SUV39H1
entrez
6839
canonical
uniprot
O43463
canonical
ensembl
ENSG00000101945
resolver
ensp
ENSP00000337976
resolver
ensp
ENSP00000365877
resolver
genesymbol
SUV39H1
resolver
genesymbol_syn
KMT1A
resolver
genesymbol_syn
SUV39H
resolver
hgnc
HGNC:11479
resolver
uniprot
B2R6E8
resolver
uniprot
B4DST0
resolver
uniprot
Q53G60
resolver
uniprot
Q6FHK6
resolver
uniprot_entry
SUV91_HUMAN
resolver
uniprot_sec
B2R6E8
resolver
uniprot_sec
B4DST0
resolver
uniprot_sec
Q53G60
resolver
uniprot_sec
Q6FHK6
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by S-adenosyl-L-homocysteine. Negatively regulated by CCAR2. {ECO:0000269|PubMed:16519522, ECO:0000269|PubMed:19218236}.
uniprot
proteins
amino_acid_sequence
MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSESTWEPRQNLKCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQKAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAFVYINEYRVGEGITLNQVAVGCECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKGIRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTESCRKYLF
uniprot
proteins
ec_number
2.1.1.-
uniprot
proteins
function
FUNCTION: Histone methyltransferase that specifically mediates trimethylation of 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' (H3K9me1) as substrate (PubMed:10949293, PubMed:11242053, PubMed:18004385, PubMed:40440427). Also weakly methylates histone H1 (in vitro) (PubMed:10949293). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones (PubMed:10949293, PubMed:11242053, PubMed:18004385). Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions (By similarity). H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats (PubMed:41094145). SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length (PubMed:11484059, PubMed:14765126, PubMed:16449642, PubMed:16818776, PubMed:16858404, PubMed:30111536). Involved in the maintenance of H3K9me3 mark following DNA replication, when histone marks are diluted: HP1 recognizes the preexisting H3K9me3 mark and serves as a platform to recruit SUV39H1 to modify the adjacent newly incorporated histones (PubMed:10949293, PubMed:11242053, PubMed:40440427). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes (PubMed:18485871). The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus (PubMed:18485871). Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation (By similarity). {ECO:0000250|UniProtKB:O54864, ECO:0000269|PubMed:10949293, ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:11484059, ECO:0000269|PubMed:14765126, ECO:0000269|PubMed:16449642, ECO:0000269|PubMed:16818776, ECO:0000269|PubMed:16858404, ECO:0000269|PubMed:18004385, ECO:0000269|PubMed:18485871, ECO:0000269|PubMed:30111536, ECO:0000269|PubMed:40440427, ECO:0000269|PubMed:41094145}.; FUNCTION: (Microbial infection) Plays a role in defense against mycobacterial infections. Methylates M.tuberculosis HupB on 'Lys-140', probably methylates HupB of M.bovis also. Methylation has an inhibitory effect on mycobacterial growth in the host. Macrophages expressing about 60% SUV39H1 are slightly more susceptible to M.bovis or M.tuberculosis infection. Chaetocin (an inhibitor of this enzyme) increases macrophage survival of M.tuberculosis. This protein inhibits biofilm formation by M.tuberculosis via 'Lys-140' trimethylation. {ECO:0000269|PubMed:29170282}.
uniprot
proteins
mass_dalton
47907
uniprot
proteins
mutagenesis
MUTAGEN 43..45; /note="FEV->AEA: Decreased localization to pericentromeric heterochromatin."; /evidence="ECO:0000269|PubMed:41094145"; MUTAGEN 64..67; /note="WRGY->ARGA: Decreased localization to pericentromeric heterochromatin."; /evidence="ECO:0000269|PubMed:41094145"; MUTAGEN 64; /note="W->A: Abolishes methyltransferase activity."; /evidence="ECO:0000269|PubMed:16519522"; MUTAGEN 67; /note="Y->A: Abolishes methyltransferase activity."; /evidence="ECO:0000269|PubMed:16519522"; MUTAGEN 138; /note="K->R: Abolished ubiquitination by the ECS(ASB7) complex."; /evidence="ECO:0000269|PubMed:40440427"; MUTAGEN 224; /note="S->A: Does not affect phosphorylation by CDK2."; /evidence="ECO:0000269|PubMed:24728993"; MUTAGEN 266; /note="K->A: Loss of SIRT1-mediated up-regulation of enzymatic activity."; /evidence="ECO:0000269|PubMed:18004385"; MUTAGEN 266; /note="K->Q: Significant loss of enzymatic activity."; /evidence="ECO:0000269|PubMed:18004385"; MUTAGEN 