSG00000206376. [Q96KQ7-1]
DR   Ensembl; ENST00000420336; ENSP00000396119; ENSG00000238134.
DR   Ensembl; ENST00000420874; ENSP00000411035; ENSG00000236759. [Q96KQ7-2]
DR   Ensembl; ENST00000421926; ENSP00000416957; ENSG00000232045.
DR   Ensembl; ENST00000429506; ENSP00000406110; ENSG00000227333. [Q96KQ7-1]
DR   Ensembl; ENST00000450075; ENSP00000392305; ENSG00000236759. [Q96KQ7-1]
DR   Ensembl; ENST00000450229; ENSP00000400838; ENSG00000227333. [Q96KQ7-2]
DR   GeneID; 10919; -.
DR   KEGG; hsa:10919; -.
DR   UCSC; uc003nxz.3; human. [Q96KQ7-1]
DR   CTD; 10919; -.
DR   DisGeNET; 10919; -.
DR   EuPathDB; HostDB:ENSG00000204371.11; -.
DR   GeneCards; EHMT2; -.
DR   H-InvDB; HIX0166078; -.
DR   H-InvDB; HIX0166345; -.
DR   H-InvDB; HIX0167369; -.
DR   H-InvDB; HIX0184162; -.
DR   HGNC; HGNC:14129; EHMT2.
DR   HPA; HPA050550; -.
DR   HPA; HPA060259; -.
DR   MIM; 604599; gene.
DR   neXtProt; NX_Q96KQ7; -.
DR   OpenTargets; ENSG00000204371; -.
DR   PharmGKB; PA25267; -.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG0666; LUCA.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000159459; -.
DR   HOVERGEN; HBG028394; -.
DR   InParanoid; Q96KQ7; -.
DR   KO; K11420; -.
DR   OrthoDB; 940057at2759; -.
DR   PhylomeDB; Q96KQ7; -.
DR   TreeFam; TF106443; -.
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-8953750; Transcriptional Regulation by E2F6.
DR   SIGNOR; Q96KQ7; -.
DR   ChiTaRS; EHMT2; human.
DR   EvolutionaryTrace; Q96KQ7; -.
DR   GeneWiki; EHMT2; -.
DR   GenomeRNAi; 10919; -.
DR   PRO; PR:Q96KQ7; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000204371; Expressed in 207 organ(s), highest expression level in nucleus accumbens.
DR   ExpressionAtlas; Q96KQ7; baseline and differential.
DR   Genevisible; Q96KQ7; HS.
DR   GO; GO:0000790; C:nuclear 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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009267; P:cellular response to starvation; IDA:MGI.
DR   GO; GO:0006306; P:DNA methylation; ISS:UniProtKB.
DR   GO; GO:0034968; P:histone lysine methylation; IDA:MGI.
DR   GO; GO:0016571; P:histone methylation; IMP:UniProtKB.
DR   GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IDA:UniProtKB.
DR   GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
DR   CDD; cd00204; ANK; 2.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR038034; EHMT2.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   PANTHER; PTHR22884:SF361; PTHR22884:SF361; 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   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; Complete proteome; Isopeptide bond;
KW   Metal-binding; Methylation; Methyltransferase; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transferase; Ubl conjugation; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:19413330,
FT                                ECO:0000244|PubMed:22814378}.
FT   CHAIN         2   1210       Histone-lysine N-methyltransferase EHMT2.
FT                                /FTId=PRO_0000186068.
FT   REPEAT      649    678       ANK 1.
FT   REPEAT      684    713       ANK 2.
FT   REPEAT      717    746       ANK 3.
FT   REPEAT      750    780       ANK 4.
FT   REPEAT      784    813       ANK 5.
FT   REPEAT      817    846       ANK 6.
FT   REPEAT      850    879       ANK 7.
FT   DOMAIN      972   1035       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN     1038   1155       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1164   1180       Post-SET.
FT   REGION      817    819       Histone H3K9me binding. {ECO:0000250}.
FT   REGION     1048   1050       S-adenosyl-L-methionine binding.
FT   REGION     1074   1093       Interaction with histone H3.
FT                                {ECO:0000250}.
FT   REGION     1112   1113       S-adenosyl-L-methionine binding.
FT   REGION     1154   1157       Interaction with histone H3.
FT                                {ECO:0000250}.
FT   COMPBIAS      2     13       Poly-Ala.
FT   COMPBIAS    160    163       Poly-Ala.
FT   COMPBIAS    300    326       Poly-Glu.
FT   METAL       974    974       Zinc 1.
FT   METAL       974    974       Zinc 2.
FT   METAL       976    976       Zinc 1.
FT   METAL       980    980       Zinc 1.
FT   METAL       980    980       Zinc 3.
FT   METAL       985    985       Zinc 1.
FT   METAL       987    987       Zinc 2.
FT   METAL      1017   1017       Zinc 2.
FT   METAL      1017   1017       Zinc 3.
FT   METAL      1021   1021       Zinc 2.
FT   METAL      1023   1023       Zinc 3.
FT   METAL      1027   1027       Zinc 3.
FT   METAL      1115   1115       Zinc 4.
FT   METAL      1168   1168       Zinc 4.
FT   METAL      1170   1170       Zinc 4.
FT   METAL      1175   1175       Zinc 4.
FT   BINDING    1067   1067       Histone H3K9me. {ECO:0000250}.
FT   BINDING    1085   1085       S-adenosyl-L-methionine.
