SUV91_HUMAN
ID SUV91_HUMAN Reviewed; 412 AA.
AC O43463; B2R6E8; B4DST0; Q53G60; Q6FHK6;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Histone-lysine N-methyltransferase SUV39H1;
DE EC=2.1.1.355 {ECO:0000269|PubMed:10949293, ECO:0000269|PubMed:18004385};
DE AltName: Full=Histone H3-K9 methyltransferase 1;
DE Short=H3-K9-HMTase 1;
DE AltName: Full=Lysine N-methyltransferase 1A;
DE AltName: Full=Position-effect variegation 3-9 homolog;
DE AltName: Full=Suppressor of variegation 3-9 homolog 1;
DE Short=Su(var)3-9 homolog 1;
GN Name=SUV39H1; Synonyms=KMT1A, SUV39H;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH CBX1.
RC TISSUE=B-cell;
RX PubMed=10202156; DOI=10.1093/emboj/18.7.1923;
RA Aagaard L., Laible G., Selenko P., Schmid M., Dorn R., Schotta G.,
RA Kuhfittig S., Wolf A., Lebersorger A., Singh P.B., Reuter G., Jenuwein T.;
RT "Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9
RT encode centromere-associated proteins which complex with the
RT heterochromatin component M31.";
RL EMBO J. 18:1923-1938(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=10671371; DOI=10.1242/jcs.113.5.817;
RA Aagaard L., Schmid M., Warburton P., Jenuwein T.;
RT "Mitotic phosphorylation of SUV39H1, a novel component of active
RT centromeres, coincides with transient accumulation at mammalian
RT centromeres.";
RL J. Cell Sci. 113:817-829(2000).
RN [9]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-320; HIS-324 AND CYS-326.
RX PubMed=10949293; DOI=10.1038/35020506;
RA Rea S., Eisenhaber F., O'Carroll D., Strahl B.D., Sun Z.-W., Schmid M.,
RA Opravil S., Mechtler K., Ponting C.P., Allis C.D., Jenuwein T.;
RT "Regulation of chromatin structure by site-specific histone H3
RT methyltransferases.";
RL Nature 406:593-599(2000).
RN [10]
RP INTERACTION WITH SBF1.
RX PubMed=10848615; DOI=10.1128/mcb.20.13.4900-4909.2000;
RA Firestein R., Cui X., Huie P., Cleary M.L.;
RT "Set domain-dependent regulation of transcriptional silencing and growth
RT control by SUV39H1, a mammalian ortholog of Drosophila Su(var)3-9.";
RL Mol. Cell. Biol. 20:4900-4909(2000).
RN [11]
RP INTERACTION WITH HISTONE H3 AND HISTONE H4.
RX PubMed=11242053; DOI=10.1038/35065132;
RA Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.;
RT "Methylation of histone H3 lysine 9 creates a binding site for HP1
RT proteins.";
RL Nature 410:116-120(2001).
RN [12]
RP INTERACTION WITH RB1.
RX PubMed=11484059; DOI=10.1038/35087620;
RA Nielsen S.J., Schneider R., Bauer U.-M., Bannister A.J., Morrison A.,
RA O'Carroll D., Firestein R., Cleary M.L., Jenuwein T., Herrera R.E.,
RA Kouzarides T.;
RT "Rb targets histone H3 methylation and HP1 to promoters.";
RL Nature 412:561-565(2001).
RN [13]
RP INTERACTION WITH MBD1.
RX PubMed=12711603; DOI=10.1074/jbc.m302283200;
RA Fujita N., Watanabe S., Ichimura T., Tsuruzoe S., Shinkai Y., Tachibana M.,
RA Chiba T., Nakao M.;
RT "Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1
RT heterochromatic complex for DNA methylation-based transcriptional
RT repression.";
RL J. Biol. Chem. 278:24132-24138(2003).
RN [14]
RP INTERACTION WITH CBX4.
RX PubMed=12101246; DOI=10.1128/mcb.22.15.5539-5553.2002;
RA Sewalt R.G.A.B., Lachner M., Vargas M., Hamer K.M., den Blaauwen J.L.,
RA Hendrix T., Melcher M., Schweizer D., Jenuwein T., Otte A.P.;
RT "Selective interactions between vertebrate polycomb homologs and the
RT SUV39H1 histone lysine methyltransferase suggest that histone H3-K9
RT methylation contributes to chromosomal targeting of Polycomb group
RT proteins.";
RL Mol. Cell. Biol. 22:5539-5553(2002).
