GenomeNet

Database: UniProt/SWISS-PROT
Entry: SUV91_MOUSE
LinkDB: SUV91_MOUSE
Original site: SUV91_MOUSE 
ID   SUV91_MOUSE             Reviewed;         412 AA.
AC   O54864; Q3TEW2; Q3UT51; Q8C2L3; Q9JLC7; Q9JLP8;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   20-JUN-2018, entry version 166.
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=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=Suv39h;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH CBX1.
RC   TISSUE=Brain;
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 [MRNA] (ISOFORM 1), AND PARTIAL NUCLEOTIDE
RP   SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Embryo;
RX   PubMed=10754099; DOI=10.1007/s003350010049;
RA   Bultman S., Magnuson T.;
RT   "Molecular and genetic analysis of the mouse homolog of the Drosophila
RT   suppressor of position-effect variegation 3-9 gene.";
RL   Mamm. Genome 11:251-254(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Egg, Liver, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-276, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=11094092; DOI=10.1128/MCB.20.24.9423-9433.2000;
RA   O'Carroll D., Scherthan H., Peters A.H.F.M., Opravil S., Haynes A.R.,
RA   Laible G., Rea S., Schmid M., Lebersorger A., Jerratsch M.,
RA   Sattler L., Mattei M.-G., Denny P., Brown S.D.M., Schweizer D.,
RA   Jenuwein T.;
RT   "Isolation and characterization of Suv39h2, a second histone H3
RT   methyltransferase gene that displays testis-specific expression.";
RL   Mol. Cell. Biol. 20:9423-9433(2000).
RN   [7]
RP   ENZYME ACTIVITY.
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   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11701123; DOI=10.1016/S0092-8674(01)00542-6;
RA   Peters A.H.F.M., O'Carroll D., Scherthan H., Mechtler K., Sauer S.,
RA   Schofer C., Weipoltshammer K., Pagani M., Lachner M., Kohlmaier A.,
RA   Opravil S., Doyle M., Sibilia M., Jenuwein T.;
RT   "Loss of the Suv39h histone methyltransferases impairs mammalian
RT   heterochromatin and genome stability.";
RL   Cell 107:323-337(2001).
RN   [9]
RP   INTERACTION WITH HISTONE DEACETYLASE COMPLEX.
RX   PubMed=11788710; DOI=10.1093/nar/30.2.475;
RA   Vaute O., Nicolas E., Vandel L., Trouche D.;
RT   "Functional and physical interaction between the histone methyl
RT   transferase Suv39H1 and histone deacetylases.";
RL   Nucleic Acids Res. 30:475-481(2002).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH DNMT3B.
RX   PubMed=12867029; DOI=10.1016/S0960-9822(03)00432-9;
RA   Lehnertz B., Ueda Y., Derijck A.A.H.A., Braunschweig U.,
RA   Perez-Burgos L., Kubicek S., Chen T., Li E., Jenuwein T.,
RA   Peters A.H.F.M.;
RT   "Suv39h-mediated histone H3 lysine 9 methylation directs DNA
RT   methylation to major satellite repeats at pericentric
RT   heterochromatin.";
RL   Curr. Biol. 13:1192-1200(2003).
RN   [11]
RP   FUNCTION.
RX   PubMed=14690609; DOI=10.1016/S1097-2765(03)00477-5;
RA   Peters A.H.F.M., Kubicek S., Mechtler K., O'Sullivan R.J.,
RA   Derijck A.A., Perez-Burgos L., Kohlmaier A., Opravil S., Tachibana M.,
RA   Shinkai Y., Martens J.H.A., Jenuwein T.;
RT   "Partitioning and plasticity of repressive histone methylation states
RT   in mammalian chromatin.";
RL   Mol. Cell 12:1577-1589(2003).
RN   [12]
RP   FUNCTION.
