GenomeNet

Database: UniProt/SWISS-PROT
Entry: SUV91_HUMAN
LinkDB: SUV91_HUMAN
Original site: 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   27-SEP-2017, entry version 180.
DE   RecName: Full=Histone-lysine N-methyltransferase SUV39H1;
DE            EC=2.1.1.43;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Jenuwein T.;
RT   "Functional mammalian homologues of the Drosophila PEV-modifier
RT   Su(var)3-9 encode centromere-associated proteins which complex with
RT   the 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [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.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   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.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   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.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   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.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   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.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX   PubMed=10671371;
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   ENZYME 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.,
RA   Schmid M., Opravil S., Mechtler K., Ponting C.P., Allis C.D.,
RA   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
RT   growth control by SUV39H1, a mammalian ortholog of Drosophila
RT   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.,
RA   Tachibana M., 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-
RT   SUV39H1-DNMT1 multimolecular complexes mediate the transcription of
RT   estrogen 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.,
RA   Naguibneva I., 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
RT   in 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.,
RA   Verwoerd N.P., 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
RP   BY 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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling 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
RT   of 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.,
RA   Stavnezer J.;
RT   "The histone methyltransferase Suv39h1 increases class switch
RT   recombination specifically to IgA.";
RL   J. Immunol. 177:1179-1188(2006).
RN   [23]
RP   ENZYME 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
RT   chromodomain in 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
RT   the oncogenic properties of the leukemia-associated PML-retinoic acid
RT   receptor 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.
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
RT   of 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
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [31]
RP   INTERACTION WITH CCAR2, AND ENZYME 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
RP   BY 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
RP   BY 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [34]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [35]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION
RP   BY 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
RT   extends lifespan in a progeria mouse model.";
RL   Nat. Commun. 4:1868-1868(2013).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-
CC       9' as substrate. Also weakly methylates histone H1 (in vitro). H3
CC       'Lys-9' trimethylation represents a specific tag for epigenetic
CC       transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or
CC       CBX5) proteins to methylated histones. Mainly functions in
CC       heterochromatin regions, thereby playing a central role in the
CC       establishment of constitutive heterochromatin at pericentric and
CC       telomere regions. H3 'Lys-9' trimethylation is also required to
CC       direct DNA methylation at pericentric repeats. SUV39H1 is targeted
CC       to histone H3 via its interaction with RB1 and is involved in many
CC       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
CC       protein, BMP-induced repression, repression of switch
CC       recombination to IgA and regulation of telomere length. Component
CC       of the eNoSC (energy-dependent nucleolar silencing) complex, a
CC       complex that mediates silencing of rDNA in response to
CC       intracellular energy status and acts by recruiting histone-
CC       modifying enzymes. The eNoSC complex is able to sense the energy
CC       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)
CC       by SUV39H1 and the formation of silent chromatin in the rDNA
CC       locus. Recruited by the large PER complex to the E-box elements of
CC       the circadian target genes such as PER2 itself or PER1,
CC       contributes to the conversion of local chromatin to a
CC       heterochromatin-like repressive state through H3 'Lys-9'
CC       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: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000255|PROSITE-ProRule:PRU00912,
CC       ECO:0000269|PubMed:10949293, ECO:0000269|PubMed:18004385}.
CC   -!- ENZYME REGULATION: Inhibited by S-adenosyl-L-homocysteine.
CC       Negatively 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
CC       RB1. Interacts with SBF1 through the SET domain. Interacts with
CC       HDAC1 and HDAC2 through the N-terminus and associates with the
CC       core histone deacetylase complex composed of HDAC1, HDAC2, RBBP4
CC       and RBBP7. Component of the eNoSC complex, composed of SIRT1,
CC       SUV39H1 and RRP8. In case of infection, interacts with HTLV-1 Tax
CC       protein, leading to abrogate Tax transactivation of HTLV-1 LTR.