RN [15]
RP INTERACTION WITH RUNX1.
RX PubMed=12917624; DOI=10.1038/sj.onc.1206600;
RA Chakraborty S., Sinha K.K., Senyuk V., Nucifora G.;
RT "SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is
RT methylated in vivo.";
RL Oncogene 22:5229-5237(2003).
RN [16]
RP IDENTIFICATION IN A COMPLEX WITH HDAC1.
RX PubMed=12789259; DOI=10.1038/sj.onc.1206578;
RA Macaluso M., Cinti C., Russo G., Russo A., Giordano A.;
RT "pRb2/p130-E2F4/5-HDAC1-SUV39H1-p300 and pRb2/p130-E2F4/5-HDAC1-SUV39H1-
RT DNMT1 multimolecular complexes mediate the transcription of estrogen
RT receptor-alpha in breast cancer.";
RL Oncogene 22:3511-3517(2003).
RN [17]
RP FUNCTION.
RX PubMed=14765126; DOI=10.1038/sj.emboj.7600074;
RA Ait-Si-Ali S., Guasconi V., Fritsch L., Yahi H., Sekhri R., Naguibneva I.,
RA Robin P., Cabon F., Polesskaya A., Harel-Bellan A.;
RT "A Suv39h-dependent mechanism for silencing S-phase genes in
RT differentiating but not in cycling cells.";
RL EMBO J. 23:605-615(2004).
RN [18]
RP INTERACTION WITH SMAD5.
RX PubMed=15107829; DOI=10.1038/sj.onc.1207660;
RA Frontelo P., Leader J.E., Yoo N., Potocki A.C., Crawford M., Kulik M.,
RA Lechleider R.J.;
RT "Suv39h histone methyltransferases interact with Smads and cooperate in
RT BMP-induced repression.";
RL Oncogene 23:5242-5251(2004).
RN [19]
RP DOMAIN, AND INTERACTION WITH CBX1.
RX PubMed=16103223; DOI=10.1083/jcb.200502154;
RA Krouwels I.M., Wiesmeijer K., Abraham T.E., Molenaar C., Verwoerd N.P.,
RA Tanke H.J., Dirks R.W.;
RT "A glue for heterochromatin maintenance: stable SUV39H1 binding to
RT heterochromatin is reinforced by the SET domain.";
RL J. Cell Biol. 170:537-549(2005).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [21]
RP INTERACTION WITH GFI1B.
RX PubMed=16688220; DOI=10.1038/sj.emboj.7601124;
RA Vassen L., Fiolka K., Moeroey T.;
RT "Gfi1b alters histone methylation at target gene promoters and sites of
RT gamma-satellite containing heterochromatin.";
RL EMBO J. 25:2409-2419(2006).
RN [22]
RP FUNCTION.
RX PubMed=16818776; DOI=10.4049/jimmunol.177.2.1179;
RA Bradley S.P., Kaminski D.A., Peters A.H.F.M., Jenuwein T., Stavnezer J.;
RT "The histone methyltransferase Suv39h1 increases class switch recombination
RT specifically to IgA.";
RL J. Immunol. 177:1179-1188(2006).
RN [23]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF TRP-64 AND TYR-67.
RX PubMed=16519522; DOI=10.1021/bi051997r;
RA Chin H.G., Patnaik D., Esteve P.-O., Jacobsen S.E., Pradhan S.;
RT "Catalytic properties and kinetic mechanism of human recombinant Lys-9
RT histone H3 methyltransferase SUV39H1: participation of the chromodomain in
RT enzymatic catalysis.";
RL Biochemistry 45:3272-3284(2006).
RN [24]
RP FUNCTION, AND INTERACTION WITH MYOD1.
RX PubMed=16858404; DOI=10.1038/sj.emboj.7601229;
RA Mal A.K.;
RT "Histone methyltransferase Suv39h1 represses MyoD-stimulated myogenic
RT differentiation.";
RL EMBO J. 25:3323-3334(2006).
RN [25]
RP FUNCTION.