RX   PubMed=14690610; DOI=10.1016/S1097-2765(03)00479-9;
RA   Rice J.C., Briggs S.D., Ueberheide B., Barber C.M., Shabanowitz J.,
RA   Hunt D.F., Shinkai Y., Allis C.D.;
RT   "Histone methyltransferases direct different degrees of methylation to
RT   define distinct chromatin domains.";
RL   Mol. Cell 12:1591-1598(2003).
RN   [13]
RP   FUNCTION.
RX   PubMed=14702045; DOI=10.1038/ng1278;
RA   Garcia-Cao M., O'Sullivan R., Peters A.H.F.M., Jenuwein T.,
RA   Blasco M.A.;
RT   "Epigenetic regulation of telomere length in mammalian cells by the
RT   Suv39h1 and Suv39h2 histone methyltransferases.";
RL   Nat. Genet. 36:94-99(2004).
RN   [14]
RP   FUNCTION, 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [17]
RP   INTERACTION WITH LMNA.
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).
RN   [18]
RP   INTERACTION WITH MECOM.
RX   PubMed=18619962; DOI=10.1016/j.febslet.2008.06.056;
RA   Spensberger D., Delwel R.;
RT   "A novel interaction between the proto-oncogene Evi1 and histone
RT   methyltransferases, SUV39H1 and G9a.";
RL   FEBS Lett. 582:2761-2767(2008).
RN   [19]
RP   FUNCTION IN CIRCADIAN RHYTHMS, AND IDENTIFICATION IN A LARGE PER
RP   COMPLEX.
RX   PubMed=24413057; DOI=10.1038/nsmb.2746;
RA   Duong H.A., Weitz C.J.;
RT   "Temporal orchestration of repressive chromatin modifiers by circadian
RT   clock Period complexes.";
RL   Nat. Struct. Mol. Biol. 21:126-132(2014).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-
CC       9' as substrate. H3 'Lys-9' trimethylation represents a specific
CC       tag for epigenetic transcriptional repression by recruiting HP1
CC       (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly
CC       functions in heterochromatin regions, thereby playing a central
CC       role in the establishment of constitutive heterochromatin at
CC       pericentric and telomere regions. H3 'Lys-9' trimethylation is
CC       also required to direct DNA methylation at pericentric repeats.
CC       SUV39H1 is targeted to histone H3 via its interaction with RB1 and
CC       is involved in many processes, such as repression of MYOD1-
CC       stimulated differentiation, regulation of the control switch for
CC       exiting the cell cycle and entering differentiation, repression by
CC       the PML-RARA fusion protein, BMP-induced repression, repression of
CC       switch recombination to IgA and regulation of telomere length.
CC       Component of the eNoSC (energy-dependent nucleolar silencing)
CC       complex, a 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 PER complex to the E-box elements of the
CC       circadian target genes such as PER2 itself or PER1, contributes to
CC       the conversion of local chromatin to a heterochromatin-like
CC       repressive state through H3 'Lys-9' trimethylation.
CC       {ECO:0000269|PubMed:11701123, ECO:0000269|PubMed:12867029,
CC       ECO:0000269|PubMed:14690609, ECO:0000269|PubMed:14690610,
CC       ECO:0000269|PubMed:14702045, ECO:0000269|PubMed:18004385,
CC       ECO:0000269|PubMed:24413057}.
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}.
CC   -!- ENZYME REGULATION: Negatively regulated by CCAR2. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CCAR2 and GFI1B. Component of the eNoSC
CC       complex, composed of SIRT1, SUV39H1 and RRP8 (By similarity).
CC       Interacts with H3 and H4 histones. Interacts with DNMT3B, CBX1,
CC       CBX4, MBD1, RUNX1, RUNX3, MYOD1, SMAD5 and RB1. Interacts with
CC       SBF1 through the SET domain. Interacts with HDAC1 and HDAC2
CC       through the N-terminus and associates with the core histone
CC       deacetylase complex composed of HDAC1, HDAC2, RBBP4 and RBBP7.
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:0000250, ECO:0000269|PubMed:10202156,
CC       ECO:0000269|PubMed:11788710, ECO:0000269|PubMed:12867029,
CC       ECO:0000269|PubMed:18619962, ECO:0000269|PubMed:23695662}.
