Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 162 (08 May 2019)
Sequence version 2 (21 Feb 2002)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

DNA (cytosine-5)-methyltransferase 1

Gene

Dnmt1

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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘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 describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei515Important for activityBy 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 sitei1151S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei1196S-adenosyl-L-methionineBy similarity1
<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 sitei1231PROSITE-ProRule annotation1
Binding sitei1582S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei1584S-adenosyl-L-methionine; via amide nitrogenBy similarity1

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 fingeri650 – 696CXXC-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

  • DNA (cytosine-5-)-methyltransferase activity Source: RGD
  • DNA binding Source: GO_Central
  • estrogen receptor binding Source: RGD
  • histone deacetylase binding Source: RGD
  • promoter-specific chromatin binding Source: UniProtKB
  • protein domain specific binding Source: RGD
  • S-adenosylmethionine-dependent methyltransferase activity Source: RGD
  • zinc ion binding Source: InterPro

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-8581

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.1.1.37 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-212300 PRC2 methylates histones and DNA
R-RNO-4655427 SUMOylation of DNA methylation proteins

Protein family/group databases

Restriction enzymes and methylases database

More...
REBASEi
3019 M.RnoDnmt1

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA (cytosine-5)-methyltransferase 1 (EC:2.1.1.37)
Short name:
Dnmt1
Alternative name(s):
DNA MTase RnoIP
Short name:
M.RnoIP
DNA methyltransferase I
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
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
620979 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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<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_00000880361 – 1622DNA (cytosine-5)-methyltransferase 1Add BLAST1622

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 residuei138PhosphoserineBy similarity1
Modified residuei139N6-methyllysine; by SETD7By similarity1
Modified residuei140Phosphoserine; by PKB/AKT1By similarity1
Modified residuei149PhosphoserineBy similarity1
Modified residuei151PhosphoserineBy similarity1
Modified residuei163PhosphothreonineBy similarity1
Modified residuei169N6-acetyllysineBy similarity1
Modified residuei304PhosphothreonineCombined sources1
Modified residuei372N6-acetyllysineBy similarity1
Modified residuei400PhosphoserineBy similarity1
Modified residuei515PhosphoserineBy similarity1
Modified residuei555PhosphoserineBy similarity1
Modified residuei718PhosphoserineCombined sources1
Modified residuei736PhosphoserineBy similarity1
Modified residuei753N6-acetyllysineBy similarity1
Modified residuei882PhosphoserineBy similarity1
Modified residuei895N6-acetyllysineBy similarity1
Modified residuei961N6-acetyllysineBy similarity1
Modified residuei980N6-acetyllysineBy similarity1
Modified residuei1116N6-acetyllysineBy similarity1
Modified residuei1118N6-acetyllysineBy similarity1
Modified residuei1120N6-acetyllysineBy similarity1
Modified residuei1122N6-acetyllysineBy similarity1
Modified residuei1124N6-acetyllysineBy similarity1
Modified residuei1126N6-acetyllysineBy similarity1
Modified residuei1354N6-acetyllysineBy similarity1
Modified residuei1436PhosphoserineCombined sources1
<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-linki1613Glycyl 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
Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates cell cycle G2/M transition. Deacetylation of Lys-1116 and Lys-1354 by SIRT1 increases methyltransferase activity (By similarity).By similarity
Phosphorylation of Ser-151 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.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9Z330

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

More...
PaxDbi
Q9Z330

PRoteomics IDEntifications database

More...
PRIDEi
Q9Z330

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
Q9Z330

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9Z330

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

More...
PhosphoSitePlusi
Q9Z330

<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

Isoforms 0 and 8 are highly expressed in placenta, brain, lung, spleen, kidney, heart, and at much lower levels in liver. Isoform 1 is expressed in cerebellum, isoform 2 in muscle and testis, isoform 3 in lung, isoform 4 in spleen and brain, and isoform 5 in brain.

