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Histone-lysine N-methyltransferase SUV39H1 (EC 2.1.1.43) (Histone H3-K9 methyltransferase 1) (H3-K9-HMTase 1) (Lysine N-methyltransferase 1A) (Position-effect variegation 3-9 homolog) (Suppressor of variegation 3-9 homolog 1) (Su(var)3-9 homolog 1)

 SUV91_HUMAN             Reviewed;         412 AA.
O43463; B2R6E8; B4DST0; Q53G60; Q6FHK6;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
27-SEP-2017, entry version 180.
RecName: Full=Histone-lysine N-methyltransferase SUV39H1;
EC=2.1.1.43;
AltName: Full=Histone H3-K9 methyltransferase 1;
Short=H3-K9-HMTase 1;
AltName: Full=Lysine N-methyltransferase 1A;
AltName: Full=Position-effect variegation 3-9 homolog;
AltName: Full=Suppressor of variegation 3-9 homolog 1;
Short=Su(var)3-9 homolog 1;
Name=SUV39H1; Synonyms=KMT1A, SUV39H;
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), AND INTERACTION WITH CBX1.
TISSUE=B-cell;
PubMed=10202156; DOI=10.1093/emboj/18.7.1923;
Aagaard L., Laible G., Selenko P., Schmid M., Dorn R., Schotta G.,
Kuhfittig S., Wolf A., Lebersorger A., Singh P.B., Reuter G.,
Jenuwein T.;
"Functional mammalian homologues of the Drosophila PEV-modifier
Su(var)3-9 encode centromere-associated proteins which complex with
the heterochromatin component M31.";
EMBO J. 18:1923-1938(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Tongue;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
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]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=10671371;
Aagaard L., Schmid M., Warburton P., Jenuwein T.;
"Mitotic phosphorylation of SUV39H1, a novel component of active
centromeres, coincides with transient accumulation at mammalian
centromeres.";
J. Cell Sci. 113:817-829(2000).
[9]
ENZYME ACTIVITY, AND MUTAGENESIS OF HIS-320; HIS-324 AND CYS-326.
PubMed=10949293; DOI=10.1038/35020506;
Rea S., Eisenhaber F., O'Carroll D., Strahl B.D., Sun Z.-W.,
Schmid M., Opravil S., Mechtler K., Ponting C.P., Allis C.D.,
Jenuwein T.;
"Regulation of chromatin structure by site-specific histone H3
methyltransferases.";
Nature 406:593-599(2000).
[10]
INTERACTION WITH SBF1.
PubMed=10848615; DOI=10.1128/MCB.20.13.4900-4909.2000;
Firestein R., Cui X., Huie P., Cleary M.L.;
"Set domain-dependent regulation of transcriptional silencing and
growth control by SUV39H1, a mammalian ortholog of Drosophila
Su(var)3-9.";
Mol. Cell. Biol. 20:4900-4909(2000).
[11]
INTERACTION WITH HISTONE H3 AND HISTONE H4.
PubMed=11242053; DOI=10.1038/35065132;
Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.;
"Methylation of histone H3 lysine 9 creates a binding site for HP1
proteins.";
Nature 410:116-120(2001).
[12]
INTERACTION WITH RB1.
PubMed=11484059; DOI=10.1038/35087620;
Nielsen S.J., Schneider R., Bauer U.-M., Bannister A.J., Morrison A.,
O'Carroll D., Firestein R., Cleary M.L., Jenuwein T., Herrera R.E.,
Kouzarides T.;
"Rb targets histone H3 methylation and HP1 to promoters.";
Nature 412:561-565(2001).
[13]
INTERACTION WITH MBD1.
PubMed=12711603; DOI=10.1074/jbc.M302283200;
Fujita N., Watanabe S., Ichimura T., Tsuruzoe S., Shinkai Y.,
Tachibana M., Chiba T., Nakao M.;
"Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1
heterochromatic complex for DNA methylation-based transcriptional
repression.";
J. Biol. Chem. 278:24132-24138(2003).
[14]
INTERACTION WITH CBX4.
