Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Histone-lysine N-methyltransferase EHMT1 (EC 2.1.1.-) (EC 2.1.1.43) (Euchromatic histone-lysine N-methyltransferase 1) (Eu-HMTase1) (G9a-like protein 1) (GLP) (GLP1) (Histone H3-K9 methyltransferase 5) (H3-K9-HMTase 5) (Lysine N-methyltransferase 1D)

 EHMT1_HUMAN             Reviewed;        1298 AA.
Q9H9B1; B1AQ58; B1AQ59; Q86X08; Q8TCN7; Q96F53; Q96JF1; Q96KH4;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
08-MAR-2011, sequence version 4.
25-OCT-2017, entry version 182.
RecName: Full=Histone-lysine N-methyltransferase EHMT1;
EC=2.1.1.-;
EC=2.1.1.43;
AltName: Full=Euchromatic histone-lysine N-methyltransferase 1;
Short=Eu-HMTase1;
AltName: Full=G9a-like protein 1;
Short=GLP;
Short=GLP1;
AltName: Full=Histone H3-K9 methyltransferase 5;
Short=H3-K9-HMTase 5;
AltName: Full=Lysine N-methyltransferase 1D;
Name=EHMT1; Synonyms=EUHMTASE1, GLP, KIAA1876, KMT1D;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 583-1298 (ISOFORM 1).
TISSUE=Brain, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 32-1298 (ISOFORM 1), FUNCTION, CATALYTIC
ACTIVITY, AND IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA;
BAT8; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
TISSUE=Cervix carcinoma;
PubMed=12004135; DOI=10.1126/science.1069861;
Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.;
"A complex with chromatin modifiers that occupies E2F- and Myc-
responsive genes in G0 cells.";
Science 296:1132-1136(2002).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 382-1298 (ISOFORM 1).
TISSUE=Brain;
Tsuritani K., Ukai Y., Yajima Y., Amemiya C., Yoshimoto M.;
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 382-1298 (ISOFORM 3), AND
TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=11347906; DOI=10.1093/dnares/8.2.85;
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 8:85-95(2001).
[7]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1089-1298 (ISOFORM 1).
TISSUE=Lymph node;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[9]
INVOLVEMENT IN KLESTS.
PubMed=16826528; DOI=10.1086/505693;
Kleefstra T., Brunner H.G., Amiel J., Oudakker A.R., Nillesen W.M.,
Magee A., Genevieve D., Cormier-Daire V., van Esch H., Fryns J.-P.,
Hamel B.C.J., Sistermans E.A., de Vries B.B.A., van Bokhoven H.;
"Loss-of-function mutations in euchromatin histone methyl transferase
1 (EHMT1) cause the 9q34 subtelomeric deletion syndrome.";
Am. J. Hum. Genet. 79:370-377(2006).
[10]
INTERACTION WITH WIZ AND EHMT2.
PubMed=16702210; DOI=10.1074/jbc.M603087200;
Ueda J., Tachibana M., Ikura T., Shinkai Y.;
"Zinc finger protein Wiz links G9a/GLP histone methyltransferases to
the co-repressor molecule CtBP.";
J. Biol. Chem. 281:20120-20128(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[12]
INTERACTION WITH CDYL AND REST, AND IDENTIFICATION IN A COMPLEX WITH
REST; CDYL; SETB1; EHMT2 AND WIZ.
PubMed=19061646; DOI=10.1016/j.molcel.2008.10.025;
Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B.,
Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J.,
Shi Y.;
"CDYL bridges REST and histone methyltransferases for gene repression
and suppression of cellular transformation.";
Mol. Cell 32:718-726(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
INTERACTION WITH MPHOSPH8.
PubMed=20871592; DOI=10.1038/emboj.2010.239;
Kokura K., Sun L., Bedford M.T., Fang J.;
"Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing
and promotes tumour cell motility and invasion.";
EMBO J. 29:3673-3687(2010).
[15]
FUNCTION, AND INTERACTION WITH TP53.
PubMed=20118233; DOI=10.1074/jbc.M109.062588;
Huang J., Dorsey J., Chuikov S., Perez-Burgos L., Zhang X.,
Jenuwein T., Reinberg D., Berger S.L.;
"G9a and Glp methylate lysine 373 in the tumor suppressor p53.";
J. Biol. Chem. 285:9636-9641(2010).
[16]
ERRATUM.
