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Histone-lysine N-methyltransferase EHMT2 (EC 2.1.1.-) (EC 2.1.1.43) (Euchromatic histone-lysine N-methyltransferase 2) (HLA-B-associated transcript 8) (Histone H3-K9 methyltransferase 3) (H3-K9-HMTase 3) (Lysine N-methyltransferase 1C) (Protein G9a)

 EHMT2_HUMAN             Reviewed;        1210 AA.
Q96KQ7; B0UZY2; Q14349; Q5JP83; Q5JQ92; Q5JQA1; Q5JQG3; Q6PK06;
Q96MH5; Q96QD0; Q9UQL8; Q9Y331;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
27-SEP-2017, entry version 181.
RecName: Full=Histone-lysine N-methyltransferase EHMT2;
EC=2.1.1.-;
EC=2.1.1.43;
AltName: Full=Euchromatic histone-lysine N-methyltransferase 2;
AltName: Full=HLA-B-associated transcript 8;
AltName: Full=Histone H3-K9 methyltransferase 3;
Short=H3-K9-HMTase 3;
AltName: Full=Lysine N-methyltransferase 1C;
AltName: Full=Protein G9a;
Name=EHMT2; Synonyms=BAT8, C6orf30, G9A, KMT1C, NG36;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM
2), TISSUE SPECIFICITY, AND VARIANT ASN-55.
PubMed=11707778; DOI=10.1007/s00335-001-3029-3;
Brown S.E., Campbell R.D., Sanderson C.M.;
"Novel NG36/G9a gene products encoded within the human and mouse MHC
class III regions.";
Mamm. Genome 12:916-924(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Salivary gland;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-55.
Hirakawa M., Yamaguchi H., Imai K., Shimada J., Shiina S., Tamiya G.,
Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-55.
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-1210 (ISOFORM 1), AND
VARIANT ASN-55.
TISSUE=Muscle, and Uterus;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 195-1210, AND FUNCTION.
TISSUE=Histiocytic lymphoma;
PubMed=8457211; DOI=10.1042/bj2900811;
Milner C.M., Campbell R.D.;
"The G9a gene in the human major histocompatibility complex encodes a
novel protein containing ankyrin-like repeats.";
Biochem. J. 290:811-818(1993).
[9]
CATALYTIC ACTIVITY, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11316813; DOI=10.1074/jbc.M101914200;
Tachibana M., Sugimoto K., Fukushima T., Shinkai Y.;
"Set domain-containing protein, G9a, is a novel lysine-preferring
mammalian histone methyltransferase with hyperactivity and specific
selectivity to lysines 9 and 27 of histone H3.";
J. Biol. Chem. 276:25309-25317(2001).
[10]
IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EHMT1; CBX3;
RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
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).
[11]
INTERACTION WITH GFI1B.
PubMed=16688220; DOI=10.1038/sj.emboj.7601124;
Vassen L., Fiolka K., Moeroey T.;
"Gfi1b alters histone methylation at target gene promoters and sites
of gamma-satellite containing heterochromatin.";
EMBO J. 25:2409-2419(2006).
[12]
INTERACTION WITH WIZ AND EHMT1.
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND 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).
[15]
INTERACTION WITH CDYL AND REST, AND IDENTIFICATION IN A COMPLEX WITH
REST; CDYL; SETB1; EHMT1 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).
[16]
FUNCTION, METHYLATION AT LYS-185, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18438403; DOI=10.1038/nchembio.88;
Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R.,
Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.;
"Protein lysine methyltransferase G9a acts on non-histone targets.";
Nat. Chem. Biol. 4:344-346(2008).
[17]
DOMAIN ANK REPEATS, AND MUTAGENESIS OF TRP-786; TRP-791; GLU-794;
GLU-817; TRP-824 AND ASP-852.
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-173; SER-232;
SER-246 AND THR-1210, AND 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).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
INTERACTION WITH UHRF1.
