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 24-JAN-2024, entry version 198. 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). RN [20] RP FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF 324-HIS--CYS-326. RX PubMed=30111536; DOI=10.15252/embj.201898981; RA Zhang Y.L., Zhao L.W., Zhang J., Le R., Ji S.Y., Chen C., Gao Y., Li D., RA Gao S., Fan H.Y.; RT "DCAF13 promotes pluripotency by negatively regulating SUV39H1 stability RT during early embryonic development."; RL EMBO J. 37:0-0(2018). 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, ECO:0000269|PubMed:30111536}. 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 {ECO:0000250|UniProtKB:O43463}. Nucleus CC lamina {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Chromosome, CC centromere. Note=Associates with centromeric constitutive CC 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 -!- PTM: Ubiquitinated by the DCX(DCAF13) E3 ubiquitin ligase complex, CC leading to its degradation. {ECO:0000269|PubMed:30111536}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSMUSP00000111300; -. DR iPTMnet; O54864; -. DR PhosphoSitePlus; O54864; -. DR EPD; O54864; -. DR jPOST; O54864; -. DR MaxQB; O54864; -. DR PaxDb; 10090-ENSMUSP00000111301; -. DR PeptideAtlas; O54864; -. DR ProteomicsDB; 258671; -. [O54864-1] DR ProteomicsDB; 258672; -. [O54864-2] DR ProteomicsDB; 258673; -. [O54864-3] DR Pumba; O54864; -. DR Antibodypedia; 11710; 446 antibodies from 39 providers. DR DNASU; 20937; -. DR Ensembl; ENSMUST00000115636.4; ENSMUSP00000111299.4; ENSMUSG00000039231.19. [O54864-3] DR Ensembl; ENSMUST00000115638.10; ENSMUSP00000111301.4; ENSMUSG00000039231.19. [O54864-1] DR GeneID; 20937; -. DR KEGG; mmu:20937; -. DR UCSC; uc009snq.2; mouse. [O54864-1] DR AGR; MGI:1099440; -. 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; HHGNISH; -. DR OrthoDB; 5481936at2759; -. DR TreeFam; TF106452; -. DR BRENDA; 2.1.1.355; 3474. DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines. DR BioGRID-ORCS; 20937; 4 hits in 82 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 259 other cell types or tissues. DR ExpressionAtlas; O54864; baseline and differential. 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:0046974; F:histone H3K9 methyltransferase activity; IDA:UniProtKB. DR GO; GO:0140949; F:histone H3K9 trimethyltransferase activity; ISO:MGI. DR GO; GO:0140947; F:histone H3K9me2 methyltransferase activity; IGI:MGI. DR GO; GO:0042054; F:histone methyltransferase activity; ISO:MGI. DR GO; GO:0008276; F:protein methyltransferase activity; TAS: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: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:0007623; P:circadian rhythm; IMP:UniProtKB. DR GO; GO:0008340; P:determination of adult lifespan; IGI:MGI. DR GO; GO:0006974; P:DNA damage response; ISO:MGI. DR GO; GO:0097009; P:energy homeostasis; ISO:MGI. DR GO; GO:0044725; P:epigenetic programming in the zygotic pronuclei; ISO:MGI. DR GO; GO:0031507; P:heterochromatin formation; TAS:UniProtKB. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0045786; P:negative regulation of cell cycle; ISO:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:MGI. DR GO; GO:0000183; P:rDNA heterochromatin formation; 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:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR CDD; cd18639; CD_SUV39H1_like; 1. DR CDD; cd10525; SET_SUV39H1; 1. DR Gene3D; 2.40.50.40; -; 1. DR Gene3D; 2.170.270.10; SET domain; 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; H3-K9_MeTrfase_SUV39H1/2-like. DR InterPro; IPR003616; Post-SET_dom. DR InterPro; IPR007728; Pre-SET_dom. DR InterPro; IPR001214; SET_dom. DR InterPro; IPR046341; SET_dom_sf. DR PANTHER; PTHR46223; HISTONE-LYSINE N-METHYLTRANSFERASE SUV39H; 1. DR PANTHER; PTHR46223:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE SUV39H1; 1. 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; Chromo domain-like; 1. DR SUPFAM; SSF82199; SET domain; 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. DR Genevisible; O54864; MM. 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; Ubl conjugation; KW 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 MUTAGEN 324..326 FT /note="HSC->LAA: No effect on rates of development into FT blastocysts." FT /evidence="ECO:0000269|PubMed:30111536" 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 //