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Database: UniProt/SWISS-PROT
Entry: KMT5A_XENTR
LinkDB: KMT5A_XENTR
Original site: KMT5A_XENTR 
ID   KMT5A_XENTR             Reviewed;         336 AA.
AC   Q0V9E9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   05-DEC-2018, entry version 77.
DE   RecName: Full=N-lysine methyltransferase KMT5A {ECO:0000305};
DE            EC=2.1.1.-;
DE   AltName: Full=Histone-lysine N-methyltransferase KMT5A;
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine-specific methylase 5A {ECO:0000250|UniProtKB:Q9NQR1};
DE   AltName: Full=SET domain-containing protein 8;
GN   Name=kmt5a {ECO:0000250|UniProtKB:Q9NQR1}; Synonyms=setd8;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6; TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) 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. Nucleosomes are preferred as
CC       substrate compared to free histones. Mediates monomethylation of
CC       p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes.
CC       Plays a negative role in TGF-beta response regulation and a
CC       positive role in cell migration (By similarity). {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   -!- 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}.
DR   EMBL; BC121601; AAI21602.1; -; mRNA.
DR   RefSeq; NP_001072815.1; NM_001079347.1.
DR   UniGene; Str.11037; -.
DR   ProteinModelPortal; Q0V9E9; -.
DR   SMR; Q0V9E9; -.
DR   STRING; 8364.ENSXETP00000012803; -.
DR   PaxDb; Q0V9E9; -.
DR   PRIDE; Q0V9E9; -.
DR   Ensembl; ENSXETT00000012803; ENSXETP00000012803; ENSXETG00000005820.
DR   GeneID; 780276; -.
DR   KEGG; xtr:780276; -.
DR   CTD; 387893; -.
DR   Xenbase; XB-GENE-489177; kmt5a.
DR   eggNOG; KOG1085; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000163293; -.
DR   HOGENOM; HOG000020818; -.
DR   HOVERGEN; HBG067546; -.
DR   InParanoid; Q0V9E9; -.
DR   KO; K11428; -.
DR   OMA; NHKLTDF; -.
DR   OrthoDB; EOG091G0UBI; -.
DR   TreeFam; TF335181; -.
DR   Reactome; R-XTR-2299718; Condensation of Prophase Chromosomes.
DR   Reactome; R-XTR-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-XTR-6804760; Regulation of TP53 Activity through Methylation.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
DR   Bgee; ENSXETG00000005820; Expressed in 18 organ(s), highest expression level in female gonad.
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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Chromatin regulator; Chromosome;
KW   Complete proteome; Methyltransferase; Mitosis; Nucleus;
KW   Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    336       N-lysine methyltransferase KMT5A.
FT                                /FTId=PRO_0000317002.
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}.
SQ   SEQUENCE   336 AA;  38237 MW;  422D7B38C168DCA1 CRC64;
     MGRGKKMSKP GDGRSGDVPD TGRTGGTNEN HPKINGEVAH LGQPKIYSFM SPTKSPSARP
     PLQEENSVAH HESKCPGKPL TETRKKAEVE KKRISSGTEL SVKPSEQRET ECNSIGEFLD
     PKQEQTDVRR NIALPPADKL NHQKMVKDKP LRRKAQRKKS PNRKLTDYYP VRRSCRKSKT
     ELESEEKKRI DELIQTGKEE GMKMDMITGK GRGVIATRDF QRGEFVVEYH GDLIEITDAK
     RREATYAQDS NTGCYMYYFQ YLNKTYCIDA TRETGRLGRL INHSKSGNCH TKLHNINNVP
     HLILVASRDI NVGEELLYDY GDRRKSSLEA HPWLKN
//
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