Huang J., Dorsey J., Chuikov S., Perez-Burgos L., Zhang X.,
Jenuwein T., Reinberg D., Berger S.L.;
J. Biol. Chem. 285:18122-18122(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-1004 AND
SER-1048, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-432, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-234, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-234 AND LYS-731, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-190; LYS-199;
LYS-231; LYS-234; LYS-317; LYS-327; LYS-432; LYS-492; LYS-559;
LYS-644; LYS-659; LYS-684 AND LYS-731, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[26]
ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
PubMed=25489052; DOI=10.1093/hmg/ddu611;
Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K.,
Arnesen T.;
"Biochemical and cellular analysis of Ogden syndrome reveals
downstream Nt-acetylation defects.";
Hum. Mol. Genet. 24:1956-1976(2015).
[27]
X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 765-999 IN COMPLEX WITH
HISTONE H3, DOMAIN ANK REPEATS, AND MUTAGENESIS OF GLU-905.
PubMed=18264113; DOI=10.1038/nsmb.1384;
Collins R.E., Northrop J.P., Horton J.R., Lee D.Y., Zhang X.,
Stallcup M.R., Cheng X.;
"The ankyrin repeats of G9a and GLP histone methyltransferases are
mono-and dimethyllysine binding modules.";
Nat. Struct. Mol. Biol. 15:245-250(2008).
[28]
X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 982-1266 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE; ZINC ION AND E72 INHIBITOR, AND ENZYME
REGULATION.
PubMed=20434463; DOI=10.1016/j.jmb.2010.04.048;
Chang Y., Ganesh T., Horton J.R., Spannhoff A., Liu J., Sun A.,
Zhang X., Bedford M.T., Shinkai Y., Snyder J.P., Cheng X.;
"Adding a lysine mimic in the design of potent inhibitors of histone
lysine methyltransferases.";
J. Mol. Biol. 400:1-7(2010).
[29]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 982-1266 IN COMPLEX WITH
HISTONE H3; S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS.
PubMed=20084102; DOI=10.1371/journal.pone.0008570;
Wu H., Min J., Lunin V.V., Antoshenko T., Dombrovski L., Zeng H.,
Allali-Hassani A., Campagna-Slater V., Vedadi M., Arrowsmith C.H.,
Plotnikov A.N., Schapira M.;
"Structural biology of human H3K9 methyltransferases.";
PLoS ONE 5:E8570-E8570(2010).
[30]
VARIANTS [LARGE SCALE ANALYSIS] VAL-43 AND PHE-1173.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[31]
VARIANT KLESTS TYR-1075.
PubMed=19264732; DOI=10.1136/jmg.2008.062950;
Kleefstra T., van Zelst-Stams W.A., Nillesen W.M., Cormier-Daire V.,
Houge G., Foulds N., van Dooren M., Willemsen M.H., Pfundt R.,
Turner A., Wilson M., McGaughran J., Rauch A., Zenker M., Adam M.P.,
Innes M., Davies C., Lopez A.G., Casalone R., Weber A., Brueton L.A.,
Navarro A.D., Bralo M.P., Venselaar H., Stegmann S.P., Yntema H.G.,
van Bokhoven H., Brunner H.G.;
"Further clinical and molecular delineation of the 9q subtelomeric
deletion syndrome supports a major contribution of EHMT1
haploinsufficiency to the core phenotype.";
J. Med. Genet. 46:598-606(2009).
-!- FUNCTION: Histone methyltransferase that specifically mono- and
dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2,
respectively) in euchromatin. H3K9me represents a specific tag for
epigenetic transcriptional repression by recruiting HP1 proteins
to methylated histones. Also weakly methylates 'Lys-27' of histone
H3 (H3K27me). Also required for DNA methylation, the histone
methyltransferase activity is not required for DNA methylation,
suggesting that these 2 activities function independently.
Probably targeted to histone H3 by different DNA-binding proteins
like E2F6, MGA, MAX and/or DP1. During G0 phase, it probably
contributes to silencing of MYC- and E2F-responsive genes,
suggesting a role in G0/G1 transition in cell cycle. In addition
to the histone methyltransferase activity, also methylates non-
histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53.
