DNMT1
entrez
1786
canonical
uniprot
P26358
canonical
ensembl
ENSG00000130816
resolver
ensp
ENSP00000345739
resolver
ensp
ENSP00000352516
resolver
ensp
ENSP00000587988
resolver
genesymbol
DNMT1
resolver
genesymbol_syn
AIM
resolver
genesymbol_syn
CXXC9
resolver
genesymbol_syn
DNMT
resolver
hgnc
HGNC:2976
resolver
uniprot
A0AV63
resolver
uniprot
B7ZLW6
resolver
uniprot
I6L9H2
resolver
uniprot
Q59FP7
resolver
uniprot
Q9UHG5
resolver
uniprot
Q9ULA2
resolver
uniprot
Q9UMZ6
resolver
uniprot_entry
DNMT1_HUMAN
resolver
uniprot_entry
I6L9H2_HUMAN
resolver
uniprot_entry
Q59FP7_HUMAN
resolver
uniprot_sec
A0AV63
resolver
uniprot_sec
B7ZLW6
resolver
uniprot_sec
Q9UHG5
resolver
uniprot_sec
Q9ULA2
resolver
uniprot_sec
Q9UMZ6
resolver
amino_acid_sequence
MPARTAPARVPTLAVPAISLPDDVRRRLKDLERDSLTEKECVKEKLNLLHEFLQTEIKNQLCDLETKLRKEELSEEGYLAKVKSLLNKDLSLENGAHAYNREVNGRLENGNQARSEARRVGMADANSPPKPLSKPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQDEKRRRVTSRERVARPLPAEEPERAKSGTRTEKEEERDEKEEKRLRSQTKEPTPKQKLKEEPDREARAGVQADEDEDGDEKDEKKHRSQPKDLAAKRRPEEKEPEKVNPQISDEKDEDEKEEKRRKTTPKEPTEKKMARAKTVMNSKTHPPKCIQCGQYLDDPDLKYGQHPPDAVDEPQMLTNEKLSIFDANESGFESYEALPQHKLTCFSVYCKHGHLCPIDTGLIEKNIELFFSGSAKPIYDDDPSLEGGVNGKNLGPINEWWITGFDGGEKALIGFSTSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSNSDSTYEDLINKIETTVPPSGLNLNRFTEDSLLRHAQFVVEQVESYDEAGDSDEQPIFLTPCMRDLIKLAGVTLGQRRAQARRQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENAFKRRRCGVCEVCQQPECGKCKACKDMVKFGGSGRSKQACQERRCPNMAMKEADDDEEVDDNIPEMPSPKKMHQGKKKKQNKNRISWVGEAVKTDGKKSYYKKVCIDAETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVKVIYKAPSENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCVSCARLAEMRQKEIPRVLEQLEDLDSRVLYYSATKNGILYRVGDGVYLPPEAFTFNIKLSSPVKRPRKEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLRTLDVFSGCGGLSEGFHQAGISDTLWAIEMWDPAAQAFRLNNPGSTVFTEDCNILLKLVMAGETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEVRNGASALEISYNGEPQSWFQRQLRGAQYQPILRDHICKDMSALVAARMRHIPLAPGSDWRDLPNIEVRLSDGTMARKLRYTHHDRKNGRSSSGALRGVCSCVEAGKACDPAARQFNTLIPWCLPHTGNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIKLCMLAKARESASAKIKEEEAAKD
uniprot
proteins
disease_involvement
DISEASE: Neuropathy, hereditary sensory, 1E (HSN1E) [MIM:614116]: A neurodegenerative disorder characterized by adult onset of progressive peripheral sensory loss associated with progressive hearing impairment and early-onset dementia. {ECO:0000269|PubMed:21532572}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cerebellar ataxia, deafness, and narcolepsy, autosomal dominant (ADCADN) [MIM:604121]: An autosomal dominant neurologic disorder characterized by adult onset of progressive cerebellar ataxia, narcolepsy, cataplexy, sensorineural deafness, and dementia. More variable features include optic atrophy, sensory neuropathy, psychosis, and depression. {ECO:0000269|PubMed:22328086}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.1.1.37
uniprot
proteins
function
FUNCTION: DNA methyltransferase that methylates CpG residues (PubMed:17200670, PubMed:18754681, PubMed:21745816, PubMed:26070743). Preferentially methylates hemimethylated DNA (PubMed:21745816, PubMed:26070743). Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance (PubMed:17200670, PubMed:21745816). Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication (PubMed:21745816). It is responsible for maintaining methylation patterns established in development (PubMed:21745816). DNA methylation is coordinated with methylation of histones (PubMed:16357870). Mediates transcriptional repression by direct binding to HDAC2 (PubMed:10888872). 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 (PubMed:18413740). 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 (PubMed:24623306). Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (PubMed:24623306). {ECO:0000269|PubMed:10888872, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:17200670, ECO:0000269|PubMed:18413740, ECO:0000269|PubMed:18754681, ECO:0000269|PubMed:21745816, ECO:0000269|PubMed:24623306, ECO:0000269|PubMed:26070743}.
