ID KMT5C_MOUSE Reviewed; 468 AA. AC Q6Q783; Q5RKP6; Q8R1C5; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 137. DE RecName: Full=Histone-lysine N-methyltransferase KMT5C {ECO:0000305}; DE AltName: Full=Lysine-specific methyltransferase 5C {ECO:0000250|UniProtKB:Q86Y97}; DE AltName: Full=Suppressor of variegation 4-20 homolog 2; DE Short=Su(var)4-20 homolog 2; DE Short=Suv4-20h2; DE AltName: Full=[histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B {ECO:0000305}; DE EC=2.1.1.362 {ECO:0000269|PubMed:15145825, ECO:0000269|PubMed:24049080, ECO:0000269|PubMed:28114273}; DE AltName: Full=[histone H4]-lysine20 N-methyltransferase KMT5B {ECO:0000305}; DE EC=2.1.1.361 {ECO:0000250|UniProtKB:Q86Y97}; GN Name=Kmt5c {ECO:0000250|UniProtKB:Q86Y97}; Synonyms=Suv420h2; 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], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR RP LOCATION, AND INTERACTION WITH CBX1; CBX3 AND CBX5. RC STRAIN=FVB/N; RX PubMed=15145825; DOI=10.1101/gad.300704; RA Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G., RA Reinberg D., Jenuwein T.; RT "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at RT constitutive heterochromatin."; RL Genes Dev. 18:1251-1262(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=Dendritic cell; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye; 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 [4] RP INTERACTION WITH RB1; RBL1 AND RBL2. RX PubMed=15750587; DOI=10.1038/ncb1235; RA Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M., RA Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T., Blasco M.A.; RT "Role of the RB1 family in stabilizing histone methylation at constitutive RT heterochromatin."; RL Nat. Cell Biol. 7:420-428(2005). RN [5] RP INTERACTION WITH RB1; RBL1 AND RBL2. RX PubMed=16612004; DOI=10.1128/mcb.26.9.3659-3671.2006; RA Isaac C.E., Francis S.M., Martens A.L., Julian L.M., Seifried L.A., RA Erdmann N., Binne U.K., Harrington L., Sicinski P., Berube N.G., RA Dyson N.J., Dick F.A.; RT "The retinoblastoma protein regulates pericentric heterochromatin."; RL Mol. Cell. Biol. 26:3659-3671(2006). RN [6] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=28114273; DOI=10.1038/nchembio.2282; RA Bromberg K.D., Mitchell T.R., Upadhyay A.K., Jakob C.G., Jhala M.A., RA Comess K.M., Lasko L.M., Li C., Tuzon C.T., Dai Y., Li F., Eram M.S., RA Nuber A., Soni N.B., Manaves V., Algire M.A., Sweis R.F., Torrent M., RA Schotta G., Sun C., Michaelides M.R., Shoemaker A.R., Arrowsmith C.H., RA Brown P.J., Santhakumar V., Martin A., Rice J.C., Chiang G.G., Vedadi M., RA Barsyte-Lovejoy D., Pappano W.N.; RT "The SUV4-20 inhibitor A-196 verifies a role for epigenetics in genomic RT integrity."; RL Nat. Chem. Biol. 13:317-324(2017). RN [7] {ECO:0007744|PDB:4AU7} RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 1-246 IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE; HISTONE H4 PEPTIDE AND ZINC, SUBUNIT, MUTAGENESIS RP OF MET-116 AND SER-161, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=24049080; DOI=10.1093/nar/gkt776; RA Southall S.M., Cronin N.B., Wilson J.R.; RT "A novel route to product specificity in the Suv4-20 family of histone RT H4K20 methyltransferases."; RL Nucleic Acids Res. 42:661-671(2014). CC -!