PubMed=19056828; DOI=10.1093/nar/gkn961;
Kim J.K., Esteve P.O., Jacobsen S.E., Pradhan S.;
"UHRF1 binds G9a and participates in p21 transcriptional regulation in
mammalian cells.";
Nucleic Acids Res. 37:493-505(2009).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
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).
[23]
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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-232 AND
SER-246, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[25]
INTERACTION WITH SMARCAD1.
PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036;
Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W.,
Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M.,
Varga-Weisz P., Mermoud J.E.;
"Maintenance of silent chromatin through replication requires SWI/SNF-
like chromatin remodeler SMARCAD1.";
Mol. Cell 42:285-296(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-232; SER-246;
SER-413 AND SER-1204, AND 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).
[27]
FUNCTION.
PubMed=22387026; DOI=10.1016/j.molcel.2012.01.019;
Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A.,
Carey M.F., Grunstein M.;
"Histone H3 lysine 56 methylation regulates DNA replication through
its interaction with PCNA.";
Mol. Cell 46:7-17(2012).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44; SER-47; SER-140;
SER-232; SER-242; SER-350 AND THR-555, 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).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, 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).
[31]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-219; LYS-229 AND LYS-634,
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).
[32]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 913-1193 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS, FUNCTION, AND CATALYTIC
ACTIVITY.
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).
-!- 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 mediates monomethylation of 'Lys-56'
of histone H3 (H3K56me1) in G1 phase, leading to promote
interaction between histone H3 and PCNA and regulating DNA
replication. 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. May also methylate histone H1. In
addition to the histone methyltransferase activity, also
methylates non-histone proteins: mediates dimethylation of 'Lys-
373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1,
ERCC6, KLF12 and itself. {ECO:0000269|PubMed:11316813,
ECO:0000269|PubMed:18438403, ECO:0000269|PubMed:20084102,
ECO:0000269|PubMed:20118233, ECO:0000269|PubMed:22387026,
ECO:0000269|PubMed:8457211}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:11316813, ECO:0000269|PubMed:20084102}.
-!- SUBUNIT: Heterodimer; heterodimerizes with EHMT1/GLP. Interacts
with GFI1B and WIZ. 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. Part of a complex composed of TRIM28,
HDAC1, HDAC2 and EHMT2. Interacts with UHRF1. 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:16688220,
ECO:0000269|PubMed:16702210, ECO:0000269|PubMed:19056828,
ECO:0000269|PubMed:19061646, ECO:0000269|PubMed:20084102,
ECO:0000269|PubMed:20118233, ECO:0000269|PubMed:21549307}.
-!- INTERACTION:
P23771:GATA3; NbExp=20; IntAct=EBI-744366, EBI-6664760;
Q99684:GFI1; NbExp=2; IntAct=EBI-744366, EBI-949368;
Q07120:Gfi1 (xeno); NbExp=3; IntAct=EBI-744366, EBI-4289236;
Q13547:HDAC1; NbExp=7; IntAct=EBI-744366, EBI-301834;
Q92831:KAT2B; NbExp=3; IntAct=EBI-744366, EBI-477430;
Q9Y4X4:KLF12; NbExp=3; IntAct=EBI-744366, EBI-750750;
Q13330:MTA1; NbExp=9; IntAct=EBI-744366, EBI-714236;
O94776:MTA2; NbExp=7; IntAct=EBI-744366, EBI-1783035;
Q9BTC8:MTA3; NbExp=18; IntAct=EBI-744366, EBI-2461787;
O60568:PLOD3; NbExp=7; IntAct=EBI-744366, EBI-741582;
Q9NQX1:PRDM5; NbExp=3; IntAct=EBI-744366, EBI-4292031;
Q5JSZ5:PRRC2B; NbExp=2; IntAct=EBI-744366, EBI-744891;
Q9P2R6:RERE; NbExp=3; IntAct=EBI-744366, EBI-948076;
O60315:ZEB2; NbExp=6; IntAct=EBI-744366, EBI-717614;
Q96JM2:ZNF462; NbExp=3; IntAct=EBI-744366, EBI-1210359;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11316813}.
