GenomeNet

Database: UniProt/SWISS-PROT
Entry: KMT5A_BOVIN
LinkDB: KMT5A_BOVIN
Original site: KMT5A_BOVIN 
ID   KMT5A_BOVIN             Reviewed;         352 AA.
AC   Q2YDJ8;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   28-MAR-2018, entry version 94.
DE   RecName: Full=N-lysine methyltransferase KMT5A {ECO:0000305};
DE            EC=2.1.1.-;
DE   AltName: Full=H4-K20-HMTase KMT5A;
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=PR/SET domain-containing protein 07;
DE            Short=PR-Set7;
DE            Short=PR/SET07;
DE   AltName: Full=SET domain-containing protein 8;
GN   Name=KMT5A {ECO:0000250|UniProtKB:Q9NQR1}; Synonyms=SETD8;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-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. 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: 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   -!- SUBUNIT: Interacts with L3MBTL1. Interacts with SIRT2
CC       (phosphorylated form); the interaction is direct, stimulates
CC       KMT5A-mediated methyltransferase activity at histone H4 'Lys-20'
CC       (H4K20me1) and is increased in a H(2)O(2)-induced oxidative
CC       stress-dependent manner (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}. Note=Specifically localizes to mitotic chromosomes.
CC       Associates with silent chromatin on euchromatic arms. Colocalized
CC       with SIRT2 at mitotic foci. Associates with chromosomes during
CC       mitosis; association is increased in a H(2)O(2)-induced oxidative
CC       stress-dependent manner. Not associated with constitutive
CC       heterochromatin (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: Although the SET domain contains the active site of
CC       enzymatic activity, both sequences upstream and downstream of the
CC       SET domain are required for methyltransferase activity.
CC       {ECO:0000250}.
CC   -!- PTM: Acetylated at Lys-131; does not change methyltransferase
CC       activity. Deacetylated at Lys-131 by SIRT2; does not change
CC       methyltransferase activity (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitinated and degraded by the DCX(DTL) complex.
CC       {ECO:0000305}.
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; BC110189; AAI10190.1; -; mRNA.
DR   RefSeq; NP_001039795.1; NM_001046330.1.
DR   UniGene; Bt.65045; -.
DR   ProteinModelPortal; Q2YDJ8; -.
DR   SMR; Q2YDJ8; -.
DR   STRING; 9913.ENSBTAP00000055591; -.
DR   PaxDb; Q2YDJ8; -.
DR   PRIDE; Q2YDJ8; -.
DR   GeneID; 532622; -.
DR   KEGG; bta:532622; -.
DR   CTD; 387893; -.
DR   eggNOG; KOG1085; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000020818; -.
DR   HOVERGEN; HBG067546; -.
DR   InParanoid; Q2YDJ8; -.
DR   KO; K11428; -.
DR   Proteomes; UP000009136; Unplaced.
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:0002039; F:p53 binding; ISS:UniProtKB.
DR   GO; GO:0016279; F:protein-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:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR   GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
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   Acetylation; Cell cycle; Cell division; Chromatin regulator;
KW   Chromosome; Complete proteome; Methyltransferase; Mitosis; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation.
FT   CHAIN         1    352       N-lysine methyltransferase KMT5A.
FT                                /FTId=PRO_0000228688.
FT   DOMAIN      216    337       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      226    228       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   REGION      298    299       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   COMPBIAS     15     26       Poly-Ala.
FT   BINDING     271    271       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000255|PROSITE-ProRule:PRU00904}.
FT   MOD_RES      59     59       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NQR1}.
FT   MOD_RES     131    131       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9NQR1}.
FT   MOD_RES     140    140       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9NQR1}.
SQ   SEQUENCE   352 AA;  39277 MW;  98BBD07941AAE9BE CRC64;
     MARGRKMSKP RAVEAAAAAA AVAATAPGPE MVERRGPGRP RTNGENVFTG QSKIYTYMSP
     NKCSGMRSPL QEENSVAQYE VKCQGKPLAG IYRKRDEKRN SGNAIRSSMK AEEQKIKDAR
     RGPLAPFPNQ KSEAAEPPKT PTSSCDTPNA AAAKQGLKKP VRGKQAPRKK AQGKTQQNRK
     LTDFYPVRRS SRKSKAELQS EERKRIDELI ESGKEEGMKI DLIDGKGRGV IATKQFSRGE
     FVVEYHGDLI EITDAKKREA LYAQDPSTGC YMYYFQYLSK TYCVDATRET NRLGRLINHS
     KCGNCQTKLH DIDGVPHLIL IASRDIEAGE ELLYDYGDRS RASIEAYPWL KH
//
DBGET integrated database retrieval system