KMT5A
entrez
387893
canonical
uniprot
Q9NQR1
canonical
ensembl
ENSG00000183955
resolver
ensp
ENSP00000384629
resolver
genesymbol
KMT5A
resolver
genesymbol
SETD8
resolver
genesymbol_syn
PRSET7
resolver
genesymbol_syn
SET07
resolver
genesymbol_syn
SET8
resolver
genesymbol_syn
SETD8
resolver
hgnc
HGNC:29489
resolver
uniprot
A8K9D0
resolver
uniprot
E3VVS3
resolver
uniprot
Q86W83
resolver
uniprot
Q8TD09
resolver
uniprot_entry
E3VVS3_HUMAN
resolver
uniprot_entry
KMT5A_HUMAN
resolver
uniprot_sec
A8K9D0
resolver
uniprot_sec
Q86W83
resolver
uniprot_sec
Q8TD09
resolver
amino_acid_sequence
MGEGGAAAALVAAAAAAAAAAAAVVAGQRRRRLGRRARCHGPGRAAGGKMSKPCAVEAAAAAVAATAPGPEMVERRGPGRPRTDGENVFTGQSKIYSYMSPNKCSGMRFPLQEENSVTHHEVKCQGKPLAGIYRKREEKRNAGNAVRSAMKSEEQKIKDARKGPLVPFPNQKSEAAEPPKTPPSSCDSTNAAIAKQALKKPIKGKQAPRKKAQGKTQQNRKLTDFYPVRRSSRKSKAELQSEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGDFVVEYHGDLIEITDAKKREALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLGRLINHSKCGNCQTKLHDIDGVPHLILIASRDIAAGEELLYDYGDRSKASIEAHPWLKH
uniprot
proteins
ec_number
2.1.1.-
uniprot
proteins
ec_number
2.1.1.361
uniprot
proteins
function
FUNCTION: Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins (PubMed:12086618, PubMed:12121615, PubMed:15964846, PubMed:17707234, PubMed:27338793). Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1) (PubMed:12086618, PubMed:12121615, PubMed:15200950, PubMed:15933069, PubMed:15933070, PubMed:15964846, PubMed:16517599, PubMed:27338793). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression (PubMed:12086618, PubMed:12121615, PubMed:15200950, PubMed:15933069, PubMed:15933070, PubMed:15964846, PubMed:16517599). Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes (PubMed:12086618, PubMed:12121615, PubMed:15200950, PubMed:15933069, PubMed:15933070, PubMed:15964846, PubMed:16517599). Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis (PubMed:12086618, PubMed:12121615, PubMed:15200950, PubMed:15933069, PubMed:15933070, PubMed:15964846, PubMed:16517599). Involved in chromosome condensation and proper cytokinesis (PubMed:12086618, PubMed:12121615, PubMed:15200950, PubMed:15933069, PubMed:15933070, PubMed:15964846, PubMed:16517599). Nucleosomes are preferred as substrate compared to free histones (PubMed:12086618, PubMed:12121615, PubMed:15200950, PubMed:15933069, PubMed:15933070, PubMed:15964846, PubMed:16517599). Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes (PubMed:17707234). Plays a negative role in TGF-beta response regulation and a positive role in cell migration (PubMed:23478445). {ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:12121615, ECO:0000269|PubMed:15200950, ECO:0000269|PubMed:15933069, ECO:0000269|PubMed:15933070, ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:16517599, ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:27338793}.
uniprot
proteins
mass_dalton
42890
uniprot
proteins
mutagenesis
MUTAGEN 162; /note="K->Q: Does not affect the interaction with SIRT2. Increases the number of mitotic foci formation. Does not affect methyltransferase activity."; /evidence="ECO:0000269|PubMed:23468428"; MUTAGEN 162; /note="K->R: Increases the interaction with SIRT2. Reduces the number of mitotic foci formation. Does not affect methyltransferase activity."; /evidence="ECO:0000269|PubMed:23468428"; MUTAGEN 286; /note="Y->A,F: Strongly reduces affinity for histone H4 and abolishes methyltransferase activity."; /evidence="ECO:0000269|PubMed:15933070"; MUTAGEN 300; /note="E->A: Strongly reduces affinity for histone H4."; /evidence="ECO:0000269|PubMed:15933070"; MUTAGEN 311; /note="C->A: Strongly reduces affinity for histone H4."; /evidence="ECO:0000269|PubMed:15933070"; MUTAGEN 336; /note="R->G: Abolishes methyltransferase activity."; /evidence="ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:23478445"; MUTAGEN 340; /note="H->A: Strongly decreases methyltransferase activity."; /evidence="ECO:0000269|PubMed:12121615"; MUTAGEN 375; /note="Y->A: Strongly reduces affinity for histone H4 and methyltransferase activity."; /evidence="ECO:0000269|PubMed:15933070"; MUTAGEN 375; /note="Y->F: Alters methyltransferase activity, so that both monomethylation and dimethylation take place."; /evidence="ECO:0000269|PubMed:15933070"; MUTAGEN 379; /note="D->A,N: Abolishes histone H4 binding and methyltransferase activity."; /evidence="ECO:0000269|PubMed:15933070, ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:23478445"; MUTAGEN 385..393; /note="Missing: Abolishes methyltransferase activity."; /evidence="ECO:0000269|PubMed:12121615"; MUTAGEN 388; /note="H->A,E: Strongly reduces affinity for histone H4."; /evidence="ECO:0000269|PubMed:15933070"; MUTAGEN 388; /note="H->F: Increases affinity for histone H4."; /evidence="ECO:0000269|PubMed:15933070
uniprot
proteins
post_translational_modification
PTM: Acetylated at Lys-162; does not affect methyltransferase activity. Deacetylated at Lys-162 possibly by SIRT2; does not change methyltransferase activity. {ECO:0000269|PubMed:23468428}.; PTM: Ubiquitinated and degraded by the DCX(DTL) complex. {ECO:0000305|PubMed:23478445}.
uniprot
proteins
protein_family
Class V-like SAM-binding methyltransferase superfamily
uniprot
proteins
protein_family
Histone-lysine methyltransferase family
uniprot
proteins
protein_family
PR/SET subfamily
uniprot
proteins
pubmed
12086618
uniprot
proteins
pubmed
12121615
uniprot
proteins
pubmed
12208845
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15200950
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15933069
uniprot
proteins
pubmed
15933070
uniprot
proteins
pubmed
15964846
uniprot
proteins
pubmed
16517599
uniprot
proteins
pubmed
17707234
uniprot
proteins
pubmed
18408754
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20870725
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23468428
uniprot
proteins
pubmed
23478445
uniprot
proteins
pubmed
27338793
uniprot
proteins
sequence_length
393
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12086618}. Chromosome {ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:12208845, ECO:0000269|PubMed:23468428}. Note=Specifically localizes to mitotic chromosomes (PubMed:12208845). Colocalized with SIRT2 at mitotic foci (PubMed:23468428). Associates with chromosomes during mitosis; association is increased in a H(2)O(2)-induced oxidative stress-dependent manner (PubMed:23468428). Associates with silent chromatin on euchromatic arms (PubMed:12086618). Not associated with constitutive heterochromatin (PubMed:12086618). {ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:12208845, ECO:0000269|PubMed:23468428}.
uniprot
proteins