RX PubMed=16449642; DOI=10.1128/mcb.26.4.1288-1296.2006;
RA Carbone R., Botrugno O.A., Ronzoni S., Insinga A., Di Croce L.,
RA Pelicci P.G., Minucci S.;
RT "Recruitment of the histone methyltransferase SUV39H1 and its role in the
RT oncogenic properties of the leukemia-associated PML-retinoic acid receptor
RT fusion protein.";
RL Mol. Cell. Biol. 26:1288-1296(2006).
RN [26]
RP INTERACTION WITH RUNX1 AND RUNX3.
RX PubMed=16652147; DOI=10.1038/sj.onc.1209591;
RA Reed-Inderbitzin E., Moreno-Miralles I., Vanden-Eynden S.K., Xie J.,
RA Lutterbach B., Durst-Goodwin K.L., Luce K.S., Irvin B.J., Cleary M.L.,
RA Brandt S.J., Hiebert S.W.;
RT "RUNX1 associates with histone deacetylases and SUV39H1 to repress
RT transcription.";
RL Oncogene 25:5777-5786(2006).
RN [27]
RP INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION).
RX PubMed=16409643; DOI=10.1186/1742-4690-3-5;
RA Kamoi K., Yamamoto K., Misawa A., Miyake A., Ishida T., Tanaka Y.,
RA Mochizuki M., Watanabe T.;
RT "SUV39H1 interacts with HTLV-1 Tax and abrogates Tax transactivation of
RT HTLV-1 LTR.";
RL Retrovirology 3:5-5(2006).
RN [28]
RP FUNCTION, CATALYTIC ACTIVITY, ACETYLATION AT LYS-266, MUTAGENESIS OF
RP LYS-266, AND SUBCELLULAR LOCATION.
RX PubMed=18004385; DOI=10.1038/nature06268;
RA Vaquero A., Scher M., Erdjument-Bromage H., Tempst P., Serrano L.,
RA Reinberg D.;
RT "SIRT1 regulates the histone methyl-transferase SUV39H1 during
RT heterochromatin formation.";
RL Nature 450:440-444(2007).
RN [29]
RP IDENTIFICATION IN THE ENOSC COMPLEX, AND FUNCTION.
RX PubMed=18485871; DOI=10.1016/j.cell.2008.03.030;
RA Murayama A., Ohmori K., Fujimura A., Minami H., Yasuzawa-Tanaka K.,
RA Kuroda T., Oie S., Daitoku H., Okuwaki M., Nagata K., Fukamizu A.,
RA Kimura K., Shimizu T., Yanagisawa J.;
RT "Epigenetic control of rDNA loci in response to intracellular energy
RT status.";
RL Cell 133:627-639(2008).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [31]
RP INTERACTION WITH CCAR2, AND ACTIVITY REGULATION.
RX PubMed=19218236; DOI=10.1074/jbc.m900956200;
RA Li Z., Chen L., Kabra N., Wang C., Fang J., Chen J.;
RT "Inhibition of SUV39H1 methyltransferase activity by DBC1.";
RL J. Biol. Chem. 284:10361-10366(2009).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [36]
RP INTERACTION WITH LMNA, AND SUBCELLULAR LOCATION.
RX PubMed=23695662; DOI=10.1038/ncomms2885;
RA Liu B., Wang Z., Zhang L., Ghosh S., Zheng H., Zhou Z.;
RT "Depleting the methyltransferase Suv39h1 improves DNA repair and extends
RT lifespan in a progeria mouse model.";
RL Nat. Commun. 4:1868-1868(2013).
CC -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate.
CC Also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation
CC represents a specific tag for epigenetic transcriptional repression by
CC recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated
CC histones. Mainly functions in heterochromatin regions, thereby playing
CC a central role in the establishment of constitutive heterochromatin at
CC pericentric and telomere regions. H3 'Lys-9' trimethylation is also
CC required to direct DNA methylation at pericentric repeats. SUV39H1 is
CC targeted to histone H3 via its interaction with RB1 and is involved in
CC many processes, such as repression of MYOD1-stimulated differentiation,
CC regulation of the control switch for exiting the cell cycle and
CC entering differentiation, repression by the PML-RARA fusion protein,
CC BMP-induced repression, repression of switch recombination to IgA and
CC regulation of telomere length. Component of the eNoSC (energy-dependent
CC nucleolar silencing) complex, a complex that mediates silencing of rDNA
CC in response to intracellular energy status and acts by recruiting
CC histone-modifying enzymes. The eNoSC complex is able to sense the
CC energy status of cell: upon glucose starvation, elevation of
CC NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3
CC deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by
CC SUV39H1 and the formation of silent chromatin in the rDNA locus.
