DNMT1

Functionⁱ

Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. 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. 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).

Promotes tumor growth (PubMed:24623306).

4 Publications

Catalytic activityⁱ

a 2'-deoxycytidine in DNA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
S-adenosyl-L-methionine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
a 5-methyl-2'-deoxycytidine in DNA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
S-adenosyl-L-homocysteine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10018
EC:
2.1.1.37
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10018
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
a 2'-deoxycytidine in DNA
dCMP residue
zoom
+
S-adenosyl-L-methionine
zoom
=
a 5-methyl-2'-deoxycytidine in DNA
5-methyl dCMP residue
zoom
+
H⁺
+
S-adenosyl-L-homocysteine
zoom

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	353	Zinc	1
Metal bindingⁱ	356	Zinc	1
Metal bindingⁱ	414	Zinc	1
Metal bindingⁱ	418	Zinc	1
Siteⁱ	509	Important for activityBy similarity	1
Metal bindingⁱ	653	Zinc 1PROSITE-ProRule annotation	1
Metal bindingⁱ	656	Zinc 1PROSITE-ProRule annotation	1
Metal bindingⁱ	659	Zinc 1PROSITE-ProRule annotation	1
Metal bindingⁱ	664	Zinc 2PROSITE-ProRule annotation	1
Metal bindingⁱ	667	Zinc 2PROSITE-ProRule annotation	1
Metal bindingⁱ	670	Zinc 2PROSITE-ProRule annotation	1
Metal bindingⁱ	686	Zinc 2PROSITE-ProRule annotation	1
Metal bindingⁱ	691	Zinc 1PROSITE-ProRule annotation	1
Binding siteⁱ	1146	S-adenosyl-L-methionine; via carbonyl oxygenBy similarity	1
Binding siteⁱ	1191	S-adenosyl-L-methionineCombined sources1 Publication	1
Active siteⁱ	1226		1
Binding siteⁱ	1578	S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication	1
Binding siteⁱ	1580	S-adenosyl-L-methionine; via amide nitrogenBy similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	646 – 692	CXXC-typePROSITE-ProRule annotationAdd BLAST		47

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Activator, Chromatin regulator, DNA-binding, Methyltransferase, Repressor, Transferase
Biological process	Transcription, Transcription regulation
Ligand	Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BRENDAⁱ	2.1.1.37, 2681
PathwayCommonsⁱ	P26358
Reactomeⁱ	R-HSA-212300, PRC2 methylates histones and DNA R-HSA-427413, NoRC negatively regulates rRNA expression R-HSA-4655427, SUMOylation of DNA methylation proteins R-HSA-5334118, DNA methylation R-HSA-9710421, Defective pyroptosis
SIGNORⁱ	P26358

Protein family/group databases

REBASEⁱ	1161, M.HsaDnmt1A 4240, M.HsaDnmt1B

REBASEⁱ

1161, M.HsaDnmt1A
4240, M.HsaDnmt1B

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: DNA (cytosine-5)-methyltransferase 1 (EC:2.1.1.37) Short name: Dnmt1 Alternative name(s): CXXC-type zinc finger protein 9 DNA methyltransferase HsaI Short name: DNA MTase HsaI Short name: M.HsaI MCMT
Gene namesⁱ	Name:DNMT1 Synonyms:AIM, CXXC9, DNMT
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:2976, DNMT1
MIMⁱ	126375, gene
neXtProtⁱ	NX_P26358
VEuPathDBⁱ	HostDB:ENSG00000130816

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Neuropathy, hereditary sensory, 1E (HSN1E)1 Publication

The disease is caused by variants affecting the gene represented in this entry.

Disease descriptionA neurodegenerative disorder characterized by adult onset of progressive peripheral sensory loss associated with progressive hearing impairment and early-onset dementia.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_065965	490 – 491	DP → EY in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase. Corresponds to variant dbSNP:rs199473691Ensembl.		2
Natural variantⁱVAR_065966	495	Y → C in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase. 1 PublicationCorresponds to variant dbSNP:rs199473690Ensembl.		1

Cerebellar ataxia, deafness, and narcolepsy, autosomal dominant (ADCADN)1 Publication

The disease is caused by variants affecting the gene represented in this entry.

Disease descriptionAn 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.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_070055	554	A → V in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509392Ensembl.	1
Natural variantⁱVAR_070056	589	G → A in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509393Ensembl.	1
Natural variantⁱVAR_070057	590	V → F in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509391Ensembl.	1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	163	R → A: Abolishes interaction with PCNA. 1 Publication	1
Mutagenesisⁱ	164	Q → A: Abolishes interaction with PCNA. 1 Publication	1
Mutagenesisⁱ	166	T → A: Abolishes interaction with PCNA. 1 Publication	1
Mutagenesisⁱ	167	I → A: Abolishes interaction with PCNA. 1 Publication	1
Mutagenesisⁱ	169	S → A: No loss of interaction with PCNA. 1 Publication	1
Mutagenesisⁱ	170	H → V: Abolishes interaction with PCNA. 1 Publication	1
Mutagenesisⁱ	171	F → V: Abolishes interaction with PCNA. 1 Publication	1
Mutagenesisⁱ	172	A → S: No loss of interaction with PCNA. 1 Publication	1
Mutagenesisⁱ	173	K → A: No loss of interaction with PCNA. 1 Publication	1
Mutagenesisⁱ	653	C → G: Reduces activity about 10-fold; when associated with G-656; G-659; G-664; G-667 and G-670. 1 Publication	1
Mutagenesisⁱ	656	C → G: Reduces activity about 10-fold; when associated with G-653; G-659; G-664; G-667 and G-670. 1 Publication	1
Mutagenesisⁱ	659	C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-664; G-667 and G-670. 1 Publication	1
Mutagenesisⁱ	664	C → F: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-667 and G-670. 1 Publication	1
Mutagenesisⁱ	667	C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-670. 1 Publication	1
Mutagenesisⁱ	670	C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-667. 1 Publication	1
Mutagenesisⁱ	1226	C → A: Loss of activity. 1 Publication	1

Keywords - Diseaseⁱ

Deafness, Disease variant, Neuropathy

Organism-specific databases

DisGeNET More...DisGeNETⁱ	1786
GeneReviewsⁱ	DNMT1
MalaCards human disease database More...MalaCardsⁱ	DNMT1
MIMⁱ	604121, phenotype 614116, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000130816
Orphanetⁱ	314404, Autosomal dominant cerebellar ataxia-deafness-narcolepsy syndrome 456318, Hereditary sensory neuropathy-deafness-dementia syndrome
PharmGKBⁱ	PA27443

Miscellaneous databases

Pharosⁱ	P26358, Tclin

Pharosⁱ

P26358, Tclin

Chemistry databases

ChEMBLⁱ	CHEMBL1993
Drug and drug target database More...DrugBankⁱ	DB00928, Azacitidine DB01262, Decitabine DB12116, Epigallocatechin gallate DB01099, Flucytosine DB05668, Palifosfamide DB01035, Procainamide DB00721, Procaine
DrugCentral More...DrugCentralⁱ	P26358
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2605