PubMed=12101246; DOI=10.1128/MCB.22.15.5539-5553.2002;
Sewalt R.G.A.B., Lachner M., Vargas M., Hamer K.M., den Blaauwen J.L.,
Hendrix T., Melcher M., Schweizer D., Jenuwein T., Otte A.P.;
"Selective interactions between vertebrate polycomb homologs and the
SUV39H1 histone lysine methyltransferase suggest that histone H3-K9
methylation contributes to chromosomal targeting of Polycomb group
proteins.";
Mol. Cell. Biol. 22:5539-5553(2002).
[15]
INTERACTION WITH RUNX1.
PubMed=12917624; DOI=10.1038/sj.onc.1206600;
Chakraborty S., Sinha K.K., Senyuk V., Nucifora G.;
"SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is
methylated in vivo.";
Oncogene 22:5229-5237(2003).
[16]
IDENTIFICATION IN A COMPLEX WITH HDAC1.
PubMed=12789259; DOI=10.1038/sj.onc.1206578;
Macaluso M., Cinti C., Russo G., Russo A., Giordano A.;
"pRb2/p130-E2F4/5-HDAC1-SUV39H1-p300 and pRb2/p130-E2F4/5-HDAC1-
SUV39H1-DNMT1 multimolecular complexes mediate the transcription of
estrogen receptor-alpha in breast cancer.";
Oncogene 22:3511-3517(2003).
[17]
FUNCTION.
PubMed=14765126; DOI=10.1038/sj.emboj.7600074;
Ait-Si-Ali S., Guasconi V., Fritsch L., Yahi H., Sekhri R.,
Naguibneva I., Robin P., Cabon F., Polesskaya A., Harel-Bellan A.;
"A Suv39h-dependent mechanism for silencing S-phase genes in
differentiating but not in cycling cells.";
EMBO J. 23:605-615(2004).
[18]
INTERACTION WITH SMAD5.
PubMed=15107829; DOI=10.1038/sj.onc.1207660;
Frontelo P., Leader J.E., Yoo N., Potocki A.C., Crawford M., Kulik M.,
Lechleider R.J.;
"Suv39h histone methyltransferases interact with Smads and cooperate
in BMP-induced repression.";
Oncogene 23:5242-5251(2004).
[19]
DOMAIN, AND INTERACTION WITH CBX1.
PubMed=16103223; DOI=10.1083/jcb.200502154;
Krouwels I.M., Wiesmeijer K., Abraham T.E., Molenaar C.,
Verwoerd N.P., Tanke H.J., Dirks R.W.;
"A glue for heterochromatin maintenance: stable SUV39H1 binding to
heterochromatin is reinforced by the SET domain.";
J. Cell Biol. 170:537-549(2005).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[21]
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).
[22]
FUNCTION.
PubMed=16818776; DOI=10.4049/jimmunol.177.2.1179;
Bradley S.P., Kaminski D.A., Peters A.H.F.M., Jenuwein T.,
Stavnezer J.;
"The histone methyltransferase Suv39h1 increases class switch
recombination specifically to IgA.";
J. Immunol. 177:1179-1188(2006).
[23]
ENZYME REGULATION, AND MUTAGENESIS OF TRP-64 AND TYR-67.
PubMed=16519522; DOI=10.1021/bi051997r;
Chin H.G., Patnaik D., Esteve P.-O., Jacobsen S.E., Pradhan S.;
"Catalytic properties and kinetic mechanism of human recombinant Lys-9
histone H3 methyltransferase SUV39H1: participation of the
chromodomain in enzymatic catalysis.";
Biochemistry 45:3272-3284(2006).
[24]
FUNCTION, AND INTERACTION WITH MYOD1.
PubMed=16858404; DOI=10.1038/sj.emboj.7601229;
Mal A.K.;
"Histone methyltransferase Suv39h1 represses MyoD-stimulated myogenic
differentiation.";
EMBO J. 25:3323-3334(2006).
[25]
FUNCTION.
PubMed=16449642; DOI=10.1128/MCB.26.4.1288-1296.2006;
Carbone R., Botrugno O.A., Ronzoni S., Insinga A., Di Croce L.,
Pelicci P.G., Minucci S.;
"Recruitment of the histone methyltransferase SUV39H1 and its role in
the oncogenic properties of the leukemia-associated PML-retinoic acid
receptor fusion protein.";
Mol. Cell. Biol. 26:1288-1296(2006).
[26]
INTERACTION WITH RUNX1 AND RUNX3.
