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 03-AUG-2022, entry version 190.
DE RecName: Full=Histone-lysine N-methyltransferase SUV39H1;
DE EC=2.1.1.355 {ECO:0000269|PubMed:10949293};
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., 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 [MRNA] (ISOFORM 1), AND PARTIAL NUCLEOTIDE SEQUENCE
RP [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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT 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 project:
RT 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., Sattler L.,
RA Mattei M.-G., Denny P., Brown S.D.M., Schweizer D., 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 CATALYTIC ACTIVITY.
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 [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 transferase
RT 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., Perez-Burgos L.,
RA Kubicek S., Chen T., Li E., Jenuwein T., Peters A.H.F.M.;
RT "Suv39h-mediated histone H3 lysine 9 methylation directs DNA methylation to
RT major satellite repeats at pericentric 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., Derijck A.A.,
RA Perez-Burgos L., Kohlmaier A., Opravil S., Tachibana M., Shinkai Y.,
RA Martens J.H.A., Jenuwein T.;
RT "Partitioning and plasticity of repressive histone methylation states in
RT 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., Blasco M.A.;
RT "Epigenetic regulation of telomere length in mammalian cells by the Suv39h1
RT 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 BY
RP 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 BY
RP 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 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 extends
RT 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 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 trimethylates
CC 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3
CC 'Lys-9' trimethylation represents a specific tag for epigenetic
CC transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5)
CC proteins to methylated histones. Mainly functions in heterochromatin
CC regions, thereby playing a central role in the establishment of
CC constitutive heterochromatin at pericentric and telomere regions. H3
CC 'Lys-9' trimethylation is also required to direct DNA methylation at
CC pericentric repeats. SUV39H1 is targeted to histone H3 via its
CC interaction with RB1 and is involved in many processes, such as
CC repression of MYOD1-stimulated differentiation, regulation of the
CC control switch for exiting the cell cycle and entering differentiation,
CC repression by the PML-RARA fusion protein, BMP-induced repression,
CC repression of switch recombination to IgA and regulation of telomere
CC length. 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-modifying
CC enzymes. The eNoSC complex is able to sense the energy status of cell:
CC upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates
CC SIRT1, leading to histone H3 deacetylation followed by dimethylation of
CC H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent
CC chromatin in the rDNA locus. Recruited by the PER complex to the E-box
CC elements of the circadian target genes such as PER2 itself or PER1,
CC contributes to the conversion of local chromatin to a heterochromatin-
CC like 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:
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};
CC -!- ACTIVITY 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). Interacts
CC with H3 and H4 histones. Interacts with DNMT3B, CBX1, CBX4, MBD1,
CC RUNX1, RUNX3, MYOD1, SMAD5 and RB1. Interacts with SBF1 through the SET
CC domain. Interacts with HDAC1 and HDAC2 through the N-terminus and
CC associates with the core histone deacetylase complex composed of HDAC1,
CC HDAC2, RBBP4 and RBBP7. Interacts (via SET domain) with MECOM; enhances
CC MECOM 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, CBX3,
CC TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the
CC 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 O54864; O70237: Gfi1b; NbExp=2; IntAct=EBI-302230, EBI-4287943;
CC O54864; P10085: Myod1; NbExp=3; IntAct=EBI-302230, EBI-4405734;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus lamina {ECO:0000250}. Nucleus,
CC nucleoplasm {ECO:0000250}. Chromosome, centromere. Note=Associates with
CC 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 Name=3;
CC IsoId=O54864-3; Sequence=VSP_024029, VSP_024030;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10202156,
CC ECO:0000269|PubMed:11094092}.
CC -!- DEVELOPMENTAL STAGE: Expression present throughout embryogenesis.
CC Higher expression between 9.5 dpc and 13 dpc.
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.
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. {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 activity.