CC   -!- INTERACTION:
CC       O70237:Gfi1b; NbExp=2; IntAct=EBI-302230, EBI-4287943;
CC       P10085:Myod1; NbExp=3; IntAct=EBI-302230, EBI-4405734;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Nucleus lamina {ECO:0000250}.
CC       Nucleus, nucleoplasm {ECO:0000250}. Chromosome, centromere.
CC       Note=Associates with centromeric constitutive heterochromatin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O54864-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O54864-2; Sequence=VSP_002208;
CC         Note=Incomplete sequence. Ref.2 (AAF60970) sequence differs from
CC         that shown due to a frameshift in position 35. {ECO:0000305};
CC       Name=3;
CC         IsoId=O54864-3; Sequence=VSP_024029, VSP_024030;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC       {ECO:0000269|PubMed:10202156, ECO:0000269|PubMed:11094092}.
CC   -!- DEVELOPMENTAL STAGE: Expression present throughout embryogenesis.
CC       Higher expression between E9.5 and E13.
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   -!- 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:0000250}.
CC   -!- PTM: Phosphorylated on serine residues, and to a lesser degree, on
CC       threonine residues. {ECO:0000250}.
CC   -!- PTM: Acetylated at Lys-266, leading to inhibition of enzyme
CC       activity. SIRT1-mediated deacetylation relieves this inhibition
CC       (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice lacking Suv39h1 and Suv39h2 display
CC       severely impaired viability and chromosomal instabilities that are
CC       associated with an increased tumor risk and perturbed chromosome
CC       interactions during male meiosis. They also show a higher level of
CC       histone H3 with phosphorylated 'Ser-10' and a reduced number of
CC       cells in G1 phase and an increased portion of cells with aberrant
CC       nuclear morphologies. {ECO:0000269|PubMed:11701123}.
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; AF019969; AAB92225.1; -; mRNA.
DR   EMBL; AF193861; AAF60969.1; -; mRNA.
DR   EMBL; AF193862; AAF60970.1; ALT_FRAME; mRNA.
DR   EMBL; AK088405; BAC40334.1; -; mRNA.
DR   EMBL; AK139757; BAE24129.1; -; mRNA.
DR   EMBL; AK169389; BAE41136.1; -; mRNA.
DR   EMBL; AL663032; CAM19494.1; -; Genomic_DNA.
DR   EMBL; AL663032; CAM19495.1; -; Genomic_DNA.
DR   EMBL; BC023860; AAH23860.1; -; mRNA.
DR   EMBL; AF149203; AAF73151.1; -; Genomic_DNA.
DR   CCDS; CCDS40846.1; -. [O54864-1]
DR   RefSeq; NP_001277645.1; NM_001290716.1.
DR   RefSeq; NP_035644.1; NM_011514.2. [O54864-1]
DR   UniGene; Mm.479743; -.
DR   UniGene; Mm.9244; -.
DR   ProteinModelPortal; O54864; -.
DR   SMR; O54864; -.
DR   BioGrid; 203586; 5.
DR   ComplexPortal; CPX-468; eNoSc complex.
DR   DIP; DIP-32590N; -.
DR   IntAct; O54864; 7.
DR   MINT; O54864; -.
DR   STRING; 10090.ENSMUSP00000111301; -.
DR   iPTMnet; O54864; -.
DR   PhosphoSitePlus; O54864; -.
DR   EPD; O54864; -.
DR   MaxQB; O54864; -.
DR   PaxDb; O54864; -.
DR   PeptideAtlas; O54864; -.
DR   PRIDE; O54864; -.
DR   Ensembl; ENSMUST00000115636; ENSMUSP00000111299; ENSMUSG00000039231. [O54864-3]
DR   Ensembl; ENSMUST00000115638; ENSMUSP00000111301; ENSMUSG00000039231. [O54864-1]
DR   GeneID; 20937; -.
DR   KEGG; mmu:20937; -.