{ECO:0000269|PubMed:12004135, ECO:0000269|PubMed:20118233}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:12004135}.
-!- ENZYME REGULATION: Methyltransferase activity is inhibited by BIX-
01294. Efficiently inhibited by compound E72, a BIX-01294
derivative in which the diazepane ring and the benzyl are replaced
with a 3-dimethylaminopropyl and a 5-aminopentyl group at sites B
and C, respectively. {ECO:0000269|PubMed:20434463}.
-!- SUBUNIT: Heterodimer; heterodimerizes with EHMT2. Interacts with
WIZ and EHMT2. Part of the E2F6.com-1 complex in G0 phase composed
of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR,
L3MBTL2 and YAF2. Interacts (via ANK repeats) with RELA (when
monomethylated at 'Lys-310'). Interacts with MPHOSPH8. Interacts
with CDYL. Interacts with REST only in the presence of CDYL. Part
of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and
EHMT2. {ECO:0000269|PubMed:12004135, ECO:0000269|PubMed:16702210,
ECO:0000269|PubMed:18264113, ECO:0000269|PubMed:19061646,
ECO:0000269|PubMed:20084102, ECO:0000269|PubMed:20118233,
ECO:0000269|PubMed:20434463, ECO:0000269|PubMed:20871592}.
-!- INTERACTION:
Q99549:MPHOSPH8; NbExp=3; IntAct=EBI-766087, EBI-2653928;
Q04206:RELA; NbExp=3; IntAct=EBI-766087, EBI-73886;
Q04207:Rela (xeno); NbExp=5; IntAct=EBI-766087, EBI-644400;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates with
euchromatic regions.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1;
IsoId=Q9H9B1-1; Sequence=Displayed;
Name=2;
IsoId=Q9H9B1-2; Sequence=VSP_002222, VSP_002223;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=3;
IsoId=Q9H9B1-3; Sequence=VSP_002224, VSP_002225;
Name=4;
IsoId=Q9H9B1-4; Sequence=VSP_040717, VSP_040718;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:11347906}.
-!- DOMAIN: The ANK repeats recognize and bind RELA subunit of NF-
kappa-B, when RELA is monomethylated at 'Lys-310' (By similarity).
They also specifically recognize and bind H3K9me1 and H3K9me2.
{ECO:0000250, ECO:0000269|PubMed:18264113}.
-!- DOMAIN: The SET domain mediates interaction with WIZ.
{ECO:0000269|PubMed:18264113}.
-!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
are arranged in a triangular cluster; some of these Cys residues
contribute to the binding of two zinc ions within the cluster.
{ECO:0000269|PubMed:18264113}.
-!- DISEASE: Kleefstra syndrome (KLESTS) [MIM:610253]: A syndrome
characterized by severe mental retardation, hypotonia,
brachy(micro)cephaly, and facial dysmorphisms. Additionally,
congenital heart defects, urogenital defects, epilepsy and
behavioral problems are frequently observed.
{ECO:0000269|PubMed:16826528, ECO:0000269|PubMed:19264732}.
Note=The disease is caused by mutations affecting the gene
represented in this entry (PubMed:16826528). The syndrome can be
either caused by intragenic EHMT1 mutations leading to
haploinsufficiency of the EHMT1 gene or by a submicroscopic 9q34.3
deletion. Although it is not known if and to what extent other
genes in the 9q34.3 region contribute to the syndrome observed in
deletion cases, EHMT1 seems to be the major determinant of the
core disease phenotype (PubMed:19264732).
{ECO:0000269|PubMed:16826528, ECO:0000269|PubMed:19264732}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
-!- SEQUENCE CAUTION:
Sequence=BAB14321.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
Sequence=CAD28534.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=CAH71077.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI17354.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK022941; BAB14321.1; ALT_SEQ; mRNA.
EMBL; AL590627; CAI17354.1; ALT_SEQ; Genomic_DNA.
EMBL; AL611925; CAI17354.1; JOINED; Genomic_DNA.
EMBL; AL590627; CAI17355.1; -; Genomic_DNA.