Genetic variation databases

BioMutaⁱ	DNMT1
DMDMⁱ	12231019

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000088034	1 – 1616	DNA (cytosine-5)-methyltransferase 1Add BLAST		1616

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	70	N6,N6-dimethyllysine1 Publication	1
Modified residueⁱ	127	PhosphoserineCombined sources	1
Modified residueⁱ	133	PhosphoserineCombined sources	1
Modified residueⁱ	137	PhosphothreonineCombined sources	1
Modified residueⁱ	141	PhosphoserineBy similarity	1
Modified residueⁱ	142	N6-methyllysine; by SETD71 Publication	1
Modified residueⁱ	143	Phosphoserine; by PKB/AKT1Combined sources1 Publication	1
Modified residueⁱ	152	PhosphoserineCombined sources	1
Modified residueⁱ	154	PhosphoserineCombined sources1 Publication	1
Modified residueⁱ	160	N6-acetyllysine1 Publication	1
Modified residueⁱ	166	PhosphothreonineCombined sources	1
Modified residueⁱ	173	N6-acetyllysineCombined sources	1
Modified residueⁱ	188	N6-acetyllysine1 Publication	1
Modified residueⁱ	259	N6-acetyllysine; alternate1 Publication	1
Cross-linkⁱ	259	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residueⁱ	312	PhosphoserineCombined sources	1
Modified residueⁱ	366	N6-acetyllysine1 Publication	1
Modified residueⁱ	394	PhosphoserineCombined sources	1
Modified residueⁱ	398	PhosphoserineCombined sources	1
Modified residueⁱ	509	PhosphoserineBy similarity	1
Modified residueⁱ	549	PhosphoserineCombined sources	1
Modified residueⁱ	714	PhosphoserineCombined sources	1
Modified residueⁱ	732	PhosphoserineCombined sources	1
Modified residueⁱ	749	N6-acetyllysine1 Publication	1
Modified residueⁱ	878	PhosphoserineCombined sources	1
Modified residueⁱ	891	N6-acetyllysine1 Publication	1
Modified residueⁱ	957	N6-acetyllysine1 Publication	1
Modified residueⁱ	961	N6-acetyllysine1 Publication	1
Modified residueⁱ	975	N6-acetyllysine1 Publication	1
Modified residueⁱ	1054	N6-acetyllysine1 Publication	1
Modified residueⁱ	1111	N6-acetyllysineCombined sources1 Publication	1
Modified residueⁱ	1113	N6-acetyllysineCombined sources1 Publication	1
Modified residueⁱ	1115	N6-acetyllysineCombined sources1 Publication	1
Modified residueⁱ	1117	N6-acetyllysine; by EHMT21 Publication	1
Modified residueⁱ	1119	N6-acetyllysineBy similarity	1
Modified residueⁱ	1121	N6-acetyllysineBy similarity	1
Modified residueⁱ	1349	N6-acetyllysine1 Publication	1
Modified residueⁱ	1415	N6-acetyllysine1 Publication	1
Cross-linkⁱ	1609	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationⁱ

Sumoylated; sumoylation increases activity.1 Publication

Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates cell cycle G₂/M transition. Deacetylation of Lys-1349 and Lys-1415 by SIRT1 increases methyltransferase activity.1 Publication

Phosphorylation of Ser-154 by CDKs is important for enzymatic activity and protein stability. Phosphorylation of Ser-143 by AKT1 prevents methylation by SETD7 therebye increasing DNMT1 stability.2 Publications

Ubiquitinated by UHRF1; interaction with USP7 counteracts ubiquitination by UHRF1 by promoting deubiquitination and preventing degradation by the proteasome.By similarity

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P26358
jPOSTⁱ	P26358
MassIVEⁱ	P26358
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P26358
PaxDbⁱ	P26358
PeptideAtlas More...PeptideAtlasⁱ	P26358
PRIDEⁱ	P26358
ProteomicsDBⁱ	54320 [P26358-1] 54321 [P26358-2] 54322 [P26358-3]

PTM databases

GlyGenⁱ	P26358, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	P26358
PhosphoSitePlusⁱ	P26358
SwissPalmⁱ	P26358

Expressionⁱ

Tissue specificityⁱ

Ubiquitous; highly expressed in fetal tissues, heart, kidney, placenta, peripheral blood mononuclear cells, and expressed at lower levels in spleen, lung, brain, small intestine, colon, liver, and skeletal muscle. Isoform 2 is less expressed than isoform 1.1 Publication

Inductionⁱ

Its abundance is reduced to non detectable levels at the G0 phase of the cell cycle and is dramatically induced upon entrance into the S-phase of the cell cycle.

Gene expression databases

Bgeeⁱ	ENSG00000130816, Expressed in oocyte and 227 other tissues
ExpressionAtlasⁱ	P26358, baseline and differential
Genevisibleⁱ	P26358, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000130816, Low tissue specificity

HPAⁱ

ENSG00000130816, Low tissue specificity

Interactionⁱ

Subunit structureⁱ

Homodimer (PubMed:19173286).

Forms a stable complex with E2F1, BB1 and HDAC1 (PubMed:10888886).

Forms a complex with DMAP1 and HDAC2, with direct interaction (PubMed:10888872).

Interacts with the PRC2/EED-EZH2 complex (PubMed:16357870). Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1 (PubMed:24623306).

Interacts with UHRF1; promoting its recruitment to hemimethylated DNA (PubMed:21745816).

Interacts with USP7, promoting its deubiquitination (PubMed:21745816).

Interacts with PCNA (PubMed:9302295).

Interacts with MBD2 and MBD3 (PubMed:10947852).

Interacts with DNMT3A and DNMT3B (PubMed:12145218).

Interacts with UBC9 (PubMed:19450230).

Interacts with CSNK1D (By similarity).

Interacts with HDAC1 (By similarity).

Interacts with BAZ2A/TIP5 (By similarity).

Interacts with SIRT7 (By similarity).

Interacts with ZNF263; recruited to the SIX3 promoter along with other proteins involved in chromatin modification and transcriptional corepression where it contributes to transcriptional repression (PubMed:32051553).

