Dnmt3a
entrez
13435
canonical
uniprot
O88508
canonical
ensembl
ENSMUSG00000020661
resolver
ensp
ENSMUSP00000020991
resolver
ensp
ENSMUSP00000133543
resolver
ensp
ENSMUSP00000134009
resolver
ensp
ENSMUSP00000307767
resolver
genesymbol
Dnmt3a
resolver
uniprot
Q3TZK8
resolver
uniprot
Q3UH24
resolver
uniprot
Q8CJ60
resolver
uniprot
Q922J0
resolver
uniprot
Q9CSE1
resolver
uniprot_entry
DNM3A_MOUSE
resolver
uniprot_sec
Q3TZK8
resolver
uniprot_sec
Q3UH24
resolver
uniprot_sec
Q8CJ60
resolver
uniprot_sec
Q922J0
resolver
uniprot_sec
Q9CSE1
resolver
activity_regulation
ACTIVITY REGULATION: Activated by binding to the regulatory factor DNMT3L (PubMed:15671018, PubMed:17713477, PubMed:21481189). Auto-methylation at Cys-706 in absence of DNA inactivates the DNA methyltransferase activity (PubMed:21481189). {ECO:0000269|PubMed:15671018, ECO:0000269|PubMed:17713477, ECO:0000269|PubMed:21481189}.
uniprot
proteins
amino_acid_sequence
MPSSGPGDTSSSSLEREDDRKEGEEQEENRGKEERQEPSATARKVGRPGRKRKHPPVESSDTPKDPAVTTKSQPMAQDSGPSDLLPNGDLEKRSEPQPEEGSPAAGQKGGAPAEGEGTETPPEASRAVENGCCVTKEGRGASAGEGKEQKQTNIESMKMEGSRGRLRGGLGWESSLRQRPMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAVMNAVEENQASGESQKVEEASPPAVQQPTDPASPTVATTPEPVGGDAGDKNATKAADDEPEYEDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAIYEVLQVASSRAGKLFPACHDSDESDSGKAVEVQNKQMIEWALGGFQPSGPKGLEPPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTTEKPKVKEIIDERTRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPARKGLYEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMIDAKEVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQGKDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKEYFACV
uniprot
proteins
ec_number
2.1.1.-
uniprot
proteins
ec_number
2.1.1.37
uniprot
proteins
function
FUNCTION: Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development (PubMed:10555141, PubMed:11399089, PubMed:11919202, PubMed:16567415, PubMed:17713477, PubMed:9662389). DNA methylation is coordinated with methylation of histones (PubMed:10555141, PubMed:11399089, PubMed:11919202, PubMed:16567415, PubMed:17713477, PubMed:9662389). It modifies DNA in a non-processive manner and also methylates non-CpG sites (PubMed:10555141, PubMed:11399089, PubMed:11919202, PubMed:16567415, PubMed:17713477, PubMed:9662389). May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1 (PubMed:18823905). Plays a role in paternal and maternal imprinting (PubMed:15215868). Required for methylation of most imprinted loci in germ cells (PubMed:15215868). Acts as a transcriptional corepressor for ZBTB18 (PubMed:11350943). Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites (PubMed:20547484). Can actively repress transcription through the recruitment of HDAC activity (PubMed:11350943). Also has weak auto-methylation activity on Cys-706 in absence of DNA (PubMed:21481189). {ECO:0000269|PubMed:10555141, ECO:0000269|PubMed:11350943, ECO:0000269|PubMed:11399089, ECO:0000269|PubMed:11919202, ECO:0000269|PubMed:15215868, ECO:0000269|PubMed:16567415, ECO:0000269|PubMed:17713477, ECO:0000269|PubMed:18823905, ECO:0000269|PubMed:20547484, ECO:0000269|PubMed:21481189, ECO:0000269|PubMed:9662389}.