- FUNCTION: Histone methyltransferase that specifically methylates CC monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2) CC of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2) CC and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription CC and maintenance of genome integrity (PubMed:15145825, PubMed:28114273). CC In vitro also methylates unmodified 'Lys-20' (H4K20me0) of histone H4 CC and nucleosomes (By similarity). H4 'Lys-20' trimethylation represents CC a specific tag for epigenetic transcriptional repression CC (PubMed:15145825). Mainly functions in pericentric heterochromatin CC regions, thereby playing a central role in the establishment of CC constitutive heterochromatin in these regions (PubMed:15145825). KMT5B CC is targeted to histone H3 via its interaction with RB1 family proteins CC (RB1, RBL1 and RBL2) (PubMed:15750587, PubMed:16612004). Facilitates CC TP53BP1 foci formation upon DNA damage and proficient non-homologous CC end-joining (NHEJ)-directed DNA repair by catalyzing the di- and CC trimethylation of 'Lys-20' of histone H4 (By similarity). May play a CC role in class switch reconbination by catalyzing the di- and CC trimethylation of 'Lys-20' of histone H4 (PubMed:28114273). CC {ECO:0000250|UniProtKB:Q86Y97, ECO:0000269|PubMed:15145825, CC ECO:0000269|PubMed:15750587, ECO:0000269|PubMed:16612004, CC ECO:0000269|PubMed:28114273}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:60348, Rhea:RHEA-COMP:15555, Rhea:RHEA- CC COMP:15556, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; EC=2.1.1.362; CC Evidence={ECO:0000269|PubMed:15145825, ECO:0000269|PubMed:24049080, CC ECO:0000269|PubMed:28114273}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60349; CC Evidence={ECO:0000269|PubMed:28114273}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L- CC methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:61992, Rhea:RHEA- CC COMP:15556, Rhea:RHEA-COMP:15998, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961, CC ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:15145825, CC ECO:0000269|PubMed:28114273}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61993; CC Evidence={ECO:0000269|PubMed:28114273}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) + CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361; CC Evidence={ECO:0000250|UniProtKB:Q86Y97}; CC -!- ACTIVITY REGULATION: Inhibited by 6,7-Dichloro-N-cyclopentyl-4- CC (pyridin-4-yl)phthalazin-1-amine (A-196). CC {ECO:0000250|UniProtKB:Q86Y97}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=510 uM for histone H4K20me1 peptide {ECO:0000269|PubMed:24049080}; CC -!- SUBUNIT: Homodimer (PubMed:24049080). Interacts with HP1 proteins CBX1, CC CBX3 and CBX5. Interacts with RB1 family proteins RB1, RBL1 and RBL2. CC {ECO:0000269|PubMed:15145825, ECO:0000269|PubMed:15750587, CC ECO:0000269|PubMed:16612004, ECO:0000269|PubMed:24049080}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15145825}. Chromosome CC {ECO:0000269|PubMed:15145825}. Note=Associated with pericentric CC heterochromatin. CBX1 and CBX5 are required for the localization to CC pericentric heterochromatin. CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. Suvar4-20 CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00903}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH24816.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH85473.2; Type=Erroneous initiation; 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; AY555193; AAT00540.1; -; mRNA. DR EMBL; AK154848; BAE32874.1; -; mRNA. DR EMBL; BC024816; AAH24816.1; ALT_INIT; mRNA. DR EMBL; BC085473; AAH85473.2; ALT_INIT; mRNA. DR CCDS; CCDS20743.2; -. DR RefSeq; NP_001108490.1; NM_001115018.1. DR RefSeq; NP_666289.2; NM_146177.2. DR RefSeq; XP_006539837.1; XM_006539774.1. DR PDB; 4AU7; X-ray; 2.07 A; A/B=1-246. DR PDBsum; 4AU7; -. DR AlphaFoldDB; Q6Q783; -. DR SMR; Q6Q783; -. DR BioGRID; 231299; 3. DR STRING; 