By similarity11 Publications

Binary interactionsⁱ

Hide details

P26358

With	#Exp.	IntAct
AKT1 [P31749]	6	EBI-719459,EBI-296087
CTNNB1 [P35222]	8	EBI-719459,EBI-491549
EED [O75530]	3	EBI-719459,EBI-923794
EZH2 [Q15910]	8	EBI-719459,EBI-530054
NRIP1 [P48552]	3	EBI-719459,EBI-746484
PARP1 [P09874]	6	EBI-719459,EBI-355676
PICK1 [Q9NRD5]	2	EBI-719459,EBI-79165
SETD7 [Q8WTS6]	9	EBI-719459,EBI-1268586
SIRT1 [Q96EB6]	11	EBI-719459,EBI-1802965
UHRF1 [Q96T88]	12	EBI-719459,EBI-1548946
KIE-2 [Q77UV9] from Human herpesvirus 8.	2	EBI-719459,EBI-2608731
LANA1 [Q9QR71] from Human herpesvirus 8 type P (isolate GK18).	2	EBI-719459,EBI-15602554

Protein-protein interaction databases

BioGRIDⁱ	108123, 164 interactors
CORUMⁱ	P26358
Database of interacting proteins More...DIPⁱ	DIP-39693N
ELMⁱ	P26358
IntActⁱ	P26358, 51 interactors
Molecular INTeraction database More...MINTⁱ	P26358
STRINGⁱ	9606.ENSP00000352516

Chemistry databases

BindingDBⁱ

P26358

Miscellaneous databases

RNActⁱ	P26358, protein

RNActⁱ

P26358, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	167 – 169	Combined sources	3
Turnⁱ	354 – 356	Combined sources	3
Beta strandⁱ	359 – 361	Combined sources	3
Helixⁱ	363 – 365	Combined sources	3
Helixⁱ	377 – 381	Combined sources	5
Helixⁱ	384 – 386	Combined sources	3
Beta strandⁱ	392 – 394	Combined sources	3
Beta strandⁱ	404 – 414	Combined sources	11
Beta strandⁱ	417 – 419	Combined sources	3
Beta strandⁱ	422 – 425	Combined sources	4
Turnⁱ	426 – 430	Combined sources	5
Beta strandⁱ	433 – 440	Combined sources	8
Beta strandⁱ	453 – 458	Combined sources	6
Beta strandⁱ	463 – 467	Combined sources	5
Beta strandⁱ	470 – 473	Combined sources	4
Beta strandⁱ	476 – 480	Combined sources	5
Beta strandⁱ	485 – 488	Combined sources	4
Turnⁱ	493 – 495	Combined sources	3
Helixⁱ	496 – 518	Combined sources	23
Helixⁱ	524 – 533	Combined sources	10
Helixⁱ	538 – 540	Combined sources	3
Helixⁱ	547 – 551	Combined sources	5
Helixⁱ	554 – 566	Combined sources	13
Beta strandⁱ	575 – 578	Combined sources	4
Helixⁱ	579 – 588	Combined sources	10
Helixⁱ	592 – 597	Combined sources	6
Helixⁱ	622 – 629	Combined sources	8
Turnⁱ	657 – 659	Combined sources	3
Helixⁱ	670 – 672	Combined sources	3
Turnⁱ	674 – 677	Combined sources	4
Helixⁱ	687 – 689	Combined sources	3
Helixⁱ	692 – 703	Combined sources	12
Beta strandⁱ	731 – 735	Combined sources	5
Beta strandⁱ	738 – 740	Combined sources	3
Beta strandⁱ	744 – 746	Combined sources	3
Beta strandⁱ	748 – 752	Combined sources	5
Beta strandⁱ	755 – 758	Combined sources	4
Beta strandⁱ	762 – 765	Combined sources	4
Beta strandⁱ	767 – 769	Combined sources	3
Beta strandⁱ	775 – 785	Combined sources	11
Turnⁱ	786 – 788	Combined sources	3
Beta strandⁱ	789 – 799	Combined sources	11
Helixⁱ	800 – 802	Combined sources	3
Beta strandⁱ	803 – 805	Combined sources	3
Helixⁱ	806 – 808	Combined sources	3
Beta strandⁱ	813 – 824	Combined sources	12
Helixⁱ	825 – 827	Combined sources	3
Beta strandⁱ	828 – 832	Combined sources	5
Beta strandⁱ	834 – 836	Combined sources	3
Helixⁱ	843 – 845	Combined sources	3
Turnⁱ	851 – 853	Combined sources	3
Helixⁱ	856 – 860	Combined sources	5
Beta strandⁱ	862 – 870	Combined sources	9
Turnⁱ	871 – 874	Combined sources	4
Beta strandⁱ	875 – 877	Combined sources	3
Beta strandⁱ	886 – 888	Combined sources	3
Turnⁱ	889 – 891	Combined sources	3
Helixⁱ	894 – 905	Combined sources	12
Beta strandⁱ	912 – 916	Combined sources	5
Beta strandⁱ	921 – 928	Combined sources	8
Beta strandⁱ	931 – 934	Combined sources	4
Beta strandⁱ	938 – 941	Combined sources	4
Turnⁱ	966 – 968	Combined sources	3
Helixⁱ	973 – 975	Combined sources	3
Helixⁱ	976 – 980	Combined sources	5
Beta strandⁱ	992 – 1001	Combined sources	10
Beta strandⁱ	1005 – 1008	Combined sources	4
Beta strandⁱ	1015 – 1020	Combined sources	6
Helixⁱ	1024 – 1026	Combined sources	3
Helixⁱ	1031 – 1034	Combined sources	4
Beta strandⁱ	1035 – 1037	Combined sources	3
Beta strandⁱ	1041 – 1044	Combined sources	4
Beta strandⁱ	1048 – 1052	Combined sources	5
Helixⁱ	1053 – 1055	Combined sources	3
Beta strandⁱ	1058 – 1064	Combined sources	7
Helixⁱ	1065 – 1067	Combined sources	3
Helixⁱ	1072 – 1077	Combined sources	6
Beta strandⁱ	1079 – 1090	Combined sources	12
Turnⁱ	1091 – 1094	Combined sources	4
Beta strandⁱ	1095 – 1097	Combined sources	3
Helixⁱ	1101 – 1103	Combined sources	3
Beta strandⁱ	1139 – 1145	Combined sources	7
Helixⁱ	1150 – 1158	Combined sources	9
Beta strandⁱ	1160 – 1167	Combined sources	8
Helixⁱ	1171 – 1180	Combined sources	10
Beta strandⁱ	1184 – 1187	Combined sources	4
Helixⁱ	1191 – 1200	Combined sources	10
Turnⁱ	1214 – 1216	Combined sources	3
Beta strandⁱ	1218 – 1222	Combined sources	5
Beta strandⁱ	1231 – 1233	Combined sources	3
Helixⁱ	1237 – 1243	Combined sources	7
Helixⁱ	1247 – 1258	Combined sources	12
Beta strandⁱ	1261 – 1268	Combined sources	8
Helixⁱ	1269 – 1272	Combined sources	4
Helixⁱ	1275 – 1277	Combined sources	3
Helixⁱ	1278 – 1289	Combined sources	12
Beta strandⁱ	1293 – 1300	Combined sources	8
Helixⁱ	1301 – 1304	Combined sources	4
Beta strandⁱ	1311 – 1318	Combined sources	8
Helixⁱ	1336 – 1338	Combined sources	3
Beta strandⁱ	1343 – 1345	Combined sources	3
Beta strandⁱ	1348 – 1350	Combined sources	3
Helixⁱ	1367 – 1371	Combined sources	5
Beta strandⁱ	1384 – 1386	Combined sources	3
Helixⁱ	1395 – 1401	Combined sources	7
Helixⁱ	1419 – 1426	Combined sources	8
Helixⁱ	1436 – 1438	Combined sources	3
Beta strandⁱ	1451 – 1453	Combined sources	3
Turnⁱ	1462 – 1464	Combined sources	3
Beta strandⁱ	1474 – 1476	Combined sources	3
Helixⁱ	1477 – 1479	Combined sources	3
Beta strandⁱ	1480 – 1482	Combined sources	3
Helixⁱ	1487 – 1489	Combined sources	3
Beta strandⁱ	1493 – 1496	Combined sources	4
Helixⁱ	1499 – 1503	Combined sources	5
Helixⁱ	1504 – 1506	Combined sources	3
Helixⁱ	1508 – 1510	Combined sources	3
Turnⁱ	1511 – 1514	Combined sources	4
Beta strandⁱ	1523 – 1525	Combined sources	3
Beta strandⁱ	1534 – 1536	Combined sources	3
Beta strandⁱ	1542 – 1547	Combined sources	6
Helixⁱ	1550 – 1556	Combined sources	7
Helixⁱ	1569 – 1578	Combined sources	10
Helixⁱ	1582 – 1598	Combined sources	17

