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Protein

DNA (cytosine-5)-methyltransferase 1

Gene

Dnmt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.

Catalytic activityi

S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.PROSITE-ProRule annotation

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
Metal bindingi359ZincBy similarity1
Metal bindingi362ZincBy similarity1
Metal bindingi420ZincBy similarity1
Metal bindingi424ZincBy similarity1
Binding sitei1149S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication1
Active sitei12291 Publication1
Binding sitei1582S-adenosyl-L-methionine; via amide nitrogenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri649 – 695CXXC-typePROSITE-ProRule annotationAdd BLAST47

GO - Molecular functioni

GO - Biological processi

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

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

Protein family/group databases

REBASEi2844 M.MmuDnmt1

Names & Taxonomyi

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
Gene namesi
Name:Dnmt1
Synonyms:Dnmt, Met1, Uim
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:94912 Dnmt1

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

ChEMBLiCHEMBL3351195

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000880351 – 1620DNA (cytosine-5)-methyltransferase 1Add BLAST1620

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
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

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

EPDiP13864
MaxQBiP13864
PaxDbiP13864
PeptideAtlasiP13864
PRIDEiP13864

PTM databases

iPTMnetiP13864
PhosphoSitePlusiP13864
SwissPalmiP13864

Expressioni

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.

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

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

Interactioni

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

Binary interactionsi

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199259, 25 interactors
CORUMiP13864
IntActiP13864, 10 interactors
MINTiP13864
STRINGi10090.ENSMUSP00000004202

Chemistry databases

BindingDBiP13864

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliP13864
SMRiP13864
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13864

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 106DMAP-interactionAdd BLAST89
Domaini758 – 884BAH 1PROSITE-ProRule annotationAdd BLAST127
Domaini976 – 1103BAH 2PROSITE-ProRule annotationAdd BLAST128
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
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
Motifi175 – 202Nuclear localization signalSequence analysisAdd BLAST28

Domaini

The N-terminal part is required for homodimerization and acts as a regulatory domain.
The CXXC-type zinc finger specifically binds to unmethylated CpG dinucleotides, positioning the autoinhibitory linker between the DNA and the active site, thus providing a mechanism to ensure that only hemimethylated CpG dinucleotides undergo methylation.1 Publication

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri649 – 695CXXC-typePROSITE-ProRule annotationAdd BLAST47

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IF68 Eukaryota
COG0270 LUCA
GeneTreeiENSGT00390000005100
HOVERGENiHBG051384
InParanoidiP13864
KOiK00558
OrthoDBiEOG091G02YU
PhylomeDBiP13864
TreeFamiTF328926

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

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 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
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

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:

Sequence cautioni

The sequence AAC52900 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Alternative sequenceiVSP_0056191 – 118Missing in isoform 2. 3 PublicationsAdd BLAST118

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

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, 25 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
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

CTDi1786
MGIiMGI:94912 Dnmt1

Phylogenomic databases

eggNOGiENOG410IF68 Eukaryota
COG0270 LUCA
GeneTreeiENSGT00390000005100
HOVERGENiHBG051384
InParanoidiP13864
KOiK00558
OrthoDBiEOG091G02YU
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

ChiTaRSiDnmt1 mouse
EvolutionaryTraceiP13864
PROiPR:P13864
SOURCEiSearch...

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
ProtoNetiSearch...

Entry informationi

Entry nameiDNMT1_MOUSE
AccessioniPrimary (citable) accession number: P13864
Secondary accession number(s): P97413
, Q80ZU3, Q9CSC6, Q9QXX6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 21, 2002
Last modified: November 7, 2018
This is version 211 of the entry and version 5 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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