FT   BINDING    1169   1169       S-adenosyl-L-methionine; via amide
FT                                nitrogen.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:19413330,
FT                                ECO:0000244|PubMed:22814378}.
FT   MOD_RES      40     40       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES      44     44       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES      47     47       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     140    140       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     173    173       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     185    185       N6,N6,N6-trimethyllysine; by EHMT2;
FT                                alternate. {ECO:0000269|PubMed:18438403}.
FT   MOD_RES     185    185       N6,N6-dimethyllysine; by EHMT2;
FT                                alternate. {ECO:0000269|PubMed:18438403}.
FT   MOD_RES     232    232       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     242    242       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     246    246       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     350    350       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     412    412       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z148}.
FT   MOD_RES     413    413       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     555    555       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     569    569       Phosphoserine.
FT                                {ECO:0000244|PubMed:17525332}.
FT   MOD_RES    1204   1204       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES    1210   1210       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   CROSSLNK    219    219       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    229    229       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    634    634       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ     195    202       PPVPEKRP -> VSGMGEMG (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_002212.
FT   VAR_SEQ     203   1210       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_002213.
FT   VAR_SEQ     373    406       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_002211.
FT   VARIANT      55     55       T -> N (in dbSNP:rs7887).
FT                                {ECO:0000269|PubMed:11707778,
FT                                ECO:0000269|PubMed:14574404,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|Ref.5}.
FT                                /FTId=VAR_027973.
FT   VARIANT    1165   1165       Y -> F (in dbSNP:rs13919).
FT                                /FTId=VAR_027974.
FT   MUTAGEN     786    786       W->A: Abolishes binding to histone H3K9me
FT                                without affecting the histone
FT                                methyltransferase activity.
FT                                {ECO:0000269|PubMed:18264113}.
FT   MUTAGEN     791    791       W->A: Abolishes binding to histone H3K9me
FT                                without affecting the histone
FT                                methyltransferase activity.
FT                                {ECO:0000269|PubMed:18264113}.
FT   MUTAGEN     794    794       E->A: Abolishes binding to histone H3K9me
FT                                without affecting the histone
FT                                methyltransferase activity.
FT                                {ECO:0000269|PubMed:18264113}.
FT   MUTAGEN     817    817       E->R: Impairs binding to histone H3K9me.
FT                                {ECO:0000269|PubMed:18264113}.
FT   MUTAGEN     824    824       W->A: Abolishes binding to histone H3K9me
FT                                without affecting the histone
FT                                methyltransferase activity.
FT                                {ECO:0000269|PubMed:18264113}.
FT   MUTAGEN     852    852       D->R: Impairs binding to histone H3K9me.
FT                                {ECO:0000269|PubMed:18264113}.
FT   CONFLICT    178    178       P -> S (in Ref. 2; CAC86666).
FT                                {ECO:0000305}.
FT   CONFLICT    985    985       C -> R (in Ref. 2; CAC86666).
FT                                {ECO:0000305}.
FT   CONFLICT    994    994       C -> R (in Ref. 8; CAA49491).
FT                                {ECO:0000305}.
FT   STRAND      920    924       {ECO:0000244|PDB:5VSC}.
FT   TURN        926    929       {ECO:0000244|PDB:5VSC}.
FT   STRAND      931    933       {ECO:0000244|PDB:5VSC}.
FT   STRAND      937    943       {ECO:0000244|PDB:5VSC}.
FT   STRAND      949    952       {ECO:0000244|PDB:5VSC}.
FT   STRAND      957    960       {ECO:0000244|PDB:5VSC}.
FT   HELIX       968    970       {ECO:0000244|PDB:5VSC}.
FT   STRAND      977    980       {ECO:0000244|PDB:3K5K}.
FT   HELIX       986    989       {ECO:0000244|PDB:5VSC}.
FT   STRAND     1008   1010       {ECO:0000244|PDB:5VSC}.
FT   STRAND     1021   1023       {ECO:0000244|PDB:5VSC}.
FT   STRAND     1027   1029       {ECO:0000244|PDB:5VSC}.
FT   HELIX      1032   1034       {ECO:0000244|PDB:5VSC}.
FT   STRAND     1040   1044       {ECO:0000244|PDB:5VSC}.
FT   STRAND     1046   1056       {ECO:0000244|PDB:5VSC}.
FT   STRAND     1063   1067       {ECO:0000244|PDB:5VSC}.
FT   STRAND     1069   1073       {ECO:0000244|PDB:5VSC}.
FT   HELIX      1074   1077       {ECO:0000244|PDB:5VSC}.
FT   STRAND     1086   1089       {ECO:0000244|PDB:5VSC}.
FT   STRAND     1092   1095       {ECO:0000244|PDB:5JIY}.
FT   STRAND     1097   1105       {ECO:0000244|PDB:5VSC}.
FT   HELIX      1107   1110       {ECO:0000244|PDB:5VSC}.
FT   STRAND     1118   1127       {ECO:0000244|PDB:5VSC}.
FT   STRAND     1135   1142       {ECO:0000244|PDB:5VSC}.
FT   HELIX      1156   1162       {ECO:0000244|PDB:5VSC}.
FT   TURN       1163   1165       {ECO:0000244|PDB:5VSC}.
FT   STRAND     1176   1178       {ECO:0000244|PDB:5VSC}.
FT   HELIX      1179   1189       {ECO:0000244|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
//
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