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UniProtKB - P13864 (DNMT1_MOUSE)

Entry version 229 (23 Feb 2022)
Sequence version 5 (21 Feb 2002)
Previous versions | rss
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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%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi359ZincBy similarity1
Metal bindingi362ZincBy similarity1
Metal bindingi420ZincBy similarity1
Metal bindingi424ZincBy similarity1
Metal bindingi656Zinc 1PROSITE-ProRule annotation1
Metal bindingi659Zinc 1PROSITE-ProRule annotation1
Metal bindingi662Zinc 1PROSITE-ProRule annotation1
Metal bindingi667Zinc 2PROSITE-ProRule annotation1
Metal bindingi670Zinc 2PROSITE-ProRule annotation1
Metal bindingi673Zinc 2PROSITE-ProRule annotation1
Metal bindingi689Zinc 2PROSITE-ProRule annotation1
Metal bindingi694Zinc 1PROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei1149S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei12291 Publication1
Binding sitei1582S-adenosyl-L-methionine; via amide nitrogenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 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

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, 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

More...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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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)

More...MGIi		MGI:94912, Dnmt1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSMUSG00000004099

<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

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%5Fand%5Fbiotech%5Fsection">'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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">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%5Fprocessing%5Fsection">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.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
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
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

More...EPDi		P13864

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P13864

MaxQB - The MaxQuant DataBase

More...MaxQBi		P13864

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

More...PaxDbi		P13864

PeptideAtlas

More...PeptideAtlasi		P13864

PRoteomics IDEntifications database

More...PRIDEi		P13864

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		277482 [P13864-1]
277483 [P13864-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P13864

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

More...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

More...Bgeei		ENSMUSG00000004099, Expressed in primary oocyte and 446 other tissues

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%5Fsection">'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%5Fsection">'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).

Interacts with SIRT7 (PubMed:28842251).

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

By similarity7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		199259, 37 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P13864

Protein interaction database and analysis system

More...IntActi		P13864, 12 interactors

Molecular INTeraction database

More...MINTi		P13864

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000004202

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P13864

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P13864, protein

<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

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

More...SMRi		P13864

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		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%5Fand%5Fdomains%5Fsection">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>Domaini16 – 109DMAP1-bindingPROSITE-ProRule annotationAdd BLAST94
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
Regioni1 – 21DisorderedSequence analysisAdd BLAST21
Regioni96 – 369DisorderedSequence analysisAdd BLAST274
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
Regioni702 – 732DisorderedSequence analysisAdd BLAST31
Regioni1097 – 1136DisorderedSequence analysisAdd BLAST40
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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi144 – 170Polar residuesSequence analysisAdd BLAST27
Compositional biasi173 – 206Basic and acidic residuesSequence analysisAdd BLAST34
Compositional biasi232 – 306Basic and acidic residuesSequence analysisAdd BLAST75
Compositional biasi314 – 337Basic and acidic residuesSequence analysisAdd BLAST24
Compositional biasi338 – 353Polar residuesSequence analysisAdd BLAST16
Compositional biasi1122 – 1136Basic and acidic residuesSequence analysisAdd BLAST15

<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

More...eggNOGi		ENOG502QPKK, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000005100

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P13864

Identification of Orthologs from Complete Genome Data

More...OMAi		RDHVCKD

Database of Orthologous Groups

More...OrthoDBi		898916at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P13864

TreeFam database of animal gene trees

More...TreeFami		TF328926

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.30.30.490, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001025, BAH_dom
IPR043151, BAH_sf
IPR018117, C5_DNA_meth_AS
IPR001525, C5_MeTfrase
IPR031303, C5_meth_CS
IPR022702, Cytosine_MeTrfase1_RFD
IPR010506, DMAP1-bd
IPR017198, DNMT1-like
IPR029063, SAM-dependent_MTases
IPR002857, Znf_CXXC

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01426, BAH, 2 hits
PF06464, DMAP_binding, 1 hit
PF00145, DNA_methylase, 1 hit
PF12047, DNMT1-RFD, 1 hit
PF02008, zf-CXXC, 1 hit

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
PS51912, DMAP1_BIND, 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%5Flength">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 (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 <p><strong>What is the canonical sequence?</strong><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 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. Extended N-terminus.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.<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

More...EMBLi

GenBank nucleotide sequence database

More...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 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

More...PIRi		S01845

NCBI Reference Sequences

More...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

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

More...GeneIDi		13433

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:13433

UCSC genome browser

More...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 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

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
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[»]
6W8VX-ray3.12A/B731-1602[»]
6W8WX-ray3.00A/B731-1602[»]
SMRiP13864
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi199259, 37 interactors
CORUMiP13864
IntActiP13864, 12 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
ProteomicsDBi277482 [P13864-1]
277483 [P13864-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1052, 1592 antibodies from 50 providers

The DNASU plasmid repository

More...DNASUi		13433

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
VEuPathDBiHostDB:ENSMUSG00000004099

Phylogenomic databases

eggNOGiENOG502QPKK, Eukaryota
GeneTreeiENSGT00390000005100
InParanoidiP13864
OMAiRDHVCKD
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

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		13433, 10 hits in 66 CRISPR screens

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
RNActiP13864, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000004099, Expressed in primary oocyte and 446 other tissues
ExpressionAtlasiP13864, baseline and differential
GenevisibleiP13864, MM

Family and domain databases

Gene3Di2.30.30.490, 2 hits
InterProiView protein in InterPro
IPR001025, BAH_dom
IPR043151, BAH_sf
IPR018117, C5_DNA_meth_AS
IPR001525, C5_MeTfrase
IPR031303, C5_meth_CS
IPR022702, Cytosine_MeTrfase1_RFD
IPR010506, DMAP1-bd
IPR017198, DNMT1-like
IPR029063, SAM-dependent_MTases
IPR002857, Znf_CXXC
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
PS51912, DMAP1_BIND, 1 hit
PS51679, SAM_MT_C5, 1 hit
PS51058, ZF_CXXC, 1 hit

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_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%5Fand%5Fisoforms">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: February 23, 2022
This is version 229 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, Direct protein sequencing, Reference proteome

Documents

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