PubMed=16652147; DOI=10.1038/sj.onc.1209591;
Reed-Inderbitzin E., Moreno-Miralles I., Vanden-Eynden S.K., Xie J.,
Lutterbach B., Durst-Goodwin K.L., Luce K.S., Irvin B.J., Cleary M.L.,
Brandt S.J., Hiebert S.W.;
"RUNX1 associates with histone deacetylases and SUV39H1 to repress
transcription.";
Oncogene 25:5777-5786(2006).
[27]
INTERACTION WITH HTLV-1 TAX.
PubMed=16409643; DOI=10.1186/1742-4690-3-5;
Kamoi K., Yamamoto K., Misawa A., Miyake A., Ishida T., Tanaka Y.,
Mochizuki M., Watanabe T.;
"SUV39H1 interacts with HTLV-1 Tax and abrogates Tax transactivation
of HTLV-1 LTR.";
Retrovirology 3:5-5(2006).
[28]
FUNCTION, CATALYTIC ACTIVITY, ACETYLATION AT LYS-266, MUTAGENESIS OF
LYS-266, AND SUBCELLULAR LOCATION.
PubMed=18004385; DOI=10.1038/nature06268;
Vaquero A., Scher M., Erdjument-Bromage H., Tempst P., Serrano L.,
Reinberg D.;
"SIRT1 regulates the histone methyl-transferase SUV39H1 during
heterochromatin formation.";
Nature 450:440-444(2007).
[29]
IDENTIFICATION IN THE ENOSC COMPLEX, AND FUNCTION.
PubMed=18485871; DOI=10.1016/j.cell.2008.03.030;
Murayama A., Ohmori K., Fujimura A., Minami H., Yasuzawa-Tanaka K.,
Kuroda T., Oie S., Daitoku H., Okuwaki M., Nagata K., Fukamizu A.,
Kimura K., Shimizu T., Yanagisawa J.;
"Epigenetic control of rDNA loci in response to intracellular energy
status.";
Cell 133:627-639(2008).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, 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).
[31]
INTERACTION WITH CCAR2, AND ENZYME REGULATION.
PubMed=19218236; DOI=10.1074/jbc.M900956200;
Li Z., Chen L., Kabra N., Wang C., Fang J., Chen J.;
"Inhibition of SUV39H1 methyltransferase activity by DBC1.";
J. Biol. Chem. 284:10361-10366(2009).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND 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).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, 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).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, 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).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, 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).
[36]
INTERACTION WITH LMNA, AND SUBCELLULAR LOCATION.
PubMed=23695662; DOI=10.1038/ncomms2885;
Liu B., Wang Z., Zhang L., Ghosh S., Zheng H., Zhou Z.;
"Depleting the methyltransferase Suv39h1 improves DNA repair and
extends lifespan in a progeria mouse model.";
Nat. Commun. 4:1868-1868(2013).
-!- FUNCTION: Histone methyltransferase that specifically
trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-
9' as substrate. Also weakly methylates histone H1 (in vitro). H3
'Lys-9' trimethylation represents a specific tag for epigenetic
transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or
CBX5) proteins to methylated histones. Mainly functions in
heterochromatin regions, thereby playing a central role in the
establishment of constitutive heterochromatin at pericentric and
telomere regions. H3 'Lys-9' trimethylation is also required to
direct DNA methylation at pericentric repeats. SUV39H1 is targeted
to histone H3 via its interaction with RB1 and is involved in many
processes, such as repression of MYOD1-stimulated differentiation,
regulation of the control switch for exiting the cell cycle and
entering differentiation, repression by the PML-RARA fusion
protein, BMP-induced repression, repression of switch
recombination to IgA and regulation of telomere length. Component
of the eNoSC (energy-dependent nucleolar silencing) complex, a
complex that mediates silencing of rDNA in response to
intracellular energy status and acts by recruiting histone-
modifying enzymes. The eNoSC complex is able to sense the energy
status of cell: upon glucose starvation, elevation of
NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3
deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2)
by SUV39H1 and the formation of silent chromatin in the rDNA
locus. Recruited by the large PER complex to the E-box elements of
the circadian target genes such as PER2 itself or PER1,
contributes to the conversion of local chromatin to a
heterochromatin-like repressive state through H3 'Lys-9'
trimethylation. {ECO:0000269|PubMed:14765126,
ECO:0000269|PubMed:16449642, ECO:0000269|PubMed:16818776,
ECO:0000269|PubMed:16858404, ECO:0000269|PubMed:18004385,
ECO:0000269|PubMed:18485871}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000255|PROSITE-ProRule:PRU00912,
ECO:0000269|PubMed:10949293, ECO:0000269|PubMed:18004385}.
