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
RC   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   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.
DR   Genevisible; Q3U8K7; MM.
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
//