CC Recruited by the large PER complex to the E-box elements of the
CC circadian target genes such as PER2 itself or PER1, contributes to the
CC conversion of local chromatin to a heterochromatin-like repressive
CC state through H3 'Lys-9' trimethylation. {ECO:0000269|PubMed:14765126,
CC ECO:0000269|PubMed:16449642, ECO:0000269|PubMed:16818776,
CC ECO:0000269|PubMed:16858404, ECO:0000269|PubMed:18004385,
CC ECO:0000269|PubMed:18485871}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00912,
CC ECO:0000269|PubMed:10949293, ECO:0000269|PubMed:18004385};
CC -!- ACTIVITY REGULATION: Inhibited by S-adenosyl-L-homocysteine. Negatively
CC regulated by CCAR2. {ECO:0000269|PubMed:16519522,
CC ECO:0000269|PubMed:19218236}.
CC -!- SUBUNIT: Interacts with H3 and H4 histones. Interacts with GFI1B,
CC DNMT3B, CBX1, CBX4, CCAR2, MBD1, RUNX1, RUNX3, MYOD1, SMAD5 and RB1.
CC Interacts with SBF1 through the SET domain. Interacts with HDAC1 and
CC HDAC2 through the N-terminus and associates with the core histone
CC deacetylase complex composed of HDAC1, HDAC2, RBBP4 and RBBP7.
CC Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8.
CC Interacts (via SET domain) with MECOM; enhances MECOM transcriptional
CC repression activity. Interacts with LMNA; the interaction increases
CC stability of SUV39H1. The large PER complex involved in the histone
CC methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or
CC SUV39H2; CBX3 mediates the formation of the complex.
CC {ECO:0000269|PubMed:10202156, ECO:0000269|PubMed:10848615,
CC ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:11484059,
CC ECO:0000269|PubMed:12101246, ECO:0000269|PubMed:12711603,
CC ECO:0000269|PubMed:12789259, ECO:0000269|PubMed:12917624,
CC ECO:0000269|PubMed:15107829, ECO:0000269|PubMed:16103223,
CC ECO:0000269|PubMed:16652147, ECO:0000269|PubMed:16688220,
CC ECO:0000269|PubMed:16858404, ECO:0000269|PubMed:18485871,
CC ECO:0000269|PubMed:19218236, ECO:0000269|PubMed:23695662}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 Tax protein,
CC leading to abrogate Tax transactivation of HTLV-1 LTR.
CC {ECO:0000269|PubMed:16409643}.
CC -!- INTERACTION:
CC O43463; O95260: ATE1; NbExp=2; IntAct=EBI-349968, EBI-1043378;
CC O43463; Q86V38: ATN1; NbExp=3; IntAct=EBI-349968, EBI-11954292;
CC O43463; Q9C0K0: BCL11B; NbExp=3; IntAct=EBI-349968, EBI-6597578;
CC O43463; Q6P047: C8orf74; NbExp=2; IntAct=EBI-349968, EBI-8466055;
CC O43463; P83916: CBX1; NbExp=4; IntAct=EBI-349968, EBI-78129;
CC O43463; Q13185: CBX3; NbExp=8; IntAct=EBI-349968, EBI-78176;
CC O43463; P45973: CBX5; NbExp=16; IntAct=EBI-349968, EBI-78219;
CC O43463; Q9BXL8: CDCA4; NbExp=2; IntAct=EBI-349968, EBI-1773949;
CC O43463; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-349968, EBI-739624;
CC O43463; P49761: CLK3; NbExp=2; IntAct=EBI-349968, EBI-745579;
CC O43463; Q5TAQ9: DCAF8; NbExp=2; IntAct=EBI-349968, EBI-740686;
CC O43463; Q92997: DVL3; NbExp=3; IntAct=EBI-349968, EBI-739789;
CC O43463; Q15910: EZH2; NbExp=2; IntAct=EBI-349968, EBI-530054;
CC O43463; Q6ZNL6: FGD5; NbExp=2; IntAct=EBI-349968, EBI-7962481;