320; /note="H->R: Strongly increases methylation of histone H3."; /evidence="ECO:0000269|PubMed:10949293"; MUTAGEN 324; /note="H->L,K: Abolishes methylation of histone H3."; /evidence="ECO:0000269|PubMed:10949293"; MUTAGEN 326; /note="C->A: Abolishes methylation of histone H3."; /evidence="ECO:0000269|PubMed:10949293"; MUTAGEN 391; /note="S->A: Abolished phosphorylation by CDK2, promoting localization to heterochromatin. Does not affect its interaction with ASB7."; /evidence="ECO:0000269|PubMed:24728993, ECO:0000269|PubMed:40440427"; MUTAGEN 391; /note="S->E,D: Mimics phosphorylation; impaired localization to heterochromatin. Does not affect its interaction with ASB7."; /evidence="ECO:0000269|PubMed:24728993, ECO:0000269|PubMed:40440427
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine residues, and to a lesser degree, on threonine residues (PubMed:10671371). The phosphorylated form is stabilized by SBF1 and is less active in its transcriptional repressor function (PubMed:10671371). Phosphorylated at Ser-391 by CDK2 during S-M phases, impairing localization to heterochromatin (PubMed:24728993). {ECO:0000269|PubMed:10671371, ECO:0000269|PubMed:24728993}.; PTM: Ubiquitinated by the DCX(DCAF13) E3 ubiquitin ligase complex, leading to its degradation (PubMed:30111536). Ubiquitinated at Lys-138 by the ECS(ASB7) complex, leading to its degradation (PubMed:40440427). {ECO:0000269|PubMed:30111536, ECO:0000269|PubMed:40440427}.; PTM: Acetylated at Lys-266, leading to inhibition of enzyme activity. SIRT1-mediated deacetylation relieves this inhibition. {ECO:0000269|PubMed:18004385}.; PTM: (Microbial infection) A higher molecular weight form is also seen in M.bovis infected cells. {ECO:0000269|PubMed:29170282}.
uniprot
proteins
protein_family
Class V-like SAM-binding methyltransferase superfamily
uniprot
proteins
protein_family
Histone-lysine methyltransferase family
uniprot
proteins
protein_family
Suvar3-9 subfamily
uniprot
proteins
pubmed
10202156
uniprot
proteins
pubmed
10671371
uniprot
proteins
pubmed
10848615
uniprot
proteins
pubmed
10949293
uniprot
proteins
pubmed
11242053
uniprot
proteins
pubmed
11484059
uniprot
proteins
pubmed
12101246
uniprot
proteins
pubmed
12711603
uniprot
proteins
pubmed
12789259
uniprot
proteins
pubmed
12917624
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14765126
uniprot
proteins
pubmed
15107829
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16103223
uniprot
proteins
pubmed
16409643
uniprot
proteins
pubmed
16449642
uniprot
proteins
pubmed
16519522
uniprot
proteins
pubmed
16652147
uniprot
proteins
pubmed
16688220
uniprot
proteins
pubmed
16818776
uniprot
proteins
pubmed
16858404
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18004385
uniprot
proteins
pubmed
18485871
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19218236
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23695662
uniprot
proteins
pubmed
24728993
uniprot
proteins
pubmed
29170282
uniprot
proteins
pubmed
30111536
uniprot
proteins
pubmed
40440427
uniprot
proteins
pubmed
41094145
uniprot
proteins
sequence_length
412
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10671371, ECO:0000269|PubMed:18004385, ECO:0000269|PubMed:29170282, ECO:0000269|PubMed:30111536}. Chromosome {ECO:0000269|PubMed:10671371, ECO:0000269|PubMed:18004385, ECO:0000269|PubMed:18485871, ECO:0000269|PubMed:24728993, ECO:0000269|PubMed:41094145}. Nucleus lamina {ECO:0000269|PubMed:23695662}. Nucleus, nucleoplasm {ECO:0000269|PubMed:23695662}. Chromosome, centromere {ECO:0000269|PubMed:10671371}. Note=Associates with centromeric constitutive heterochromatin (PubMed:10671371). Recruited to pericentromeric heterochromatin via its chromo domain, which specifically recognizes and binds histone H3 monoubiquitinated at 'Lys-14' (H3K14ub) (PubMed:41094145). {ECO:0000269|PubMed:10671371, ECO:0000269|PubMed:41094145}.; SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome lumen {ECO:0000269|PubMed:29170282}. Cell membrane {ECO:0000269|PubMed:29170282}. Note=(Microbial infection) Upon infection with M.bovis most protein is found associated with bacteria in phagolysosomes, while part is also found in the cell membrane; localization requires bacterial HupB, when it is deleted SUV39H1 is not phagosomal. {ECO:0000269|PubMed:29170282}.
uniprot
proteins