Chromosome {ECO:0000269|PubMed:11316813}. Note=Associates with
euchromatic regions. Does not associate with heterochromatin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q96KQ7-1; Sequence=Displayed;
Name=2; Synonyms=NG36G9a-SPI;
IsoId=Q96KQ7-2; Sequence=VSP_002211;
Name=3; Synonyms=NG36;
IsoId=Q96KQ7-3; Sequence=VSP_002212, VSP_002213;
-!- TISSUE SPECIFICITY: Expressed in all tissues examined, with high
levels in fetal liver, thymus, lymph node, spleen and peripheral
blood leukocytes and lower level in bone marrow.
{ECO:0000269|PubMed:11707778}.
-!- DOMAIN: The SET domain mediates interaction with WIZ.
{ECO:0000269|PubMed:18264113}.
-!- DOMAIN: The ANK repeats bind H3K9me1 and H3K9me2.
{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}.
-!- PTM: Methylated at Lys-185; automethylated.
{ECO:0000269|PubMed:18438403}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
-!- CAUTION: While NG36 and G9a were originally thought to derive from
2 separate genes, all G9A transcripts also contain the in frame
coding sequence of NG36. {ECO:0000305|PubMed:11707778}.
-!- CAUTION: It is uncertain whether Met-1 or Met-21 is the initiator
methionine. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD21811.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAD21812.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAH02686.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH09351.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH18718.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH20970.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB63294.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAB63295.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAA49491.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AJ315532; CAC86666.1; -; mRNA.
EMBL; AK056936; BAB71314.1; -; mRNA.
EMBL; AF134726; AAD21811.1; ALT_SEQ; Genomic_DNA.
EMBL; AF134726; AAD21812.1; ALT_SEQ; Genomic_DNA.
EMBL; BA000025; BAB63294.1; ALT_SEQ; Genomic_DNA.
EMBL; BA000025; BAB63295.1; ALT_SEQ; Genomic_DNA.
EMBL; AL662834; CAI17747.2; -; Genomic_DNA.
EMBL; AL662834; CAI17748.1; -; Genomic_DNA.
EMBL; AL671762; CAI18224.2; -; Genomic_DNA.
EMBL; AL671762; CAI18226.2; -; Genomic_DNA.
EMBL; AL844853; CAI41852.1; -; Genomic_DNA.
EMBL; AL844853; CAI41853.1; -; Genomic_DNA.
EMBL; CR388219; CAQ07473.1; -; Genomic_DNA.
EMBL; CR388202; CAQ07473.1; JOINED; Genomic_DNA.
EMBL; CR388219; CAQ07474.1; -; Genomic_DNA.
EMBL; CR388202; CAQ07474.1; JOINED; Genomic_DNA.
EMBL; CR936237; CAQ09159.1; -; Genomic_DNA.
EMBL; CR759784; CAQ09311.1; -; Genomic_DNA.
EMBL; CR388202; CAQ09508.1; -; Genomic_DNA.
EMBL; CR388219; CAQ09508.1; JOINED; Genomic_DNA.
EMBL; CR388202; CAQ09509.1; -; Genomic_DNA.
EMBL; CR388219; CAQ09509.1; JOINED; Genomic_DNA.
EMBL; CH471081; EAX03542.1; -; Genomic_DNA.
EMBL; BC002686; AAH02686.2; ALT_INIT; mRNA.
EMBL; BC009351; AAH09351.1; ALT_INIT; mRNA.
EMBL; BC018718; AAH18718.1; ALT_INIT; mRNA.
EMBL; BC020970; AAH20970.2; ALT_INIT; mRNA.
EMBL; X69838; CAA49491.1; ALT_INIT; mRNA.
CCDS; CCDS4725.1; -. [Q96KQ7-1]
CCDS; CCDS4726.1; -. [Q96KQ7-2]
RefSeq; NP_001276342.1; NM_001289413.1.