EMBL; AL611925; CAI17355.1; JOINED; Genomic_DNA.
EMBL; AL611925; CAH71076.1; -; Genomic_DNA.
EMBL; AL590627; CAH71076.1; JOINED; Genomic_DNA.
EMBL; AL611925; CAH71077.1; ALT_SEQ; Genomic_DNA.
EMBL; AL590627; CAH71077.1; JOINED; Genomic_DNA.
EMBL; BC011608; AAH11608.2; -; mRNA.
EMBL; BC047504; AAH47504.1; -; mRNA.
EMBL; AY083210; AAM09024.1; -; mRNA.
EMBL; AB028932; BAB56104.1; -; mRNA.
EMBL; AB058779; BAB47505.2; -; mRNA.
EMBL; AL713772; CAD28534.1; ALT_SEQ; mRNA.
CCDS; CCDS56595.1; -. [Q9H9B1-4]
CCDS; CCDS7050.2; -. [Q9H9B1-1]
RefSeq; NP_001138999.1; NM_001145527.1. [Q9H9B1-4]
RefSeq; NP_079033.4; NM_024757.4. [Q9H9B1-1]
UniGene; Hs.495511; -.
PDB; 2IGQ; X-ray; 2.00 A; A/B=982-1266.
PDB; 2RFI; X-ray; 1.59 A; A/B=982-1266.
PDB; 3B7B; X-ray; 2.99 A; A/B=765-999.
PDB; 3B95; X-ray; 2.99 A; A/B=765-999.
PDB; 3FPD; X-ray; 2.40 A; A/B=1006-1266.
PDB; 3HNA; X-ray; 1.50 A; A/B=982-1266.
PDB; 3MO0; X-ray; 2.78 A; A/B=982-1266.
PDB; 3MO2; X-ray; 2.49 A; A/B/C/D=982-1266.
PDB; 3MO5; X-ray; 2.14 A; A/B/C/D=982-1266.
PDB; 3SW9; X-ray; 3.05 A; A/B=982-1266.
PDB; 3SWC; X-ray; 2.33 A; A/B=982-1266.
PDB; 4I51; X-ray; 1.90 A; A/B=982-1266.
PDB; 5TTG; X-ray; 1.66 A; A/B=982-1266.
PDB; 5TUZ; X-ray; 1.95 A; A/B=1006-1266.
PDB; 5VSD; X-ray; 1.85 A; A/B=1006-1266.
PDB; 5VSF; X-ray; 1.70 A; A/B=1006-1266.
PDBsum; 2IGQ; -.
PDBsum; 2RFI; -.
PDBsum; 3B7B; -.
PDBsum; 3B95; -.
PDBsum; 3FPD; -.
PDBsum; 3HNA; -.
PDBsum; 3MO0; -.
PDBsum; 3MO2; -.
PDBsum; 3MO5; -.
PDBsum; 3SW9; -.
PDBsum; 3SWC; -.
PDBsum; 4I51; -.
PDBsum; 5TTG; -.
PDBsum; 5TUZ; -.
PDBsum; 5VSD; -.
PDBsum; 5VSF; -.
ProteinModelPortal; Q9H9B1; -.
SMR; Q9H9B1; -.
BioGrid; 122908; 47.
CORUM; Q9H9B1; -.
DIP; DIP-34585N; -.
IntAct; Q9H9B1; 30.
MINT; MINT-7945009; -.
STRING; 9606.ENSP00000417980; -.
BindingDB; Q9H9B1; -.
ChEMBL; CHEMBL6031; -.
GuidetoPHARMACOLOGY; 2651; -.
iPTMnet; Q9H9B1; -.
PhosphoSitePlus; Q9H9B1; -.
BioMuta; EHMT1; -.
DMDM; 325511404; -.
EPD; Q9H9B1; -.
MaxQB; Q9H9B1; -.
PaxDb; Q9H9B1; -.
PeptideAtlas; Q9H9B1; -.
PRIDE; Q9H9B1; -.
Ensembl; ENST00000371394; ENSP00000485945; ENSG00000181090. [Q9H9B1-2]
Ensembl; ENST00000460843; ENSP00000417980; ENSG00000181090. [Q9H9B1-1]
Ensembl; ENST00000462484; ENSP00000417328; ENSG00000181090. [Q9H9B1-4]
GeneID; 79813; -.
