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Database: UniProt
Entry: Q9H9B1
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Original site: Q9H9B1 
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   13-FEB-2019, entry version 194.
DE   RecName: Full=Histone-lysine N-methyltransferase EHMT1;
DE            EC=2.1.1.-;
DE            EC=2.1.1.43;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
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   [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.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   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.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   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.,
RA   Rogers J., 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
RP   SEQUENCE [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
RT   project: 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;
RP   BAT8; 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-
RT   responsive 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
RP   TISSUE 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.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large 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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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
RT   1 (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
RT   the 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,
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   [12]
RP   INTERACTION WITH CDYL AND REST, AND IDENTIFICATION IN A COMPLEX WITH
RP   REST; 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.,
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   [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
RT   and 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.,
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   [16]
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   [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.,
RA   Buerckstuemmer T., 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   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.,
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   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-1004 AND
RP   SER-1048, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, 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   [21]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-432, AND IDENTIFICATION BY
RP   MASS 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   [22]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22, AND IDENTIFICATION BY
RP   MASS 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   [23]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-234, AND IDENTIFICATION BY
RP   MASS 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   [24]
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.,
RA   Arnesen T.;
RT   "Biochemical and cellular analysis of Ogden syndrome reveals
RT   downstream Nt-acetylation defects.";
RL   Hum. Mol. Genet. 24:1956-1976(2015).
RN   [25]
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
RT   replication stress reveals novel small ubiquitin-like modified target
RT   proteins and acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [26]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-190; LYS-199;
RP   LYS-231; LYS-234; LYS-317; LYS-327; LYS-432; LYS-492; LYS-559;
RP   LYS-644; LYS-659; LYS-684 AND LYS-731, AND IDENTIFICATION BY MASS
RP   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   [27]
RP   X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 765-999 IN COMPLEX WITH
RP   HISTONE 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   [28]
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.,
RA   Zhang X., Bedford M.T., Shinkai Y., Snyder J.P., Cheng X.;
RT   "Adding a lysine mimic in the design of potent inhibitors of histone
RT   lysine methyltransferases.";
RL   J. Mol. Biol. 400:1-7(2010).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 982-1266 IN COMPLEX WITH
RP   HISTONE 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   [30]
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.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
RN   [31]
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.,
RA   Turner A., Wilson M., McGaughran J., Rauch A., Zenker M., Adam M.P.,
RA   Innes M., Davies C., Lopez A.G., Casalone R., Weber A., Brueton L.A.,
RA   Navarro A.D., Bralo M.P., Venselaar H., Stegmann S.P., Yntema H.G.,
RA   van Bokhoven H., Brunner H.G.;
RT   "Further clinical and molecular delineation of the 9q subtelomeric
RT   deletion syndrome supports a major contribution of EHMT1
RT   haploinsufficiency to the 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,
CC       respectively) in euchromatin. H3K9me represents a specific tag for
CC       epigenetic transcriptional repression by recruiting HP1 proteins
CC       to methylated histones. Also weakly methylates 'Lys-27' of histone
CC       H3 (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. During G0 phase, it probably
CC       contributes to silencing of MYC- and E2F-responsive genes,
CC       suggesting a role in G0/G1 transition in cell cycle. In addition
CC       to the histone methyltransferase activity, also methylates non-
CC       histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53.
CC       {ECO:0000269|PubMed:12004135, ECO:0000269|PubMed:20118233}.
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:12004135};
CC   -!- ACTIVITY REGULATION: Methyltransferase activity is inhibited by
CC       BIX-01294. Efficiently inhibited by compound E72, a BIX-01294
CC       derivative in which the diazepane ring and the benzyl are replaced
CC       with a 3-dimethylaminopropyl and a 5-aminopentyl group at sites B
CC       and C, respectively. {ECO:0000269|PubMed:20434463}.