CC O43463; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-349968, EBI-5916454;
CC O43463; Q9NWQ4: GPATCH2L; NbExp=2; IntAct=EBI-349968, EBI-5666657;
CC O43463; Q9BX10: GTPBP2; NbExp=2; IntAct=EBI-349968, EBI-6115579;
CC O43463; Q13547: HDAC1; NbExp=3; IntAct=EBI-349968, EBI-301834;
CC O43463; Q92769: HDAC2; NbExp=3; IntAct=EBI-349968, EBI-301821;
CC O43463; V9HWG0: HEL25; NbExp=3; IntAct=EBI-349968, EBI-10183977;
CC O43463; Q96ED9: HOOK2; NbExp=4; IntAct=EBI-349968, EBI-743290;
CC O43463; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-349968, EBI-10961706;
CC O43463; P49639: HOXA1; NbExp=2; IntAct=EBI-349968, EBI-740785;
CC O43463; P09017: HOXC4; NbExp=2; IntAct=EBI-349968, EBI-3923226;
CC O43463; Q8TBB5: KLHDC4; NbExp=2; IntAct=EBI-349968, EBI-8472352;
CC O43463; Q92876: KLK6; NbExp=3; IntAct=EBI-349968, EBI-2432309;
CC O43463; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-349968, EBI-10172290;
CC O43463; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-349968, EBI-10171774;
CC O43463; Q9BRK4: LZTS2; NbExp=6; IntAct=EBI-349968, EBI-741037;
CC O43463; Q9UIS9: MBD1; NbExp=5; IntAct=EBI-349968, EBI-867196;
CC O43463; Q13133: NR1H3; NbExp=2; IntAct=EBI-349968, EBI-781356;
CC O43463; A5D8V7: ODAD3; NbExp=2; IntAct=EBI-349968, EBI-8466445;
CC O43463; Q6TGC4: PADI6; NbExp=3; IntAct=EBI-349968, EBI-10892722;
CC O43463; Q5T6S3: PHF19; NbExp=2; IntAct=EBI-349968, EBI-2339674;
CC O43463; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-349968, EBI-710402;
CC O43463; P62191: PSMC1; NbExp=2; IntAct=EBI-349968, EBI-357598;
CC O43463; P54725: RAD23A; NbExp=3; IntAct=EBI-349968, EBI-746453;
CC O43463; Q9NS23: RASSF1; NbExp=2; IntAct=EBI-349968, EBI-367363;
CC O43463; P50749: RASSF2; NbExp=2; IntAct=EBI-349968, EBI-960081;
CC O43463; O43159: RRP8; NbExp=3; IntAct=EBI-349968, EBI-2008793;
CC O43463; P50454: SERPINH1; NbExp=3; IntAct=EBI-349968, EBI-350723;
CC O43463; Q96EB6: SIRT1; NbExp=5; IntAct=EBI-349968, EBI-1802965;
CC O43463; Q96BD6: SPSB1; NbExp=2; IntAct=EBI-349968, EBI-2659201;
CC O43463; Q8N4C7: STX19; NbExp=2; IntAct=EBI-349968, EBI-8484990;
CC O43463; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-349968, EBI-750487;
CC O43463; P37173: TGFBR2; NbExp=3; IntAct=EBI-349968, EBI-296151;
CC O43463; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-349968, EBI-725997;
CC O43463; Q01081: U2AF1; NbExp=2; IntAct=EBI-349968, EBI-632461;
CC O43463; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-349968, EBI-2515601;
CC O43463; Q9Y2L8: ZKSCAN5; NbExp=2; IntAct=EBI-349968, EBI-2876965;
CC O43463; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-349968, EBI-740727;
CC O43463; Q9C0F3: ZNF436; NbExp=2; IntAct=EBI-349968, EBI-8489702;
CC O43463; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-349968, EBI-11962468;
CC O43463; Q9BS31: ZNF649; NbExp=2; IntAct=EBI-349968, EBI-4395789;
CC O43463; Q9BS34: ZNF670; NbExp=2; IntAct=EBI-349968, EBI-745276;
CC O43463; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-349968, EBI-527853;
CC O43463; P68432; Xeno; NbExp=2; IntAct=EBI-349968, EBI-79764;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus lamina. Nucleus, nucleoplasm.