Show more details

3D structure databases

SMRⁱ	P26358
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P26358

EvolutionaryTraceⁱ

P26358

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	16 – 109	DMAP1-bindingPROSITE-ProRule annotationAdd BLAST	94
Domainⁱ	755 – 880	BAH 1PROSITE-ProRule annotationAdd BLAST	126
Domainⁱ	972 – 1100	BAH 2PROSITE-ProRule annotationAdd BLAST	129
Repeatⁱ	1109 – 1110	1	2
Repeatⁱ	1111 – 1112	2	2
Repeatⁱ	1113 – 1114	3	2
Repeatⁱ	1115 – 1116	4	2
Repeatⁱ	1117 – 1118	5	2
Repeatⁱ	1119 – 1120	6; approximate	2
Domainⁱ	1139 – 1599	SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd BLAST	461

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 336	Interaction with the PRC2/EED-EZH2 complexBy similarityAdd BLAST	336
Regionⁱ	1 – 148	Interaction with DNMT3A1 PublicationAdd BLAST	148
Regionⁱ	1 – 120	Interaction with DMAP11 PublicationAdd BLAST	120
Regionⁱ	103 – 349	DisorderedSequence analysisAdd BLAST	247
Regionⁱ	149 – 217	Interaction with DNMT3B1 PublicationAdd BLAST	69
Regionⁱ	163 – 174	Interaction with PCNA1 PublicationAdd BLAST	12
Regionⁱ	308 – 606	Interaction with the PRC2/EED-EZH2 complexBy similarityAdd BLAST	299
Regionⁱ	310 – 502	HomodimerizationAdd BLAST	193
Regionⁱ	331 – 550	DNA replication foci-targeting sequenceBy similarityAdd BLAST	220
Regionⁱ	651 – 697	Required for activityAdd BLAST	47
Regionⁱ	693 – 754	Autoinhibitory linkerAdd BLAST	62
Regionⁱ	699 – 729	DisorderedSequence analysisAdd BLAST	31
Regionⁱ	1095 – 1130	DisorderedSequence analysisAdd BLAST	36
Regionⁱ	1109 – 1120	6 X 2 AA tandem repeats of K-GAdd BLAST	12
Regionⁱ	1121 – 1616	Interaction with the PRC2/EED-EZH2 complexBy similarityAdd BLAST	496
Regionⁱ	1139 – 1616	CatalyticAdd BLAST	478
Regionⁱ	1150 – 1151	S-adenosyl-L-methionine bindingBy similarity	2
Regionⁱ	1168 – 1169	S-adenosyl-L-methionine bindingCombined sources1 Publication	2
Regionⁱ	1190 – 1191	S-adenosyl-L-methionine bindingBy similarity	2

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	177 – 205	Nuclear localization signalSequence analysisAdd BLAST		29

Compositional bias

Feature key	Position(s)	DescriptionActions	Length
Compositional biasⁱ	155 – 171	Polar residuesSequence analysisAdd BLAST	17
Compositional biasⁱ	175 – 271	Basic and acidic residuesSequence analysisAdd BLAST	97
Compositional biasⁱ	279 – 341	Basic and acidic residuesSequence analysisAdd BLAST	63

Domainⁱ

The N-terminal part is required for homodimerization and acts as a regulatory domain.

The CXXC-type zinc finger specifically binds to unmethylated CpG dinucleotides, positioning the autoinhibitory linker between the DNA and the active site, thus providing a mechanism to ensure that only hemimethylated CpG dinucleotides undergo methylation.1 Publication

Sequence similaritiesⁱ

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.PROSITE-ProRule annotation

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	646 – 692	CXXC-typePROSITE-ProRule annotationAdd BLAST		47

Keywords - Domainⁱ

Repeat, Zinc-finger

Phylogenomic databases

eggNOGⁱ	ENOG502QPKK, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000005100
HOGENOMⁱ	CLU_003040_0_0_1
InParanoidⁱ	P26358
OMAⁱ	RDHVCKD
PhylomeDBⁱ	P26358
TreeFamⁱ	TF328926