RefSeq; NP_001305762.1; NM_001318833.1.
RefSeq; NP_006700.3; NM_006709.4. [Q96KQ7-1]
RefSeq; NP_079532.5; NM_025256.6. [Q96KQ7-2]
UniGene; Hs.709218; -.
PDB; 2O8J; X-ray; 1.80 A; A/B/C/D=913-1193.
PDB; 3DM1; X-ray; 2.40 A; B/D/F/H=179-190.
PDB; 3K5K; X-ray; 1.70 A; A/B=913-1193.
PDB; 3RJW; X-ray; 2.56 A; A/B=913-1193.
PDB; 4NVQ; X-ray; 2.03 A; A/B=913-1193.
PDB; 5JHN; X-ray; 1.67 A; A/B=916-1189.
PDB; 5JIN; X-ray; 1.85 A; A/B=916-1189.
PDB; 5JIY; X-ray; 1.48 A; A/B=916-1189.
PDB; 5JJ0; X-ray; 1.72 A; A/B=916-1189.
PDB; 5T0K; X-ray; 1.70 A; A/B=913-1193.
PDB; 5T0M; X-ray; 1.90 A; A/B=913-1193.
PDB; 5TTF; X-ray; 1.72 A; A/B/C/D=913-1193.
PDB; 5TUY; X-ray; 2.60 A; A/B=921-1187.
PDBsum; 2O8J; -.
PDBsum; 3DM1; -.
PDBsum; 3K5K; -.
PDBsum; 3RJW; -.
PDBsum; 4NVQ; -.
PDBsum; 5JHN; -.
PDBsum; 5JIN; -.
PDBsum; 5JIY; -.
PDBsum; 5JJ0; -.
PDBsum; 5T0K; -.
PDBsum; 5T0M; -.
PDBsum; 5TTF; -.
PDBsum; 5TUY; -.
ProteinModelPortal; Q96KQ7; -.
SMR; Q96KQ7; -.
BioGrid; 116123; 122.
CORUM; Q96KQ7; -.
DIP; DIP-34461N; -.
IntAct; Q96KQ7; 89.
MINT; MINT-1441977; -.
STRING; 9606.ENSP00000364687; -.
BindingDB; Q96KQ7; -.
ChEMBL; CHEMBL6032; -.
GuidetoPHARMACOLOGY; 2652; -.
iPTMnet; Q96KQ7; -.
PhosphoSitePlus; Q96KQ7; -.
BioMuta; EHMT2; -.
DMDM; 116241348; -.
EPD; Q96KQ7; -.
MaxQB; Q96KQ7; -.
PaxDb; Q96KQ7; -.
PeptideAtlas; Q96KQ7; -.
PRIDE; Q96KQ7; -.
Ensembl; ENST00000375530; ENSP00000364680; ENSG00000204371. [Q96KQ7-2]
Ensembl; ENST00000375537; ENSP00000364687; ENSG00000204371. [Q96KQ7-1]
Ensembl; ENST00000383372; ENSP00000372863; ENSG00000206376. [Q96KQ7-2]
Ensembl; ENST00000383373; ENSP00000372864; ENSG00000206376. [Q96KQ7-1]
Ensembl; ENST00000420336; ENSP00000396119; ENSG00000238134.
Ensembl; ENST00000420874; ENSP00000411035; ENSG00000236759. [Q96KQ7-2]
Ensembl; ENST00000421926; ENSP00000416957; ENSG00000232045.
Ensembl; ENST00000429506; ENSP00000406110; ENSG00000227333. [Q96KQ7-1]
Ensembl; ENST00000450075; ENSP00000392305; ENSG00000236759. [Q96KQ7-1]
Ensembl; ENST00000450229; ENSP00000400838; ENSG00000227333. [Q96KQ7-2]
GeneID; 10919; -.
KEGG; hsa:10919; -.
UCSC; uc003nxz.3; human. [Q96KQ7-1]
CTD; 10919; -.
