KMT5C_MOUSE
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 03-AUG-2022, entry version 129.
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};
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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; Q6Q783; -.
DR PeptideAtlas; Q6Q783; -.
DR PRIDE; Q6Q783; -.
DR ProteomicsDB; 264788; -.
DR Antibodypedia; 46420; 80 antibodies from 20 providers.
DR DNASU; 232811; -.
DR Ensembl; ENSMUST00000098853; ENSMUSP00000096452; ENSMUSG00000059851.
DR Ensembl; ENSMUST00000108582; ENSMUSP00000104223; ENSMUSG00000059851.
DR Ensembl; ENSMUST00000108583; ENSMUSP00000104224; ENSMUSG00000059851.
DR GeneID; 232811; -.
DR KEGG; mmu:232811; -.
DR UCSC; uc009eyi.2; mouse.
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; GGWTAHY; -.
DR OrthoDB; 236983at2759; -.
DR PhylomeDB; Q6Q783; -.
DR TreeFam; TF106433; -.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR BioGRID-ORCS; 232811; 3 hits in 76 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 252 other tissues.
DR ExpressionAtlas; Q6Q783; baseline and differential.
DR Genevisible; Q6Q783; MM.
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 methyltransferase activity (H4-K20 specific); IDA:MGI.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0034772; P:histone H4-K20 dimethylation; IEA:InterPro.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IDA:MGI.
DR GO; GO:0016571; P:histone methylation; IDA:MGI.
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; -; 1.
DR Gene3D; 2.170.270.10; -; 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; PTHR12977; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR PROSITE; PS50280; SET; 1.
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 S-adenosyl-L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:24049080"
FT MUTAGEN 161
FT /note="S->A: Does not methylates 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