CC   -!- SUBUNIT: Heterodimer; heterodimerizes with EHMT2. Interacts with
CC       WIZ and EHMT2. Part of the E2F6.com-1 complex in G0 phase composed
CC       of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR,
CC       L3MBTL2 and YAF2. Interacts (via ANK repeats) with RELA (when
CC       monomethylated at 'Lys-310'). Interacts with MPHOSPH8. Interacts
CC       with CDYL. Interacts with REST only in the presence of CDYL. Part
CC       of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and
CC       EHMT2. {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   -!- INTERACTION:
CC       Q99549:MPHOSPH8; NbExp=3; IntAct=EBI-766087, EBI-2653928;
CC       Q04206:RELA; NbExp=3; IntAct=EBI-766087, EBI-73886;
CC       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
CC         isoforms.;
CC       Name=1;
CC         IsoId=Q9H9B1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H9B1-2; Sequence=VSP_002222, VSP_002223;
CC         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay.;
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.
CC       {ECO:0000269|PubMed:11347906}.
CC   -!- DOMAIN: The ANK repeats recognize and bind RELA subunit of NF-
CC       kappa-B, when RELA is monomethylated at 'Lys-310' (By similarity).
CC       They also specifically recognize and bind H3K9me1 and H3K9me2.
CC       {ECO:0000250, 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
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   -!- DISEASE: Kleefstra syndrome 1 (KLEFS1) [MIM:610253]: A form of
CC       Kleefstra syndrome, an autosomal dominant disease characterized by
CC       variable mental retardation, psychomotor developmental delay,
CC       seizures, behavioral abnormalities, and facial dysmorphisms.
CC       KLEFS1 patients additionally manifest brachy(micro)cephaly,
CC       congenital heart defects, and urogenital defects.
CC       {ECO:0000269|PubMed:16826528, ECO:0000269|PubMed:19264732}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry (PubMed:16826528). 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
CC       genes in the 9q34.3 region contribute to the syndrome observed in
CC       deletion cases, EHMT1 seems to be the major determinant of the
CC       core disease phenotype (PubMed:19264732).
CC       {ECO:0000269|PubMed:16826528, ECO:0000269|PubMed:19264732}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       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};
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   UniGene; Hs.495511; -.
DR   UniGene; Hs.721002; -.
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   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   ProteinModelPortal; Q9H9B1; -.
DR   SMR; Q9H9B1; -.
DR   BioGrid; 122908; 54.
DR   CORUM; Q9H9B1; -.
DR   DIP; DIP-34585N; -.
DR   IntAct; Q9H9B1; 34.
DR   MINT; Q9H9B1; -.
DR   STRING; 9606.ENSP00000417980; -.
DR   BindingDB; Q9H9B1; -.
DR   ChEMBL; CHEMBL6031; -.
DR   GuidetoPHARMACOLOGY; 2651; -.
DR   iPTMnet; Q9H9B1; -.
DR   PhosphoSitePlus; Q9H9B1; -.
DR   BioMuta; EHMT1; -.
DR   DMDM; 325511404; -.
DR   EPD; Q9H9B1; -.
DR   jPOST; Q9H9B1; -.
DR   MaxQB; Q9H9B1; -.
DR   PaxDb; Q9H9B1; -.
DR   PeptideAtlas; Q9H9B1; -.
DR   PRIDE; Q9H9B1; -.
DR   ProteomicsDB; 81307; -.
DR   ProteomicsDB; 81308; -. [Q9H9B1-2]
DR   ProteomicsDB; 81309; -. [Q9H9B1-3]
DR   ProteomicsDB; 81310; -. [Q9H9B1-4]
DR   Ensembl; ENST00000371394; ENSP00000485945; ENSG00000181090. [Q9H9B1-2]
DR   Ensembl; ENST00000460843; ENSP00000417980; ENSG00000181090. [Q9H9B1-1]
DR   Ensembl; ENST00000462484; ENSP00000417328; ENSG00000181090. [Q9H9B1-4]
DR   GeneID; 79813; -.
DR   KEGG; hsa:79813; -.
DR   UCSC; uc004coa.3; human. [Q9H9B1-1]
DR   CTD; 79813; -.
DR   DisGeNET; 79813; -.
DR   EuPathDB; HostDB:ENSG00000181090.17; -.
DR   GeneCards; EHMT1; -.
DR   GeneReviews; EHMT1; -.
DR   HGNC; HGNC:24650; EHMT1.
DR   HPA; HPA060022; -.
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   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG0666; LUCA.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000156002; -.
DR   HOVERGEN; HBG028394; -.
