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Database: UniProt/SWISS-PROT
Entry: KT5AA_XENLA
LinkDB: KT5AA_XENLA
Original site: KT5AA_XENLA 
ID   KT5AA_XENLA             Reviewed;         335 AA.
AC   Q08AY6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   23-MAY-2018, entry version 58.
DE   RecName: Full=N-lysine methyltransferase KMT5A-A {ECO:0000305};
DE            EC=2.1.1.-;
DE   AltName: Full=Histone-lysine N-methyltransferase KMT5A-A;
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine-specific methylase 5A-A {ECO:0000250|UniProtKB:Q9NQR1};
DE   AltName: Full=SET domain-containing protein 8-A;
GN   Name=kmt5a-a {ECO:0000250|UniProtKB:Q9NQR1}; Synonyms=setd8-a;
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 [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-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 (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {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; BC124952; AAI24953.1; -; mRNA.
DR   RefSeq; NP_001121300.1; NM_001127828.1.
DR   UniGene; Xl.61899; -.
DR   ProteinModelPortal; Q08AY6; -.
DR   SMR; Q08AY6; -.
DR   PRIDE; Q08AY6; -.
DR   GeneID; 100158384; -.
DR   KEGG; xla:100158384; -.
DR   CTD; 100158384; -.
DR   Xenbase; XB-GENE-865841; kmt5a.
DR   HOVERGEN; HBG067546; -.
DR   KO; K11428; -.
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:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; 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   Methyltransferase; Mitosis; Nucleus; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN         1    335       N-lysine methyltransferase KMT5A-A.
FT                                /FTId=PRO_0000317000.
FT   DOMAIN      199    320       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      209    211       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   REGION      281    282       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   BINDING     254    254       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000255|PROSITE-ProRule:PRU00904}.
SQ   SEQUENCE   335 AA;  38092 MW;  4300EFC00C1210A9 CRC64;
     MGRGKKMSKP GDGRSGDVSD TGRNGGTNEN HPKTNGEVVH CGQAKIYSYM SPTKSPSARP
     PLQEENSVTH HESKCLGKPS TETRKKAEVE KKKILSTELS VKPSEQRETE CNSIGEFLEP
     KLELNDVQRN LALPPEDKLQ SQKMVKNKPL RKKTQRQKSP NRKLTDYYPV RRSSRKNKTE
     IESEEKKRID ELIQTGKEEG IKMHMITGKG RGVIATRDFQ RGEFVVEYHG DLIEITDAKR
     REASYAQDSA TGCYMYYFQY LNTSYCIDAT RETGRLGRLI NHSKSGNCHT KLHNINNVPH
     LILVASRDIN VGEELLYDYG DRRKSSIDAH PWLKN
//
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