KEGG; hsa:79813; -.
UCSC; uc004coa.3; human. [Q9H9B1-1]
CTD; 79813; -.
DisGeNET; 79813; -.
EuPathDB; HostDB:ENSG00000181090.17; -.
GeneCards; EHMT1; -.
GeneReviews; EHMT1; -.
HGNC; HGNC:24650; EHMT1.
HPA; HPA060022; -.
MalaCards; EHMT1; -.
MIM; 607001; gene.
MIM; 610253; phenotype.
neXtProt; NX_Q9H9B1; -.
OpenTargets; ENSG00000181090; -.
Orphanet; 96147; Kleefstra syndrome due to 9q34 microdeletion.
Orphanet; 261652; Kleefstra syndrome due to a point mutation.
PharmGKB; PA134941393; -.
eggNOG; KOG1082; Eukaryota.
eggNOG; COG0666; LUCA.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00780000121845; -.
HOVERGEN; HBG028394; -.
InParanoid; Q9H9B1; -.
KO; K11420; -.
OrthoDB; EOG091G00U6; -.
PhylomeDB; Q9H9B1; -.
TreeFam; TF106443; -.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
ChiTaRS; EHMT1; human.
EvolutionaryTrace; Q9H9B1; -.
GeneWiki; EHMT1; -.
GenomeRNAi; 79813; -.
PRO; PR:Q9H9B1; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000181090; -.
CleanEx; HS_EHMT1; -.
ExpressionAtlas; Q9H9B1; baseline and differential.
Genevisible; Q9H9B1; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0070742; F:C2H2 zinc finger domain binding; IEA:Ensembl.
GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); ISS:UniProtKB.
GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); ISS:UniProtKB.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006325; P:chromatin organization; IDA:UniProtKB.
GO; GO:0006306; P:DNA methylation; ISS:UniProtKB.
GO; GO:0009790; P:embryo development; ISS:UniProtKB.
GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0018027; P:peptidyl-lysine dimethylation; IDA:UniProtKB.
GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0060992; P:response to fungicide; IEA:Ensembl.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 3.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR007728; Pre-SET_dom.
InterPro; IPR001214; SET_dom.
Pfam; PF12796; Ank_2; 2.
Pfam; PF05033; Pre-SET; 1.
Pfam; PF00856; SET; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 7.
SMART; SM00468; PreSET; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 5.
PROSITE; PS50867; PRE_SET; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ANK repeat;
Chromatin regulator; Chromosome; Complete proteome; Disease mutation;
Isopeptide bond; Mental retardation; Metal-binding; Methyltransferase;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
S-adenosyl-L-methionine; Transferase; Ubl conjugation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:25489052}.
CHAIN 2 1298 Histone-lysine N-methyltransferase EHMT1.
/FTId=PRO_0000186067.
REPEAT 737 766 ANK 1.
REPEAT 772 801 ANK 2.
REPEAT 805 834 ANK 3.
REPEAT 838 868 ANK 4.
REPEAT 872 901 ANK 5.
REPEAT 905 934 ANK 6.
REPEAT 938 967 ANK 7.
REPEAT 971 1004 ANK 8.
DOMAIN 1060 1123 Pre-SET. {ECO:0000255|PROSITE-
ProRule:PRU00157}.
DOMAIN 1126 1243 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
REGION 905 907 Histone H3K9me binding.
REGION 1136 1138 S-adenosyl-L-methionine binding.
REGION 1162 1181 Interaction with histone H3.
REGION 1200 1201 S-adenosyl-L-methionine binding.
REGION 1242 1245 Interaction with histone H3.
COMPBIAS 406 409 Poly-Glu.
COMPBIAS 442 449 Poly-Arg.
COMPBIAS 1292 1295 Poly-Ala.
METAL 1062 1062 Zinc 1.
METAL 1062 1062 Zinc 2.
METAL 1064 1064 Zinc 1.
METAL 1068 1068 Zinc 1.
METAL 1068 1068 Zinc 3.
METAL 1073 1073 Zinc 1.
METAL 1075 1075 Zinc 2.
