KT5BB_XENLA
ID KT5BB_XENLA Reviewed; 785 AA.
AC Q5RJX8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Histone-lysine N-methyltransferase KMT5B-B {ECO:0000305};
DE AltName: Full=Lysine-specific methyltransferase 5B-B {ECO:0000250|UniProtKB:Q4FZB7};
DE AltName: Full=Suppressor of variegation 4-20 homolog 1-B;
DE Short=Su(var)4-20 homolog 1-B;
DE Short=Suv4-20h1-B;
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-b {ECO:0000250|UniProtKB:Q4FZB7}; Synonyms=suv420h1-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2004) 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 -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}.
CC Note=Associated with pericentric heterochromatin. {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; BC086459; AAH86459.1; -; mRNA.
DR RefSeq; NP_001088653.1; NM_001095184.1.
DR AlphaFoldDB; Q5RJX8; -.
DR SMR; Q5RJX8; -.
DR DNASU; 495826; -.
DR GeneID; 495826; -.
DR KEGG; xla:495826; -.
DR CTD; 495826; -.
DR Xenbase; XB-GENE-6253211; kmt5b.L.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 495826; Expressed in lung and 19 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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: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; Isopeptide bond; Metal-binding;
KW Methyltransferase; Myogenesis; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Zinc.
FT CHAIN 1..785
FT /note="Histone-lysine N-methyltransferase KMT5B-B"
FT /id="PRO_0000281792"
FT DOMAIN 99..214
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 268..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..748
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 109..112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 178..179
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
FT CROSSLNK 458
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4FZB7"
SQ SEQUENCE 785 AA; 89547 MW; 44C18929602CC834 CRC64;
MSAKELCEND DLATSLVLDP YLGFQTHKMN TRFRPIKGRQ EELKEVIENF KKNEQLEKTF
KNLVAGDWAR HYFLHKNKMQ ETHFKAHVFI YLRMFATSSG FEILPCCRYS SERNGAKIVA
TKDWKRNDKI ELLVGCIAEL SEAEENMLLR HGENDFSVMY STRKNCAQLW LGPAAFINHD
CRPNCKFVST GRDTACVKAL RDIEPGEEIS CYYGDGFFGE NNEFCECYTC ERRATGAFKS
RVGLNEPGPV INSKYGLRET DKRLNRLKKL GDNGKNSDSQ SVSSNTDADT SQEKNTANRK
SNGLRKKSKS RTLRRQSMSR IPISSSSTSS KLPHINNSRV PKRLRKTAKP LHSKLKIRCH
RKKVEQKKTS KKLDVSNLVL KEPKVVLYKN LAIKKDRESQ GAVQVTETTG CLTRHAAREY
KLNSFKGAYA HGDTSPCTYI TRSSLRTRFN SKDMSEAKLQ PNSVDGYRSS HGTVIQLDTG
DPLFQSTRKN ELLQETSRQS MRFQRNNFNT SRRNSRQNRY ITQASKVEDS VSIYNSSSID
NSLPDLGNSH CDLGEGNALI HTSPDYKNIK SSTDEYPLVT SEITKSKKNI RTVKNKKRRR
ITRYDAQLIL ENSTGIPKLT LRRRHDSNSS KTNEKENEGM GSSKISIKLS KDHEKDKNSL
YVAKLNNGFN SGSGSTSTKL KIQLKRDEEN RMAFPNENGM YCSDTLSLLG TRMEVDGYDH
YEEESVGESS TEEEEEEEDE FDDEFEDDFI PLPPAKRLRL IVGKDSIDID ISSRRREDQS
LRLNA