-!- ENZYME REGULATION: Inhibited by S-adenosyl-L-homocysteine.
Negatively regulated by CCAR2. {ECO:0000269|PubMed:16519522,
ECO:0000269|PubMed:19218236}.
-!- SUBUNIT: Interacts with H3 and H4 histones. Interacts with GFI1B,
DNMT3B, CBX1, CBX4, CCAR2, MBD1, RUNX1, RUNX3, MYOD1, SMAD5 and
RB1. Interacts with SBF1 through the SET domain. Interacts with
HDAC1 and HDAC2 through the N-terminus and associates with the
core histone deacetylase complex composed of HDAC1, HDAC2, RBBP4
and RBBP7. Component of the eNoSC complex, composed of SIRT1,
SUV39H1 and RRP8. In case of infection, interacts with HTLV-1 Tax
protein, leading to abrogate Tax transactivation of HTLV-1 LTR.
Interacts (via SET domain) with MECOM; enhances MECOM
transcriptional repression activity. Interacts with LMNA; the
interaction increases stability of SUV39H1. The large PER complex
involved in the histone methylation is composed of at least PER2,
CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation
of the complex. {ECO:0000269|PubMed:10202156,
ECO:0000269|PubMed:10848615, ECO:0000269|PubMed:11242053,
ECO:0000269|PubMed:11484059, ECO:0000269|PubMed:12101246,
ECO:0000269|PubMed:12711603, ECO:0000269|PubMed:12789259,
ECO:0000269|PubMed:12917624, ECO:0000269|PubMed:15107829,
ECO:0000269|PubMed:16103223, ECO:0000269|PubMed:16409643,
ECO:0000269|PubMed:16652147, ECO:0000269|PubMed:16688220,
ECO:0000269|PubMed:16858404, ECO:0000269|PubMed:18485871,
ECO:0000269|PubMed:19218236, ECO:0000269|PubMed:23695662}.
-!- INTERACTION:
P68432:- (xeno); NbExp=2; IntAct=EBI-349968, EBI-79764;
O95260:ATE1; NbExp=2; IntAct=EBI-349968, EBI-1043378;
Q9C0K0:BCL11B; NbExp=3; IntAct=EBI-349968, EBI-6597578;
Q6P047:C8orf74; NbExp=2; IntAct=EBI-349968, EBI-8466055;
P83916:CBX1; NbExp=3; IntAct=EBI-349968, EBI-78129;
Q13185:CBX3; NbExp=6; IntAct=EBI-349968, EBI-78176;
P45973:CBX5; NbExp=8; IntAct=EBI-349968, EBI-78219;
A5D8V7:CCDC151; NbExp=2; IntAct=EBI-349968, EBI-8466445;
Q9BXL8:CDCA4; NbExp=2; IntAct=EBI-349968, EBI-1773949;
Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-349968, EBI-739624;
P49761:CLK3; NbExp=2; IntAct=EBI-349968, EBI-745579;
Q5TAQ9:DCAF8; NbExp=2; IntAct=EBI-349968, EBI-740686;
Q15910:EZH2; NbExp=2; IntAct=EBI-349968, EBI-530054;
Q6ZNL6:FGD5; NbExp=2; IntAct=EBI-349968, EBI-7962481;
Q9NWQ4:GPATCH2L; NbExp=2; IntAct=EBI-349968, EBI-5666657;
Q9BX10:GTPBP2; NbExp=2; IntAct=EBI-349968, EBI-6115579;
Q13547:HDAC1; NbExp=3; IntAct=EBI-349968, EBI-301834;
Q92769:HDAC2; NbExp=3; IntAct=EBI-349968, EBI-301821;
V9HWG0:HEL25; NbExp=3; IntAct=EBI-349968, EBI-10183977;
Q96ED9:HOOK2; NbExp=4; IntAct=EBI-349968, EBI-743290;
P49639:HOXA1; NbExp=2; IntAct=EBI-349968, EBI-740785;
P09017:HOXC4; NbExp=2; IntAct=EBI-349968, EBI-3923226;
Q8TBB5:KLHDC4; NbExp=2; IntAct=EBI-349968, EBI-8472352;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-349968, EBI-10172290;
Q9BRK4:LZTS2; NbExp=5; IntAct=EBI-349968, EBI-741037;
