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Protein

DNA (cytosine-5)-methyltransferase 1

Gene

Dnmt1

Organism
Mus musculus (Mouse)
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 (By similarity). Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (By similarity). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (By similarity). Promotes tumor growth (By similarity).By similarity3 Publications

Miscellaneous

There are three 5' exons, one specific to the oocyte (1c), one specific to the pachytene spermatocyte and also found in skeletal muscle (1b) and one found in somatic cells (1a). Three different mRNAs can be produced which give rise to two different translation products: isoform 1 (mRNAs-1a) and isoform 2 (mRNA-1b or -1c). Association of DNMT1 with the replication machinery is not strictly required for maintaining global methylation but still enhances methylation efficiency by 2-fold. Pre-existing cytosine methylation at CpG and non-CpG sites enhances methylation activity.

<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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Allosterically regulated. The binding of 5-methylcytosine-containing DNA to the N-terminal parts of DNMT1 causes an allosteric activation of the catalytic domain by a direct interaction of its Zn-binding domain with the catalytic domain.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi359ZincBy similarity1
Metal bindingi362ZincBy similarity1
Metal bindingi420ZincBy similarity1
Metal bindingi424ZincBy similarity1
<p>This subsection of the ‘Function’ 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 sitei1149S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication1
<p>This subsection of the ‘Function’ 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 sitei12291 Publication1
Binding sitei1582S-adenosyl-L-methionine; via amide nitrogenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 fingeri649 – 695CXXC-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

GO - Biological processi

<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, Allosteric enzyme, 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 3474

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-MMU-212300 PRC2 methylates histones and DNA
R-MMU-4655427 SUMOylation of DNA methylation proteins

Protein family/group databases

Restriction enzymes and methylases database

More...
REBASEi
2844 M.MmuDnmt1

<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
Short name:
Met-1
Alternative name(s):
DNA methyltransferase MmuI
Short name:
DNA MTase MmuI
Short name:
M.MmuI
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:Dnmt, Met1, Uim
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 9

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:94912 Dnmt1

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, 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

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>Mutagenesisi162Q → E: Abolishes interaction with PCNA. No effect on activity. 1 Publication1
Mutagenesisi169F → S: Abolishes interaction with PCNA. No effect on activity. 1 Publication1
Mutagenesisi515S → A: Loss of activity. No effect on DNA-binding capacity. 1 Publication1
Mutagenesisi515S → E: Slightly reduces activity. 1 Publication1
Mutagenesisi1229C → W: Loss of activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3351195

<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_00000880351 – 1620DNA (cytosine-5)-methyltransferase 1Add BLAST1620

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 residuei15PhosphoserineCombined sources1
Modified residuei70N6,N6-dimethyllysine; by EHMT2By similarity1
Modified residuei138PhosphoserineCombined sources1
Modified residuei139N6-methyllysine; by SETD7By similarity1
Modified residuei140PhosphoserineCombined sources1
Modified residuei146Phosphoserine; by CK1Combined sources1 Publication1
Modified residuei150PhosphoserineCombined sources1
Modified residuei152PhosphoserineCombined sources1
Modified residuei164PhosphothreonineBy similarity1
Modified residuei171N6-acetyllysineBy similarity1
Modified residuei240PhosphoserineCombined sources1
Modified residuei255N6-acetyllysine; alternateBy similarity1
<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-linki255Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei372N6-acetyllysineBy similarity1
Modified residuei515Phosphoserine2 Publications1
Modified residuei555PhosphoserineBy similarity1
Modified residuei713PhosphoserineCombined sources1
Modified residuei717PhosphoserineCombined sources1
Modified residuei735PhosphoserineBy similarity1
Modified residuei752N6-acetyllysineBy similarity1
Modified residuei882PhosphoserineBy similarity1
Modified residuei895N6-acetyllysineBy similarity1
Modified residuei961N6-acetyllysineBy similarity1
Modified residuei965N6-acetyllysineBy similarity1
Modified residuei979N6-acetyllysineBy similarity1
Modified residuei1114N6-acetyllysineBy similarity1
Modified residuei1116N6-acetyllysineBy similarity1
Modified residuei1118N6-acetyllysineBy similarity1
Modified residuei1120N6-acetyllysineBy similarity1
Modified residuei1122N6-acetyllysineCombined sources1
Modified residuei1124N6-acetyllysineCombined sources1
Modified residuei1352N6-acetyllysineBy similarity1
Modified residuei1418N6-acetyllysineBy similarity1
Cross-linki1611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