10090.ENSMUSP00000104223; -. DR iPTMnet; Q6Q783; -. DR PhosphoSitePlus; Q6Q783; -. DR EPD; Q6Q783; -. DR jPOST; Q6Q783; -. DR MaxQB; Q6Q783; -. DR PaxDb; 10090-ENSMUSP00000104223; -. DR PeptideAtlas; Q6Q783; -. DR ProteomicsDB; 264788; -. DR Antibodypedia; 46420; 115 antibodies from 21 providers. DR DNASU; 232811; -. DR Ensembl; ENSMUST00000098853.9; ENSMUSP00000096452.3; ENSMUSG00000059851.16. DR Ensembl; ENSMUST00000108582.10; ENSMUSP00000104223.4; ENSMUSG00000059851.16. DR Ensembl; ENSMUST00000108583.9; ENSMUSP00000104224.3; ENSMUSG00000059851.16. DR GeneID; 232811; -. DR KEGG; mmu:232811; -. DR UCSC; uc009eyi.2; mouse. DR AGR; MGI:2385262; -. DR CTD; 84787; -. DR MGI; MGI:2385262; Kmt5c. DR VEuPathDB; HostDB:ENSMUSG00000059851; -. DR eggNOG; KOG2589; Eukaryota. DR GeneTree; ENSGT00940000161700; -. DR HOGENOM; CLU_040002_0_0_1; -. DR InParanoid; Q6Q783; -. DR OMA; GCGPHCC; -. DR OrthoDB; 5396777at2759; -. DR PhylomeDB; Q6Q783; -. DR TreeFam; TF106433; -. DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines. DR BioGRID-ORCS; 232811; 3 hits in 82 CRISPR screens. DR ChiTaRS; Suv420h2; mouse. DR PRO; PR:Q6Q783; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q6Q783; Protein. DR Bgee; ENSMUSG00000059851; Expressed in retinal neural layer and 255 other cell types or tissues. DR ExpressionAtlas; Q6Q783; baseline and differential. DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI. DR GO; GO:0000792; C:heterochromatin; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005721; C:pericentric heterochromatin; ISO:MGI. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0042393; F:histone binding; IDA:UniProtKB. DR GO; GO:0042799; F:histone H4K20 methyltransferase activity; IDA:MGI. DR GO; GO:0140944; F:histone H4K20 monomethyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0140941; F:histone H4K20me methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB. DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB. DR GO; GO:0045830; P:positive regulation of isotype switching; IMP:UniProtKB. DR CDD; cd19185; SET_KMT5C; 1. DR Gene3D; 1.10.10.1700; Histone-lysine N-methyltransferase; 1. DR Gene3D; 2.170.270.10; SET domain; 1. DR InterPro; IPR041938; Hist-Lys_N-MTase_N. DR InterPro; IPR044425; KMT5C_SET. DR InterPro; IPR001214; SET_dom. DR InterPro; IPR046341; SET_dom_sf. DR InterPro; IPR039977; Suv4-20/Set9. DR InterPro; IPR025790; Suv4-20_animal. DR PANTHER; PTHR12977:SF11; HISTONE-LYSINE N-METHYLTRANSFERASE KMT5C; 1. DR PANTHER; PTHR12977; SUPPRESSOR OF VARIEGATION 4-20-RELATED; 1. DR Pfam; PF00856; SET; 1. DR SMART; SM00317; SET; 1. DR SUPFAM; SSF82199; SET domain; 1. DR PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1. DR PROSITE; PS50280; SET; 1. DR Genevisible; Q6Q783; MM. PE 1: Evidence at protein level; KW 3D-structure; Chromatin regulator; Chromosome; Metal-binding; KW Methyltransferase; Nucleus; Reference proteome; Repressor; KW S-adenosyl-L-methionine; Transcription; Transcription regulation; KW Transferase; Zinc. FT CHAIN 1..468 FT /note="Histone-lysine N-methyltransferase KMT5C" FT /id="PRO_0000281794" FT DOMAIN 104..218 FT /note="SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT REGION 150..166 FT /note="Histone H4 binding" FT /evidence="ECO:0000269|PubMed:24049080, FT ECO:0007744|PDB:4AU7" FT REGION 348..441 FT /note="Required for heterochromatin localization" FT BINDING 32 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:24049080, FT ECO:0007744|PDB:4AU7" FT BINDING 92 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007744|PDB:4AU7" FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:24049080, FT