Q9UIS9:MBD1; NbExp=5; IntAct=EBI-349968, EBI-867196;
Q13133:NR1H3; NbExp=2; IntAct=EBI-349968, EBI-781356;
Q6TGC4:PADI6; NbExp=4; IntAct=EBI-349968, EBI-10892722;
Q5T6S3:PHF19; NbExp=2; IntAct=EBI-349968, EBI-2339674;
Q15156:PML-RAR; NbExp=4; IntAct=EBI-349968, EBI-867256;
P62191:PSMC1; NbExp=2; IntAct=EBI-349968, EBI-357598;
Q9NS23:RASSF1; NbExp=2; IntAct=EBI-349968, EBI-367363;
P50749:RASSF2; NbExp=2; IntAct=EBI-349968, EBI-960081;
O43159:RRP8; NbExp=3; IntAct=EBI-349968, EBI-2008793;
Q96BD6:SPSB1; NbExp=2; IntAct=EBI-349968, EBI-2659201;
Q8N4C7:STX19; NbExp=2; IntAct=EBI-349968, EBI-8484990;
Q01081:U2AF1; NbExp=2; IntAct=EBI-349968, EBI-632461;
Q9Y2L8:ZKSCAN5; NbExp=2; IntAct=EBI-349968, EBI-2876965;
Q9C0F3:ZNF436; NbExp=2; IntAct=EBI-349968, EBI-8489702;
Q9BS31:ZNF649; NbExp=2; IntAct=EBI-349968, EBI-4395789;
Q9BS34:ZNF670; NbExp=2; IntAct=EBI-349968, EBI-745276;
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus lamina. Nucleus,
nucleoplasm. Chromosome, centromere. Note=Associates with
centromeric constitutive heterochromatin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O43463-1; Sequence=Displayed;
Name=2;
IsoId=O43463-2; Sequence=VSP_054286;
Note=No experimental confirmation available.;
-!- DEVELOPMENTAL STAGE: Accumulates during mitosis at centromeres
during prometaphase, but dissociates from the centromere at the
meta- to anaphase transition.
-!- DOMAIN: Although the SET domain contains the active site of
enzymatic activity, both pre-SET and post-SET domains are required
for methyltransferase activity. The SET domain also participates
in stable binding to heterochromatin.
{ECO:0000269|PubMed:16103223}.
-!- 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:16103223}.
-!- PTM: Phosphorylated on serine residues, and to a lesser degree, on
threonine residues. The phosphorylated form is stabilized by SBF1
and is less active in its transcriptional repressor function.
{ECO:0000269|PubMed:10671371}.
-!- PTM: Acetylated at Lys-266, leading to inhibition of enzyme
activity. SIRT1-mediated deacetylation relieves this inhibition.
{ECO:0000269|PubMed:18004385}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00912}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF019968; AAB92224.1; -; mRNA.
EMBL; CR541746; CAG46546.1; -; mRNA.
EMBL; AK223071; BAD96791.1; -; mRNA.
EMBL; AK299900; BAG61742.1; -; mRNA.
EMBL; AK312547; BAG35445.1; -; mRNA.
EMBL; AF196970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471224; EAW50756.1; -; Genomic_DNA.
EMBL; CH471224; EAW50757.1; -; Genomic_DNA.
EMBL; BC006238; AAH06238.1; -; mRNA.
CCDS; CCDS14304.1; -. [O43463-1]
CCDS; CCDS65252.1; -. [O43463-2]
RefSeq; NP_001269095.1; NM_001282166.1. [O43463-2]
RefSeq; NP_003164.1; NM_003173.3. [O43463-1]
UniGene; Hs.522639; -.
PDB; 3MTS; X-ray; 2.20 A; A/B/C=44-106.
PDBsum; 3MTS; -.
ProteinModelPortal; O43463; -.
SMR; O43463; -.