<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.By similarity
Phosphorylation at Ser-146 by CK1 reduces DNA-binding activity.3 Publications
Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates cell cycle G2/M transition. Deacetylation of Lys-1352 and Lys-1418 by SIRT1 increases methyltransferase activity (By similarity).By similarity
Phosphorylation of Ser-152 by CDKs is important for enzymatic activity and protein stability. Phosphorylation of Ser-140 by AKT1 prevents methylation by SETD7 therebye increasing DNMT1 stability (By similarity).By similarity
Methylation at Lys-139 by SETD7 promotes DNMT1 proteasomal degradation.By similarity
Ubiquitinated by UHRF1; interaction with USP7 counteracts ubiquitination by UHRF1 by promoting deubiquitination and preventing degradation by the proteasome.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P13864

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P13864

MaxQB - The MaxQuant DataBase

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MaxQBi
P13864

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

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PaxDbi
P13864

PeptideAtlas

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PeptideAtlasi
P13864

PRoteomics IDEntifications database

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PRIDEi
P13864

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P13864

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

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PhosphoSitePlusi
P13864

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P13864

<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

Isoform 1 is expressed in embryonic stem cells and in somatic tissues. Isoform 2 is expressed in oocytes, preimplantation embryos, testis and in skeletal muscle during myogenesis.

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

In germ cells, it is present at high levels in spermatogonia and spermatocytes until the pachytene stage, where it falls to undetectable levels. The transient drop at the pachytene stage coincides with the disappearance of the 5.2 kb mRNA and the accumulation of a larger 6.0 kb mRNA. Oocytes accumulate very large amounts of Dnmt1 protein during the growth phase.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000004099 Expressed in 435 organ(s), highest expression level in primary oocyte

CleanEx database of gene expression profiles

More...
CleanExi
MM_DNMT1

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P13864 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P13864 MM

<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 (By similarity). Forms a stable complex with E2F1, BB1 and HDAC1 (By similarity). 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 (By similarity). Interacts with UHRF1; promoting its recruitment to hemimethylated DNA (PubMed:21268065). Interacts with USP7, promoting its deubiquitination (PubMed:21268065). Interacts with BAZ2A/TIP5 (PubMed:16085498). Interacts with PCNA (By similarity). Interacts with MBD2 and MBD3 (By similarity). Interacts with DNMT3A and DNMT3B (By similarity). Interacts with UBC9 (By similarity). Interacts with HDAC1 (PubMed:10615135). Interacts with CSNK1D (PubMed:20192920).By similarity6 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

WithEntry#Exp.IntActNotes
Hdac1O091063EBI-301927,EBI-301912

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
199259, 26 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P13864

Protein interaction database and analysis system

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IntActi
P13864, 10 interactors

Molecular INTeraction database

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MINTi
P13864

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000004202

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P13864

<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

11620
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AV4X-ray2.75A291-1620[»]
3AV5X-ray3.25A291-1620[»]
3AV6X-ray3.09A291-1620[»]
3PT6X-ray3.00A/B650-1602[»]
3PT9X-ray2.50A731-1602[»]
4DA4X-ray2.60A/B731-1602[»]
5GUTX-ray2.10A731-1602[»]
5GUVX-ray3.08A731-1602[»]
5WY1X-ray3.27A291-1620[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P13864

