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UniProtKB - P26358 (DNMT1_HUMAN)

Entry version 219 (16 Oct 2019)
Sequence version 2 (11 Jan 2001)
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Protein

DNA (cytosine-5)-methyltransferase 1

Gene

DNMT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi353Zinc1
Metal bindingi356Zinc1
Metal bindingi414Zinc1
Metal bindingi418Zinc1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei509Important for activityBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1146S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei1191S-adenosyl-L-methionineCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei12261
Binding sitei1578S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication1
Binding sitei1580S-adenosyl-L-methionine; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri646 – 692CXXC-typePROSITE-ProRule annotationAdd BLAST47

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Chromatin regulator, DNA-binding, Methyltransferase, Repressor, Transferase
Biological processTranscription, Transcription regulation
LigandMetal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.1.1.37 2681

Reactome - a knowledgebase of biological pathways and processes

More...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

SIGNOR Signaling Network Open Resource

More...SIGNORi		P26358

Protein family/group databases

Restriction enzymes and methylases database

More...REBASEi		1161 M.HsaDnmt1A

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DNMT1
Synonyms:AIM, CXXC9, DNMT
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:2976 DNMT1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		126375 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P26358

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Neuropathy, hereditary sensory, 1E (HSN1E)1 Publication
The disease is caused by mutations 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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065965490 – 491DP → 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_065966495Y → 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 mutations 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 keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070055554A → V in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509392Ensembl.1
Natural variantiVAR_070056589G → A in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509393Ensembl.1
Natural variantiVAR_070057590V → F in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509391Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi163R → A: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi164Q → A: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi166T → A: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi167I → A: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi169S → A: No loss of interaction with PCNA. 1 Publication1
Mutagenesisi170H → V: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi171F → V: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi172A → S: No loss of interaction with PCNA. 1 Publication1
Mutagenesisi173K → A: No loss of interaction with PCNA. 1 Publication1
Mutagenesisi653C → G: Reduces activity about 10-fold; when associated with G-656; G-659; G-664; G-667 and G-670. 1 Publication1
Mutagenesisi656C → G: Reduces activity about 10-fold; when associated with G-653; G-659; G-664; G-667 and G-670. 1 Publication1
Mutagenesisi659C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-664; G-667 and G-670. 1 Publication1
Mutagenesisi664C → F: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-667 and G-670. 1 Publication1
Mutagenesisi667C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-670. 1 Publication1
Mutagenesisi670C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-667. 1 Publication1
Mutagenesisi1226C → A: Loss of activity. 1 Publication1

Keywords - Diseasei

Deafness, Disease mutation, Neuropathy

Organism-specific databases

DisGeNET

More...DisGeNETi		1786

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		DNMT1

MalaCards human disease database

More...MalaCardsi		DNMT1
MIMi604121 phenotype
614116 phenotype

Open Targets

More...OpenTargetsi		ENSG00000130816

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		314404 Autosomal dominant cerebellar ataxia-deafness-narcolepsy syndrome
456318 Hereditary sensory neuropathy-deafness-dementia syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27443

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P26358

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1993

Drug and drug target database

More...DrugBanki		DB00928 Azacitidine
DB01262 Decitabine
DB12116 Epigallocatechin gallate
DB01099 Flucytosine
DB05668 Palifosfamide
DB01035 Procainamide

DrugCentral

More...DrugCentrali		P26358

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2605

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		DNMT1

Domain mapping of disease mutations (DMDM)

More...DMDMi		12231019

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000880341 – 1616DNA (cytosine-5)-methyltransferase 1Add BLAST1616