DisGeNET; 10919; -.
EuPathDB; HostDB:ENSG00000204371.11; -.
GeneCards; EHMT2; -.
H-InvDB; HIX0166078; -.
H-InvDB; HIX0166345; -.
H-InvDB; HIX0167369; -.
H-InvDB; HIX0184162; -.
HGNC; HGNC:14129; EHMT2.
HPA; HPA050550; -.
HPA; HPA060259; -.
MIM; 604599; gene.
neXtProt; NX_Q96KQ7; -.
OpenTargets; ENSG00000204371; -.
PharmGKB; PA25267; -.
eggNOG; KOG1082; Eukaryota.
eggNOG; COG0666; LUCA.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00780000121845; -.
HOVERGEN; HBG028394; -.
InParanoid; Q96KQ7; -.
KO; K11420; -.
PhylomeDB; Q96KQ7; -.
TreeFam; TF106443; -.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
SIGNOR; Q96KQ7; -.
ChiTaRS; EHMT2; human.
EvolutionaryTrace; Q96KQ7; -.
GeneWiki; EHMT2; -.
GenomeRNAi; 10919; -.
PRO; PR:Q96KQ7; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204371; -.
CleanEx; HS_EHMT2; -.
ExpressionAtlas; Q96KQ7; baseline and differential.
Genevisible; Q96KQ7; HS.
GO; GO:0000790; C:nuclear chromatin; IDA:MGI.
GO; GO:0016607; C:nuclear speck; 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; IPI:UniProtKB.
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:MGI.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0009267; P:cellular response to starvation; IDA:MGI.
GO; GO:0006306; P:DNA methylation; ISS:UniProtKB.
GO; GO:0034968; P:histone lysine methylation; IDA:MGI.
GO; GO:0016571; P:histone methylation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0018027; P:peptidyl-lysine dimethylation; IDA:UniProtKB.
GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 3.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR007728; Pre-SET_dom.
InterPro; IPR001214; SET_dom.
Pfam; PF12796; Ank_2; 3.
Pfam; PF05033; Pre-SET; 1.
Pfam; PF00856; SET; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 6.
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; Isopeptide bond;
Metal-binding; Methylation; Methyltransferase; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
S-adenosyl-L-methionine; Transferase; Ubl conjugation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
CHAIN 2 1210 Histone-lysine N-methyltransferase EHMT2.
/FTId=PRO_0000186068.
REPEAT 649 678 ANK 1.
REPEAT 684 713 ANK 2.
REPEAT 717 746 ANK 3.
REPEAT 750 780 ANK 4.
REPEAT 784 813 ANK 5.
REPEAT 817 846 ANK 6.
REPEAT 850 879 ANK 7.
DOMAIN 972 1035 Pre-SET. {ECO:0000255|PROSITE-
ProRule:PRU00157}.
DOMAIN 1038 1155 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 1164 1180 Post-SET.
REGION 817 819 Histone H3K9me binding. {ECO:0000250}.
REGION 1048 1050 S-adenosyl-L-methionine binding.
REGION 1074 1093 Interaction with histone H3.
{ECO:0000250}.
REGION 1112 1113 S-adenosyl-L-methionine binding.
REGION 1154 1157 Interaction with histone H3.
{ECO:0000250}.
COMPBIAS 2 13 Poly-Ala.
COMPBIAS 160 163 Poly-Ala.
COMPBIAS 300 326 Poly-Glu.
METAL 974 974 Zinc 1.
METAL 974 974 Zinc 2.
METAL 976 976 Zinc 1.
METAL 980 980 Zinc 1.
METAL 980 980 Zinc 3.
METAL 985 985 Zinc 1.
METAL 987 987 Zinc 2.
METAL 1017 1017 Zinc 2.
METAL 1017 1017 Zinc 3.
METAL 1021 1021 Zinc 2.
METAL 1023 1023 Zinc 3.
METAL 1027 1027 Zinc 3.
METAL 1115 1115 Zinc 4.