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

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SMRi
P13864

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P13864

<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 – 106DMAP-interactionAdd BLAST89
Domaini758 – 884BAH 1PROSITE-ProRule annotationAdd BLAST127
Domaini976 – 1103BAH 2PROSITE-ProRule annotationAdd BLAST128
<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>Repeati1112 – 111312
Repeati1114 – 111522
Repeati1116 – 111732
Repeati1118 – 111942
Repeati1120 – 112152
Repeati1122 – 112362
Repeati1124 – 11257; approximate2
Domaini1142 – 1601SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd BLAST460

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 – 343Interaction with the PRC2/EED-EZH2 complexAdd BLAST343
Regioni1 – 145Interaction with DNMT3ABy similarityAdd BLAST145
Regioni1 – 120Interaction with DMAP11 PublicationAdd BLAST120
Regioni147 – 217Interaction with DNMT3BBy similarityAdd BLAST71
Regioni161 – 172Interaction with PCNAAdd BLAST12
Regioni305 – 609Interaction with the PRC2/EED-EZH2 complexAdd BLAST305
Regioni328 – 556DNA replication foci-targeting sequenceBy similarityAdd BLAST229
Regioni696 – 813Interaction with HDAC11 PublicationAdd BLAST118
Regioni696 – 757Autoinhibitory linkerAdd BLAST62
Regioni1112 – 11257 X 2 AA tandem repeats of K-GAdd BLAST14
Regioni1124 – 1620Interaction with the PRC2/EED-EZH2 complexAdd BLAST497
Regioni1142 – 1620CatalyticAdd BLAST479
Regioni1153 – 1154S-adenosyl-L-methionine bindingCombined sources1 Publication2
Regioni1171 – 1172S-adenosyl-L-methionine bindingCombined sources1 Publication2
Regioni1193 – 1194S-adenosyl-L-methionine bindingCombined sources1 Publication2

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>Motifi175 – 202Nuclear localization signalSequence analysisAdd BLAST28

<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 fingeri649 – 695CXXC-typePROSITE-ProRule annotationAdd BLAST47

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IF68 Eukaryota
COG0270 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000005100

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG051384

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P13864

KEGG Orthology (KO)

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KOi
K00558

Database of Orthologous Groups

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OrthoDBi
898916at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P13864

TreeFam database of animal gene trees

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TreeFami
TF328926

Family and domain databases

Integrated resource of protein families, domains and functional sites

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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

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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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)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 2 <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 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P13864-1) [UniParc]FASTAAdd to basket
Also known as: Long

