Dnmt1
entrez
13433
canonical
uniprot
P13864
canonical
ensembl
ENSMUSG00000004099
resolver
ensp
ENSMUSP00000004202
resolver
ensp
ENSMUSP00000136669
resolver
ensp
ENSMUSP00000136982
resolver
ensp
ENSMUSP00000150433
resolver
ensp
ENSMUSP00000162937
resolver
ensp
ENSMUSP00000162939
resolver
ensp
ENSMUSP00000162940
resolver
enst
ENSMUST00000177754
resolver
enst
ENSMUST00000178110
resolver
genesymbol
Dnmt1
resolver
genesymbol_syn
Dnmt
resolver
genesymbol_syn
Met1
resolver
genesymbol_syn
Uim
resolver
uniprot
J3QNW0
resolver
uniprot
P97413
resolver
uniprot
Q3UHZ3
resolver
uniprot
Q3UWN4
resolver
uniprot
Q7TSJ0
resolver
uniprot
Q80ZU3
resolver
uniprot
Q9CSC6
resolver
uniprot
Q9QXX6
resolver
uniprot_entry
DNMT1_MOUSE
resolver
uniprot_entry
J3QNW0_MOUSE
resolver
uniprot_entry
Q3UHZ3_MOUSE
resolver
uniprot_entry
Q3UWN4_MOUSE
resolver
uniprot_entry
Q7TSJ0_MOUSE
resolver
uniprot_sec
P97413
resolver
uniprot_sec
Q80ZU3
resolver
uniprot_sec
Q9CSC6
resolver
uniprot_sec
Q9QXX6
resolver
activity_regulation
ACTIVITY REGULATION: Allosterically regulated. The binding of 5-methylcytosine-containing DNA to the N-terminal parts of DNMT1 causes an allosteric activation of the catalytic domain by a direct interaction of its Zn-binding domain with the catalytic domain. {ECO:0000269|PubMed:1628623}.
uniprot
proteins
amino_acid_sequence
MPARTAPARVPALASPAGSLPDHVRRRLKDLERDGLTEKECVREKLNLLHEFLQTEIKSQLCDLETKLHKEELSEEGYLAKVKSLLNKDLSLENGTHTLTQKANGCPANGSRPTWRAEMADSNRSPRSRPKPRGPRRSKSDSDTLSVETSPSSVATRRTTRQTTITAHFTKGPTKRKPKEESEEGNSAESAAEERDQDKKRRVVDTESGAAAAVEKLEEVTAGTQLGPEEPCEQEDDNRSLRRHTRELSLRRKSKEDPDREARPETHLDEDEDGKKDKRSSRPRSQPRDPAAKRRPKEAEPEQVAPETPEDRDEDEREEKRRKTTRKKLESHTVPVQSRSERKAAQSKSVIPKINSPKCPECGQHLDDPNLKYQQHPEDAVDEPQMLTSEKLSIYDSTSTWFDTYEDSPMHRFTSFSVYCSRGHLCPVDTGLIEKNVELYFSGCAKAIHDENPSMEGGINGKNLGPINQWWLSGFDGGEKVLIGFSTAFAEYILMEPSKEYEPIFGLMQEKIYISKIVVEFLQNNPDAVYEDLINKIETTVPPSTINVNRFTEDSLLRHAQFVVSQVESYDEAKDDDETPIFLSPCMRALIHLAGVSLGQRRATRRVMGATKEKDKAPTKATTTKLVYQIFDTFFSEQIEKYDKEDKENAMKRRRCGVCEVCQQPECGKCKACKDMVKFGGTGRSKQACLKRRCPNLAVKEADDDEEADDDVSEMPSPKKLHQGKKKKQNKDRISWLGQPMKIEENRTYYQKVSIDEEMLEVGDCVSVIPDDSSKPLYLARVTALWEDKNGQMMFHAHWFCAGTDTVLGATSDPLELFLVGECENMQLSYIHSKVKVIYKAPSENWAMEGGTDPETTLPGAEDGKTYFFQLWYNQEYARFESPPKTQPTEDNKHKFCLSCIRLAELRQKEMPKVLEQIEEVDGRVYCSSITKNGVVYRLGDSVYLPPEAFTFNIKVASPVKRPKKDPVNETLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIHCGKKKGKVNEADIKLRLYKFYRPENTHRSYNGSYHTDINMLYWSDEEAVVNFSDVQGRCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNFEDPPNHARSPGNKGKGKGKGKGKGKHQVSEPKEPEAAIKLPKLRTLDVFSGCGGLSEGFHQAGISETLWAIEMWDPAAQAFRLNNPGTTVFTEDCNVLLKLVMAGEVTNSLGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEIQNGASNSEIPYNGEPLSWFQRQLRGSHYQPILRDHICKDMSPLVAARMRHIPLFPGSDWRDLPNIQVRLGDGVIAHKLQYTFHDVKNGYSSTGALRGVCSCAEGKACDPESRQFSTLIPWCLPHTGNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDSYRFFGNILDRHRQVGNAVPPPLAKAIGLEIKLCLLSSARESASAAVKAKEEAATKD
uniprot
proteins
ec_number
2.1.1.37
uniprot
proteins
function