CC       Interacts (via SET domain) with MECOM; enhances MECOM
CC       transcriptional repression activity. Interacts with LMNA; the
CC       interaction increases stability of SUV39H1. The large PER complex
CC       involved in the histone methylation is composed of at least PER2,
CC       CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation
CC       of the complex. {ECO:0000269|PubMed:10202156,
CC       ECO:0000269|PubMed:10848615, ECO:0000269|PubMed:11242053,
CC       ECO:0000269|PubMed:11484059, ECO:0000269|PubMed:12101246,
CC       ECO:0000269|PubMed:12711603, ECO:0000269|PubMed:12789259,
CC       ECO:0000269|PubMed:12917624, ECO:0000269|PubMed:15107829,
CC       ECO:0000269|PubMed:16103223, ECO:0000269|PubMed:16409643,
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   -!- INTERACTION:
CC       P68432:- (xeno); NbExp=2; IntAct=EBI-349968, EBI-79764;
CC       O95260:ATE1; NbExp=2; IntAct=EBI-349968, EBI-1043378;
CC       Q9C0K0:BCL11B; NbExp=3; IntAct=EBI-349968, EBI-6597578;
CC       Q6P047:C8orf74; NbExp=2; IntAct=EBI-349968, EBI-8466055;
CC       P83916:CBX1; NbExp=3; IntAct=EBI-349968, EBI-78129;
CC       Q13185:CBX3; NbExp=6; IntAct=EBI-349968, EBI-78176;
CC       P45973:CBX5; NbExp=8; IntAct=EBI-349968, EBI-78219;
CC       A5D8V7:CCDC151; NbExp=2; IntAct=EBI-349968, EBI-8466445;
CC       Q9BXL8:CDCA4; NbExp=2; IntAct=EBI-349968, EBI-1773949;
CC       Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-349968, EBI-739624;
CC       P49761:CLK3; NbExp=2; IntAct=EBI-349968, EBI-745579;
CC       Q5TAQ9:DCAF8; NbExp=2; IntAct=EBI-349968, EBI-740686;
CC       Q15910:EZH2; NbExp=2; IntAct=EBI-349968, EBI-530054;
CC       Q6ZNL6:FGD5; NbExp=2; IntAct=EBI-349968, EBI-7962481;
CC       Q9NWQ4:GPATCH2L; NbExp=2; IntAct=EBI-349968, EBI-5666657;
CC       Q9BX10:GTPBP2; NbExp=2; IntAct=EBI-349968, EBI-6115579;
CC       Q13547:HDAC1; NbExp=3; IntAct=EBI-349968, EBI-301834;
CC       Q92769:HDAC2; NbExp=3; IntAct=EBI-349968, EBI-301821;
CC       V9HWG0:HEL25; NbExp=3; IntAct=EBI-349968, EBI-10183977;
CC       Q96ED9:HOOK2; NbExp=4; IntAct=EBI-349968, EBI-743290;
CC       P49639:HOXA1; NbExp=2; IntAct=EBI-349968, EBI-740785;
CC       P09017:HOXC4; NbExp=2; IntAct=EBI-349968, EBI-3923226;
CC       Q8TBB5:KLHDC4; NbExp=2; IntAct=EBI-349968, EBI-8472352;
CC       P60409:KRTAP10-7; NbExp=3; IntAct=EBI-349968, EBI-10172290;
CC       Q9BRK4:LZTS2; NbExp=5; IntAct=EBI-349968, EBI-741037;
CC       Q9UIS9:MBD1; NbExp=5; IntAct=EBI-349968, EBI-867196;
CC       Q13133:NR1H3; NbExp=2; IntAct=EBI-349968, EBI-781356;
CC       Q6TGC4:PADI6; NbExp=4; IntAct=EBI-349968, EBI-10892722;
CC       Q5T6S3:PHF19; NbExp=2; IntAct=EBI-349968, EBI-2339674;
CC       Q15156:PML-RAR; NbExp=4; IntAct=EBI-349968, EBI-867256;
CC       P62191:PSMC1; NbExp=2; IntAct=EBI-349968, EBI-357598;
CC       Q9NS23:RASSF1; NbExp=2; IntAct=EBI-349968, EBI-367363;
CC       P50749:RASSF2; NbExp=2; IntAct=EBI-349968, EBI-960081;
CC       O43159:RRP8; NbExp=3; IntAct=EBI-349968, EBI-2008793;
CC       Q96BD6:SPSB1; NbExp=2; IntAct=EBI-349968, EBI-2659201;
CC       Q8N4C7:STX19; NbExp=2; IntAct=EBI-349968, EBI-8484990;
CC       Q01081:U2AF1; NbExp=2; IntAct=EBI-349968, EBI-632461;
CC       Q9Y2L8:ZKSCAN5; NbExp=2; IntAct=EBI-349968, EBI-2876965;
CC       Q9C0F3:ZNF436; NbExp=2; IntAct=EBI-349968, EBI-8489702;
CC       Q9BS31:ZNF649; NbExp=2; IntAct=EBI-349968, EBI-4395789;
CC       Q9BS34:ZNF670; NbExp=2; IntAct=EBI-349968, EBI-745276;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Nucleus lamina. Nucleus,
CC       nucleoplasm. Chromosome, centromere. Note=Associates with
CC       centromeric constitutive 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         Note=No experimental confirmation available.;
CC   -!- DEVELOPMENTAL STAGE: Accumulates during mitosis at centromeres
CC       during prometaphase, but dissociates from the centromere at the
CC       meta- to anaphase transition.