BioGrid; 112706; 170.
CORUM; O43463; -.
DIP; DIP-32589N; -.
IntAct; O43463; 134.
MINT; MINT-191763; -.
STRING; 9606.ENSP00000365877; -.
BindingDB; O43463; -.
ChEMBL; CHEMBL1795118; -.
GuidetoPHARMACOLOGY; 2715; -.
iPTMnet; O43463; -.
PhosphoSitePlus; O43463; -.
EPD; O43463; -.
MaxQB; O43463; -.
PaxDb; O43463; -.
PeptideAtlas; O43463; -.
PRIDE; O43463; -.
DNASU; 6839; -.
Ensembl; ENST00000337852; ENSP00000337976; ENSG00000101945. [O43463-2]
Ensembl; ENST00000376687; ENSP00000365877; ENSG00000101945. [O43463-1]
GeneID; 6839; -.
KEGG; hsa:6839; -.
UCSC; uc004dkn.5; human. [O43463-1]
CTD; 6839; -.
DisGeNET; 6839; -.
EuPathDB; HostDB:ENSG00000101945.16; -.
GeneCards; SUV39H1; -.
HGNC; HGNC:11479; SUV39H1.
MIM; 300254; gene.
neXtProt; NX_O43463; -.
OpenTargets; ENSG00000101945; -.
PharmGKB; PA36264; -.
eggNOG; KOG1082; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00780000121845; -.
HOGENOM; HOG000231244; -.
HOVERGEN; HBG055621; -.
InParanoid; O43463; -.
KO; K11419; -.
OMA; NTFVMEY; -.
OrthoDB; EOG091G0Y4N; -.
PhylomeDB; O43463; -.
TreeFam; TF106452; -.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA Expression.
SIGNOR; O43463; -.
ChiTaRS; SUV39H1; human.
GeneWiki; SUV39H1; -.
GenomeRNAi; 6839; -.
PRO; PR:O43463; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000101945; -.
CleanEx; HS_SUV39H1; -.
Genevisible; O43463; HS.
GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
GO; GO:0000794; C:condensed nuclear chromosome; TAS:ProtInc.
GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
GO; GO:0005652; C:nuclear lamina; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0033553; C:rDNA heterochromatin; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; TAS:ProtInc.
GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB.
GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:UniProtKB.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
GO; GO:0006325; P:chromatin organization; TAS:ProtInc.
GO; GO:0000183; P:chromatin silencing at rDNA; IDA:UniProtKB.
GO; GO:0036123; P:histone H3-K9 dimethylation; ISS:UniProtKB.
GO; GO:0036124; P:histone H3-K9 trimethylation; ISS:UniProtKB.
GO; GO:0042754; P:negative regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR023780; Chromo_domain.
InterPro; IPR016197; Chromodomain-like.
InterPro; IPR023779; Chromodomain_CS.
InterPro; IPR011381; Histone_H3-K9_MeTrfase.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR007728; Pre-SET_dom.
InterPro; IPR001214; SET_dom.
Pfam; PF00385; Chromo; 1.
Pfam; PF05033; Pre-SET; 1.
Pfam; PF00856; SET; 1.
PIRSF; PIRSF009343; SUV39_SET; 1.
SMART; SM00298; CHROMO; 1.
SMART; SM00508; PostSET; 1.
SMART; SM00468; PreSET; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF54160; SSF54160; 1.
PROSITE; PS00598; CHROMO_1; 1.
PROSITE; PS50013; CHROMO_2; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50867; PRE_SET; 1.
PROSITE; PS51579; SAM_MT43_SUVAR39_3; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Biological rhythms;
Cell cycle; Centromere; Chromatin regulator; Chromosome;
Complete proteome; Differentiation; Host-virus interaction;
Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
Reference proteome; Repressor; rRNA processing;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Zinc.
CHAIN 1 412 Histone-lysine N-methyltransferase
SUV39H1.
/FTId=PRO_0000186057.
DOMAIN 43 101 Chromo. {ECO:0000255|PROSITE-
ProRule:PRU00053}.
DOMAIN 179 240 Pre-SET. {ECO:0000255|PROSITE-
ProRule:PRU00157}.
DOMAIN 243 366 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 396 412 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
REGION 1 89 Interaction with SIRT1.