METAL 1105 1105 Zinc 2.
METAL 1105 1105 Zinc 3.
METAL 1109 1109 Zinc 2.
METAL 1111 1111 Zinc 3.
METAL 1115 1115 Zinc 3.
METAL 1203 1203 Zinc 4.
METAL 1256 1256 Zinc 4.
METAL 1258 1258 Zinc 4.
METAL 1263 1263 Zinc 4.
BINDING 1155 1155 Histone H3K9me.
{ECO:0000269|PubMed:18264113,
ECO:0000269|PubMed:20084102}.
BINDING 1173 1173 S-adenosyl-L-methionine.
BINDING 1257 1257 S-adenosyl-L-methionine; via amide
nitrogen.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:25489052}.
MOD_RES 435 435 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1004 1004 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1048 1048 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 22 22 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 22 22 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 190 190 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 199 199 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 231 231 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 234 234 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 317 317 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 327 327 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 432 432 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 492 492 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 559 559 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 644 644 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 659 659 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 684 684 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 731 731 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 8 66 AVPARGEPQQDCCVKTELLGEETPMAADEGSAEKQAGEAHM
AADGETNGSCENSDASSH -> RHLWLPMKAQQRNRQERPT
WLRTVRPMGLVKTAMPAVMQMLQSTLRTAQGSTPRMAPTH
(in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_002222.
VAR_SEQ 67 1298 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_002223.
VAR_SEQ 795 808 AGANIDTCSEDQRT -> FCRLGSPRSRGCLW (in
isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040717.
VAR_SEQ 809 1298 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040718.
VAR_SEQ 1181 1184 DGEV -> ISSA (in isoform 3).
{ECO:0000303|PubMed:11347906}.
/FTId=VSP_002224.
VAR_SEQ 1185 1298 Missing (in isoform 3).
{ECO:0000303|PubMed:11347906}.
/FTId=VSP_002225.
VARIANT 43 43 A -> V (in a breast cancer sample;
somatic mutation; dbSNP:rs79514677).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036345.
VARIANT 388 388 A -> T (in dbSNP:rs11137198).
/FTId=VAR_027642.
VARIANT 1075 1075 C -> Y (in KLESTS).
{ECO:0000269|PubMed:19264732}.
/FTId=VAR_069183.
VARIANT 1173 1173 Y -> F (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036346.
MUTAGEN 905 905 E->A: Abolishes binding to histone
H3K9me. {ECO:0000269|PubMed:18264113}.
CONFLICT 555 555 N -> D (in Ref. 3; AAH47504).
{ECO:0000305}.
CONFLICT 561 561 E -> G (in Ref. 1; AAM09024 and 2;
BAB14321). {ECO:0000305}.
HELIX 776 783 {ECO:0000244|PDB:3B7B}.
HELIX 786 794 {ECO:0000244|PDB:3B7B}.
HELIX 809 815 {ECO:0000244|PDB:3B7B}.
HELIX 819 826 {ECO:0000244|PDB:3B7B}.
TURN 827 829 {ECO:0000244|PDB:3B7B}.
HELIX 842 848 {ECO:0000244|PDB:3B7B}.
HELIX 852 859 {ECO:0000244|PDB:3B7B}.
TURN 860 862 {ECO:0000244|PDB:3B7B}.
HELIX 876 882 {ECO:0000244|PDB:3B7B}.
HELIX 886 894 {ECO:0000244|PDB:3B7B}.
HELIX 909 916 {ECO:0000244|PDB:3B7B}.
HELIX 919 926 {ECO:0000244|PDB:3B7B}.
TURN 927 929 {ECO:0000244|PDB:3B7B}.
HELIX 942 948 {ECO:0000244|PDB:3B7B}.
HELIX 952 959 {ECO:0000244|PDB:3B7B}.
TURN 960 962 {ECO:0000244|PDB:3B7B}.
HELIX 975 978 {ECO:0000244|PDB:3B7B}.
HELIX 983 994 {ECO:0000244|PDB:3HNA}.
STRAND 1008 1012 {ECO:0000244|PDB:3HNA}.
TURN 1014 1017 {ECO:0000244|PDB:3HNA}.