CC Chromosome, centromere. Note=Associates with centromeric constitutive
CC heterochromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43463-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43463-2; Sequence=VSP_054286;
CC -!- DEVELOPMENTAL STAGE: Accumulates during mitosis at centromeres during
CC prometaphase, but dissociates from the centromere at the meta- to
CC anaphase transition.
CC -!- DOMAIN: Although the SET domain contains the active site of enzymatic
CC activity, both pre-SET and post-SET domains are required for
CC methyltransferase activity. The SET domain also participates in stable
CC binding to heterochromatin. {ECO:0000269|PubMed:16103223}.
CC -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are
CC arranged in a triangular cluster; some of these Cys residues contribute
CC to the binding of two zinc ions within the cluster.
CC {ECO:0000269|PubMed:16103223}.
CC -!- PTM: Phosphorylated on serine residues, and to a lesser degree, on
CC threonine residues. The phosphorylated form is stabilized by SBF1 and
CC is less active in its transcriptional repressor function.
CC {ECO:0000269|PubMed:10671371}.
CC -!- PTM: Acetylated at Lys-266, leading to inhibition of enzyme activity.
CC SIRT1-mediated deacetylation relieves this inhibition.
CC {ECO:0000269|PubMed:18004385}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00912}.
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DR EMBL; AF019968; AAB92224.1; -; mRNA.
DR EMBL; CR541746; CAG46546.1; -; mRNA.
DR EMBL; AK223071; BAD96791.1; -; mRNA.
DR EMBL; AK299900; BAG61742.1; -; mRNA.
DR EMBL; AK312547; BAG35445.1; -; mRNA.
DR EMBL; AF196970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471224; EAW50756.1; -; Genomic_DNA.
DR EMBL; CH471224; EAW50757.1; -; Genomic_DNA.
DR EMBL; BC006238; AAH06238.1; -; mRNA.
DR CCDS; CCDS14304.1; -. [O43463-1]
DR CCDS; CCDS65252.1; -. [O43463-2]
DR RefSeq; NP_001269095.1; NM_001282166.1. [O43463-2]
DR RefSeq; NP_003164.1; NM_003173.3. [O43463-1]
DR PDB; 3MTS; X-ray; 2.20 A; A/B/C=44-106.
DR PDBsum; 3MTS; -.
DR AlphaFoldDB; O43463; -.
DR SMR; O43463; -.
DR BioGRID; 112706; 222.
DR ComplexPortal; CPX-467; eNoSc complex.
DR CORUM; O43463; -.
DR DIP; DIP-32589N; -.
DR IntAct; O43463; 157.
DR MINT; O43463; -.
DR STRING; 9606.ENSP00000337976; -.
DR BindingDB; O43463; -.
DR ChEMBL; CHEMBL1795118; -.
DR GuidetoPHARMACOLOGY; 2715; -.
DR iPTMnet; O43463; -.
DR PhosphoSitePlus; O43463; -.
DR SwissPalm; O43463; -.
DR BioMuta; SUV39H1; -.
DR EPD; O43463; -.
DR jPOST; O43463; -.
DR MassIVE; O43463; -.
DR MaxQB; O43463; -.
DR PaxDb; O43463; -.
DR PeptideAtlas; O43463; -.
DR PRIDE; O43463; -.
DR ProteomicsDB; 48957; -. [O43463-1]
DR ProteomicsDB; 5048; -.
DR Antibodypedia; 11710; 415 antibodies from 39 providers.
DR DNASU; 6839; -.
DR Ensembl; ENST00000337852.10; ENSP00000337976.6; ENSG00000101945.17. [O43463-2]
DR Ensembl; ENST00000376687.4; ENSP00000365877.4; ENSG00000101945.17. [O43463-1]
DR GeneID; 6839; -.
DR KEGG; hsa:6839; -.
DR MANE-Select; ENST00000376687.4; ENSP00000365877.4; NM_003173.4; NP_003164.1.
DR UCSC; uc004dkn.5; human. [O43463-1]
DR CTD; 6839; -.
DR DisGeNET; 6839; -.
DR GeneCards; SUV39H1; -.
DR HGNC; HGNC:11479; SUV39H1.
DR HPA; ENSG00000101945; Low tissue specificity.
DR MIM; 300254; gene.
DR neXtProt; NX_O43463; -.
DR OpenTargets; ENSG00000101945; -.
DR PharmGKB; PA36264; -.