This isoform has been chosen as the 'canonical' 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 PALASPAGSL PDHVRRRLKD LERDGLTEKE CVREKLNLLH
60 70 80 90 100
EFLQTEIKSQ LCDLETKLHK EELSEEGYLA KVKSLLNKDL SLENGTHTLT
110 120 130 140 150
QKANGCPANG SRPTWRAEMA DSNRSPRSRP KPRGPRRSKS DSDTLSVETS
160 170 180 190 200
PSSVATRRTT RQTTITAHFT KGPTKRKPKE ESEEGNSAES AAEERDQDKK
210 220 230 240 250
RRVVDTESGA AAAVEKLEEV TAGTQLGPEE PCEQEDDNRS LRRHTRELSL
260 270 280 290 300
RRKSKEDPDR EARPETHLDE DEDGKKDKRS SRPRSQPRDP AAKRRPKEAE
310 320 330 340 350
PEQVAPETPE DRDEDEREEK RRKTTRKKLE SHTVPVQSRS ERKAAQSKSV
360 370 380 390 400
IPKINSPKCP ECGQHLDDPN LKYQQHPEDA VDEPQMLTSE KLSIYDSTST
410 420 430 440 450
WFDTYEDSPM HRFTSFSVYC SRGHLCPVDT GLIEKNVELY FSGCAKAIHD
460 470 480 490 500
ENPSMEGGIN GKNLGPINQW WLSGFDGGEK VLIGFSTAFA EYILMEPSKE
510 520 530 540 550
YEPIFGLMQE KIYISKIVVE FLQNNPDAVY EDLINKIETT VPPSTINVNR
560 570 580 590 600
FTEDSLLRHA QFVVSQVESY DEAKDDDETP IFLSPCMRAL IHLAGVSLGQ
610 620 630 640 650
RRATRRVMGA TKEKDKAPTK ATTTKLVYQI FDTFFSEQIE KYDKEDKENA
660 670 680 690 700
MKRRRCGVCE VCQQPECGKC KACKDMVKFG GTGRSKQACL KRRCPNLAVK
710 720 730 740 750
EADDDEEADD DVSEMPSPKK LHQGKKKKQN KDRISWLGQP MKIEENRTYY
760 770 780 790 800
QKVSIDEEML EVGDCVSVIP DDSSKPLYLA RVTALWEDKN GQMMFHAHWF
810 820 830 840 850
CAGTDTVLGA TSDPLELFLV GECENMQLSY IHSKVKVIYK APSENWAMEG
860 870 880 890 900
GTDPETTLPG AEDGKTYFFQ LWYNQEYARF ESPPKTQPTE DNKHKFCLSC
910 920 930 940 950
IRLAELRQKE MPKVLEQIEE VDGRVYCSSI TKNGVVYRLG DSVYLPPEAF
960 970 980 990 1000
TFNIKVASPV KRPKKDPVNE TLYPEHYRKY SDYIKGSNLD APEPYRIGRI
1010 1020 1030 1040 1050
KEIHCGKKKG KVNEADIKLR LYKFYRPENT HRSYNGSYHT DINMLYWSDE
1060 1070 1080 1090 1100
EAVVNFSDVQ GRCTVEYGED LLESIQDYSQ GGPDRFYFLE AYNSKTKNFE
1110 1120 1130 1140 1150
DPPNHARSPG NKGKGKGKGK GKGKHQVSEP KEPEAAIKLP KLRTLDVFSG
1160 1170 1180 1190 1200
CGGLSEGFHQ AGISETLWAI EMWDPAAQAF RLNNPGTTVF TEDCNVLLKL
1210 1220 1230 1240 1250
VMAGEVTNSL GQRLPQKGDV EMLCGGPPCQ GFSGMNRFNS RTYSKFKNSL
1260 1270 1280 1290 1300
VVSFLSYCDY YRPRFFLLEN VRNFVSYRRS MVLKLTLRCL VRMGYQCTFG
1310 1320 1330 1340 1350
VLQAGQYGVA QTRRRAIILA AAPGEKLPLF PEPLHVFAPR ACQLSVVVDD
1360 1370 1380 1390 1400
KKFVSNITRL SSGPFRTITV RDTMSDLPEI QNGASNSEIP YNGEPLSWFQ
1410 1420 1430 1440 1450
RQLRGSHYQP ILRDHICKDM SPLVAARMRH IPLFPGSDWR DLPNIQVRLG
1460 1470 1480 1490 1500
DGVIAHKLQY TFHDVKNGYS STGALRGVCS CAEGKACDPE SRQFSTLIPW
1510 1520 1530 1540 1550
CLPHTGNRHN HWAGLYGRLE WDGFFSTTVT NPEPMGKQGR VLHPEQHRVV
1560 1570 1580 1590 1600
SVRECARSQG FPDSYRFFGN ILDRHRQVGN AVPPPLAKAI GLEIKLCLLS
1610 1620
SARESASAAV KAKEEAATKD
Length:1,620
Mass (Da):183,189
Last modified:February 21, 2002 - v5
<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:i4F9A98CEAF09F037
GO
Isoform 2 (identifier: P13864-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.