CC SIRT1-mediated deacetylation relieves this inhibition (By similarity).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Suv39h1 and Suv39h2 display severely
CC impaired viability and chromosomal instabilities that are associated
CC with an increased tumor risk and perturbed chromosome interactions
CC during male meiosis. They also show a higher level of histone H3 with
CC phosphorylated 'Ser-10' and a reduced number of cells in G1 phase and
CC an increased portion of cells with aberrant nuclear morphologies.
CC {ECO:0000269|PubMed:11701123}.
CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
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}.
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=AAF60970.1; Type=Frameshift; Evidence={ECO:0000305};
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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; -; NOT_ANNOTATED_CDS; 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 AlphaFoldDB; O54864; -.
DR SMR; O54864; -.
DR BioGRID; 203586; 8.
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 jPOST; O54864; -.
DR MaxQB; O54864; -.
DR PaxDb; O54864; -.
DR PeptideAtlas; O54864; -.
DR PRIDE; O54864; -.
DR ProteomicsDB; 258671; -. [O54864-1]
DR ProteomicsDB; 258672; -. [O54864-2]
DR ProteomicsDB; 258673; -. [O54864-3]
DR Antibodypedia; 11710; 415 antibodies from 39 providers.
DR DNASU; 20937; -.
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 VEuPathDB; HostDB:ENSMUSG00000039231; -.
DR eggNOG; KOG1082; Eukaryota.
DR GeneTree; ENSGT00940000160063; -.
DR HOGENOM; CLU_020840_8_0_1; -.
DR InParanoid; O54864; -.
DR OMA; DKFTDPD; -.
DR OrthoDB; 753093at2759; -.
DR TreeFam; TF106452; -.
DR BRENDA; 2.1.1.355; 3474.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR Reactome; R-MMU-427359; SIRT1 negatively regulates rRNA expression.
DR BioGRID-ORCS; 20937; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Suv39h1; mouse.
DR PRO; PR:O54864; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O54864; protein.
DR Bgee; ENSMUSG00000039231; Expressed in floor plate of midbrain and 256 other tissues.
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:0061773; C:eNoSc complex; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0005652; C:nuclear lamina; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; 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 transcription 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 cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
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:0042149; P:cellular response to glucose starvation; ISO:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0051276; P:chromosome organization; TAS:MGI.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:MGI.
DR GO; GO:0097009; P:energy homeostasis; ISO:MGI.
DR GO; GO:0031507; P:heterochromatin assembly; TAS:UniProtKB.
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:0045786; P:negative regulation of cell cycle; ISO: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:0031065; P:positive regulation of histone deacetylation; ISO:MGI.
DR GO; GO:1900114; P:positive regulation of histone H3-K9 trimethylation; IMP:MGI.
DR GO; GO:0031062; P:positive regulation of histone methylation; ISO:MGI.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; ISO:MGI.
DR GO; GO:0030500; P:regulation of bone mineralization; IGI:MGI.
DR GO; GO:2000772; P:regulation of cellular senescence; IMP:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IMP:MGI.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IGI:MGI.
DR GO; GO:0046015; P:regulation of transcription by glucose; ISO:MGI.
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 Acetylation; Alternative splicing; Biological rhythms; Cell cycle;
KW Centromere; Chromatin regulator; Chromosome; Differentiation;
KW Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; rRNA processing; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase; Zinc.
FT CHAIN 1..412
FT /note="Histone-lysine N-methyltransferase SUV39H1"
FT /id="PRO_0000186058"
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:0000269|PubMed:18619962"
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:0000250|UniProtKB:O43463"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..6
FT /note="MAENLK -> LKEKVAATRGKRRLSVTVTLSVSTGDAGRGGRSGTDPLLKMG
FT EPATL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002208"
FT VAR_SEQ 277..286
FT /note="IITSEEAERR -> VPPGCYLLGK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024029"
FT VAR_SEQ 287..412
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024030"
FT CONFLICT 364
FT /note="D -> G (in Ref. 3; BAC40334)"
FT /evidence="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