CC   -!- DOMAIN: Although the SET domain contains the active site of
CC       enzymatic activity, both pre-SET and post-SET domains are required
CC       for methyltransferase activity. The SET domain also participates
CC       in stable binding to heterochromatin.
CC       {ECO:0000269|PubMed:16103223}.
CC   -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
CC       are arranged in a triangular cluster; some of these Cys residues
CC       contribute to the binding of two zinc ions within the cluster.
CC       {ECO:0000269|PubMed:16103223}.
CC   -!- PTM: Phosphorylated on serine residues, and to a lesser degree, on
CC       threonine residues. The phosphorylated form is stabilized by SBF1
CC       and is less active in its transcriptional repressor function.
CC       {ECO:0000269|PubMed:10671371}.
CC   -!- PTM: Acetylated at Lys-266, leading to inhibition of enzyme
CC       activity. SIRT1-mediated deacetylation relieves this inhibition.
CC       {ECO:0000269|PubMed:18004385}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00912}.
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   UniGene; Hs.522639; -.
DR   PDB; 3MTS; X-ray; 2.20 A; A/B/C=44-106.
DR   PDBsum; 3MTS; -.
DR   ProteinModelPortal; O43463; -.
DR   SMR; O43463; -.
DR   BioGrid; 112706; 170.
DR   CORUM; O43463; -.
DR   DIP; DIP-32589N; -.
DR   IntAct; O43463; 134.
DR   MINT; MINT-191763; -.
DR   STRING; 9606.ENSP00000365877; -.
DR   BindingDB; O43463; -.
DR   ChEMBL; CHEMBL1795118; -.
DR   GuidetoPHARMACOLOGY; 2715; -.
DR   iPTMnet; O43463; -.
DR   PhosphoSitePlus; O43463; -.
DR   EPD; O43463; -.
DR   MaxQB; O43463; -.
DR   PaxDb; O43463; -.
DR   PeptideAtlas; O43463; -.
DR   PRIDE; O43463; -.
DR   DNASU; 6839; -.
DR   Ensembl; ENST00000337852; ENSP00000337976; ENSG00000101945. [O43463-2]
DR   Ensembl; ENST00000376687; ENSP00000365877; ENSG00000101945. [O43463-1]
DR   GeneID; 6839; -.
DR   KEGG; hsa:6839; -.
DR   UCSC; uc004dkn.5; human. [O43463-1]
DR   CTD; 6839; -.
DR   DisGeNET; 6839; -.
DR   EuPathDB; HostDB:ENSG00000101945.16; -.
DR   GeneCards; SUV39H1; -.
DR   HGNC; HGNC:11479; SUV39H1.
DR   MIM; 300254; gene.
DR   neXtProt; NX_O43463; -.
DR   OpenTargets; ENSG00000101945; -.
DR   PharmGKB; PA36264; -.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00780000121845; -.
DR   HOGENOM; HOG000231244; -.
DR   HOVERGEN; HBG055621; -.
DR   InParanoid; O43463; -.
DR   KO; K11419; -.
DR   OMA; NTFVMEY; -.
DR   OrthoDB; EOG091G0Y4N; -.
DR   PhylomeDB; O43463; -.
DR   TreeFam; TF106452; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA Expression.
DR   SIGNOR; O43463; -.
DR   ChiTaRS; SUV39H1; human.
DR   GeneWiki; SUV39H1; -.
DR   GenomeRNAi; 6839; -.
DR   PRO; PR:O43463; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; ENSG00000101945; -.
