KT5AA_DANRE
ID KT5AA_DANRE Reviewed; 344 AA.
AC Q071E0; Q0P3X5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=N-lysine methyltransferase KMT5A-A {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9NQR1};
DE AltName: Full=Histone-lysine N-methyltransferase KMT5A-A;
DE EC=2.1.1.361 {ECO:0000250|UniProtKB:Q9NQR1};
DE AltName: Full=Lysine-specific methylase 5A-A {ECO:0000250|UniProtKB:Q9NQR1};
DE AltName: Full=SET domain-containing protein 8-A;
GN Name=kmt5aa {ECO:0000250|UniProtKB:Q9NQR1}; Synonyms=set8a, setd8, setd8a;
GN ORFNames=zgc:153719;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2006) 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 -!- 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}.
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DR EMBL; DQ343297; ABC68593.1; -; mRNA.
DR EMBL; BC122396; AAI22397.1; -; mRNA.
DR RefSeq; NP_001038814.2; NM_001045349.2.
DR AlphaFoldDB; Q071E0; -.
DR SMR; Q071E0; -.
DR BioGRID; 591485; 1.
DR STRING; 7955.ENSDARP00000089529; -.
DR PaxDb; Q071E0; -.
DR GeneID; 751629; -.
DR KEGG; dre:751629; -.
DR CTD; 751629; -.
DR ZFIN; ZDB-GENE-060825-37; kmt5aa.
DR eggNOG; KOG1085; Eukaryota.
DR InParanoid; Q071E0; -.
DR OrthoDB; 1460495at2759; -.
DR PhylomeDB; Q071E0; -.
DR Reactome; R-DRE-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DRE-6804760; Regulation of TP53 Activity through Methylation.
DR PRO; PR:Q071E0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005700; C:polytene chromosome; IBA:GO_Central.
DR GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IBA:GO_Central.
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 GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
DR GO; GO:0034771; P:histone H4-K20 monomethylation; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ZFIN.
DR GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 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; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..344
FT /note="N-lysine methyltransferase KMT5A-A"
FT /id="PRO_0000316999"
FT DOMAIN 208..329
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 143..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 218..220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00904"
FT BINDING 263
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 290..291
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00904"
FT CONFLICT 16
FT /note="D -> E (in Ref. 2; AAI22397)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="V -> A (in Ref. 2; AAI22397)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="P -> R (in Ref. 2; AAI22397)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="S -> P (in Ref. 2; AAI22397)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 39155 MW; 93FE1D36C3AEF976 CRC64;
MFPAVNEIKV QTWRRDQRGE CPRRSAQCRL FSCAHRECAP AARSLENRGP ENRTARPEAT
MSGDVLCNGH SAFHRLLKHS SSRTHEALVV KIIQENKNTP LFCTAPEPRR DSGVNGEFLL
NSAELQDEQT LPLHCIHSAA DITSSKHRKP ARRKVKRSTK RAAESKSPAN RKVTDYFPIR
RSSRKSKSEL KYEEKQHIDT LISNGIEDGM MVRFIEGKGR GVFATQPFQK GQYVVEYHGD
LLQITDAKQR EALYAQDPST GCYMYYFQYL SKTYCVDATK ESDRLGRLIN HSKNGNCQTK
LHAIAGKPHL ILVASRDIQE GEELLYDYGD RSKSSIEAHP WLKH