METAL 1168 1168 Zinc 4.
METAL 1170 1170 Zinc 4.
METAL 1175 1175 Zinc 4.
BINDING 1067 1067 Histone H3K9me. {ECO:0000250}.
BINDING 1085 1085 S-adenosyl-L-methionine.
BINDING 1169 1169 S-adenosyl-L-methionine; via amide
nitrogen.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 44 44 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 173 173 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 185 185 N6,N6,N6-trimethyllysine; by EHMT2;
alternate. {ECO:0000269|PubMed:18438403}.
MOD_RES 185 185 N6,N6-dimethyllysine; by EHMT2;
alternate. {ECO:0000269|PubMed:18438403}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 412 412 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z148}.
MOD_RES 413 413 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 555 555 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 1204 1204 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1210 1210 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
CROSSLNK 219 219 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 229 229 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 634 634 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 195 202 PPVPEKRP -> VSGMGEMG (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_002212.
VAR_SEQ 203 1210 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_002213.
VAR_SEQ 373 406 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_002211.
VARIANT 55 55 T -> N (in dbSNP:rs7887).
{ECO:0000269|PubMed:11707778,
ECO:0000269|PubMed:14574404,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.5}.
/FTId=VAR_027973.
VARIANT 1165 1165 Y -> F (in dbSNP:rs13919).
/FTId=VAR_027974.
MUTAGEN 786 786 W->A: Abolishes binding to histone H3K9me
without affecting the histone
methyltransferase activity.
{ECO:0000269|PubMed:18264113}.
MUTAGEN 791 791 W->A: Abolishes binding to histone H3K9me
without affecting the histone
methyltransferase activity.
{ECO:0000269|PubMed:18264113}.
MUTAGEN 794 794 E->A: Abolishes binding to histone H3K9me
without affecting the histone
methyltransferase activity.
{ECO:0000269|PubMed:18264113}.
MUTAGEN 817 817 E->R: Impairs binding to histone H3K9me.
{ECO:0000269|PubMed:18264113}.
MUTAGEN 824 824 W->A: Abolishes binding to histone H3K9me
without affecting the histone
methyltransferase activity.
{ECO:0000269|PubMed:18264113}.
MUTAGEN 852 852 D->R: Impairs binding to histone H3K9me.
{ECO:0000269|PubMed:18264113}.
CONFLICT 178 178 P -> S (in Ref. 2; CAC86666).
{ECO:0000305}.
CONFLICT 985 985 C -> R (in Ref. 2; CAC86666).
{ECO:0000305}.
CONFLICT 994 994 C -> R (in Ref. 8; CAA49491).
{ECO:0000305}.
STRAND 920 924 {ECO:0000244|PDB:5JIY}.
TURN 926 929 {ECO:0000244|PDB:5JIY}.
STRAND 931 933 {ECO:0000244|PDB:5JIY}.
STRAND 937 943 {ECO:0000244|PDB:5JIY}.
STRAND 949 952 {ECO:0000244|PDB:5JIY}.
STRAND 957 960 {ECO:0000244|PDB:5JIY}.
HELIX 968 970 {ECO:0000244|PDB:5JIY}.
STRAND 977 980 {ECO:0000244|PDB:3K5K}.
HELIX 986 989 {ECO:0000244|PDB:5JIY}.
STRAND 1008 1010 {ECO:0000244|PDB:5JIY}.
STRAND 1021 1023 {ECO:0000244|PDB:5JIY}.
STRAND 1027 1029 {ECO:0000244|PDB:5JHN}.
HELIX 1032 1034 {ECO:0000244|PDB:5JIY}.
STRAND 1040 1044 {ECO:0000244|PDB:5JIY}.
STRAND 1046 1056 {ECO:0000244|PDB:5JIY}.
STRAND 1063 1067 {ECO:0000244|PDB:5JIY}.
STRAND 1069 1073 {ECO:0000244|PDB:5JIY}.