Family and domain databases

Gene3Dⁱ	2.30.30.490, 1 hit
InterProⁱ	View protein in InterPro IPR001025, BAH_dom IPR043151, BAH_sf IPR018117, C5_DNA_meth_AS IPR001525, C5_MeTfrase IPR031303, C5_meth_CS IPR022702, Cytosine_MeTrfase1_RFD IPR010506, DMAP1-bd IPR017198, DNMT1-like IPR029063, SAM-dependent_MTases IPR002857, Znf_CXXC
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01426, BAH, 2 hits PF06464, DMAP_binding, 1 hit PF00145, DNA_methylase, 1 hit PF12047, DNMT1-RFD, 1 hit PF02008, zf-CXXC, 1 hit
PIRSFⁱ	PIRSF037404, DNMT1, 1 hit
PRINTSⁱ	PR00105, C5METTRFRASE
SMARTⁱ	View protein in SMART SM00439, BAH, 2 hits SM01137, DMAP_binding, 1 hit
SUPFAMⁱ	SSF53335, SSF53335, 1 hit
PROSITEⁱ	View protein in PROSITE PS51038, BAH, 2 hits PS00094, C5_MTASE_1, 1 hit PS00095, C5_MTASE_2, 1 hit PS51912, DMAP1_BIND, 1 hit PS51679, SAM_MT_C5, 1 hit PS51058, ZF_CXXC, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 19 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P26358-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPARTAPARV PTLAVPAISL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH 
        60         70         80         90        100
EFLQTEIKNQ LCDLETKLRK EELSEEGYLA KVKSLLNKDL SLENGAHAYN 
       110        120        130        140        150
REVNGRLENG NQARSEARRV GMADANSPPK PLSKPRTPRR SKSDGEAKPE 
       160        170        180        190        200
PSPSPRITRK STRQTTITSH FAKGPAKRKP QEESERAKSD ESIKEEDKDQ 
       210        220        230        240        250
DEKRRRVTSR ERVARPLPAE EPERAKSGTR TEKEEERDEK EEKRLRSQTK 
       260        270        280        290        300
EPTPKQKLKE EPDREARAGV QADEDEDGDE KDEKKHRSQP KDLAAKRRPE 
       310        320        330        340        350
EKEPEKVNPQ ISDEKDEDEK EEKRRKTTPK EPTEKKMARA KTVMNSKTHP 
       360        370        380        390        400
PKCIQCGQYL DDPDLKYGQH PPDAVDEPQM LTNEKLSIFD ANESGFESYE 
       410        420        430        440        450
ALPQHKLTCF SVYCKHGHLC PIDTGLIEKN IELFFSGSAK PIYDDDPSLE 
       460        470        480        490        500
GGVNGKNLGP INEWWITGFD GGEKALIGFS TSFAEYILMD PSPEYAPIFG 
       510        520        530        540        550
LMQEKIYISK IVVEFLQSNS DSTYEDLINK IETTVPPSGL NLNRFTEDSL 
       560        570        580        590        600
LRHAQFVVEQ VESYDEAGDS DEQPIFLTPC MRDLIKLAGV TLGQRRAQAR 
       610        620        630        640        650
RQTIRHSTRE KDRGPTKATT TKLVYQIFDT FFAEQIEKDD REDKENAFKR 
       660        670        680        690        700
RRCGVCEVCQ QPECGKCKAC KDMVKFGGSG RSKQACQERR CPNMAMKEAD 
       710        720        730        740        750
DDEEVDDNIP EMPSPKKMHQ GKKKKQNKNR ISWVGEAVKT DGKKSYYKKV 
       760        770        780        790        800
CIDAETLEVG DCVSVIPDDS SKPLYLARVT ALWEDSSNGQ MFHAHWFCAG 
       810        820        830        840        850
TDTVLGATSD PLELFLVDEC EDMQLSYIHS KVKVIYKAPS ENWAMEGGMD 
       860        870        880        890        900
PESLLEGDDG KTYFYQLWYD QDYARFESPP KTQPTEDNKF KFCVSCARLA 
       910        920        930        940        950
EMRQKEIPRV LEQLEDLDSR VLYYSATKNG ILYRVGDGVY LPPEAFTFNI 
       960        970        980        990       1000
KLSSPVKRPR KEPVDEDLYP EHYRKYSDYI KGSNLDAPEP YRIGRIKEIF 
      1010       1020       1030       1040       1050
CPKKSNGRPN ETDIKIRVNK FYRPENTHKS TPASYHADIN LLYWSDEEAV 
      1060       1070       1080       1090       1100
VDFKAVQGRC TVEYGEDLPE CVQVYSMGGP NRFYFLEAYN AKSKSFEDPP 
      1110       1120       1130       1140       1150
NHARSPGNKG KGKGKGKGKP KSQACEPSEP EIEIKLPKLR TLDVFSGCGG 
      1160       1170       1180       1190       1200
LSEGFHQAGI SDTLWAIEMW DPAAQAFRLN NPGSTVFTED CNILLKLVMA 
      1210       1220       1230       1240       1250
GETTNSRGQR LPQKGDVEML CGGPPCQGFS GMNRFNSRTY SKFKNSLVVS 
      1260       1270       1280       1290       1300
FLSYCDYYRP RFFLLENVRN FVSFKRSMVL KLTLRCLVRM GYQCTFGVLQ 
      1310       1320       1330       1340       1350
AGQYGVAQTR RRAIILAAAP GEKLPLFPEP LHVFAPRACQ LSVVVDDKKF 
      1360       1370       1380       1390       1400
VSNITRLSSG PFRTITVRDT MSDLPEVRNG ASALEISYNG EPQSWFQRQL 
      1410       1420       1430       1440       1450
RGAQYQPILR DHICKDMSAL VAARMRHIPL APGSDWRDLP NIEVRLSDGT 
      1460       1470       1480       1490       1500
MARKLRYTHH DRKNGRSSSG ALRGVCSCVE AGKACDPAAR QFNTLIPWCL 
      1510       1520       1530       1540       1550
PHTGNRHNHW AGLYGRLEWD GFFSTTVTNP EPMGKQGRVL HPEQHRVVSV 
      1560       1570       1580       1590       1600
RECARSQGFP DTYRLFGNIL DKHRQVGNAV PPPLAKAIGL EIKLCMLAKA 
      1610 
RESASAKIKE EEAAKD

Length:1,616

Mass (Da):183,165

Last modified:January 11, 2001 - v2

Checksum:ⁱ1E833192D22AFA5B

GO

Isoform 2 (identifier: P26358-2) [UniParc]FASTA Add to basket

Also known as: Dnmt1b

The sequence of this isoform differs from the canonical sequence as follows:
149-149: P → RSRDPPASASQVTGIRA

