ID KMT5B_MOUSE Reviewed; 883 AA.
AC Q3U8K7; Q3UTP6; Q6DI74; Q6Q784; Q8BU67; Q8BUN0; Q8BUT7; Q8BW73; Q8BZ24;
AC Q91X81;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 24-JAN-2024, entry version 131.
DE RecName: Full=Histone-lysine N-methyltransferase KMT5B {ECO:0000305};
DE AltName: Full=Lysine-specific methyltransferase 5B {ECO:0000250|UniProtKB:Q4FZB7};
DE AltName: Full=Suppressor of variegation 4-20 homolog 1;
DE Short=Su(var)4-20 homolog 1;
DE Short=Suv4-20h1;
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:Q4FZB7};
GN Name=Kmt5b {ECO:0000312|MGI:MGI:2444557}; Synonyms=Suv420h1;
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), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CBX1; CBX3 AND CBX5.
RC STRAIN=C57BL/6J;
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] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Cerebellum, Hippocampus, Lung, Oviduct, and Vagina;
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] (ISOFORMS 4 AND 5).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor, and Salivary 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 [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, INTERACTION WITH FRG1, AND DISRUPTION PHENOTYPE.
RX PubMed=23720823; DOI=10.1093/jmcb/mjt018;
RA Neguembor M.V., Xynos A., Onorati M.C., Caccia R., Bortolanza S., Godio C.,
RA Pistoni M., Corona D.F., Schotta G., Gabellini D.;
RT "FSHD muscular dystrophy region gene 1 binds Suv4-20h1 histone
RT methyltransferase and impairs myogenesis.";
RL J. Mol. Cell Biol. 5:294-307(2013).
RN [7]
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 [8] {ECO:0007744|PDB:4BUP}
RP X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 70-336 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE AND ZINC, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF PHE-282.
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:28114273, PubMed:24049080,
CC PubMed:15145825). In vitro also methylates unmodified 'Lys-20'
CC (H4K20me0) of histone H4 and nucleosomes (By similarity). H4 'Lys-20'
CC trimethylation represents a specific tag for epigenetic transcriptional
CC repression (PubMed:15145825). Mainly functions in pericentric
CC heterochromatin regions, thereby playing a central role in the
CC establishment of constitutive heterochromatin in these regions
CC (PubMed:15145825). KMT5B is targeted to histone H3 via its interaction
CC with RB1 family proteins (RB1, RBL1 and RBL2) (PubMed:16612004,
CC PubMed:15750587). Plays a role in myogenesis by regulating the
CC expression of target genes, such as EID3 (PubMed:23720823). 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:Q4FZB7, ECO:0000269|PubMed:15145825,
CC ECO:0000269|PubMed:15750587, ECO:0000269|PubMed:16612004,
CC ECO:0000269|PubMed:23720823, ECO:0000269|PubMed:24049080,
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:Q4FZB7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60345;
CC Evidence={ECO:0000250|UniProtKB:Q4FZB7};
CC -!- ACTIVITY REGULATION: Inhibited by 6,7-Dichloro-N-cyclopentyl-4-
CC (pyridin-4-yl)phthalazin-1-amine (A-196). A-196 is competitive with the
CC histone peptide substrate H4K20me1 but non competitive with S-adenosyl-
CC L-methionine. {ECO:0000250|UniProtKB:Q4FZB7}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=46 uM for histone H4K20me1 peptide {ECO:0000269|PubMed:24049080};
CC -!- SUBUNIT: Homodimer (PubMed:24049080). Interacts with HP1 proteins CBX1,
CC CBX3 and CBX5 (PubMed:15145825). Interacts with RB1 family proteins
CC RB1, RBL1 and RBL2 (PubMed:15750587, PubMed:16612004). Interacts (via
CC C-terminus) with FRG1 (PubMed:23720823). {ECO:0000269|PubMed:15145825,
CC ECO:0000269|PubMed:15750587, ECO:0000269|PubMed:16612004,
CC ECO:0000269|PubMed:23720823, 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q3U8K7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U8K7-2; Sequence=VSP_024055, VSP_024056;
CC Name=3;
CC IsoId=Q3U8K7-3; Sequence=VSP_024053;
CC Name=4;
CC IsoId=Q3U8K7-4; Sequence=VSP_024054;
CC Name=5;
CC IsoId=Q3U8K7-5; Sequence=VSP_024053, VSP_024057;
CC -!- DISRUPTION PHENOTYPE: Partial muscle-specific knockout mice display
CC several signs of muscular dystrophy including necrosis and an increased
CC number of centrally nucleated myofibers. RNAi-mediated knockdown in
CC C2C12 muscle cells causes reduced myogenic differentiation of the
CC cells. {ECO:0000269|PubMed:23720823}.