REGION 254 256 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 255 377 Mediates interaction with MECOM.
{ECO:0000250}.
REGION 323 324 S-adenosyl-L-methionine binding.
{ECO:0000250}.
METAL 181 181 Zinc 1. {ECO:0000250}.
METAL 181 181 Zinc 2. {ECO:0000250}.
METAL 183 183 Zinc 1. {ECO:0000250}.
METAL 186 186 Zinc 1. {ECO:0000250}.
METAL 186 186 Zinc 3. {ECO:0000250}.
METAL 194 194 Zinc 1. {ECO:0000250}.
METAL 195 195 Zinc 1. {ECO:0000250}.
METAL 195 195 Zinc 2. {ECO:0000250}.
METAL 222 222 Zinc 2. {ECO:0000250}.
METAL 222 222 Zinc 3. {ECO:0000250}.
METAL 226 226 Zinc 2. {ECO:0000250}.
METAL 228 228 Zinc 3. {ECO:0000250}.
METAL 232 232 Zinc 3. {ECO:0000250}.
METAL 326 326 Zinc 4. {ECO:0000250}.
METAL 400 400 Zinc 4. {ECO:0000250}.
METAL 402 402 Zinc 4. {ECO:0000250}.
METAL 407 407 Zinc 4. {ECO:0000250}.
BINDING 297 297 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
MOD_RES 266 266 N6-acetyllysine.
{ECO:0000269|PubMed:18004385}.
MOD_RES 391 391 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 6 MAENLK -> MVGMSRLRNDRLADPLT (in isoform
2). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_054286.
MUTAGEN 64 64 W->A: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:16519522}.
MUTAGEN 67 67 Y->A: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:16519522}.
MUTAGEN 266 266 K->A: Loss of SIRT1-mediated up-
regulation of enzymatic activity.
{ECO:0000269|PubMed:18004385}.
MUTAGEN 266 266 K->Q: Significant loss of enzymatic
activity. {ECO:0000269|PubMed:18004385}.
MUTAGEN 320 320 H->R: Strongly increases methylation of
histone H3.
{ECO:0000269|PubMed:10949293}.
MUTAGEN 324 324 H->L,K: Abolishes methylation of histone
H3. {ECO:0000269|PubMed:10949293}.
MUTAGEN 326 326 C->A: Abolishes methylation of histone
H3. {ECO:0000269|PubMed:10949293}.
CONFLICT 213 213 L -> P (in Ref. 4; BAD96791).
{ECO:0000305}.
STRAND 45 53 {ECO:0000244|PDB:3MTS}.
STRAND 58 64 {ECO:0000244|PDB:3MTS}.
HELIX 69 71 {ECO:0000244|PDB:3MTS}.
STRAND 73 76 {ECO:0000244|PDB:3MTS}.
HELIX 77 79 {ECO:0000244|PDB:3MTS}.
HELIX 83 103 {ECO:0000244|PDB:3MTS}.
SEQUENCE 412 AA; 47907 MW; AF6F959AD20C6C76 CRC64;
MAENLKGCSV CCKSSWNQLQ DLCRLAKLSC PALGISKRNL YDFEVEYLCD YKKIREQEYY
LVKWRGYPDS ESTWEPRQNL KCVRILKQFH KDLERELLRR HHRSKTPRHL DPSLANYLVQ
KAKQRRALRR WEQELNAKRS HLGRITVENE VDLDGPPRAF VYINEYRVGE GITLNQVAVG
CECQDCLWAP TGGCCPGASL HKFAYNDQGQ VRLRAGLPIY ECNSRCRCGY DCPNRVVQKG
IRYDLCIFRT DDGRGWGVRT LEKIRKNSFV MEYVGEIITS EEAERRGQIY DRQGATYLFD
LDYVEDVYTV DAAYYGNISH FVNHSCDPNL QVYNVFIDNL DERLPRIAFF ATRTIRAGEE
LTFDYNMQVD PVDMESTRMD SNFGLAGLPG SPKKRVRIEC KCGTESCRKY LF


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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
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
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
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
EIAAB13541 Enhancer of zeste homolog 2,ENX-1,EZH2,Histone-lysine N-methyltransferase EZH2,Homo sapiens,Human,KMT6,Lysine N-methyltransferase 6
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


 

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