uniprot
proteins
mass_dalton
183165
uniprot
proteins
mutagenesis
MUTAGEN 142; /note="K->A: Loss of interaction with L3MBTL3 and DCAF5. Loss of ubiquitination by the CRL4-DCAF5 E3 ubiquitin ligase complex."; /evidence="ECO:0000269|PubMed:29691401"; MUTAGEN 163; /note="R->A: Abolishes interaction with PCNA."; /evidence="ECO:0000269|PubMed:9302295"; MUTAGEN 164; /note="Q->A: Abolishes interaction with PCNA."; /evidence="ECO:0000269|PubMed:9302295"; MUTAGEN 166; /note="T->A: Abolishes interaction with PCNA."; /evidence="ECO:0000269|PubMed:9302295"; MUTAGEN 167; /note="I->A: Abolishes interaction with PCNA."; /evidence="ECO:0000269|PubMed:9302295"; MUTAGEN 169; /note="S->A: No loss of interaction with PCNA."; /evidence="ECO:0000269|PubMed:9302295"; MUTAGEN 170; /note="H->V: Abolishes interaction with PCNA."; /evidence="ECO:0000269|PubMed:9302295"; MUTAGEN 171; /note="F->V: Abolishes interaction with PCNA."; /evidence="ECO:0000269|PubMed:9302295"; MUTAGEN 172; /note="A->S: No loss of interaction with PCNA."; /evidence="ECO:0000269|PubMed:9302295"; MUTAGEN 173; /note="K->A: No loss of interaction with PCNA."; /evidence="ECO:0000269|PubMed:9302295"; MUTAGEN 582; /note="R->E: Slightly increased association with hemimethylated DNA."; /evidence="ECO:0000269|PubMed:26070743"; MUTAGEN 653; /note="C->G: Reduces activity about 10-fold; when associated with G-656; G-659; G-664; G-667 and G-670."; /evidence="ECO:0000269|PubMed:18754681"; MUTAGEN 656; /note="C->G: Reduces activity about 10-fold; when associated with G-653; G-659; G-664; G-667 and G-670."; /evidence="ECO:0000269|PubMed:18754681"; MUTAGEN 659; /note="C->G: Reduces activity about 10-fold; when associated with G-653; G-656; G-664; G-667 and G-670."; /evidence="ECO:0000269|PubMed:18754681"; MUTAGEN 664; /note="C->F: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-667 and G-670."; /evidence="ECO:0000269|PubMed:18754681"; MUTAGEN 667; /note="C->G: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-670."; /evidence="ECO:0000269|PubMed:18754681"; MUTAGEN 670; /note="C->G: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-667."; /evidence="ECO:0000269|PubMed:18754681"; MUTAGEN 1226; /note="C->A: Loss of activity."; /evidence="ECO:0000269|PubMed:19450230
uniprot
proteins
post_translational_modification
PTM: Sumoylated; sumoylation increases activity. {ECO:0000269|PubMed:19450230}.; PTM: Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates cell cycle G(2)/M transition (PubMed:21947282). Deacetylation of Lys-1349 and Lys-1415 by SIRT1 increases methyltransferase activity (PubMed:21947282). {ECO:0000269|PubMed:21947282}.; PTM: Phosphorylation of Ser-154 by CDKs is important for enzymatic activity and protein stability. Phosphorylation of Ser-143 by AKT1 prevents methylation by SETD7 thereby increasing DNMT1 stability. {ECO:0000269|PubMed:21151116, ECO:0000269|PubMed:21565170}.; PTM: Methylation at Lys-142 by SETD7 is necessary for the regulation of DNMT1 proteasomal degradation. {ECO:0000269|PubMed:18438403, ECO:0000269|PubMed:21151116, ECO:0000269|PubMed:24492612, ECO:0000269|PubMed:29691401}.; PTM: Ubiquitinated by UHRF1; interaction with USP7 counteracts ubiquitination by UHRF1 by promoting deubiquitination and preventing degradation by the proteasome. {ECO:0000250|UniProtKB:P13864}.
uniprot
proteins
protein_family
C5-methyltransferase family
uniprot
proteins
protein_family
Class I-like SAM-binding methyltransferase superfamily
uniprot
proteins
pubmed
10325416
uniprot
proteins
pubmed
10449766
uniprot
proteins
pubmed
10753866
uniprot
proteins
pubmed
10888872
uniprot
proteins
pubmed
10888886
uniprot
proteins
pubmed
10947852
uniprot
proteins
pubmed
12145218
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1594447
uniprot
proteins
pubmed
16357870
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17200670
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18413740
uniprot
proteins
pubmed
18438403
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18754681
uniprot
proteins
pubmed
19173286
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19450230
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21151116
uniprot
proteins
pubmed
21163962
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21389349
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21532572
uniprot
proteins
pubmed
21565170
uniprot
proteins
pubmed
21745816
uniprot
proteins
pubmed
21947282
uniprot
proteins
pubmed
22328086
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24492612
uniprot
proteins
pubmed
24623306
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
26070743
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29053958
uniprot
proteins
pubmed
29691401
uniprot
proteins
pubmed
32051553
uniprot
proteins
pubmed
8940105
uniprot
proteins
pubmed
9302295
uniprot
proteins
sequence_length
1616
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12145218, ECO:0000269|PubMed:24492612}. Chromosome {ECO:0000269|PubMed:29053958}. Note=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:29053958). Localized to the perinucleolar region (PubMed:24492612). {ECO:0000269|PubMed:24492612, ECO:0000269|PubMed:29053958}.
uniprot
proteins