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=AAH11214.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAT00539.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC39834.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE23934.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY555192; AAT00539.1; ALT_INIT; mRNA.
DR EMBL; AK036880; BAC29617.1; -; mRNA.
DR EMBL; AK054093; BAC35652.1; -; mRNA.
DR EMBL; AK082660; BAC38565.1; -; mRNA.
DR EMBL; AK083227; BAC38817.1; -; mRNA.
DR EMBL; AK087267; BAC39834.1; ALT_INIT; mRNA.
DR EMBL; AK139255; BAE23934.1; ALT_SEQ; mRNA.
DR EMBL; AK152179; BAE31010.1; -; mRNA.
DR EMBL; BC011214; AAH11214.1; ALT_INIT; mRNA.
DR EMBL; BC075709; AAH75709.1; -; mRNA.
DR CCDS; CCDS29399.1; -. [Q3U8K7-3]
DR CCDS; CCDS50343.1; -. [Q3U8K7-1]
DR CCDS; CCDS50344.1; -. [Q3U8K7-2]
DR CCDS; CCDS50345.1; -. [Q3U8K7-4]
DR RefSeq; NP_001161356.1; NM_001167884.1. [Q3U8K7-4]
DR RefSeq; NP_001161357.1; NM_001167885.1. [Q3U8K7-1]
DR RefSeq; NP_001161358.1; NM_001167886.1. [Q3U8K7-3]
DR RefSeq; NP_001161359.1; NM_001167887.1. [Q3U8K7-1]
DR RefSeq; NP_001161360.1; NM_001167888.1. [Q3U8K7-4]
DR RefSeq; NP_001161361.1; NM_001167889.1. [Q3U8K7-2]
DR RefSeq; NP_659120.3; NM_144871.4. [Q3U8K7-3]
DR RefSeq; XP_006531790.1; XM_006531727.3. [Q3U8K7-1]
DR RefSeq; XP_006531791.1; XM_006531728.3. [Q3U8K7-1]
DR RefSeq; XP_006531794.1; XM_006531731.2.
DR RefSeq; XP_011246925.1; XM_011248623.2.
DR RefSeq; XP_011246926.1; XM_011248624.2. [Q3U8K7-3]
DR RefSeq; XP_017173632.1; XM_017318143.1.
DR PDB; 4BUP; X-ray; 2.17 A; A/B=70-336.
DR PDBsum; 4BUP; -.
DR AlphaFoldDB; Q3U8K7; -.
DR SMR; Q3U8K7; -.
DR BioGRID; 230441; 16.
DR STRING; 10090.ENSMUSP00000109606; -.
DR iPTMnet; Q3U8K7; -.
DR PhosphoSitePlus; Q3U8K7; -.
DR EPD; Q3U8K7; -.
DR jPOST; Q3U8K7; -.
DR MaxQB; Q3U8K7; -.
DR PaxDb; 10090-ENSMUSP00000109605; -.
DR PeptideAtlas; Q3U8K7; -.
DR ProteomicsDB; 263668; -. [Q3U8K7-1]
DR ProteomicsDB; 263669; -. [Q3U8K7-2]
DR ProteomicsDB; 263670; -. [Q3U8K7-3]
DR ProteomicsDB; 263671; -. [Q3U8K7-4]
DR ProteomicsDB; 263672; -. [Q3U8K7-5]
DR Antibodypedia; 30535; 264 antibodies from 22 providers.
DR DNASU; 225888; -.