FUNCTION: DNA methyltransferase that methylates CpG residues (PubMed:11290321, PubMed:11399088, PubMed:17576694, PubMed:17893328, PubMed:22323818). Preferentially methylates hemimethylated DNA (PubMed:11399088, PubMed:17576694, PubMed:17893328, PubMed:22323818). Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance (PubMed:11399088, PubMed:17576694, PubMed:22323818). Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication (PubMed:11399088, PubMed:15550930, PubMed:17576694). It is responsible for maintaining methylation patterns established in development (PubMed:11399088, PubMed:17576694). DNA methylation is coordinated with methylation of histones (By similarity). Mediates transcriptional repression by direct binding to HDAC2 (By similarity). In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9 (By similarity). Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (By similarity). Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (By similarity). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (By similarity). {ECO:0000250|UniProtKB:P26358, ECO:0000269|PubMed:11290321, ECO:0000269|PubMed:11399088, ECO:0000269|PubMed:15550930, ECO:0000269|PubMed:17576694, ECO:0000269|PubMed:17893328, ECO:0000269|PubMed:22323818}.
uniprot
proteins
mass_dalton
183189
uniprot
proteins
mutagenesis
MUTAGEN 162; /note="Q->E: Abolishes interaction with PCNA. No effect on activity."; /evidence="ECO:0000269|PubMed:17576694"; MUTAGEN 169; /note="F->S: Abolishes interaction with PCNA. No effect on activity."; /evidence="ECO:0000269|PubMed:17576694"; MUTAGEN 382..396; /note="DEPQMLTSEKLSIYD->AAPQALTSEKLAIYA: Decreased binding to ubiquitinated histones."; /evidence="ECO:0000269|PubMed:26065575"; MUTAGEN 382..393; /note="DEPQMLTSEKLS->AAPQMLTSEKLA: Decreased binding to ubiquitinated histones."; /evidence="ECO:0000269|PubMed:26065575"; MUTAGEN 515; /note="S->A: Loss of activity. No effect on DNA-binding capacity."; /evidence="ECO:0000269|PubMed:17965600"; MUTAGEN 515; /note="S->E: Slightly reduces activity."; /evidence="ECO:0000269|PubMed:17965600"; MUTAGEN 981..985; /note="SDYIK->ADAIA: Decreased DNA methyltransferase activity."; /evidence="ECO:0000269|PubMed:22323818"; MUTAGEN 1229; /note="C->S: Loss of DNA methyltransferase activity; knockin mice die shortly after gastrulation due to a near-complete loss of DNA methylation and an altered distribution of repressive chromatin markers in the nuclei."; /evidence="ECO:0000269|PubMed:17893328"; MUTAGEN 1229; /note="C->W: Loss of activity."; /evidence="ECO:0000269|PubMed:17576694"; MUTAGEN 1235; /note="M->A: Strongly decreased DNA methyltransferase activity."; /evidence="ECO:0000269|PubMed:22323818"; MUTAGEN 1512; /note="W->A: Strongly decreased DNA methyltransferase activity."; /evidence="ECO:0000269|PubMed:22323818"; MUTAGEN 1537; /note="K->A: Decreased DNA methyltransferase activity."; /evidence="ECO:0000269|PubMed:22323818
uniprot
proteins
post_translational_modification
PTM: Sumoylated; sumoylation increases activity. {ECO:0000250|UniProtKB:P26358}.; PTM: Phosphorylation at Ser-146 by CK1 reduces DNA-binding activity. {ECO:0000269|PubMed:17965600, ECO:0000269|PubMed:20192920, ECO:0000269|PubMed:9211941}.; PTM: Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates cell cycle G(2)/M transition. Deacetylation of Lys-1352 and Lys-1418 by SIRT1 increases methyltransferase activity. {ECO:0000250|UniProtKB:P26358}.; PTM: Phosphorylation of Ser-152 by CDKs is important for enzymatic activity and protein stability. Phosphorylation of Ser-140 by AKT1 prevents methylation by SETD7 thereby increasing DNMT1 stability. {ECO:0000250|UniProtKB:P26358}.; PTM: Methylation at Lys-139 by SETD7 is necessary for the regulation of DNMT1 proteasomal degradation. {ECO:0000250|UniProtKB:P26358}.; PTM: Ubiquitinated by UHRF1; interaction with USP7 counteracts ubiquitination by UHRF1 by promoting deubiquitination and preventing degradation by the proteasome. {ECO:0000269|PubMed:21268065}.