« Hide

        10         20         30         40         50
MPARTAPARV PTLAVPAISL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH 
        60         70         80         90        100
EFLQTEIKNQ LCDLETKLRK EELSEEGYLA KVKSLLNKDL SLENGAHAYN 
       110        120        130        140        150
REVNGRLENG NQARSEARRV GMADANSPPK PLSKPRTPRR SKSDGEAKRS 
       160        170        180        190        200
RDPPASASQV TGIRAEPSPS PRITRKSTRQ TTITSHFAKG PAKRKPQEES 
       210        220        230        240        250
ERAKSDESIK EEDKDQDEKR RRVTSRERVA RPLPAEEPER AKSGTRTEKE 
       260        270        280        290        300
EERDEKEEKR LRSQTKEPTP KQKLKEEPDR EARAGVQADE DEDGDEKDEK 
       310        320        330        340        350
KHRSQPKDLA AKRRPEEKEP EKVNPQISDE KDEDEKEEKR RKTTPKEPTE 
       360        370        380        390        400
KKMARAKTVM NSKTHPPKCI QCGQYLDDPD LKYGQHPPDA VDEPQMLTNE 
       410        420        430        440        450
KLSIFDANES GFESYEALPQ HKLTCFSVYC KHGHLCPIDT GLIEKNIELF 
       460        470        480        490        500
FSGSAKPIYD DDPSLEGGVN GKNLGPINEW WITGFDGGEK ALIGFSTSFA 
       510        520        530        540        550
EYILMDPSPE YAPIFGLMQE KIYISKIVVE FLQSNSDSTY EDLINKIETT 
       560        570        580        590        600
VPPSGLNLNR FTEDSLLRHA QFVVEQVESY DEAGDSDEQP IFLTPCMRDL 
       610        620        630        640        650
IKLAGVTLGQ RRAQARRQTI RHSTREKDRG PTKATTTKLV YQIFDTFFAE 
       660        670        680        690        700
QIEKDDREDK ENAFKRRRCG VCEVCQQPEC GKCKACKDMV KFGGSGRSKQ 
       710        720        730        740        750
ACQERRCPNM AMKEADDDEE VDDNIPEMPS PKKMHQGKKK KQNKNRISWV 
       760        770        780        790        800
GEAVKTDGKK SYYKKVCIDA ETLEVGDCVS VIPDDSSKPL YLARVTALWE 
       810        820        830        840        850
DSSNGQMFHA HWFCAGTDTV LGATSDPLEL FLVDECEDMQ LSYIHSKVKV 
       860        870        880        890        900
IYKAPSENWA MEGGMDPESL LEGDDGKTYF YQLWYDQDYA RFESPPKTQP 
       910        920        930        940        950
TEDNKFKFCV SCARLAEMRQ KEIPRVLEQL EDLDSRVLYY SATKNGILYR 
       960        970        980        990       1000
VGDGVYLPPE AFTFNIKLSS PVKRPRKEPV DEDLYPEHYR KYSDYIKGSN 
      1010       1020       1030       1040       1050
LDAPEPYRIG RIKEIFCPKK SNGRPNETDI KIRVNKFYRP ENTHKSTPAS 
      1060       1070       1080       1090       1100
YHADINLLYW SDEEAVVDFK AVQGRCTVEY GEDLPECVQV YSMGGPNRFY 
      1110       1120       1130       1140       1150
FLEAYNAKSK SFEDPPNHAR SPGNKGKGKG KGKGKPKSQA CEPSEPEIEI 
      1160       1170       1180       1190       1200
KLPKLRTLDV FSGCGGLSEG FHQAGISDTL WAIEMWDPAA QAFRLNNPGS 
      1210       1220       1230       1240       1250
TVFTEDCNIL LKLVMAGETT NSRGQRLPQK GDVEMLCGGP PCQGFSGMNR 
      1260       1270       1280       1290       1300
FNSRTYSKFK NSLVVSFLSY CDYYRPRFFL LENVRNFVSF KRSMVLKLTL 
      1310       1320       1330       1340       1350
RCLVRMGYQC TFGVLQAGQY GVAQTRRRAI ILAAAPGEKL PLFPEPLHVF 
      1360       1370       1380       1390       1400
APRACQLSVV VDDKKFVSNI TRLSSGPFRT ITVRDTMSDL PEVRNGASAL 
      1410       1420       1430       1440       1450
EISYNGEPQS WFQRQLRGAQ YQPILRDHIC KDMSALVAAR MRHIPLAPGS 
      1460       1470       1480       1490       1500
DWRDLPNIEV RLSDGTMARK LRYTHHDRKN GRSSSGALRG VCSCVEAGKA 
      1510       1520       1530       1540       1550
CDPAARQFNT LIPWCLPHTG NRHNHWAGLY GRLEWDGFFS TTVTNPEPMG 
      1560       1570       1580       1590       1600
KQGRVLHPEQ HRVVSVRECA RSQGFPDTYR LFGNILDKHR QVGNAVPPPL 
      1610       1620       1630 
AKAIGLEIKL CMLAKARESA SAKIKEEEAA KD

Show »

Length:1,632

Mass (Da):184,819

Checksum:ⁱ650AA14F73A75649

GO

Isoform 3 (identifier: P26358-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-336: Missing.

« Hide

        10         20         30         40         50
MARAKTVMNS KTHPPKCIQC GQYLDDPDLK YGQHPPDAVD EPQMLTNEKL 
        60         70         80         90        100
SIFDANESGF ESYEALPQHK LTCFSVYCKH GHLCPIDTGL IEKNIELFFS 
       110        120        130        140        150
GSAKPIYDDD PSLEGGVNGK NLGPINEWWI TGFDGGEKAL IGFSTSFAEY 
       160        170        180        190        200
ILMDPSPEYA PIFGLMQEKI YISKIVVEFL QSNSDSTYED LINKIETTVP 
       210        220        230        240        250
PSGLNLNRFT EDSLLRHAQF VVEQVESYDE AGDSDEQPIF LTPCMRDLIK 
       260        270        280        290        300
LAGVTLGQRR AQARRQTIRH STREKDRGPT KATTTKLVYQ IFDTFFAEQI 
       310        320        330        340        350
EKDDREDKEN AFKRRRCGVC EVCQQPECGK CKACKDMVKF GGSGRSKQAC 
       360        370        380        390        400
QERRCPNMAM KEADDDEEVD DNIPEMPSPK KMHQGKKKKQ NKNRISWVGE 
       410        420        430        440        450
AVKTDGKKSY YKKVCIDAET LEVGDCVSVI PDDSSKPLYL ARVTALWEDS 
       460        470        480        490        500
SNGQMFHAHW FCAGTDTVLG ATSDPLELFL VDECEDMQLS YIHSKVKVIY 
       510        520        530        540        550
KAPSENWAME GGMDPESLLE GDDGKTYFYQ LWYDQDYARF ESPPKTQPTE 
       560        570        580        590        600
DNKFKFCVSC ARLAEMRQKE IPRVLEQLED LDSRVLYYSA TKNGILYRVG 
       610        620        630        640        650
DGVYLPPEAF TFNIKLSSPV KRPRKEPVDE DLYPEHYRKY SDYIKGSNLD 
       660        670        680        690        700
APEPYRIGRI KEIFCPKKSN GRPNETDIKI RVNKFYRPEN THKSTPASYH 
       710        720        730        740        750
ADINLLYWSD EEAVVDFKAV QGRCTVEYGE DLPECVQVYS MGGPNRFYFL 
       760        770        780        790        800
EAYNAKSKSF EDPPNHARSP GNKGKGKGKG KGKPKSQACE PSEPEIEIKL 
       810        820        830        840        850
PKLRTLDVFS GCGGLSEGFH QAGISDTLWA IEMWDPAAQA FRLNNPGSTV 
       860        870        880        890        900
FTEDCNILLK LVMAGETTNS RGQRLPQKGD VEMLCGGPPC QGFSGMNRFN 
       910        920        930        940        950
SRTYSKFKNS LVVSFLSYCD YYRPRFFLLE NVRNFVSFKR SMVLKLTLRC 
       960        970        980        990       1000
LVRMGYQCTF GVLQAGQYGV AQTRRRAIIL AAAPGEKLPL FPEPLHVFAP 
      1010       1020       1030       1040       1050
RACQLSVVVD DKKFVSNITR LSSGPFRTIT VRDTMSDLPE VRNGASALEI 
      1060       1070       1080       1090       1100
SYNGEPQSWF QRQLRGAQYQ PILRDHICKD MSALVAARMR HIPLAPGSDW 
      1110       1120       1130       1140       1150
RDLPNIEVRL SDGTMARKLR YTHHDRKNGR SSSGALRGVC SCVEAGKACD 
      1160       1170       1180       1190       1200
PAARQFNTLI PWCLPHTGNR HNHWAGLYGR LEWDGFFSTT VTNPEPMGKQ 
      1210       1220       1230       1240       1250
GRVLHPEQHR VVSVRECARS QGFPDTYRLF GNILDKHRQV GNAVPPPLAK 
      1260       1270       1280
AIGLEIKLCM LAKARESASA KIKEEEAAKD