uniprot
proteins
mass_dalton
101672
uniprot
proteins
mutagenesis
MUTAGEN 293; /note="Missing: Decreased protein abundance."; /evidence="ECO:0000269|PubMed:30478443"; MUTAGEN 302..303; /note="WP->ST: Prevents accumulation in pericentric heterochromatin."; /evidence="ECO:0000269|PubMed:15456878"; MUTAGEN 306; /note="I->N: Decreased protein abundance."; /evidence="ECO:0000269|PubMed:30478443"; MUTAGEN 326; /note="W->R: The protein is stably expressed."; /evidence="ECO:0000269|PubMed:30478443"; MUTAGEN 636; /note="F->A: Reduces activity about 20-fold. Loss of substrate binding."; /evidence="ECO:0000269|PubMed:16472822"; MUTAGEN 660; /note="E->A: Reduces activity about 15-fold. Loss of substrate binding."; /evidence="ECO:0000269|PubMed:16472822"; MUTAGEN 682; /note="D->A: Strongly reduces substrate binding. No effect on activity."; /evidence="ECO:0000269|PubMed:16472822"; MUTAGEN 705..706; /note="PC->VD: No effect on localization."; /evidence="ECO:0000269|PubMed:15456878"; MUTAGEN 706; /note="C->A: Reduces activity about 5-fold. Reduces DNA-binding capacity. Abolished cysteine-methylation."; /evidence="ECO:0000269|PubMed:16472822, ECO:0000269|PubMed:21481189"; MUTAGEN 707; /note="N->Q: Reduces activity about 3-fold."; /evidence="ECO:0000269|PubMed:16472822"; MUTAGEN 710; /note="S->A: No effect on activity."; /evidence="ECO:0000269|PubMed:16472822"; MUTAGEN 716; /note="R->A: Reduces activity about 30-fold. Reduces DNA-binding capacity."; /evidence="ECO:0000269|PubMed:16472822"; MUTAGEN 717; /note="K->A: Reduces activity about 3-fold."; /evidence="ECO:0000269|PubMed:16472822"; MUTAGEN 728; /note="F->A: Loss of activity due to the incapacity to bind the regulatory subunit DNMT3L."; /evidence="ECO:0000269|PubMed:17713477"; MUTAGEN 752; /note="E->A: Reduces activity about 10-fold."; /evidence="ECO:0000269|PubMed:16472822"; MUTAGEN 753; /note="N->A: Reduces activity about 10-fold."; /evidence="ECO:0000269|PubMed:16472822"; MUTAGEN 788; /note="R->A: Reduces activity about 15-fold."; /evidence="ECO:0000269|PubMed:16472822"; MUTAGEN 827; /note="R->A: Reduces activity about 2-fold. Reduces DNA-binding capacity."; /evidence="ECO:0000269|PubMed:16472822"; MUTAGEN 832; /note="R->A: Reduces DNA-binding capacity. No effect on activity."; /evidence="ECO:0000269|PubMed:16472822"; MUTAGEN 878; /note="R->A: Reduces activity about 6-fold. Reduces DNA-binding capacity."; /evidence="ECO:0000269|PubMed:16472822"; MUTAGEN 881; /note="R->A: Loss of activity. Strongly reduces substrate binding."; /evidence="ECO:0000269|PubMed:16472822"; MUTAGEN 883; /note="R->A: Reduces activity about 3-fold. Reduces DNA-binding capacity."; /evidence="ECO:0000269|PubMed:16472822
uniprot
proteins
post_translational_modification
PTM: Auto-methylated at Cys-706: auto-methylation takes place in absence of DNA substrate and inactivates the DNA methyltransferase activity (PubMed:21481189). Inactivation by auto-methylation may be used to inactivate unused DNA methyltransferases in the cell (PubMed:21481189). {ECO:0000269|PubMed:21481189}.; PTM: Sumoylated; sumoylation disrupts the ability to interact with histone deacetylases (HDAC1 and HDAC2) and repress transcription. {ECO:0000269|PubMed:14752048}.
uniprot
proteins
protein_family
C5-methyltransferase family
uniprot
proteins
protein_family
Class I-like SAM-binding methyltransferase superfamily
uniprot
proteins
pubmed
10555141
uniprot
proteins
pubmed
11350943
uniprot
proteins
pubmed
11399089
uniprot
proteins
pubmed
11919202
uniprot
proteins
pubmed
12138111
uniprot
proteins
pubmed
12616525
uniprot
proteins
pubmed
14752048
uniprot
proteins
pubmed
15215868
uniprot
proteins
pubmed
15456878
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15671018
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16357870
uniprot
proteins
pubmed
16472822
uniprot
proteins
pubmed
16567415
uniprot
proteins
pubmed
17713477
uniprot
proteins
pubmed
18823905
uniprot
proteins
pubmed
19798101
uniprot
proteins
pubmed
20547484
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21481189
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
30478443
uniprot
proteins
pubmed
32674113
uniprot
proteins
pubmed
9662389
uniprot
proteins
sequence_length
908
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12138111, ECO:0000269|PubMed:15456878, ECO:0000269|PubMed:20547484}. Chromosome {ECO:0000269|PubMed:20547484}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y6K1}. Note=Accumulates in the major satellite repeats at pericentric heterochromatin. {ECO:0000269|PubMed:20547484}.
uniprot
proteins