DR   InParanoid; Q9H9B1; -.
DR   KO; K11420; -.
DR   OrthoDB; 753093at2759; -.
DR   PhylomeDB; Q9H9B1; -.
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-6804760; Regulation of TP53 Activity through Methylation.
DR   Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR   ChiTaRS; EHMT1; human.
DR   EvolutionaryTrace; Q9H9B1; -.
DR   GeneWiki; EHMT1; -.
DR   GenomeRNAi; 79813; -.
DR   PRO; PR:Q9H9B1; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000181090; Expressed in 199 organ(s), highest expression level in testis.
DR   ExpressionAtlas; Q9H9B1; baseline and differential.
DR   Genevisible; Q9H9B1; HS.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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: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:0016571; P:histone methylation; IDA: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; IEA:Ensembl.
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:0060992; P:response to fungicide; IEA:Ensembl.
DR   CDD; cd00204; ANK; 1.
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; IPR038035; EHMT1.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   PANTHER; PTHR22884:SF364; PTHR22884:SF364; 1.
DR   Pfam; PF12796; Ank_2; 2.
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   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; Disease mutation;
KW   Isopeptide bond; Mental retardation; Metal-binding; Methyltransferase;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transferase; Ubl conjugation; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:25489052}.
FT   CHAIN         2   1298       Histone-lysine N-methyltransferase EHMT1.
FT                                /FTId=PRO_0000186067.
FT   REPEAT      737    766       ANK 1.
FT   REPEAT      772    801       ANK 2.
FT   REPEAT      805    834       ANK 3.
FT   REPEAT      838    868       ANK 4.
FT   REPEAT      872    901       ANK 5.
FT   REPEAT      905    934       ANK 6.
FT   REPEAT      938    967       ANK 7.
FT   REPEAT      971   1004       ANK 8.
FT   DOMAIN     1060   1123       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN     1126   1243       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      905    907       Histone H3K9me binding.
FT   REGION     1136   1138       S-adenosyl-L-methionine binding.
FT   REGION     1162   1181       Interaction with histone H3.
FT   REGION     1200   1201       S-adenosyl-L-methionine binding.
FT   REGION     1242   1245       Interaction with histone H3.
FT   COMPBIAS    406    409       Poly-Glu.
FT   COMPBIAS    442    449       Poly-Arg.
FT   COMPBIAS   1292   1295       Poly-Ala.
FT   METAL      1062   1062       Zinc 1.
FT   METAL      1062   1062       Zinc 2.
FT   METAL      1064   1064       Zinc 1.
FT   METAL      1068   1068       Zinc 1.
FT   METAL      1068   1068       Zinc 3.
FT   METAL      1073   1073       Zinc 1.
FT   METAL      1075   1075       Zinc 2.
FT   METAL      1105   1105       Zinc 2.
FT   METAL      1105   1105       Zinc 3.
FT   METAL      1109   1109       Zinc 2.
FT   METAL      1111   1111       Zinc 3.
FT   METAL      1115   1115       Zinc 3.
FT   METAL      1203   1203       Zinc 4.
FT   METAL      1256   1256       Zinc 4.
FT   METAL      1258   1258       Zinc 4.
FT   METAL      1263   1263       Zinc 4.
FT   BINDING    1155   1155       Histone H3K9me.
FT                                {ECO:0000269|PubMed:18264113,
FT                                ECO:0000269|PubMed:20084102}.
FT   BINDING    1173   1173       S-adenosyl-L-methionine.
FT   BINDING    1257   1257       S-adenosyl-L-methionine; via amide
FT                                nitrogen.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000269|PubMed:25489052}.
FT   MOD_RES     435    435       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     483    483       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1004   1004       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1048   1048       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   CROSSLNK     22     22       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate. {ECO:0000244|PubMed:25114211}.
FT   CROSSLNK     22     22       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate. {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    190    190       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    199    199       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    231    231       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    234    234       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:25772364,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    317    317       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    327    327       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    432    432       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25218447,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    492    492       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    559    559       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    644    644       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    659    659       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    684    684       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    731    731       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ       8     66       AVPARGEPQQDCCVKTELLGEETPMAADEGSAEKQAGEAHM
FT                                AADGETNGSCENSDASSH -> RHLWLPMKAQQRNRQERPT
FT                                WLRTVRPMGLVKTAMPAVMQMLQSTLRTAQGSTPRMAPTH
FT                                (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_002222.
