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Database: UniProt
Entry: Q498E6
LinkDB: Q498E6
Original site: Q498E6 
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   16-JAN-2019, entry version 60.
DE   RecName: Full=N-lysine methyltransferase KMT5A-B;
DE            EC=2.1.1.-;
DE   AltName: Full=Histone-lysine N-methyltransferase KMT5A-B;
DE            EC=2.1.1.43;
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;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   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
CC       both histones and non-histone proteins. Specifically
CC       monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is
CC       enriched during mitosis and represents a specific tag for
CC       epigenetic transcriptional repression. Mainly functions in
CC       euchromatin regions, thereby playing a central role in the
CC       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
CC       condensation and proper cytokinesis (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00904};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}. Note=Specifically localizes to mitotic chromosomes.
CC       Associates with silent chromatin on euchromatic arms (By
CC       similarity). {ECO:0000250}.
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
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. PR/SET subfamily. {ECO:0000255|PROSITE-ProRule:PRU00904}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM33245.1; Type=Frameshift; Positions=10, 137, 155; Evidence={ECO:0000305};
DR   EMBL; AF419150; AAM33245.1; ALT_FRAME; mRNA.
DR   EMBL; BC100246; AAI00247.1; -; mRNA.
DR   RefSeq; NP_001082246.1; NM_001088777.1.
DR   UniGene; Xl.2518; -.
DR   ProteinModelPortal; Q498E6; -.
DR   SMR; Q498E6; -.
DR   PRIDE; Q498E6; -.
DR   GeneID; 398318; -.
DR   KEGG; xla:398318; -.
DR   CTD; 398318; -.
DR   Xenbase; XB-GENE-17338855; kmt5a.
DR   HOVERGEN; HBG067546; -.
DR   KO; K11428; -.
DR   OrthoDB; 1460495at2759; -.
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   InterPro; IPR016858; Hist_H4-K20_MeTrfase.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF027717; Histone_H4-K20_mtfrase; 1.
DR   SMART; SM00317; SET; 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   Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    336       N-lysine methyltransferase KMT5A-B.
FT                                /FTId=PRO_0000317001.
FT   DOMAIN      200    321       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      210    212       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   REGION      282    283       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   BINDING     255    255       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   VAR_SEQ       1     49       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11818060}.
FT                                /FTId=VSP_030852.
FT   CONFLICT     69     69       A -> V (in Ref. 1; AAM33245).
FT                                {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
//
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