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei70N6,N6-dimethyllysine1 Publication1
Modified residuei127PhosphoserineCombined sources1
Modified residuei133PhosphoserineCombined sources1
Modified residuei137PhosphothreonineCombined sources1
Modified residuei141PhosphoserineBy similarity1
Modified residuei142N6-methyllysine; by SETD71 Publication1
Modified residuei143Phosphoserine; by PKB/AKT1Combined sources1 Publication1
Modified residuei152PhosphoserineCombined sources1
Modified residuei154PhosphoserineCombined sources1 Publication1
Modified residuei160N6-acetyllysine1 Publication1
Modified residuei166PhosphothreonineCombined sources1
Modified residuei173N6-acetyllysineCombined sources1
Modified residuei188N6-acetyllysine1 Publication1
Modified residuei259N6-acetyllysine; alternate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki259Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei312PhosphoserineCombined sources1
Modified residuei366N6-acetyllysine1 Publication1
Modified residuei394PhosphoserineCombined sources1
Modified residuei398PhosphoserineCombined sources1
Modified residuei509PhosphoserineBy similarity1
Modified residuei549PhosphoserineCombined sources1
Modified residuei714PhosphoserineCombined sources1
Modified residuei732PhosphoserineCombined sources1
Modified residuei749N6-acetyllysine1 Publication1
Modified residuei878PhosphoserineCombined sources1
Modified residuei891N6-acetyllysine1 Publication1
Modified residuei957N6-acetyllysine1 Publication1
Modified residuei961N6-acetyllysine1 Publication1
Modified residuei975N6-acetyllysine1 Publication1
Modified residuei1054N6-acetyllysine1 Publication1
Modified residuei1111N6-acetyllysineCombined sources1 Publication1
Modified residuei1113N6-acetyllysineCombined sources1 Publication1
Modified residuei1115N6-acetyllysineCombined sources1 Publication1
Modified residuei1117N6-acetyllysine; by EHMT21 Publication1
Modified residuei1119N6-acetyllysineBy similarity1
Modified residuei1121N6-acetyllysineBy similarity1
Modified residuei1349N6-acetyllysine1 Publication1
Modified residuei1415N6-acetyllysine1 Publication1
Cross-linki1609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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
Methylation at Lys-142 by SETD7 promotes DNMT1 proteasomal degradation.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

Encyclopedia of Proteome Dynamics

More...EPDi		P26358

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P26358

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P26358

MaxQB - The MaxQuant DataBase

More...MaxQBi		P26358

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P26358

PeptideAtlas

More...PeptideAtlasi		P26358

PRoteomics IDEntifications database

More...PRIDEi		P26358

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		54320 [P26358-1]
54321 [P26358-2]
54322 [P26358-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P26358

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P26358

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P26358

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000130816 Expressed in 215 organ(s), highest expression level in oocyte

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P26358 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P26358 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB005876
HPA002694

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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).

By similarity10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108123, 122 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P26358

Database of interacting proteins

More...DIPi		DIP-39693N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P26358

Protein interaction database and analysis system

More...IntActi		P26358, 40 interactors

Molecular INTeraction database

More...MINTi		P26358

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000352516

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P26358

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11616
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P26358

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P26358

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini18 – 103DMAP-interactionAdd BLAST86
Domaini755 – 880BAH 1PROSITE-ProRule annotationAdd BLAST126
Domaini972 – 1100BAH 2PROSITE-ProRule annotationAdd BLAST129
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati1109 – 111012
Repeati1111 – 111222
Repeati1113 – 111432
Repeati1115 – 111642
Repeati1117 – 111852
Repeati1119 – 11206; approximate2
Domaini1139 – 1599SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd BLAST461

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 336Interaction with the PRC2/EED-EZH2 complexBy similarityAdd BLAST336
Regioni1 – 148Interaction with DNMT3A1 PublicationAdd BLAST148
Regioni1 – 120Interaction with DMAP11 PublicationAdd BLAST120
Regioni149 – 217Interaction with DNMT3B1 PublicationAdd BLAST69
Regioni163 – 174Interaction with PCNA1 PublicationAdd BLAST12
Regioni308 – 606Interaction with the PRC2/EED-EZH2 complexBy similarityAdd BLAST299
Regioni310 – 502HomodimerizationAdd BLAST193
Regioni331 – 550DNA replication foci-targeting sequenceBy similarityAdd BLAST220
Regioni651 – 697Required for activityAdd BLAST47
Regioni693 – 754Autoinhibitory linkerAdd BLAST62
Regioni1109 – 11206 X 2 AA tandem repeats of K-GAdd BLAST12
Regioni1121 – 1616Interaction with the PRC2/EED-EZH2 complexBy similarityAdd BLAST496
Regioni1139 – 1616CatalyticAdd BLAST478
Regioni1150 – 1151S-adenosyl-L-methionine bindingBy similarity2
Regioni1168 – 1169S-adenosyl-L-methionine bindingCombined sources1 Publication2
Regioni1190 – 1191S-adenosyl-L-methionine bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi177 – 205Nuclear localization signalSequence analysisAdd BLAST29