uniprot
proteins
protein_family
C5-methyltransferase family
uniprot
proteins
protein_family
Class I-like SAM-binding methyltransferase superfamily
uniprot
proteins
pubmed
10615135
uniprot
proteins
pubmed
10715201
uniprot
proteins
pubmed
10888872
uniprot
proteins
pubmed
11063128
uniprot
proteins
pubmed
11290321
uniprot
proteins
pubmed
11399088
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15550930
uniprot
proteins
pubmed
16085498
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
1628623
uniprot
proteins
pubmed
16357870
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17576694
uniprot
proteins
pubmed
17893328
uniprot
proteins
pubmed
17965600
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
20192920
uniprot
proteins
pubmed
21163962
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21268065
uniprot
proteins
pubmed
21518897
uniprot
proteins
pubmed
22323818
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
26065575
uniprot
proteins
pubmed
28842251
uniprot
proteins
pubmed
29053958
uniprot
proteins
pubmed
3210246
uniprot
proteins
pubmed
8898232
uniprot
proteins
pubmed
8917520
uniprot
proteins
pubmed
8940105
uniprot
proteins
pubmed
9211941
uniprot
proteins
pubmed
9449671
uniprot
proteins
pubmed
9830015
uniprot
proteins
sequence_length
1620
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11290321, ECO:0000269|PubMed:9449671}. Chromosome {ECO:0000269|PubMed:10888872, ECO:0000269|PubMed:17576694, ECO:0000269|PubMed:17893328, ECO:0000269|PubMed:29053958}. Cytoplasm {ECO:0000269|PubMed:11290321, ECO:0000269|PubMed:26065575, ECO:0000269|PubMed:9449671}. Note=It is nucleoplasmic through most of the cell cycle and Associates with replication foci during S-phase: recruited to hemimethylated DNA sites via its RFTS domain, which specifically recognizes and binds histone H3 ubiquitinated at 'Lys-14', 'Lys-18' and 'Lys-23' (H3K14ub, H3K18ub and H3K23ub, respectively) (PubMed:11290321, PubMed:17893328, PubMed:26065575, PubMed:29053958). In germ cells, spermatogonia, preleptotene and leptotene spermatocytes all express high levels of nuclear protein, while the protein is not detected in pachytene spermatocytes, despite the fact they expressed high levels of mRNA (PubMed:9449671). In females, the protein is not detected in non-growing oocytes, in contrast to the growing oocytes (PubMed:9449671). During the growing, the protein is no longer detectable in nuclei but accumulates to very high levels first throughout the cytoplasm (PubMed:9449671). At the time of ovulation, all the protein is cytoplasmic and is actively associated with the oocyte cortex (PubMed:9449671). After fecondation, in the preimplantation embryo, the protein remains cytoplasmic and after implantation, it is exclusively nuclear in all tissue types (PubMed:9449671). Isoform 2 is sequestered in the cytoplasm of maturing oocytes and of preimplantation embryos, except for the 8-cell stage, while isoform 1 is exclusively nuclear (PubMed:9449671). {ECO:0000269|PubMed:11290321, ECO:0000269|PubMed:17893328, ECO:0000269|PubMed:26065575, ECO:0000269|PubMed:29053958, ECO:0000269|PubMed:9449671}.
uniprot
proteins