DR Ensembl; ENSMUST00000005518.16; ENSMUSP00000005518.10; ENSMUSG00000045098.20. [Q3U8K7-4]
DR Ensembl; ENSMUST00000052699.13; ENSMUSP00000060162.7; ENSMUSG00000045098.20. [Q3U8K7-2]
DR Ensembl; ENSMUST00000113968.9; ENSMUSP00000109601.3; ENSMUSG00000045098.20. [Q3U8K7-4]
DR Ensembl; ENSMUST00000113970.8; ENSMUSP00000109603.2; ENSMUSG00000045098.20. [Q3U8K7-2]
DR Ensembl; ENSMUST00000113972.9; ENSMUSP00000109605.3; ENSMUSG00000045098.20. [Q3U8K7-1]
DR Ensembl; ENSMUST00000113973.8; ENSMUSP00000109606.2; ENSMUSG00000045098.20. [Q3U8K7-1]
DR Ensembl; ENSMUST00000113974.11; ENSMUSP00000109607.5; ENSMUSG00000045098.20. [Q3U8K7-3]
DR Ensembl; ENSMUST00000113977.9; ENSMUSP00000109610.3; ENSMUSG00000045098.20. [Q3U8K7-3]
DR Ensembl; ENSMUST00000176262.8; ENSMUSP00000135563.2; ENSMUSG00000045098.20. [Q3U8K7-3]
DR Ensembl; ENSMUST00000237440.2; ENSMUSP00000158061.2; ENSMUSG00000045098.20. [Q3U8K7-4]
DR GeneID; 225888; -.
DR KEGG; mmu:225888; -.
DR UCSC; uc008fww.2; mouse. [Q3U8K7-4]
DR UCSC; uc008fwz.2; mouse. [Q3U8K7-2]
DR UCSC; uc008fxa.2; mouse. [Q3U8K7-1]
DR UCSC; uc008fxc.2; mouse. [Q3U8K7-3]
DR AGR; MGI:2444557; -.
DR CTD; 51111; -.
DR MGI; MGI:2444557; Kmt5b.
DR VEuPathDB; HostDB:ENSMUSG00000045098; -.
DR eggNOG; KOG2589; Eukaryota.
DR GeneTree; ENSGT00940000156431; -.
DR HOGENOM; CLU_328991_0_0_1; -.
DR InParanoid; Q3U8K7; -.
DR OMA; NDHAQTK; -.
DR OrthoDB; 5396777at2759; -.
DR PhylomeDB; Q3U8K7; -.
DR TreeFam; TF106433; -.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR BioGRID-ORCS; 225888; 5 hits in 82 CRISPR screens.
DR ChiTaRS; Suv420h1; mouse.
DR PRO; PR:Q3U8K7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3U8K7; Protein.
DR Bgee; ENSMUSG00000045098; Expressed in embryonic post-anal tail and 259 other cell types or tissues.
DR ExpressionAtlas; Q3U8K7; baseline and differential.
DR Genevisible; Q3U8K7; MM.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042799; F:histone H4K20 methyltransferase activity; IDA:UniProtKB.
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:0042054; F:histone methyltransferase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; 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; cd19184; SET_KMT5B; 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; IPR044424; KMT5B_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:SF12; HISTONE-LYSINE N-METHYLTRANSFERASE KMT5B; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Chromosome;
KW Isopeptide bond; Metal-binding; Methyltransferase; Myogenesis; Nucleus;
KW Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc.
FT CHAIN 1..883
FT /note="Histone-lysine N-methyltransferase KMT5B"
FT /id="PRO_0000281788"
FT DOMAIN 194..309
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..846
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24049080,
FT ECO:0007744|PDB:4BUP"
FT BINDING 204..207
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24049080,
FT ECO:0007744|PDB:4BUP"
FT BINDING 211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24049080,
FT ECO:0007744|PDB:4BUP"
FT BINDING 258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24049080,
FT ECO:0007744|PDB:4BUP"
FT BINDING 273..274
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24049080,
FT ECO:0007744|PDB:4BUP"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24049080,
FT ECO:0007744|PDB:4BUP"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24049080,
FT ECO:0007744|PDB:4BUP"
FT BINDING 321
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:24049080,
FT ECO:0007744|PDB:4BUP"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24049080,
FT ECO:0007744|PDB:4BUP"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24049080,
FT ECO:0007744|PDB:4BUP"
FT CROSSLNK 556
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT VAR_SEQ 104..126
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_024053"
FT VAR_SEQ 328..883
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_024054"
FT VAR_SEQ 393..394
FT /note="TS -> SK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024055"
FT VAR_SEQ 395..883
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024056"
FT VAR_SEQ 831..883
FT /note="EGEEEEEDCEDDFDDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLN
FT A -> SGKAAEANCW (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024057"
FT MUTAGEN 282
FT /note="F->Y: Loss of methyltransferase activity for
FT H4K20me1 peptide."
