ID SUV92_HUMAN Reviewed; 410 AA. AC Q9H5I1; D3DRT4; Q5JSS4; Q5JSS5; Q6I9Y3; Q8ND06; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 15-NOV-2002, sequence version 2. DT 24-JAN-2024, entry version 195. DE RecName: Full=Histone-lysine N-methyltransferase SUV39H2; DE EC=2.1.1.355; DE AltName: Full=Histone H3-K9 methyltransferase 2; DE Short=H3-K9-HMTase 2; DE AltName: Full=Lysine N-methyltransferase 1B; DE AltName: Full=Suppressor of variegation 3-9 homolog 2; DE Short=Su(var)3-9 homolog 2; GN Name=SUV39H2; Synonyms=KMT1B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [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 GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Bone marrow, and Muscle; 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 [LARGE SCALE MRNA] OF 96-410. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP FUNCTION. RX PubMed=14765126; DOI=10.1038/sj.emboj.7600074; RA Ait-Si-Ali S., Guasconi V., Fritsch L., Yahi H., Sekhri R., Naguibneva I., RA Robin P., Cabon F., Polesskaya A., Harel-Bellan A.; RT "A Suv39h-dependent mechanism for silencing S-phase genes in RT differentiating but not in cycling cells."; RL EMBO J. 23:605-615(2004). RN [8] RP INTERACTION WITH SMAD5. RX PubMed=15107829; DOI=10.1038/sj.onc.1207660; RA Frontelo P., Leader J.E., Yoo N., Potocki A.C., Crawford M., Kulik M., RA Lechleider R.J.; RT "Suv39h histone methyltransferases interact with Smads and cooperate in RT BMP-induced repression."; RL Oncogene 23:5242-5251(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND SER-388, AND RP IDENTIFICATION 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381; SER-384 AND SER-388, AND RP IDENTIFICATION 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., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381; SER-384 AND SER-388, AND RP IDENTIFICATION 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 [13] RP SUBCELLULAR LOCATION, AND UBIQUITINATION. 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). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 112-410 IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE AND ZINC IONS. RX PubMed=20084102; DOI=10.1371/journal.pone.0008570; RA Wu H., Min J., Lunin V.V., Antoshenko T., Dombrovski L., Zeng H., RA Allali-Hassani A., Campagna-Slater V., Vedadi M., Arrowsmith C.H., RA Plotnikov A.N., Schapira M.; RT "Structural biology of human H3K9 methyltransferases."; RL PLoS ONE 5:E8570-E8570(2010). RN [15] RP VARIANT [LARGE SCALE ANALYSIS] HIS-383. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). 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 cell CC cycle regulation, transcriptional repression and regulation of telomere CC length. May participate in regulation of higher-order chromatin CC organization during spermatogenesis. Recruited by the large PER complex CC to the E-box elements of the circadian target genes such as PER2 itself CC or PER1, 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 -!- 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 -!- SUBUNIT: Interacts with SMAD5. The large PER complex involved in the CC histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 CC and/or SUV39H2; CBX3 mediates the formation of the complex. CC {ECO:0000269|PubMed:15107829, ECO:0000269|PubMed:20084102}. CC -!