DR VEuPathDB; HostDB:ENSG00000101945; -.
DR eggNOG; KOG1082; Eukaryota.
DR GeneTree; ENSGT00940000160063; -.
DR HOGENOM; CLU_020840_8_0_1; -.
DR InParanoid; O43463; -.
DR OMA; DKFTDPD; -.
DR OrthoDB; 753093at2759; -.
DR PhylomeDB; O43463; -.
DR TreeFam; TF106452; -.
DR BioCyc; MetaCyc:HS02321-MON; -.
DR BRENDA; 2.1.1.355; 2681.
DR PathwayCommons; O43463; -.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression.
DR SignaLink; O43463; -.
DR SIGNOR; O43463; -.
DR BioGRID-ORCS; 6839; 26 hits in 725 CRISPR screens.
DR ChiTaRS; SUV39H1; human.
DR GeneWiki; SUV39H1; -.
DR GenomeRNAi; 6839; -.
DR Pharos; O43463; Tchem.
DR PRO; PR:O43463; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O43463; protein.
DR Bgee; ENSG00000101945; Expressed in granulocyte and 135 other tissues.
DR Genevisible; O43463; HS.
DR GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000794; C:condensed nuclear chromosome; TAS:ProtInc.
DR GO; GO:0061773; C:eNoSc complex; IPI:ComplexPortal.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0005652; C:nuclear lamina; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; TAS:ProtInc.
DR GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:UniProtKB.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:ComplexPortal.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
DR GO; GO:0006325; P:chromatin organization; TAS:ProtInc.
DR GO; GO:0097009; P:energy homeostasis; IMP:ComplexPortal.
DR GO; GO:0036123; P:histone H3-K9 dimethylation; ISS:UniProtKB.
DR GO; GO:0036124; P:histone H3-K9 trimethylation; ISS:UniProtKB.
DR GO; GO:0034968; P:histone lysine methylation; IBA:GO_Central.
DR GO; GO:0045786; P:negative regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0042754; P:negative regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IMP:ComplexPortal.
DR GO; GO:0031062; P:positive regulation of histone methylation; IMP:ComplexPortal.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IDA:UniProtKB.
DR GO; GO:0046015; P:regulation of transcription by glucose; IMP:ComplexPortal.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR011381; Histone_H3-K9_MeTrfase.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF009343; SUV39_SET; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS51579; SAM_MT43_SUVAR39_3; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Biological rhythms;
KW Cell cycle; Centromere; Chromatin regulator; Chromosome; Differentiation;
KW Host-virus interaction; Metal-binding; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; rRNA processing;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Zinc.
FT CHAIN 1..412
FT /note="Histone-lysine N-methyltransferase SUV39H1"
FT /id="PRO_0000186057"
FT DOMAIN 43..101
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 179..240
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 243..366
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 396..412
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..89
FT /note="Interaction with SIRT1"
FT REGION 255..377
FT /note="Mediates interaction with MECOM"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 254..256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 323..324
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT MOD_RES 266
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18004385"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..6
FT /note="MAENLK -> MVGMSRLRNDRLADPLT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054286"
FT MUTAGEN 64
FT /note="W->A: Abolishes methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:16519522"
FT MUTAGEN 67
FT /note="Y->A: Abolishes methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:16519522"
FT MUTAGEN 266
FT /note="K->A: Loss of SIRT1-mediated up-regulation of
FT enzymatic activity."
FT /evidence="ECO:0000269|PubMed:18004385"
FT MUTAGEN 266
FT /note="K->Q: Significant loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:18004385"
FT MUTAGEN 320
FT /note="H->R: Strongly increases methylation of histone H3."
FT /evidence="ECO:0000269|PubMed:10949293"
FT MUTAGEN 324
FT /note="H->L,K: Abolishes methylation of histone H3."
FT /evidence="ECO:0000269|PubMed:10949293"
FT MUTAGEN 326
FT /note="C->A: Abolishes methylation of histone H3."
FT /evidence="ECO:0000269|PubMed:10949293"
FT CONFLICT 213
FT /note="L -> P (in Ref. 4; BAD96791)"
FT /evidence="ECO:0000305"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:3MTS"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:3MTS"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:3MTS"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:3MTS"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3MTS"
FT HELIX 83..103
FT /evidence="ECO:0007829|PDB:3MTS"
SQ 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