STRAND 1019 1021 {ECO:0000244|PDB:3HNA}.
STRAND 1025 1031 {ECO:0000244|PDB:3HNA}.
STRAND 1037 1040 {ECO:0000244|PDB:3HNA}.
STRAND 1045 1048 {ECO:0000244|PDB:3HNA}.
HELIX 1056 1058 {ECO:0000244|PDB:3HNA}.
STRAND 1065 1068 {ECO:0000244|PDB:3HNA}.
HELIX 1074 1078 {ECO:0000244|PDB:3HNA}.
STRAND 1096 1098 {ECO:0000244|PDB:3HNA}.
STRAND 1109 1111 {ECO:0000244|PDB:3HNA}.
STRAND 1115 1117 {ECO:0000244|PDB:5TTG}.
HELIX 1120 1122 {ECO:0000244|PDB:3HNA}.
STRAND 1128 1132 {ECO:0000244|PDB:3HNA}.
STRAND 1134 1144 {ECO:0000244|PDB:3HNA}.
STRAND 1151 1155 {ECO:0000244|PDB:3HNA}.
STRAND 1157 1161 {ECO:0000244|PDB:3HNA}.
HELIX 1162 1166 {ECO:0000244|PDB:3HNA}.
STRAND 1174 1177 {ECO:0000244|PDB:3HNA}.
STRAND 1180 1183 {ECO:0000244|PDB:3HNA}.
STRAND 1185 1193 {ECO:0000244|PDB:3HNA}.
HELIX 1195 1198 {ECO:0000244|PDB:3HNA}.
STRAND 1206 1215 {ECO:0000244|PDB:3HNA}.
STRAND 1223 1230 {ECO:0000244|PDB:3HNA}.
HELIX 1244 1250 {ECO:0000244|PDB:3HNA}.
TURN 1251 1253 {ECO:0000244|PDB:3HNA}.
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


Related products :

Catalog number Product name Quantity
EIAAB12653 EHMT1,Euchromatic histone-lysine N-methyltransferase 1,EUHMTASE1,Eu-HMTase1,G9a-like protein 1,GLP,GLP,GLP1,H3-K9-HMTase 5,Histone H3-K9 methyltransferase 5,Histone-lysine N-methyltransferase EHMT1,Ho
EIAAB12652 Ehmt1,Euchromatic histone-lysine N-methyltransferase 1,Euhmtase1,Eu-HMTase1,G9a-like protein 1,GLP,Glp,GLP1,Histone-lysine N-methyltransferase EHMT1,Kmt1d,Lysine N-methyltransferase 1D,Mouse,Mus muscu
EIAAB11717 DOT1L,DOT1-like protein,H3-K79-HMTase,Histone H3-K79 methyltransferase,Histone-lysine N-methyltransferase, H3 lysine-79 specific,Homo sapiens,Human,KIAA1814,KMT4,Lysine N-methyltransferase 4
EIAAB12655 BAT8,C6orf30,EHMT2,Euchromatic histone-lysine N-methyltransferase 2,G9A,H3-K9-HMTase 3,Histone H3-K9 methyltransferase 3,Histone-lysine N-methyltransferase EHMT2,HLA-B-associated transcript 8,Homo sap
EIAAB12654 Bat8,Ehmt2,Euchromatic histone-lysine N-methyltransferase 2,G9a,H3-K9-HMTase 3,Histone H3-K9 methyltransferase 3,Histone-lysine N-methyltransferase EHMT2,HLA-B-associated transcript 8,Mouse,Mus muscul
EIAAB37955 ERG-associated protein with SET domain,ESET,H3-K9-HMTase 4,Histone H3-K9 methyltransferase 4,Histone-lysine N-methyltransferase SETDB1,Homo sapiens,Human,KIAA0067,KMT1E,Lysine N-methyltransferase 1E,S
EIAAB40615 H3-K9-HMTase 1,Histone H3-K9 methyltransferase 1,Histone-lysine N-methyltransferase SUV39H1,Homo sapiens,Human,KMT1A,Lysine N-methyltransferase 1A,Position-effect variegation 3-9 homolog,Su(var)3-9 ho
EIAAB40618 H3-K9-HMTase 2,Histone H3-K9 methyltransferase 2,Histone-lysine N-methyltransferase SUV39H2,Homo sapiens,Human,KMT1B,Lysine N-methyltransferase 1B,Su(var)3-9 homolog 2,Suppressor of variegation 3-9 ho
EIAAB37975 H3-K4-HMTase SETD7,Histone H3-K4 methyltransferase SETD7,Histone-lysine N-methyltransferase SETD7,Homo sapiens,Human,KIAA1717,KMT7,Lysine N-methyltransferase 7,SET domain-containing protein 7,SET7,SET