- INTERACTION: CC Q9H5I1; Q8NEU8: APPL2; NbExp=6; IntAct=EBI-723127, EBI-741261; CC Q9H5I1; Q9BXL8: CDCA4; NbExp=2; IntAct=EBI-723127, EBI-1773949; CC Q9H5I1; V9HWG0: HEL25; NbExp=3; IntAct=EBI-723127, EBI-10183977; CC Q9H5I1; Q8N5Z5: KCTD17; NbExp=2; IntAct=EBI-723127, EBI-743960; CC Q9H5I1; Q8TBB5: KLHDC4; NbExp=2; IntAct=EBI-723127, EBI-8472352; CC Q9H5I1; Q9Y605: MRFAP1; NbExp=2; IntAct=EBI-723127, EBI-995714; CC Q9H5I1; P16333: NCK1; NbExp=2; IntAct=EBI-723127, EBI-389883; CC Q9H5I1; Q5T6S3: PHF19; NbExp=2; IntAct=EBI-723127, EBI-2339674; CC Q9H5I1; Q8ND90: PNMA1; NbExp=5; IntAct=EBI-723127, EBI-302345; CC Q9H5I1; Q9UDV6: ZNF212; NbExp=2; IntAct=EBI-723127, EBI-1640204; CC Q9H5I1-2; Q8NEU8: APPL2; NbExp=3; IntAct=EBI-11977575, EBI-741261; CC Q9H5I1-2; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-11977575, EBI-5916454; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30111536}. CC Chromosome, centromere {ECO:0000250}. Note=Associates with centromeric CC constitutive heterochromatin. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=3; CC IsoId=Q9H5I1-1; Sequence=Displayed; CC Name=1; CC IsoId=Q9H5I1-2; Sequence=VSP_002209; CC Name=2; CC IsoId=Q9H5I1-3; Sequence=VSP_002210; 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 (By similarity). {ECO:0000250}. CC -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are CC arranged in a triangular cluster; some of these Cys residues contribute CC to the binding of two zinc ions within the cluster. CC -!- PTM: Ubiquitinated by the DCX(DCAF13) E3 ubiquitin ligase complex, CC leading to its degradation. {ECO:0000269|PubMed:30111536}. 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 --------------------------------------------------------------------------- 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; AK027067; BAB15645.1; -; mRNA. DR EMBL; CR457372; CAG33653.1; -; mRNA. DR EMBL; AC069544; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL360083; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471072; EAW86254.1; -; Genomic_DNA. DR EMBL; CH471072; EAW86253.1; -; Genomic_DNA. DR EMBL; CH471072; EAW86255.1; -; Genomic_DNA. DR EMBL; CH471072; EAW86256.1; -; Genomic_DNA. DR EMBL; BC007754; AAH07754.1; -; mRNA. DR EMBL; BC029360; AAH29360.1; -; mRNA. DR EMBL; AL834488; CAD39146.1; -; mRNA. DR CCDS; CCDS53493.1; -. [Q9H5I1-3] DR CCDS; CCDS53494.1; -. [Q9H5I1-1] DR CCDS; CCDS7104.1; -. [Q9H5I1-2] DR RefSeq; NP_001180353.1; NM_001193424.1. [Q9H5I1-1] DR RefSeq; NP_001180354.1; NM_001193425.1. [Q9H5I1-2] DR RefSeq; NP_001180355.1; NM_001193426.1. [Q9H5I1-3] DR RefSeq; NP_001180356.1; NM_001193427.1. DR RefSeq; NP_078946.1; NM_024670.3. [Q9H5I1-2] DR RefSeq; XP_006717566.1; XM_006717503.3. DR RefSeq; XP_011517964.1; XM_011519662.2. [Q9H5I1-2] DR RefSeq; XP_016872126.1; XM_017016637.1. DR PDB; 2R3A; X-ray; 2.00 A; A=112-410. DR PDB; 6P0R; X-ray; 2.40 A; A/B=112-410. DR PDBsum; 2R3A; -. DR PDBsum; 6P0R; -. DR AlphaFoldDB; Q9H5I1; -. DR SMR; Q9H5I1; -. DR BioGRID; 122838; 82. DR IntAct; Q9H5I1; 66. DR MINT; Q9H5I1; -. DR STRING; 9606.ENSP00000346997; -. DR BindingDB; Q9H5I1; -. DR ChEMBL; CHEMBL1795177; -. DR GuidetoPHARMACOLOGY; 2716; -. DR GlyGen; Q9H5I1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H5I1; -. DR PhosphoSitePlus; Q9H5I1; -. DR BioMuta; SUV39H2; -. DR DMDM; 25091325; -. DR EPD; Q9H5I1; -. DR jPOST; Q9H5I1; -. DR MassIVE; Q9H5I1; -. DR MaxQB; Q9H5I1; -. DR PaxDb; 9606-ENSP00000346997; -. DR PeptideAtlas; Q9H5I1; -. DR ProteomicsDB; 80906; -. [Q9H5I1-1] DR ProteomicsDB; 80907; -. [Q9H5I1-2] DR ProteomicsDB; 80908; -. [Q9H5I1-3] DR Pumba; Q9H5I1; -. DR Antibodypedia; 24975; 413 antibodies from 37 providers. DR