KMT5B_BOVIN
ID KMT5B_BOVIN Reviewed; 393 AA.
AC Q29RP8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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:0000250|UniProtKB:Q4FZB7};
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:0000250|UniProtKB:Q4FZB7}; Synonyms=SUV420H1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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. In vitro also methylates
CC unmodified 'Lys-20' (H4K20me0) of histone H4 and nucleosomes (By
CC similarity). H4 'Lys-20' trimethylation represents a specific tag for
CC epigenetic transcriptional repression. Mainly functions in pericentric
CC heterochromatin regions, thereby playing a central role in the
CC establishment of constitutive heterochromatin in these regions. KMT5B
CC is targeted to histone H3 via its interaction with RB1 family proteins
CC (RB1, RBL1 and RBL2) (By similarity). Plays a role in myogenesis by
CC regulating the expression of target genes, such as EID3. 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q3U8K7, ECO:0000250|UniProtKB:Q4FZB7}.
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:0000250|UniProtKB:Q4FZB7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60349;
CC Evidence={ECO:0000250|UniProtKB:Q4FZB7};
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:0000250|UniProtKB:Q4FZB7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61993;
CC Evidence={ECO:0000250|UniProtKB:Q4FZB7};
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 -!- SUBUNIT: Homodimer (By similarity). Interacts with HP1 proteins CBX1,
CC CBX3 and CBX5. Interacts with RB1 family proteins RB1, RBL1 and RBL2
CC (By similarity). Interacts (via C-terminus) with FRG1 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q4FZB7}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}.
CC Note=Associated with pericentric heterochromatin. CBX1 and CBX5 are
CC required for the localization to pericentric heterochromatin (By
CC similarity). {ECO:0000250}.
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}.
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DR EMBL; BC114079; AAI14080.1; -; mRNA.
DR RefSeq; NP_001070019.1; NM_001076551.2.
DR AlphaFoldDB; Q29RP8; -.
DR SMR; Q29RP8; -.
DR STRING; 9913.ENSBTAP00000051412; -.
DR PaxDb; Q29RP8; -.
DR PRIDE; Q29RP8; -.
DR GeneID; 767828; -.
DR KEGG; bta:767828; -.
DR CTD; 51111; -.
DR eggNOG; KOG2589; Eukaryota.
DR InParanoid; Q29RP8; -.
DR OrthoDB; 236983at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); ISS:UniProtKB.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISS:UniProtKB.
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; IBA:GO_Central.
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; ISS:UniProtKB.
DR CDD; cd19184; SET_KMT5B; 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; 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; 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 2: Evidence at transcript level;
KW Chromatin regulator; Chromosome; Metal-binding; Methyltransferase;
KW Myogenesis; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Zinc.
FT CHAIN 1..393
FT /note="Histone-lysine N-methyltransferase KMT5B"
FT /id="PRO_0000281786"
FT DOMAIN 193..308
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 13..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 203..206
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 210
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 257
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 272..273
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 320
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
SQ SEQUENCE 393 AA; 44552 MW; B793EC4D45BF608C CRC64;
MKWLGESKNM VVNGRRHGGK LSNDHQQNQS KLQHSGKDNV KAGRNAGERR SSRCNGNSGF
EGQSRYVPSS GMSAKELCEN DDLATSLVLD PYLGFQTHKM NTSAFPPRSS RHFSKSDSFS
HNNPVRFRPI KGRQEELKEV IERFKKDEHL EKAFKCLTSG EWARHYFLNK NKMQEKLFKE
HVFIYLRMFA TDSGFEILPC NRYSSEQNGA KIVATKEWKR NDKIELLVGC IAELSEIEEN
MLLRHGENDF SVMYSTRKNC AQLWLGPAAF INHDCRPNCK FVSTGRDTAC VKALRDIEPG
EEISCYYGDG FFGENNEFCE CYTCERRGTG AFKSRVGLPA PAPVINSKYG LRETDKRLNR
LKKLGDSSKN SDSQSVSSNT DADTTQGRND ASK
