KT5AB_XENLA
ID KT5AB_XENLA Reviewed; 336 AA.
AC Q498E6; Q8JJ44;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=N-lysine methyltransferase KMT5A-B;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9NQR1};
DE AltName: Full=Histone-lysine N-methyltransferase KMT5A-B;
DE EC=2.1.1.361 {ECO:0000250|UniProtKB:Q9NQR1};
DE AltName: Full=Lysine-specific methylase 5A-B {ECO:0000250|UniProtKB:Q9NQR1};
DE AltName: Full=Mitotic phosphoprotein 36;
DE AltName: Full=SET domain-containing protein 8-B;
GN Name=kmt5a-b {ECO:0000250|UniProtKB:Q9NQR1}; Synonyms=mp36, setd8-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 [MRNA] (ISOFORM 2), AND PHOSPHORYLATION.
RX PubMed=11818060; DOI=10.1016/s0960-9822(01)00662-5;
RA Georgi A.B., Stukenberg P.T., Kirschner M.W.;
RT "Timing of events in mitosis.";
RL Curr. Biol. 12:105-114(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein-lysine N-methyltransferase that monomethylates both
CC histones and non-histone proteins. Specifically monomethylates 'Lys-20'
CC of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and
CC represents a specific tag for epigenetic transcriptional repression.
CC Mainly functions in euchromatin regions, thereby playing a central role
CC in the silencing of euchromatic genes. Required for cell proliferation,
CC probably by contributing to the maintenance of proper higher-order
CC structure of DNA during mitosis. Involved in chromosome condensation
CC and proper cytokinesis. {ECO:0000250|UniProtKB:Q9NQR1}.
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:Q9NQR1, ECO:0000255|PROSITE-
CC ProRule:PRU00904};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000250|UniProtKB:Q9NQR1};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NQR1}.
CC Chromosome {ECO:0000250|UniProtKB:Q9NQR1}. Note=Specifically localizes
CC to mitotic chromosomes. Associates with silent chromatin on euchromatic
CC arms (By similarity). {ECO:0000250|UniProtKB:Q9NQR1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q498E6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q498E6-2; Sequence=VSP_030852;
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000269|PubMed:11818060}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. PR/SET subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00904}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM33245.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF419150; AAM33245.1; ALT_FRAME; mRNA.
DR EMBL; BC100246; AAI00247.1; -; mRNA.
DR RefSeq; NP_001082246.1; NM_001088777.1.
DR AlphaFoldDB; Q498E6; -.
DR SMR; Q498E6; -.
DR GeneID; 398318; -.
DR KEGG; xla:398318; -.
DR CTD; 398318; -.
DR Xenbase; XB-GENE-17338855; kmt5a.L.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 398318; Expressed in gastrula 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:0018024; F:histone-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR016858; Hist_H4-K20_MeTrfase.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF027717; Histone_H4-K20_mtfrase; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51571; SAM_MT43_PR_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Chromatin regulator;
KW Chromosome; Methyltransferase; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..336
FT /note="N-lysine methyltransferase KMT5A-B"
FT /id="PRO_0000317001"
FT DOMAIN 200..321
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210..212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00904"
FT BINDING 255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190,
FT ECO:0000255|PROSITE-ProRule:PRU00904"
FT BINDING 282..283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00904"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11818060"
FT /id="VSP_030852"
FT CONFLICT 69
FT /note="A -> V (in Ref. 1; AAM33245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 38291 MW; 91D6AAC31DC97E6C CRC64;
MGRGKKMSKP GDGRSGDVPE TCRTGGTNEN HPKMNGEVVH LGQPKIYSYM SPTKSPSGRP
PLQEENSVAH HESKNLGKPT TETRKKAEVE KKRISSATEL SVKSSKQRET ECNSIGEYFQ
TKQELTDVQR NTALTPVDKL QSQKMVKNKS QRRKAQRKKS PNRKLTDYYP VRRSCRKSKT
ELESEEKMRI DELIQTGKED GMKMDMIIGK GRGVIATRDF QRGEFVVEYH GDLIEITDAK
RREASYAQDS ATGCYMYYFQ YLNKTYCIDA TRETGRLGRL INHSKSGNCH TKLHNISNVP
HLILVASRDI LVGEELLYDY GDRRKSSIEA HPWLKN