DR   CleanEx; HS_SUV39H1; -.
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:0000792; C:heterochromatin; IDA:UniProtKB.
DR   GO; GO:0005652; C:nuclear lamina; IEA:UniProtKB-SubCell.
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 regulatory region sequence-specific DNA 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:0071456; P:cellular response to hypoxia; IDA:MGI.
DR   GO; GO:0006325; P:chromatin organization; TAS:ProtInc.
DR   GO; GO:0000183; P:chromatin silencing at rDNA; IDA:UniProtKB.
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:0042754; P:negative regulation of circadian rhythm; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR016197; Chromodomain-like.
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   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   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;
KW   Complete proteome; Differentiation; Host-virus interaction;
KW   Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; rRNA processing;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc.
FT   CHAIN         1    412       Histone-lysine N-methyltransferase
FT                                SUV39H1.
FT                                /FTId=PRO_0000186057.
FT   DOMAIN       43    101       Chromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      179    240       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      243    366       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      396    412       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION        1     89       Interaction with SIRT1.
FT   REGION      254    256       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      255    377       Mediates interaction with MECOM.
FT                                {ECO:0000250}.
FT   REGION      323    324       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       181    181       Zinc 1. {ECO:0000250}.
FT   METAL       181    181       Zinc 2. {ECO:0000250}.
FT   METAL       183    183       Zinc 1. {ECO:0000250}.
FT   METAL       186    186       Zinc 1. {ECO:0000250}.
FT   METAL       186    186       Zinc 3. {ECO:0000250}.
FT   METAL       194    194       Zinc 1. {ECO:0000250}.
FT   METAL       195    195       Zinc 1. {ECO:0000250}.
FT   METAL       195    195       Zinc 2. {ECO:0000250}.
FT   METAL       222    222       Zinc 2. {ECO:0000250}.
FT   METAL       222    222       Zinc 3. {ECO:0000250}.
FT   METAL       226    226       Zinc 2. {ECO:0000250}.
FT   METAL       228    228       Zinc 3. {ECO:0000250}.
FT   METAL       232    232       Zinc 3. {ECO:0000250}.
FT   METAL       326    326       Zinc 4. {ECO:0000250}.
FT   METAL       400    400       Zinc 4. {ECO:0000250}.
FT   METAL       402    402       Zinc 4. {ECO:0000250}.
FT   METAL       407    407       Zinc 4. {ECO:0000250}.
FT   BINDING     297    297       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   MOD_RES     266    266       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:18004385}.
FT   MOD_RES     391    391       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ       1      6       MAENLK -> MVGMSRLRNDRLADPLT (in isoform
FT                                2). {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054286.
FT   MUTAGEN      64     64       W->A: Abolishes methyltransferase
FT                                activity. {ECO:0000269|PubMed:16519522}.
FT   MUTAGEN      67     67       Y->A: Abolishes methyltransferase
FT                                activity. {ECO:0000269|PubMed:16519522}.
FT   MUTAGEN     266    266       K->A: Loss of SIRT1-mediated up-
FT                                regulation of enzymatic activity.
FT                                {ECO:0000269|PubMed:18004385}.
FT   MUTAGEN     266    266       K->Q: Significant loss of enzymatic
FT                                activity. {ECO:0000269|PubMed:18004385}.
FT   MUTAGEN     320    320       H->R: Strongly increases methylation of
FT                                histone H3.
FT                                {ECO:0000269|PubMed:10949293}.
FT   MUTAGEN     324    324       H->L,K: Abolishes methylation of histone
FT                                H3. {ECO:0000269|PubMed:10949293}.
FT   MUTAGEN     326    326       C->A: Abolishes methylation of histone
FT                                H3. {ECO:0000269|PubMed:10949293}.
FT   CONFLICT    213    213       L -> P (in Ref. 4; BAD96791).
FT                                {ECO:0000305}.
FT   STRAND       45     53       {ECO:0000244|PDB:3MTS}.
FT   STRAND       58     64       {ECO:0000244|PDB:3MTS}.
FT   HELIX        69     71       {ECO:0000244|PDB:3MTS}.
FT   STRAND       73     76       {ECO:0000244|PDB:3MTS}.
FT   HELIX        77     79       {ECO:0000244|PDB:3MTS}.
FT   HELIX        83    103       {ECO:0000244|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
//
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