Show »
Length:1,502
Mass (Da):169,996
Checksum:i4364F6D494EA67E4
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3QNW0J3QNW0_MOUSE
DNA (cytosine-5)-methyltransferase
Dnmt1
1,501Annotation score:

Annotation score:3 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 AAC52900 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti146 – 147SV → F in CAA32910 (PubMed:3210246).Curated2
Sequence conflicti146 – 147SV → F in AAC40061 (PubMed:9449671).Curated2
Sequence conflicti299 – 309AEPEQVAPETP → VRARAGSSRDS in CAA32910 (PubMed:3210246).CuratedAdd BLAST11
Sequence conflicti299 – 309AEPEQVAPETP → VRARAGSSRDS in AAC40061 (PubMed:9449671).CuratedAdd BLAST11
Sequence conflicti936V → C in CAA32910 (PubMed:3210246).Curated1
Sequence conflicti936V → C in AAC40061 (PubMed:9449671).Curated1
Sequence conflicti947P → R in CAA32910 (PubMed:3210246).Curated1
Sequence conflicti947P → R in AAC40061 (PubMed:9449671).Curated1
Sequence conflicti969 – 976NETLYPEH → KENPVPRDT in CAA32910 (PubMed:3210246).Curated8
Sequence conflicti969 – 976NETLYPEH → KENPVPRDT in AAC40061 (PubMed:9449671).Curated8
Sequence conflicti987S → R in CAA32910 (PubMed:3210246).Curated1
Sequence conflicti987S → R in AAC40061 (PubMed:9449671).Curated1
Sequence conflicti1046Y → C in CAA32910 (PubMed:3210246).Curated1
Sequence conflicti1046Y → C in AAC40061 (PubMed:9449671).Curated1
Sequence conflicti1068G → R in CAA32910 (PubMed:3210246).Curated1
Sequence conflicti1068G → R in AAC40061 (PubMed:9449671).Curated1
Sequence conflicti1429R → P in CAA32910 (PubMed:3210246).Curated1
Sequence conflicti1429R → P in AAC40061 (PubMed:9449671).Curated1
Sequence conflicti1456H → D in CAA32910 (PubMed:3210246).Curated1
Sequence conflicti1456H → D in AAC40061 (PubMed:9449671).Curated1

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0056191 – 118Missing in isoform 2. 3 PublicationsAdd BLAST118

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X14805 mRNA Translation: CAA32910.1
AF175432 mRNA Translation: AAF97695.1
AF162282 mRNA Translation: AAF19352.1
AF175431
, AF175412, AF175413, AF175414, AF244089, AF244090, AF175416, AF175417, AF175418, AF175419, AF175420, AF175421, AF175422, AF175423, AF234317, AF175424, AF175425, AF175426, AF234318, AF175427, AF175428, AF175429, AF175430 Genomic DNA Translation: AAF60965.1
BC048148 mRNA Translation: AAH48148.2
AF036007 mRNA Translation: AAC40061.1
AF036008 Genomic DNA Translation: AAC53551.1
U70051 mRNA Translation: AAC52900.1 Different initiation.
AK013247 mRNA Translation: BAB28743.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS57654.1 [P13864-2]
CCDS57655.1 [P13864-1]

Protein sequence database of the Protein Information Resource

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PIRi
S01845

NCBI Reference Sequences

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RefSeqi
NP_001186360.2, NM_001199431.1 [P13864-1]
NP_001186361.1, NM_001199432.1
NP_001186362.1, NM_001199433.1 [P13864-2]
NP_001300940.1, NM_001314011.1
NP_034196.5, NM_010066.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.128580
Mm.485562

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000004202; ENSMUSP00000004202; ENSMUSG00000004099 [P13864-1]
ENSMUST00000216540; ENSMUSP00000150433; ENSMUSG00000004099 [P13864-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
13433