Show »

Length:1,280

Mass (Da):144,465

Checksum:ⁱ70ECEE72AE313EE9

GO

Computationally mapped potential isoform sequencesⁱ

There are 19 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name	Protein names	Gene names	Length	Annotation

	A0A7I2V490	A0A7I2V490_HUMAN	DNA (cytosine-5)-methyltransferase DNA (cytosine-5)-methyltransferase, EC 2.1.1.37	DNMT1	1,658	Annotation score:
	A0A7I2V5D0	A0A7I2V5D0_HUMAN	DNA (cytosine-5)-methyltransferase DNA (cytosine-5)-methyltransferase, EC 2.1.1.37	DNMT1	1,655	Annotation score:
	A0A7I2V5F1	A0A7I2V5F1_HUMAN	DNA (cytosine-5)-methyltransferase DNA (cytosine-5)-methyltransferase, EC 2.1.1.37	DNMT1	1,580	Annotation score:
	A0A7I2YQA8	A0A7I2YQA8_HUMAN	DNA (cytosine-5)-methyltransferase DNA (cytosine-5)-methyltransferase, EC 2.1.1.37	DNMT1	1,577	Annotation score:
	A0A7I2YQQ0	A0A7I2YQQ0_HUMAN	DNA (cytosine-5)-methyltransferase DNA (cytosine-5)-methyltransferase, EC 2.1.1.37	DNMT1	1,613	Annotation score:
	A0A7I2V311	A0A7I2V311_HUMAN	DNA (cytosine-5)-methyltransferase ... DNA (cytosine-5)-methyltransferase 1, EC 2.1.1.37	DNMT1	1,150	Annotation score:
	A0A7I2V5F6	A0A7I2V5F6_HUMAN	DNA (cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase, EC 2.1.1.37	DNMT1	1,114	Annotation score:
	K7ENW7	K7ENW7_HUMAN	DNA (cytosine-5)-methyltransferase ... DNA (cytosine-5)-methyltransferase 1	DNMT1	389	Annotation score:
	K7EJL0	K7EJL0_HUMAN	DNA (cytosine-5)-methyltransferase ... DNA (cytosine-5)-methyltransferase 1	DNMT1	255	Annotation score:
	K7ENQ6	K7ENQ6_HUMAN	DNA (cytosine-5)-methyltransferase ... DNA (cytosine-5)-methyltransferase 1	DNMT1	119	Annotation score:
There are more potential isoformsShow all

Sequence cautionⁱ

The sequence AAD54507 differs from that shown. Reason: Erroneous gene model prediction.Curated

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_024605	97	H → R. Corresponds to variant dbSNP:rs16999593EnsemblClinVar.	1
Natural variantⁱVAR_051960	311	I → V. Corresponds to variant dbSNP:rs2228612Ensembl.	1
Natural variantⁱVAR_065965	490 – 491	DP → EY in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase. Corresponds to variant dbSNP:rs199473691Ensembl.	2
Natural variantⁱVAR_065966	495	Y → C in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase. 1 PublicationCorresponds to variant dbSNP:rs199473690Ensembl.	1
Natural variantⁱVAR_070055	554	A → V in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509392Ensembl.	1
Natural variantⁱVAR_070056	589	G → A in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509393Ensembl.	1
Natural variantⁱVAR_070057	590	V → F in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509391Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_005617	1 – 336	Missing in isoform 3. 1 PublicationAdd BLAST		336
Alternative sequenceⁱVSP_005618	149	P → RSRDPPASASQVTGIRA in isoform 2. 1 Publication		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X63692 mRNA Translation: CAA45219.1 AF180682 mRNA Translation: AAF23609.1 AC010077 Genomic DNA Translation: AAD54507.1 Sequence problems. AC011511 Genomic DNA No translation available. AC020931 Genomic DNA No translation available. BC126227 mRNA Translation: AAI26228.1 BC144093 mRNA Translation: AAI44094.1 AH008119 Genomic DNA Translation: AAD51619.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS12228.1 [P26358-1] CCDS45958.1 [P26358-2]
PIRⁱ	S22610
NCBI Reference Sequences More...RefSeqⁱ	NP_001124295.1, NM_001130823.2 [P26358-2] NP_001305659.1, NM_001318730.1 NP_001305660.1, NM_001318731.1 NP_001370.1, NM_001379.3 [P26358-1]

Genome annotation databases

Ensemblⁱ	ENST00000340748; ENSP00000345739; ENSG00000130816 [P26358-1] ENST00000359526; ENSP00000352516; ENSG00000130816 [P26358-2]
GeneIDⁱ	1786
KEGGⁱ	hsa:1786
UCSC genome browser More...UCSCⁱ	uc002mng.4, human [P26358-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P26358	DNA (cytosine-5)-methyltransferase		HUMAN		1678	UniRef100_P26358
DNA (cytosine-5)-methyltransferase 1		PANPA		1280
DNMT1 isoform 1 (Fragment)		PANTR		119
Isoform 3 of DNA (cytosine-5)-methyltransferase 1		HUMAN		1280
DNA (cytosine-5)-methyltransferase 1 (Fragment)		HUMAN		119
P26358-2	DNA (cytosine-5)-methyltransferase		HUMAN		1511	UniRef100_I6L9H2

Protein	Similar proteins		Species	Score	Length	Source
P26358	DNA (cytosine-5)-methyltransferase		HUMAN		1678	UniRef90_P26358
DNA (cytosine-5)-methyltransferase 1		PANPA		1280
DNMT1 isoform 1 (Fragment)		PANTR		119
DNA (cytosine-5)-methyltransferase		MACMU		1717
DNA (cytosine-5)-methyltransferase		MACFA		1717
+139

Protein	Similar proteins		Species	Score	Length	Source
P26358	DNA (cytosine-5)-methyltransferase 1	)	BOVIN		1611	UniRef50_P26358
DNA (cytosine-5)-methyltransferase		HUMAN		1678
DNA (cytosine-5)-methyltransferase 1		PANPA		1280
DNMT1 isoform 1 (Fragment)		PANTR		119
DNA (cytosine-5)-methyltransferase		MACMU		1717
+562