<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. Forms a stable complex with E2F1, BB1 and HDAC1. Forms a complex with DMAP1 and HDAC2, with direct interaction. Interacts with the PRC2/EED-EZH2 complex. Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1. Interacts with UHRF1; promoting its recruitment to hemimethylated DNA. Interacts with USP7, promoting its deubiquitination. Interacts with BAZ2A/TIP5. Interacts with PCNA. Interacts with MBD2 and MBD3. Interacts with DNMT3A and DNMT3B. Interacts with UBC9. Interacts with HDAC1. Interacts with CSNK1D.By similarity

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q9Z330, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000063831

<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

3D structure databases

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

More...
SMRi
Q9Z330

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 – 105DMAP-interactionAdd BLAST88
Domaini759 – 884BAH 1PROSITE-ProRule annotationAdd BLAST126
Domaini977 – 1105BAH 2PROSITE-ProRule annotationAdd BLAST129
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati1114 – 111512
Repeati1116 – 111722
Repeati1118 – 111932
Repeati1120 – 112142
Repeati1122 – 112352
Repeati1124 – 112562
Repeati1126 – 11277; approximate2
Domaini1144 – 1603SAM-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 – 342Interaction with the PRC2/EED-EZH2 complexBy similarityAdd BLAST342
Regioni1 – 145Interaction with DNMT3ABy similarityAdd BLAST145
Regioni146 – 213Interaction with DNMT3BBy similarityAdd BLAST68
Regioni304 – 610Interaction with the PRC2/EED-EZH2 complexBy similarityAdd BLAST307
Regioni327 – 556DNA replication foci-targeting sequenceAdd BLAST230
Regioni697 – 758Autoinhibitory linkerAdd BLAST62
Regioni1114 – 11277 X 2 AA tandem repeats of K-GAdd BLAST14
Regioni1126 – 1622Interaction with the PRC2/EED-EZH2 complexBy similarityAdd BLAST497
Regioni1144 – 1622CatalyticAdd BLAST479
Regioni1155 – 1156S-adenosyl-L-methionine bindingBy similarity2
Regioni1173 – 1174S-adenosyl-L-methionine bindingBy similarity2
Regioni1195 – 1196S-adenosyl-L-methionine bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi173 – 200Nuclear 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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi149 – 152Poly-Ser4
Compositional biasi269 – 274Poly-Asp6
Compositional biasi726 – 729Poly-Lys4

<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.By similarity

<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 fingeri650 – 696CXXC-typePROSITE-ProRule annotationAdd BLAST47

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IF68 Eukaryota
COG0270 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000082497

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9Z330

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9Z330

Family and domain databases

Integrated resource of protein families, domains and functional sites

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

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF037404 DNMT1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00105 C5METTRFRASE

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53335 SSF53335, 1 hit

PROSITE; a protein domain and family database

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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (9+)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 9 <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
Note: Additional isoforms seem to exist.

This entry has 9 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9Z330-1) [UniParc]FASTAAdd to basket