FT   VAR_SEQ      67   1298       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_002223.
FT   VAR_SEQ     795    808       AGANIDTCSEDQRT -> FCRLGSPRSRGCLW (in
FT                                isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_040717.
FT   VAR_SEQ     809   1298       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_040718.
FT   VAR_SEQ    1181   1184       DGEV -> ISSA (in isoform 3).
FT                                {ECO:0000303|PubMed:11347906}.
FT                                /FTId=VSP_002224.
FT   VAR_SEQ    1185   1298       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:11347906}.
FT                                /FTId=VSP_002225.
FT   VARIANT      43     43       A -> V (in a breast cancer sample;
FT                                somatic mutation; dbSNP:rs79514677).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036345.
FT   VARIANT     388    388       A -> T (in dbSNP:rs11137198).
FT                                /FTId=VAR_027642.
FT   VARIANT    1075   1075       C -> Y (in KLEFS1).
FT                                {ECO:0000269|PubMed:19264732}.
FT                                /FTId=VAR_069183.
FT   VARIANT    1173   1173       Y -> F (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036346.
FT   MUTAGEN     905    905       E->A: Abolishes binding to histone
FT                                H3K9me. {ECO:0000269|PubMed:18264113}.
FT   CONFLICT    555    555       N -> D (in Ref. 3; AAH47504).
FT                                {ECO:0000305}.
FT   CONFLICT    561    561       E -> G (in Ref. 1; AAM09024 and 2;
FT                                BAB14321). {ECO:0000305}.
FT   HELIX       739    748       {ECO:0000244|PDB:6BY9}.
FT   HELIX       751    759       {ECO:0000244|PDB:6BY9}.
FT   TURN        769    773       {ECO:0000244|PDB:6BY9}.
FT   HELIX       776    783       {ECO:0000244|PDB:6BY9}.
FT   HELIX       786    795       {ECO:0000244|PDB:6BY9}.
FT   HELIX       809    815       {ECO:0000244|PDB:6BY9}.
FT   HELIX       819    828       {ECO:0000244|PDB:6BY9}.
FT   HELIX       842    848       {ECO:0000244|PDB:6BY9}.
FT   HELIX       852    860       {ECO:0000244|PDB:6BY9}.
FT   HELIX       876    882       {ECO:0000244|PDB:6BY9}.
FT   HELIX       886    894       {ECO:0000244|PDB:6BY9}.
FT   HELIX       909    916       {ECO:0000244|PDB:6BY9}.
FT   HELIX       919    927       {ECO:0000244|PDB:6BY9}.
FT   HELIX       942    948       {ECO:0000244|PDB:6BY9}.
FT   HELIX       952    960       {ECO:0000244|PDB:6BY9}.
FT   STRAND      970    972       {ECO:0000244|PDB:6BY9}.
FT   HELIX       975    978       {ECO:0000244|PDB:6BY9}.
FT   HELIX       983    994       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1008   1012       {ECO:0000244|PDB:3HNA}.
FT   TURN       1014   1017       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1019   1021       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1025   1031       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1037   1040       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1045   1048       {ECO:0000244|PDB:3HNA}.
FT   HELIX      1056   1058       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1065   1068       {ECO:0000244|PDB:3HNA}.
FT   HELIX      1074   1078       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1096   1098       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1109   1111       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1115   1117       {ECO:0000244|PDB:5TTG}.
FT   HELIX      1120   1122       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1128   1132       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1134   1144       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1151   1155       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1157   1161       {ECO:0000244|PDB:3HNA}.
FT   HELIX      1162   1166       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1174   1177       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1180   1183       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1185   1193       {ECO:0000244|PDB:3HNA}.
FT   HELIX      1195   1198       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1206   1215       {ECO:0000244|PDB:3HNA}.
FT   STRAND     1223   1230       {ECO:0000244|PDB:3HNA}.
FT   HELIX      1244   1250       {ECO:0000244|PDB:3HNA}.
FT   TURN       1251   1253       {ECO:0000244|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
//
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