HELIX 1074 1077 {ECO:0000244|PDB:5JIY}.
STRAND 1084 1089 {ECO:0000244|PDB:5JIY}.
STRAND 1092 1095 {ECO:0000244|PDB:5JIY}.
STRAND 1097 1105 {ECO:0000244|PDB:5JIY}.
HELIX 1107 1110 {ECO:0000244|PDB:5JIY}.
STRAND 1118 1127 {ECO:0000244|PDB:5JIY}.
STRAND 1135 1142 {ECO:0000244|PDB:5JIY}.
HELIX 1156 1162 {ECO:0000244|PDB:5JIY}.
TURN 1163 1165 {ECO:0000244|PDB:5JIY}.
STRAND 1176 1178 {ECO:0000244|PDB:5JIY}.
HELIX 1179 1187 {ECO:0000244|PDB:5JIY}.
HELIX 1188 1192 {ECO:0000244|PDB:3RJW}.
SEQUENCE 1210 AA; 132370 MW; A6C5DC6B72801520 CRC64;
MAAAAGAAAA AAAEGEAPAE MGALLLEKET RGATERVHGS LGDTPRSEET LPKATPDSLE
PAGPSSPASV TVTVGDEGAD TPVGATPLIG DESENLEGDG DLRGGRILLG HATKSFPSSP
SKGGSCPSRA KMSMTGAGKS PPSVQSLAMR LLSMPGAQGA AAAGSEPPPA TTSPEGQPKV
HRARKTMSKP GNGQPPVPEK RPPEIQHFRM SDDVHSLGKV TSDLAKRRKL NSGGGLSEEL
GSARRSGEVT LTKGDPGSLE EWETVVGDDF SLYYDSYSVD ERVDSDSKSE VEALTEQLSE
EEEEEEEEEE EEEEEEEEEE EEEDEESGNQ SDRSGSSGRR KAKKKWRKDS PWVKPSRKRR
KREPPRAKEP RGVNGVGSSG PSEYMEVPLG SLELPSEGTL SPNHAGVSND TSSLETERGF
EELPLCSCRM EAPKIDRISE RAGHKCMATE SVDGELSGCN AAILKRETMR PSSRVALMVL
CETHRARMVK HHCCPGCGYF CTAGTFLECH PDFRVAHRFH KACVSQLNGM VFCPHCGEDA
SEAQEVTIPR GDGVTPPAGT AAPAPPPLSQ DVPGRADTSQ PSARMRGHGE PRRPPCDPLA
DTIDSSGPSL TLPNGGCLSA VGLPLGPGRE ALEKALVIQE SERRKKLRFH PRQLYLSVKQ
GELQKVILML LDNLDPNFQS DQQSKRTPLH AAAQKGSVEI CHVLLQAGAN INAVDKQQRT
PLMEAVVNNH LEVARYMVQR GGCVYSKEED GSTCLHHAAK IGNLEMVSLL LSTGQVDVNA
QDSGGWTPII WAAEHKHIEV IRMLLTRGAD VTLTDNEENI CLHWASFTGS AAIAEVLLNA
RCDLHAVNYH GDTPLHIAAR ESYHDCVLLF LSRGANPELR NKEGDTAWDL TPERSDVWFA
LQLNRKLRLG VGNRAIRTEK IICRDVARGY ENVPIPCVNG VDGEPCPEDY KYISENCETS
TMNIDRNITH LQHCTCVDDC SSSNCLCGQL SIRCWYDKDG RLLQEFNKIE PPLIFECNQA
CSCWRNCKNR VVQSGIKVRL QLYRTAKMGW GVRALQTIPQ GTFICEYVGE LISDAEADVR
EDDSYLFDLD NKDGEVYCID ARYYGNISRF INHLCDPNII PVRVFMLHQD LRFPRIAFFS
SRDIRTGEEL GFDYGDRFWD IKSKYFTCQC GSEKCKHSAE AIALEQSRLA RLDPHPELLP
ELGSLPPVNT


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