DNASU; 79723; -. DR Ensembl; ENST00000313519.9; ENSP00000319208.5; ENSG00000152455.16. [Q9H5I1-2] DR Ensembl; ENST00000354919.11; ENSP00000346997.6; ENSG00000152455.16. [Q9H5I1-1] DR Ensembl; ENST00000378325.7; ENSP00000367576.3; ENSG00000152455.16. [Q9H5I1-3] DR GeneID; 79723; -. DR KEGG; hsa:79723; -. DR MANE-Select; ENST00000354919.11; ENSP00000346997.6; NM_001193424.2; NP_001180353.1. DR UCSC; uc001ing.4; human. [Q9H5I1-1] DR AGR; HGNC:17287; -. DR CTD; 79723; -. DR DisGeNET; 79723; -. DR GeneCards; SUV39H2; -. DR HGNC; HGNC:17287; SUV39H2. DR HPA; ENSG00000152455; Tissue enriched (testis). DR MIM; 606503; gene. DR neXtProt; NX_Q9H5I1; -. DR OpenTargets; ENSG00000152455; -. DR PharmGKB; PA134868807; -. DR VEuPathDB; HostDB:ENSG00000152455; -. DR eggNOG; KOG1082; Eukaryota. DR GeneTree; ENSGT00940000156788; -. DR HOGENOM; CLU_020840_8_0_1; -. DR InParanoid; Q9H5I1; -. DR OMA; CECADCP; -. DR OrthoDB; 5481936at2759; -. DR PhylomeDB; Q9H5I1; -. DR TreeFam; TF106452; -. DR BioCyc; MetaCyc:HS07820-MONOMER; -. DR PathwayCommons; Q9H5I1; -. DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines. DR SignaLink; Q9H5I1; -. DR BioGRID-ORCS; 79723; 15 hits in 1173 CRISPR screens. DR ChiTaRS; SUV39H2; human. DR EvolutionaryTrace; Q9H5I1; -. DR GeneWiki; SUV39H2; -. DR GenomeRNAi; 79723; -. DR Pharos; Q9H5I1; Tchem. DR PRO; PR:Q9H5I1; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q9H5I1; Protein. DR Bgee; ENSG00000152455; Expressed in sperm and 135 other cell types or tissues. DR ExpressionAtlas; Q9H5I1; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProt. DR GO; GO:0140938; F:histone H3 methyltransferase activity; TAS:Reactome. DR GO; GO:0046974; F:histone H3K9 methyltransferase activity; IDA:UniProtKB. DR GO; GO:0140949; F:histone H3K9 trimethyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB. DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:UniProt. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI. DR GO; GO:0006325; P:chromatin organization; IMP:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB. DR GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB. DR GO; GO:0044725; P:epigenetic programming in the zygotic pronuclei; IDA:UniProt. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI. DR CDD; cd18639; CD_SUV39H1_like; 1. DR CDD; cd10532; SET_SUV39H2; 1. DR DisProt; DP02654; -. DR Gene3D; 2.40.50.40; -; 1. DR Gene3D; 2.170.270.10; SET domain; 1. DR IDEAL; IID00498; -. 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:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SUV39H2; 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; Q9H5I1; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Biological rhythms; Cell cycle; KW Centromere; Chromatin regulator; Chromosome; Differentiation; KW Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; KW Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription; KW Transcription regulation; Transferase; Ubl conjugation; Zinc. FT CHAIN 1..410 FT /note="Histone-lysine N-methyltransferase SUV39H2" FT /id="PRO_0000186059" FT DOMAIN 47..105 FT /note="Chromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053" FT DOMAIN 189..247 FT /note="Pre-SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157" FT DOMAIN 250..373 FT /note="SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT DOMAIN 394..410 FT /note="Post-SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155" FT BINDING 191 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 