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 CVKEKLNLLH
60 70 80 90 100
EFLQTEIKSQ LCDLETKLHK EELSEEGYLA KVKTLLNKDL CLENGTLSLT
110 120 130 140 150
QKANGCPANG SRPTWKAEMA DSNRSPRSRP KPRGPRRSKS DSETMIEASS
160 170 180 190 200
SSVATRRTTR QTTITSHFKG PAKRKPKEDS EKGNANESAA EERDQDKKRR
210 220 230 240 250
VAGTESRASR AGESVEKPER VRPGTQLCQE EQGEQEDDRR PRRQTRELAS
260 270 280 290 300
RRKSREDPDR EARPGTHLDV DDDDEKDKRS SRPRSQPRDL ATKRRPKEEV
310 320 330 340 350
EQITPEPPEG KDEDEREEKR RKTTRKKPEP LSIPVQSRVE RKASQGKASA
360 370 380 390 400
IPKLNPPQCP ECGQYLDDPD LKYQQHPVDA VDEPQMLTNE ALSVFDSNSS
410 420 430 440 450
WFETYDSSPM HKFTFFSVYC SRGHLCPVDT GLIEKNVELY FSGVAKAIHE
460 470 480 490 500
ENPSVEGGVN GKNLGPINQW WISGFDGGEK ALIGFSTAFA EYFLMEPSPE
510 520 530 540 550
YAPIFGLMQE KIYISKIVVE FLQSNPDAVY EDLINKIETT VPPSAINVNR
560 570 580 590 600
FTEDSLLRHA QFVVSQVESY DDAKDDDETP IFLSPCMRSL IHLAGVSLGQ
610 620 630 640 650
RRATRRTVIN SAKVKRKGPT KATTTKLVYQ IFDTFFSEQI EKDDKEDKEN
660 670 680 690 700
TMKRRRCGVC EVCQQPECGK CKACKDMVKF GGTGRSKQAC LKRRCPNLAV
710 720 730 740 750
KEADEDEEAD DDIPELPSPK KLHQGKKKKQ NKDRISWLGE PVKIEENRTY
760 770 780 790 800
YWKVSIDEET LEVGDCVSVI PDDPSKPLYL ARVTALWEDK NGQMFHAHWF
810 820 830 840 850
CAGTDTVLGA TSDPLELFLV GECENMQLSY IHSKVKVIYR GPSPNWAMEG
860 870 880 890 900
GMDPEAMLPG AEDGKTYFYQ FWYSQDYARF ESPPKTQPAE DNKHKFCLSC
910 920 930 940 950
IRLAELRQKE MPKVLEQLEE VDGRVYCSSI TKNGVVYRLG DSVYLPPEAF
960 970 980 990 1000
TFNIKMASPM KRSKRDPVNE NPVPRDTYRK YSDYIKGSNL DAPEPYRIGR
1010 1020 1030 1040 1050
IKEIYCGKKK GGKVNEADIK IRLYKFYRPE NTHKSIQATY HADINLLYWS
1060 1070 1080 1090 1100
DEEAVVDFSD VQGRCTVEYG EDLLESIQDY SQGGPDRFYF LEAYNSKTKS
1110 1120 1130 1140 1150
FEDPPNHARS PGNKGKGKGK GKGKGKPQVS EPKEPEAAIK LPKLRTLDVF
1160 1170 1180 1190 1200
SGCGGLTEGF HQAGISETLW AIEMWEPAAQ AFRLNNPGTT VFTEDCNVLL
1210 1220 1230 1240 1250
KLVMAGEVTN SLGQRLPQKG DVEMLCGGPP CQGFSGMNRF NSRTYSKFKN
1260 1270 1280 1290 1300
SLVVSFLSYC DYYRPRFFLL ENVRNFVSFR RSMVLKLTLR CLVRMGYQCT
1310 1320 1330 1340 1350
FGVLQAGQYG VAQTRRRAII LAAAPGEKLP LFPEPLHVFA PRACQLSVVV
1360 1370 1380 1390 1400
DDKKFVSNIT RLSSGPFRTI TMRDTMSDLP EIQNGASAPE ISYKWRATVL
1410 1420 1430 1440 1450
VPEAAARVAL PAHPQGPYPQ VHERAGGCRM RHIPLSPGSD WRDLPNIQVR
1460 1470 1480 1490 1500
LRDGVITNKL RYTFHDTKNG CSSTGALRGV CSCAEGKTCD PASRQFNTLI
1510 1520 1530 1540 1550
PWCLPHTGNR HNHWAGLYGR LEWDGFFSTT VTNPEPMGKQ GRVLHPEQHR
1560 1570 1580 1590 1600
VVSVRECARS QGFPDTYRLF GNILDRHRQV GNAVPPPLAK AIGLEIKLCL
1610 1620
LASAQESASA AVKGKEETTT ED
Length:1,622
Mass (Da):182,774
Last modified:February 21, 2002 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFCFA4AAA69E234BA
GO
Isoform 2 (identifier: Q9Z330-2) [UniParc]FASTAAdd to basket
Also known as: SF1

The sequence of this isoform differs from the canonical sequence as follows:
     1323-1403: Missing.

Show »
Length:1,541
Mass (Da):173,853
Checksum:i9F1B86D1D13B45AB
GO
Isoform 3 (identifier: Q9Z330-3) [UniParc]FASTAAdd to basket
Also known as: SF2

The sequence of this isoform differs from the canonical sequence as follows:
     1252-1482: Missing.

Show »
Length:1,391
Mass (Da):156,880
Checksum:i7F92F4E446BBD358
GO
Isoform 4 (identifier: Q9Z330-4) [UniParc]FASTAAdd to basket
Also known as: SF3

The sequence of this isoform differs from the canonical sequence as follows:
     1226-1477: Missing.

Show »
Length:1,370
Mass (Da):154,529
Checksum:i9137E151ED3EED0B
GO
Isoform 5 (identifier: Q9Z330-5) [UniParc]FASTAAdd to basket
Also known as: SF4

The sequence of this isoform differs from the canonical sequence as follows:
     1218-1430: QKGDVEMLCG...VHERAGGCRM → VC

Show »
Length:1,411
Mass (Da):159,119
Checksum:i961F53E307E2447E
GO
Isoform 6 (identifier: Q9Z330-6) [UniParc]FASTAAdd to basket
Also known as: SF5

The sequence of this isoform differs from the canonical sequence as follows:
     1202-1410: Missing.

Show »
Length:1,413
Mass (Da):159,421
Checksum:iAE3F0037058D8167
GO
Isoform 7 (identifier: Q9Z330-7) [UniParc]FASTAAdd to basket
Also known as: SF6

The sequence of this isoform differs from the canonical sequence as follows:
     1259-1481: Missing.