DR   UCSC; uc009snq.2; mouse. [O54864-1]
DR   CTD; 6839; -.
DR   MGI; MGI:1099440; Suv39h1.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00780000121845; -.
DR   HOGENOM; HOG000231244; -.
DR   HOVERGEN; HBG055621; -.
DR   InParanoid; O54864; -.
DR   KO; K11419; -.
DR   TreeFam; TF106452; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-MMU-427359; SIRT1 negatively regulates rRNA expression.
DR   PRO; PR:O54864; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   Bgee; ENSMUSG00000039231; -.
DR   ExpressionAtlas; O54864; baseline and differential.
DR   Genevisible; O54864; MM.
DR   GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR   GO; GO:0005720; C:nuclear heterochromatin; TAS:MGI.
DR   GO; GO:0005652; C:nuclear lamina; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0033553; C:rDNA heterochromatin; ISO:MGI.
DR   GO; GO:0042054; F:histone methyltransferase activity; ISO:MGI.
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:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008276; F:protein methyltransferase activity; TAS:MGI.
DR   GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISO:MGI.
DR   GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA: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; ISO:MGI.
DR   GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR   GO; GO:0006342; P:chromatin silencing; TAS:UniProtKB.
DR   GO; GO:0000183; P:chromatin silencing at rDNA; ISO:MGI.
DR   GO; GO:0006323; P:DNA packaging; TAS:MGI.
DR   GO; GO:0036123; P:histone H3-K9 dimethylation; IMP:UniProtKB.
DR   GO; GO:0051567; P:histone H3-K9 methylation; IDA:MGI.
DR   GO; GO:0036124; P:histone H3-K9 trimethylation; IMP:UniProtKB.
DR   GO; GO:0034968; P:histone lysine methylation; IGI:MGI.
DR   GO; GO:0042754; P:negative regulation of circadian rhythm; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP: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   CDD; cd00024; CHROMO; 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   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   Acetylation; Alternative splicing; Biological rhythms; Cell cycle;
KW   Centromere; Chromatin regulator; Chromosome; Complete proteome;
KW   Differentiation; 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       Histone-lysine N-methyltransferase
FT                                SUV39H1.
FT                                /FTId=PRO_0000186058.
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:0000269|PubMed:18619962}.
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:0000250|UniProtKB:O43463}.
FT   MOD_RES     391    391       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   VAR_SEQ       1      6       MAENLK -> LKEKVAATRGKRRLSVTVTLSVSTGDAGRGG
FT                                RSGTDPLLKMGEPATL (in isoform 2).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_002208.
FT   VAR_SEQ     277    286       IITSEEAERR -> VPPGCYLLGK (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024029.
FT   VAR_SEQ     287    412       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_024030.
FT   CONFLICT    364    364       D -> G (in Ref. 3; BAC40334).
FT                                {ECO:0000305}.
SQ   SEQUENCE   412 AA;  47754 MW;  6B690F4FE7FD997C CRC64;
     MAENLKGCSV CCKSSWNQLQ DLCRLAKLSC PALGVSKKNL YDFEVEYLCD YKKIREQEYY
     LVKWRGYPDS ENTWEPRQNL KCIRVLKQFH KDLERELVRR HRRSKPPRHL DPNLANYLVQ
     KAKQRRALQR WEQELNAKRS HLGRITVENE VDLDGPPRSF VYINEYRVGE GITLNQVAVG
     CECQDCLLAP TGGCCPGASL HKFAYNDQGQ VRLKAGQPIY ECNSRCCCGY DCPNRVVQKG
     IRYDLCIFRT NDGRGWGVRT LEKIRKNSFV MEYVGEIITS EEAERRGQIY DRQGATYLFD
     LDYVEDVYTV DAAYYGNISH FVNHSCDPNL QVYNVFIDNL DERLPRIAFF ATRTIWAGEE
     LTFDYNMQVD PVDMESTRMD SNFGLAGLPG SPKKRVRIEC KCGTTACRKY LF
//
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