ECO:0007744|PDB:4AU7" FT BINDING 114..117 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:Q86Y97" FT BINDING 121 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:24049080, FT ECO:0007744|PDB:4AU7" FT BINDING 141 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:24049080, FT ECO:0007744|PDB:4AU7" FT BINDING 160 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:Q86Y97" FT BINDING 169 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:Q86Y97" FT BINDING 182..183 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:24049080, FT ECO:0007744|PDB:4AU7" FT BINDING 185 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:24049080, FT ECO:0007744|PDB:4AU7" FT BINDING 185 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q86Y97" FT BINDING 229 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:24049080, FT ECO:0007744|PDB:4AU7" FT BINDING 229 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q86Y97" FT BINDING 230 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000269|PubMed:24049080, FT ECO:0007744|PDB:4AU7" FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:24049080, FT ECO:0007744|PDB:4AU7" FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q86Y97" FT BINDING 234 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:24049080, FT ECO:0007744|PDB:4AU7" FT BINDING 234 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q86Y97" FT SITE 217 FT /note="Histone H4 binding; via carbonyl oxygen" FT /evidence="ECO:0000269|PubMed:24049080, FT ECO:0007744|PDB:4AU7" FT MUTAGEN 116 FT /note="M->S: Does not affect affinity for FT S-adenosyl-L-methionine." FT /evidence="ECO:0000269|PubMed:24049080" FT MUTAGEN 161 FT /note="S->A: Does not methylate either an unmodified or FT monomethylated H4K20 substrate. Methylates a di-methylated FT H4K20 peptide." FT /evidence="ECO:0000269|PubMed:24049080" FT HELIX 8..21 FT /evidence="ECO:0007829|PDB:4AU7" FT HELIX 23..27 FT /evidence="ECO:0007829|PDB:4AU7" FT HELIX 45..58 FT /evidence="ECO:0007829|PDB:4AU7" FT HELIX 61..68 FT /evidence="ECO:0007829|PDB:4AU7" FT HELIX 74..77 FT /evidence="ECO:0007829|PDB:4AU7" FT TURN 78..81 FT /evidence="ECO:0007829|PDB:4AU7" FT HELIX 83..99 FT /evidence="ECO:0007829|PDB:4AU7" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:4AU7" FT STRAND 106..111 FT /evidence="ECO:0007829|PDB:4AU7" FT STRAND 118..127 FT /evidence="ECO:0007829|PDB:4AU7" FT STRAND 134..144 FT /evidence="ECO:0007829|PDB:4AU7" FT HELIX 147..152 FT /evidence="ECO:0007829|PDB:4AU7" FT TURN 155..157 FT /evidence="ECO:0007829|PDB:4AU7" FT STRAND 160..165 FT /evidence="ECO:0007829|PDB:4AU7" FT TURN 166..169 FT /evidence="ECO:0007829|PDB:4AU7" FT STRAND 170..176 FT /evidence="ECO:0007829|PDB:4AU7" FT HELIX 177..180 FT /evidence="ECO:0007829|PDB:4AU7" FT STRAND 188..193 FT /evidence="ECO:0007829|PDB:4AU7" FT STRAND 195..205 FT /evidence="ECO:0007829|PDB:4AU7" FT TURN 219..222 FT /evidence="ECO:0007829|PDB:4AU7" FT HELIX 232..237 FT /evidence="ECO:0007829|PDB:4AU7" FT HELIX 240..243 FT /evidence="ECO:0007829|PDB:4AU7" SQ SEQUENCE 468 AA; 53159 MW; D43D7A25DBDF3BB1 CRC64; MGPDRVTARE LCENDDLATS LVLDPYLGFR THKMNVSPVP TLRRQHHLRS ALEAFLRQRD LEAAFRALTL GGWMAHYFQS RAPRQEAALK THIFCYLRAF LPESGFTILP CTRYSMETNG AKIVSTRAWK KNEKLELLVG CIAELREEDE DLLRAGENDF SIMYSTRKRS AQLWLGPAAF INHDCKPNCK FVPSDGNTAC VKVLRDIEPG DEVTCFYGEG FFGEKNEHCE CYTCERKGEG AFRLQPREPE LRPKPLDKYE LRETKRRLQQ GLVSSQQSLM SRWACSHLSP LRPDPFCAAC QPSCLLPASP HMDYLPLWLQ RAPQPQPIVP PRKRHRRRRP RIRQASLPPV LRTACVPLHR WGGCGPHCQL RAEAMVTLHL RPQTRWTPQQ DWYWARRYGL PSVGRVELTR LAPALPAAPA PAGNPGPVPT PDFIPKQALA FAPFCPPKRL RLVVSHGSID LDINSGEP //