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:13433

UCSC genome browser

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UCSCi
uc009ojo.2 mouse [P13864-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14805 mRNA Translation: CAA32910.1
AF175432 mRNA Translation: AAF97695.1
AF162282 mRNA Translation: AAF19352.1
AF175431
, AF175412, AF175413, AF175414, AF244089, AF244090, AF175416, AF175417, AF175418, AF175419, AF175420, AF175421, AF175422, AF175423, AF234317, AF175424, AF175425, AF175426, AF234318, AF175427, AF175428, AF175429, AF175430 Genomic DNA Translation: AAF60965.1
BC048148 mRNA Translation: AAH48148.2
AF036007 mRNA Translation: AAC40061.1
AF036008 Genomic DNA Translation: AAC53551.1
U70051 mRNA Translation: AAC52900.1 Different initiation.
AK013247 mRNA Translation: BAB28743.1
CCDSiCCDS57654.1 [P13864-2]
CCDS57655.1 [P13864-1]
PIRiS01845
RefSeqiNP_001186360.2, NM_001199431.1 [P13864-1]
NP_001186361.1, NM_001199432.1
NP_001186362.1, NM_001199433.1 [P13864-2]
NP_001300940.1, NM_001314011.1
NP_034196.5, NM_010066.4
UniGeneiMm.128580
Mm.485562

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AV4X-ray2.75A291-1620[»]
3AV5X-ray3.25A291-1620[»]
3AV6X-ray3.09A291-1620[»]
3PT6X-ray3.00A/B650-1602[»]
3PT9X-ray2.50A731-1602[»]
4DA4X-ray2.60A/B731-1602[»]
5GUTX-ray2.10A731-1602[»]
5GUVX-ray3.08A731-1602[»]
5WY1X-ray3.27A291-1620[»]
ProteinModelPortaliP13864
SMRiP13864
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199259, 26 interactors
CORUMiP13864
IntActiP13864, 10 interactors
MINTiP13864
STRINGi10090.ENSMUSP00000004202

Chemistry databases

BindingDBiP13864
ChEMBLiCHEMBL3351195

Protein family/group databases

REBASEi2844 M.MmuDnmt1

PTM databases

iPTMnetiP13864
PhosphoSitePlusiP13864
SwissPalmiP13864

Proteomic databases

EPDiP13864
jPOSTiP13864
MaxQBiP13864
PaxDbiP13864
PeptideAtlasiP13864
PRIDEiP13864

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004202; ENSMUSP00000004202; ENSMUSG00000004099 [P13864-1]
ENSMUST00000216540; ENSMUSP00000150433; ENSMUSG00000004099 [P13864-2]
GeneIDi13433
KEGGimmu:13433
UCSCiuc009ojo.2 mouse [P13864-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1786
MGIiMGI:94912 Dnmt1

Phylogenomic databases

eggNOGiENOG410IF68 Eukaryota
COG0270 LUCA
GeneTreeiENSGT00390000005100
HOVERGENiHBG051384
InParanoidiP13864
KOiK00558
OrthoDBi898916at2759
PhylomeDBiP13864
TreeFamiTF328926

Enzyme and pathway databases

BRENDAi2.1.1.37 3474
ReactomeiR-MMU-212300 PRC2 methylates histones and DNA
R-MMU-4655427 SUMOylation of DNA methylation proteins

Miscellaneous databases

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

More...
ChiTaRSi
Dnmt1 mouse
EvolutionaryTraceiP13864

Protein Ontology

More...
PROi
PR:P13864

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000004099 Expressed in 435 organ(s), highest expression level in primary oocyte
CleanExiMM_DNMT1
ExpressionAtlasiP13864 baseline and differential
GenevisibleiP13864 MM

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...

<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_MOUSE
<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: P13864
Secondary accession number(s): P97413
, Q80ZU3, Q9CSC6, Q9QXX6
<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: January 1, 1990
Last sequence update: February 21, 2002
Last modified: January 16, 2019
This is version 213 of the entry and version 5 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

<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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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