EIAAB37977 H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,Homo sapiens,Human,KMT5A,Lysine N-methyltransferase 5A,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PRSET7
EIAAB37951 Histone-lysine N-methyltransferase SETD1A,Homo sapiens,hSET1A,Human,KIAA0339,KMT2F,Lysine N-methyltransferase 2F,SET domain-containing protein 1A,SET1,Set1_Ash2 histone methyltransferase complex subun
18-003-42222 Histone-lysine N-methyltransferase. H3 lysine-9 specific 1 - EC 2.1.1.43; Histone H3-K9 methyltransferase 1; H3-K9-HMTase 1; Suppressor of variegation 3-9 homolog 1; Su(var)3-9 homolog 1 Polyclonal 0.1 mg Protein A
EI24 EHMT1 Gene euchromatic histone-lysine N-methyltransferase 1
EIAAB27931 H3-K36-HMTase,H4-K20-HMTase,Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific,Mouse,Mus musculus,NR-binding SET domain-containing protein,Nsd1,Nuclear receptor-binding SET dom
EIAAB38899 Histone methyltransferase SMYD2,Homo sapiens,HSKM-B,Human,KMT3C,Lysine N-methyltransferase 3C,N-lysine methyltransferase SMYD2,SET and MYND domain-containing protein 2,SMYD2
EIAAB37976 H3-K4-HMTase SETD7,Histone H3-K4 methyltransferase SETD7,Histone-lysine N-methyltransferase SETD7,Kiaa1717,Mouse,Mus musculus,SET domain-containing protein 7,Set7,SET7_9,Set9,Setd7
EIAAB37958 C13orf4,Chronic lymphocytic leukemia deletion region gene 8 protein,CLLD8,Histone-lysine N-methyltransferase SETDB2,Homo sapiens,Human,KMT1F,Lysine N-methyltransferase 1F,SET domain bifurcated 2,SETDB
EIAAB40613 H3-K9-HMTase 1,Histone H3-K9 methyltransferase 1,Histone-lysine N-methyltransferase SUV39H1,Mouse,Mus musculus,Position-effect variegation 3-9 homolog,Su(var)3-9 homolog 1,Suppressor of variegation 3-
EIAAB37979 Bos taurus,Bovine,H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PR-Set7,SET domain-containing protein 8,SET
EIAAB37978 H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,Mouse,Mus musculus,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PR-Set7,SET domain-containing protein 8,Se
EIAAB37954 Histone-lysine N-methyltransferase SETD1B,Homo sapiens,hSET1B,Human,KIAA1076,KMT2G,Lysine N-methyltransferase 2G,SET domain-containing protein 1B,SET1B,SETD1B
EIAAB40617 H3-K9-HMTase 2,Histone H3-K9 methyltransferase 2,Histone-lysine N-methyltransferase SUV39H2,Mouse,Mus musculus,Su(var)3-9 homolog 2,Suppressor of variegation 3-9 homolog 2,Suv39h2
EIAAB13541 Enhancer of zeste homolog 2,ENX-1,EZH2,Histone-lysine N-methyltransferase EZH2,Homo sapiens,Human,KMT6,Lysine N-methyltransferase 6
EIAAB27934 DC28,Histone-lysine N-methyltransferase NSD3,Homo sapiens,Human,NSD3,Nuclear SET domain-containing protein 3,Protein whistle,WHSC1L1,WHSC1-like 1 isoform 9 with methyltransferase activity to lysine,WH
EIAAB27930 Androgen receptor coactivator 267 kDa protein,Androgen receptor-associated protein of 267 kDa,ARA267,H3-K36-HMTase,H4-K20-HMTase,Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 speci


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur