EHMT1_HUMAN
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 03-AUG-2022, entry version 213.
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). {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};
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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 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 AlphaFoldDB; Q9H9B1; -.
DR SMR; Q9H9B1; -.
DR BioGRID; 122908; 146.
DR CORUM; Q9H9B1; -.
DR DIP; DIP-34585N; -.
DR IntAct; Q9H9B1; 81.
DR MINT; Q9H9B1; -.
DR STRING; 9606.ENSP00000417980; -.
DR BindingDB; Q9H9B1; -.
DR ChEMBL; CHEMBL6031; -.
DR GuidetoPHARMACOLOGY; 2651; -.
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; Q9H9B1; -.
DR PeptideAtlas; Q9H9B1; -.
DR PRIDE; Q9H9B1; -.
DR ProteomicsDB; 81307; -. [Q9H9B1-1]
DR ProteomicsDB; 81308; -. [Q9H9B1-2]
DR ProteomicsDB; 81309; -. [Q9H9B1-3]
DR ProteomicsDB; 81310; -. [Q9H9B1-4]
DR ABCD; Q9H9B1; 1 sequenced antibody.
DR Antibodypedia; 32511; 524 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 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; LHAHKRE; -.
DR OrthoDB; 753093at2759; -.
DR PhylomeDB; Q9H9B1; -.
DR TreeFam; TF106443; -.
DR BioCyc; MetaCyc:HS17627-MON; -.
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; 70 hits in 1097 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 170 other tissues.
DR ExpressionAtlas; Q9H9B1; baseline and differential.
DR Genevisible; Q9H9B1; HS.
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 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:UniProtKB.
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:0051567; P:histone H3-K9 methylation; IBA:GO_Central.
DR GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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:0051570; P:regulation of histone H3-K9 methylation; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR IDEAL; IID00500; -.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR038035; EHMT1.
DR InterPro; IPR043550; EHMT1/EHMT2.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR46307; PTHR46307; 1.
DR PANTHER; PTHR46307:SF2; PTHR46307:SF2; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 7.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW 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 RELA K310me1,
FT histone H3K9me1 and H3K9me2."
FT /evidence="ECO:0000269|PubMed:21515635"
FT MUTAGEN 882
FT /note="E->A: Abolishes binding to methylated RELA K310me1,
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 RELA K310me1,
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