FT /evidence="ECO:0000269|PubMed:24049080"
FT CONFLICT 53
FT /note="S -> N (in Ref. 3; AAH75709)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="K -> E (in Ref. 2; AAH11214)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="V -> L (in Ref. 1; BAC39834)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="R -> Q (in Ref. 2; BAE31010)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="P -> A (in Ref. 3; AAH75709)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="E -> G (in Ref. 1; BAC38817)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="N -> S (in Ref. 3; AAH75709)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="P -> H (in Ref. 1; BAC38817)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="R -> G (in Ref. 2; BAE31010)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="H -> Y (in Ref. 3; AAH75709)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="A -> T (in Ref. 3; AAH75709)"
FT /evidence="ECO:0000305"
FT HELIX 75..89
FT /evidence="ECO:0007829|PDB:4BUP"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:4BUP"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:4BUP"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:4BUP"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:4BUP"
FT HELIX 173..187
FT /evidence="ECO:0007829|PDB:4BUP"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4BUP"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:4BUP"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:4BUP"
FT STRAND 224..235
FT /evidence="ECO:0007829|PDB:4BUP"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:4BUP"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:4BUP"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:4BUP"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:4BUP"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:4BUP"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:4BUP"
FT STRAND 279..296
FT /evidence="ECO:0007829|PDB:4BUP"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:4BUP"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:4BUP"
FT HELIX 323..328
FT /evidence="ECO:0007829|PDB:4BUP"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:4BUP"
SQ SEQUENCE 883 AA; 98580 MW; 2B24461F582CC5F1 CRC64;
MKWLGDSKNM VVNGRRNGGK LSNDHQQNQS KLQQHSGKDT LKTGRNAVER RSSRCHGNSG
FEGQSRYVPS SGMSAKELCE NDDLATSLVL DPYLGFQTHK MNTSAFPSRS SRHISKADSF
SHNNPVRFRP IKGRQEELKE VIERFKKDEH LEKAFKCLTS GEWARHYFLN KNKMQEKLFK
EHVFIYLRMF ATDSGFEILP CNRYSSEQNG AKIVATKEWK RNDKIELLVG CIAELSEIEE
NMLLRHGEND FSVMYSTRKN CAQLWLGPAA FINHDCRPNC KFVSTGRDTA CVKALRDIEP
GEEISCYYGD GFFGENNEFC ECYTCERRGT GAFKSRVGLP APAPVINSKY GLRETDKRLN
RLKKLGDSSK NSDSQSVSSN TDADTTQEKD NATSNRKSSV GVKKSSKSRA LTRPSMPRVP
AASNSTSPKL VHTNNPRVPK KLRKPAKPLL SKIRLRNHCK RLDQKSASRK LEMGSLVLKE
PKVVLYKNLP IKKEREPEGP AHAAVGSGCL TRHAAREHRQ NHGRGAHSQG DSLPCTYTTR
RSLRTRTGLK ETTDIKLEPS PLDGYKNGIL EPCPDSGQQP TPEVLEELAP ETAHREEASQ
ECPKNDSCLS RKKFRQVKPV KHLAKTEDCS PEHSFPGKDG LPDLPGSHPD QGEPSGTVRV
PVSHTDSAPS PVGCSVVAPD SFTKDSFRTA QSKKKRRVTR YDAQLILENS SGIPKLTLRR
RHDSSSKTND HESDGVNSSK ISIKLSKDHD SDSNLYVAKL SNGVSAGPGS SSTKLKIQLK
RDEESRGPCA EGLHENGVCC SDPLSLLESQ MEVDDYSQYE EDSTDESSSS EGEEEEEDCE
DDFDDDFIPL PPAKRLRLIV GKDSIDIDIS SRRREDQSLR LNA
//