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri646 – 692CXXC-typePROSITE-ProRule annotationAdd BLAST47

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IF68 Eukaryota
COG0270 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000005100

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000082497

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P26358

KEGG Orthology (KO)

More...KOi		K00558

Identification of Orthologs from Complete Genome Data

More...OMAi		HLCAFDT

Database of Orthologous Groups

More...OrthoDBi		898916at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P26358

TreeFam database of animal gene trees

More...TreeFami		TF328926

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001025 BAH_dom
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

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF037404 DNMT1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00105 C5METTRFRASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00439 BAH, 2 hits
SM01137 DMAP_binding, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53335 SSF53335, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51038 BAH, 2 hits
PS00094 C5_MTASE_1, 1 hit
PS00095 C5_MTASE_2, 1 hit
PS51679 SAM_MT_C5, 1 hit
PS51058 ZF_CXXC, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 10 potential isoforms that are computationally mapped.Show allAlign All

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

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1E833192D22AFA5B
GO
Isoform 2 (identifier: P26358-2) [UniParc]FASTAAdd to basket
Also known as: Dnmt1b

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

Show »
Length:1,632
Mass (Da):184,819
Checksum:i650AA14F73A75649
GO
Isoform 3 (identifier: P26358-3) [UniParc]FASTAAdd to basket

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

Show »
Length:1,280
Mass (Da):144,465
Checksum:i70ECEE72AE313EE9
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7ENW7K7ENW7_HUMAN
DNA (cytosine-5)-methyltransferase ...
DNMT1
389Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ERQ1K7ERQ1_HUMAN
DNA (cytosine-5)-methyltransferase ...
DNMT1
71Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EJL0K7EJL0_HUMAN
DNA (cytosine-5)-methyltransferase ...
DNMT1
255Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ELB1K7ELB1_HUMAN
DNA (cytosine-5)-methyltransferase ...
DNMT1
94Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ENQ6K7ENQ6_HUMAN
DNA (cytosine-5)-methyltransferase ...
DNMT1
119Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7ER10K7ER10_HUMAN
DNA (cytosine-5)-methyltransferase ...
DNMT1
77Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EKC3K7EKC3_HUMAN
DNA (cytosine-5)-methyltransferase ...
DNMT1
25Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EMU8K7EMU8_HUMAN
DNA (cytosine-5)-methyltransferase ...
DNMT1
89Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EIZ6K7EIZ6_HUMAN
DNA (cytosine-5)-methyltransferase ...
DNMT1
40Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EP77K7EP77_HUMAN
DNA (cytosine-5)-methyltransferase ...
DNMT1
55Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<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

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02460597H → R. Corresponds to variant dbSNP:rs16999593EnsemblClinVar.1
Natural variantiVAR_051960311I → V. Corresponds to variant dbSNP:rs2228612Ensembl.1
Natural variantiVAR_065965490 – 491DP → 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_065966495Y → 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_070055554A → V in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509392Ensembl.1
Natural variantiVAR_070056589G → A in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509393Ensembl.1
Natural variantiVAR_070057590V → F in ADCADN. 1 PublicationCorresponds to variant dbSNP:rs397509391Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0056171 – 336Missing in isoform 3. 1 PublicationAdd BLAST336
Alternative sequenceiVSP_005618149P → RSRDPPASASQVTGIRA in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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]

Protein sequence database of the Protein Information Resource

More...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

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000340748; ENSP00000345739; ENSG00000130816 [P26358-1]
ENST00000359526; ENSP00000352516; ENSG00000130816 [P26358-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1786