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X63692 mRNA Translation: CAA45219.1 AF180682 mRNA Translation: AAF23609.1 AC010077 Genomic DNA Translation: AAD54507.1 Sequence problems. AC011511 Genomic DNA No translation available. AC020931 Genomic DNA No translation available. BC126227 mRNA Translation: AAI26228.1 BC144093 mRNA Translation: AAI44094.1 AH008119 Genomic DNA Translation: AAD51619.1
CCDSⁱ	CCDS12228.1 [P26358-1] CCDS45958.1 [P26358-2]
PIRⁱ	S22610
RefSeqⁱ	NP_001124295.1, NM_001130823.2 [P26358-2] NP_001305659.1, NM_001318730.1 NP_001305660.1, NM_001318731.1 NP_001370.1, NM_001379.3 [P26358-1]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3EPZ	X-ray	2.31	A/B	351-600	[»]
	3PTA	X-ray	3.60	A	646-1600	[»]
	3SWR	X-ray	2.49	A	601-1600	[»]
	4WXX	X-ray	2.62	A/B	351-1600	[»]
	4YOC	X-ray	2.92	A	600-1600	[»]
	4Z96	X-ray	2.85	C	1098-1129	[»]
	4Z97	X-ray	3.00	C	1098-1129	[»]
	5WVO	X-ray	2.00	C	351-600	[»]
	5YDR	X-ray	2.00	B	351-599	[»]
	6K3A	X-ray	2.30	B/D/F	161-180	[»]
SMRⁱ	P26358
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	108123, 164 interactors
CORUMⁱ	P26358
DIPⁱ	DIP-39693N
ELMⁱ	P26358
IntActⁱ	P26358, 51 interactors
MINTⁱ	P26358
STRINGⁱ	9606.ENSP00000352516

Chemistry databases

BindingDBⁱ	P26358
ChEMBLⁱ	CHEMBL1993
DrugBankⁱ	DB00928, Azacitidine DB01262, Decitabine DB12116, Epigallocatechin gallate DB01099, Flucytosine DB05668, Palifosfamide DB01035, Procainamide DB00721, Procaine
DrugCentralⁱ	P26358
GuidetoPHARMACOLOGYⁱ	2605

Protein family/group databases

REBASEⁱ	1161, M.HsaDnmt1A 4240, M.HsaDnmt1B

REBASEⁱ

1161, M.HsaDnmt1A
4240, M.HsaDnmt1B

PTM databases

GlyGenⁱ	P26358, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	P26358
PhosphoSitePlusⁱ	P26358
SwissPalmⁱ	P26358

Genetic variation databases

BioMutaⁱ	DNMT1
DMDMⁱ	12231019

Proteomic databases

EPDⁱ	P26358
jPOSTⁱ	P26358
MassIVEⁱ	P26358
MaxQBⁱ	P26358
PaxDbⁱ	P26358
PeptideAtlasⁱ	P26358
PRIDEⁱ	P26358
ProteomicsDBⁱ	54320 [P26358-1] 54321 [P26358-2] 54322 [P26358-3]

Protocols and materials databases

ABCDⁱ	P26358, 1 sequenced antibody
Antibodypediaⁱ	1052, 1583 antibodies
The DNASU plasmid repository More...DNASUⁱ	1786

Genome annotation databases

Ensemblⁱ	ENST00000340748; ENSP00000345739; ENSG00000130816 [P26358-1] ENST00000359526; ENSP00000352516; ENSG00000130816 [P26358-2]
GeneIDⁱ	1786
KEGGⁱ	hsa:1786
UCSCⁱ	uc002mng.4, human [P26358-1]

Organism-specific databases

CTDⁱ	1786
DisGeNETⁱ	1786
GeneCardsⁱ	DNMT1
GeneReviewsⁱ	DNMT1
HGNCⁱ	HGNC:2976, DNMT1
HPAⁱ	ENSG00000130816, Low tissue specificity
MalaCardsⁱ	DNMT1
MIMⁱ	126375, gene 604121, phenotype 614116, phenotype
neXtProtⁱ	NX_P26358
OpenTargetsⁱ	ENSG00000130816
Orphanetⁱ	314404, Autosomal dominant cerebellar ataxia-deafness-narcolepsy syndrome 456318, Hereditary sensory neuropathy-deafness-dementia syndrome
PharmGKBⁱ	PA27443
VEuPathDBⁱ	HostDB:ENSG00000130816
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG502QPKK, Eukaryota
GeneTreeⁱ	ENSGT00390000005100
HOGENOMⁱ	CLU_003040_0_0_1
InParanoidⁱ	P26358
OMAⁱ	RDHVCKD
PhylomeDBⁱ	P26358
TreeFamⁱ	TF328926

Enzyme and pathway databases

BRENDAⁱ	2.1.1.37, 2681
PathwayCommonsⁱ	P26358
Reactomeⁱ	R-HSA-212300, PRC2 methylates histones and DNA R-HSA-427413, NoRC negatively regulates rRNA expression R-HSA-4655427, SUMOylation of DNA methylation proteins R-HSA-5334118, DNA methylation R-HSA-9710421, Defective pyroptosis
SIGNORⁱ	P26358

Miscellaneous databases

BioGRID-ORCSⁱ	1786, 329 hits in 1034 CRISPR screens
ChiTaRSⁱ	DNMT1, human
EvolutionaryTraceⁱ	P26358
GeneWikiⁱ	DNMT1
GenomeRNAiⁱ	1786
Pharosⁱ	P26358, Tclin
Protein Ontology More...PROⁱ	PR:P26358
RNActⁱ	P26358, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000130816, Expressed in oocyte and 227 other tissues
ExpressionAtlasⁱ	P26358, baseline and differential
Genevisibleⁱ	P26358, HS

Family and domain databases

Gene3Dⁱ	2.30.30.490, 1 hit
InterProⁱ	View protein in InterPro IPR001025, BAH_dom IPR043151, BAH_sf IPR018117, C5_DNA_meth_AS IPR001525, C5_MeTfrase IPR031303, C5_meth_CS IPR022702, Cytosine_MeTrfase1_RFD IPR010506, DMAP1-bd IPR017198, DNMT1-like IPR029063, SAM-dependent_MTases IPR002857, Znf_CXXC
Pfamⁱ	View protein in Pfam PF01426, BAH, 2 hits PF06464, DMAP_binding, 1 hit PF00145, DNA_methylase, 1 hit PF12047, DNMT1-RFD, 1 hit PF02008, zf-CXXC, 1 hit
PIRSFⁱ	PIRSF037404, DNMT1, 1 hit
PRINTSⁱ	PR00105, C5METTRFRASE
SMARTⁱ	View protein in SMART SM00439, BAH, 2 hits SM01137, DMAP_binding, 1 hit
SUPFAMⁱ	SSF53335, SSF53335, 1 hit
PROSITEⁱ	View protein in PROSITE PS51038, BAH, 2 hits PS00094, C5_MTASE_1, 1 hit PS00095, C5_MTASE_2, 1 hit PS51912, DMAP1_BIND, 1 hit PS51679, SAM_MT_C5, 1 hit PS51058, ZF_CXXC, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DNMT1_HUMAN
Accessionⁱ	P26358Primary (citable) accession number: P26358 Secondary accession number(s): A0AV63 , B7ZLW6, Q9UHG5, Q9ULA2, Q9UMZ6
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
	Last sequence update:	January 11, 2001
	Last modified:	September 29, 2021
	This is version 231 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

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UniProtKB - P26358 (DNMT1_HUMAN)

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DNA (cytosine-5)-methyltransferase 1

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P26358

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Zinc finger

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<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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Keywords - Coding sequence diversityi

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

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Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

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Keywords - PTMⁱ

Expressionⁱ

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Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