191 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 193 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 196 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 196 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 201 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 202 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 229 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 229 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 233 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 235 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 239 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 261..263 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 330..331 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 333 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 372 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT BINDING 398 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 399 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 400 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT BINDING 405 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000269|PubMed:20084102, FT ECO:0007744|PDB:2R3A" FT MOD_RES 381 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 384 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 388 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..60 FT /note="Missing (in isoform 1)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2" FT /id="VSP_002209" FT VAR_SEQ 104..283 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_002210" FT VARIANT 383 FT /note="D -> H (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036344" FT HELIX 125..147 FT /evidence="ECO:0007829|PDB:2R3A" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:2R3A" FT STRAND 154..157 FT /evidence="ECO:0007829|PDB:2R3A" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:2R3A" FT TURN 196..198 FT /evidence="ECO:0007829|PDB:2R3A" FT HELIX 202..205 FT /evidence="ECO:0007829|PDB:2R3A" FT STRAND 216..218 FT /evidence="ECO:0007829|PDB:6P0R" FT HELIX 244..246 FT /evidence="ECO:0007829|PDB:2R3A" FT STRAND 252..256 FT /evidence="ECO:0007829|PDB:2R3A" FT STRAND 258..260 FT /evidence="ECO:0007829|PDB:2R3A" FT STRAND 263..269 FT /evidence="ECO:0007829|PDB:2R3A" FT STRAND 276..280 FT /evidence="ECO:0007829|PDB:2R3A" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:2R3A" FT HELIX 287..295 FT /evidence="ECO:0007829|PDB:2R3A" FT HELIX 299..303 FT /evidence="ECO:0007829|PDB:2R3A" FT STRAND 305..307 FT /evidence="ECO:0007829|PDB:2R3A" FT TURN 309..311 FT /evidence="ECO:0007829|PDB:6P0R" FT STRAND 313..318 FT /evidence="ECO:0007829|PDB:2R3A" FT STRAND 320..323 FT /evidence="ECO:0007829|PDB:2R3A" FT HELIX 325..328 FT /evidence="ECO:0007829|PDB:2R3A" FT STRAND 336..345 FT /evidence="ECO:0007829|PDB:2R3A" FT STRAND 353..360 FT /evidence="ECO:0007829|PDB:2R3A" FT STRAND 367..370 FT /evidence="ECO:0007829|PDB:2R3A" FT HELIX 372..374 FT /evidence="ECO:0007829|PDB:2R3A" SQ SEQUENCE 410 AA; 46682 MW; ED8BBF80AE838C69 CRC64; MAAVGAEARG AWCVPCLVSL DTLQELCRKE KLTCKSIGIT KRNLNNYEVE YLCDYKVVKD MEYYLVKWKG WPDSTNTWEP LQNLKCPLLL QQFSNDKHNY LSQVKKGKAI TPKDNNKTLK PAIAEYIVKK AKQRIALQRW QDELNRRKNH KGMIFVENTV DLEGPPSDFY YINEYKPAPG ISLVNEATFG CSCTDCFFQK CCPAEAGVLL AYNKNQQIKI PPGTPIYECN SRCQCGPDCP NRIVQKGTQY SLCIFRTSNG RGWGVKTLVK IKRMSFVMEY VGEVITSEEA ERRGQFYDNK GITYLFDLDY ESDEFTVDAA RYGNVSHFVN HSCDPNLQVF NVFIDNLDTR LPRIALFSTR TINAGEELTF DYQMKGSGDI SSDSIDHSPA KKRVRTVCKC GAVTCRGYLN //