Show »
Length:1,399
Mass (Da):157,713
Checksum:i28C6F61C3085A7ED
GO
Isoform 8 (identifier: Q9Z330-8) [UniParc]FASTAAdd to basket
Also known as: SF7

The sequence of this isoform differs from the canonical sequence as follows:
     1216-1504: Missing.

Show »
Length:1,333
Mass (Da):150,479
Checksum:iD8713CC5B748BFC2
GO
Isoform 9 (identifier: Q9Z330-9) [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:1,504
Mass (Da):169,645
Checksum:iC880386135929522
GO

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

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1LQT9F1LQT9_RAT
DNA (cytosine-5)-methyltransferase
Dnmt1 rCG_31827
1,621Annotation score:

Annotation score:4 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>
D3ZS06D3ZS06_RAT
DNA (cytosine-5)-methyltransferase
Dnmt1
1,620Annotation score:

Annotation score:2 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 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 conflicti17 – 25AGSLPDHVR → RQARPRPCP in BAA20854 (PubMed:8667030).Curated9
Sequence conflicti189A → V in BAA20854 (PubMed:8667030).Curated1
Sequence conflicti1276F → S in BAA37118 (PubMed:9878564).Curated1
Sequence conflicti1300T → I in AAD28102 (PubMed:9722504).Curated1
Sequence conflicti1372M → V in BAA37118 (PubMed:9878564).Curated1
Sequence conflicti1394 – 1428KWRAT…RAGGC → NGEPQSWFQRQLRGSHYQPI LRDHICKDMSALVAA in BAA37118 (PubMed:9878564).CuratedAdd BLAST35

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_0056201 – 118Missing in isoform 9. CuratedAdd BLAST118
Alternative sequenceiVSP_0056221202 – 1410Missing in isoform 6. CuratedAdd BLAST209
Alternative sequenceiVSP_0056231216 – 1504Missing in isoform 8. CuratedAdd BLAST289
Alternative sequenceiVSP_0056211218 – 1430QKGDV…GGCRM → VC in isoform 5. CuratedAdd BLAST213
Alternative sequenceiVSP_0056241226 – 1477Missing in isoform 4. CuratedAdd BLAST252
Alternative sequenceiVSP_0056251252 – 1482Missing in isoform 3. CuratedAdd BLAST231
Alternative sequenceiVSP_0056261259 – 1481Missing in isoform 7. CuratedAdd BLAST223
Alternative sequenceiVSP_0056271323 – 1403Missing in isoform 2. CuratedAdd BLAST81

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
AB012214 mRNA Translation: BAA37118.1
AF116344 mRNA Translation: AAD32541.1
AF116345 Genomic DNA Translation: AAD32542.1
D64060 mRNA Translation: BAA20854.1
AH007612 Genomic DNA Translation: AAD28102.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JE0378

Genome annotation databases

UCSC genome browser

More...
UCSCi
RGD:620979 rat [Q9Z330-1]

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
AB012214 mRNA Translation: BAA37118.1
AF116344 mRNA Translation: AAD32541.1
AF116345 Genomic DNA Translation: AAD32542.1
D64060 mRNA Translation: BAA20854.1
AH007612 Genomic DNA Translation: AAD28102.1
PIRiJE0378

3D structure databases

SMRiQ9Z330
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Z330, 2 interactors
STRINGi10116.ENSRNOP00000063831

Protein family/group databases

REBASEi3019 M.RnoDnmt1

PTM databases

CarbonylDBiQ9Z330
iPTMnetiQ9Z330
PhosphoSitePlusiQ9Z330

Proteomic databases

jPOSTiQ9Z330
PaxDbiQ9Z330
PRIDEiQ9Z330

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:620979 rat [Q9Z330-1]

Organism-specific databases

RGDi620979 Dnmt1

Phylogenomic databases

eggNOGiENOG410IF68 Eukaryota
COG0270 LUCA
HOGENOMiHOG000082497
InParanoidiQ9Z330
PhylomeDBiQ9Z330

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8581
BRENDAi2.1.1.37 5301
ReactomeiR-RNO-212300 PRC2 methylates histones and DNA
R-RNO-4655427 SUMOylation of DNA methylation proteins

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q9Z330

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_RAT
<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: Q9Z330
Secondary accession number(s): P70487
, Q9R252, Q9WTX3, Q9WU57
<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: February 21, 2002
Last sequence update: February 21, 2002
Last modified: May 8, 2019
This is version 162 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again