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:1786

UCSC genome browser

More...UCSCi		uc002mng.4 human [P26358-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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
CCDSiCCDS12228.1 [P26358-1]
CCDS45958.1 [P26358-2]
PIRiS22610
RefSeqiNP_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 entryMethodResolution (Å)ChainPositionsPDBsum
3EPZX-ray2.31A/B351-600[»]
3PTAX-ray3.60A646-1600[»]
3SWRX-ray2.49A601-1600[»]
4WXXX-ray2.62A/B351-1600[»]
4YOCX-ray2.92A600-1600[»]
4Z96X-ray2.85C1098-1129[»]
4Z97X-ray3.00C1098-1129[»]
5WVOX-ray2.00C351-600[»]
5YDRX-ray2.00B351-599[»]
SMRiP26358
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi108123, 122 interactors
CORUMiP26358
DIPiDIP-39693N
ELMiP26358
IntActiP26358, 40 interactors
MINTiP26358
STRINGi9606.ENSP00000352516

Chemistry databases

BindingDBiP26358
ChEMBLiCHEMBL1993
DrugBankiDB00928 Azacitidine
DB01262 Decitabine
DB12116 Epigallocatechin gallate
DB01099 Flucytosine
DB05668 Palifosfamide
DB01035 Procainamide
DrugCentraliP26358
GuidetoPHARMACOLOGYi2605

Protein family/group databases

REBASEi1161 M.HsaDnmt1A

PTM databases

iPTMnetiP26358
PhosphoSitePlusiP26358
SwissPalmiP26358

Polymorphism and mutation databases

BioMutaiDNMT1
DMDMi12231019

Proteomic databases

EPDiP26358
jPOSTiP26358
MassIVEiP26358
MaxQBiP26358
PaxDbiP26358
PeptideAtlasiP26358
PRIDEiP26358
ProteomicsDBi54320 [P26358-1]
54321 [P26358-2]
54322 [P26358-3]

Genome annotation databases

EnsembliENST00000340748; ENSP00000345739; ENSG00000130816 [P26358-1]
ENST00000359526; ENSP00000352516; ENSG00000130816 [P26358-2]
GeneIDi1786
KEGGihsa:1786
UCSCiuc002mng.4 human [P26358-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1786
DisGeNETi1786

GeneCards: human genes, protein and diseases

More...GeneCardsi		DNMT1
GeneReviewsiDNMT1
HGNCiHGNC:2976 DNMT1
HPAiCAB005876
HPA002694
MalaCardsiDNMT1
MIMi126375 gene
604121 phenotype
614116 phenotype
neXtProtiNX_P26358
OpenTargetsiENSG00000130816
Orphaneti314404 Autosomal dominant cerebellar ataxia-deafness-narcolepsy syndrome
456318 Hereditary sensory neuropathy-deafness-dementia syndrome
PharmGKBiPA27443

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IF68 Eukaryota
COG0270 LUCA
GeneTreeiENSGT00390000005100
HOGENOMiHOG000082497
InParanoidiP26358
KOiK00558
OMAiHLCAFDT
OrthoDBi898916at2759
PhylomeDBiP26358
TreeFamiTF328926

Enzyme and pathway databases

BRENDAi2.1.1.37 2681
ReactomeiR-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
SIGNORiP26358

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		DNMT1 human
EvolutionaryTraceiP26358

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		DNMT1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		1786
PharosiP26358

Protein Ontology

More...PROi		PR:P26358

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000130816 Expressed in 215 organ(s), highest expression level in oocyte
ExpressionAtlasiP26358 baseline and differential
GenevisibleiP26358 HS

Family and domain databases

InterProiView protein in InterPro
IPR001025 BAH_dom
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
PfamiView 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
PIRSFiPIRSF037404 DNMT1, 1 hit
PRINTSiPR00105 C5METTRFRASE
SMARTiView protein in SMART
SM00439 BAH, 2 hits
SM01137 DMAP_binding, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51038 BAH, 2 hits
PS00094 C5_MTASE_1, 1 hit
PS00095 C5_MTASE_2, 1 hit
PS51679 SAM_MT_C5, 1 hit
PS51058 ZF_CXXC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDNMT1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P26358
Secondary accession number(s): A0AV63
, B7ZLW6, Q9UHG5, Q9ULA2, Q9UMZ6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 11, 2001
Last modified: October 16, 2019
This is version 219 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
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