UniProtKB - P13864 (DNMT1_MOUSE)
DNA (cytosine-5)-methyltransferase 1
Dnmt1
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 PublicationsMiscellaneous
Catalytic activityi
- a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H+ + S-adenosyl-L-homocysteinePROSITE-ProRule annotationEC:2.1.1.37PROSITE-ProRule annotation
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 359 | ZincBy similarity | 1 | |
Metal bindingi | 362 | ZincBy similarity | 1 | |
Metal bindingi | 420 | ZincBy similarity | 1 | |
Metal bindingi | 424 | ZincBy similarity | 1 | |
Metal bindingi | 656 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 659 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 662 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 667 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 670 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 673 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 689 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 694 | Zinc 1PROSITE-ProRule annotation | 1 | |
Binding sitei | 1149 | S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication | 1 | |
Active sitei | 1229 | 1 Publication | 1 | |
Binding sitei | 1582 | S-adenosyl-L-methionine; via amide nitrogenCombined sources1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 649 – 695 | CXXC-typePROSITE-ProRule annotationAdd BLAST | 47 |
GO - Molecular functioni
- chromatin binding Source: MGI
- DNA (cytosine-5-)-methyltransferase activity Source: MGI
- DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates Source: Reactome
- DNA binding Source: MGI
- DNA-methyltransferase activity Source: MGI
- estrogen receptor binding Source: MGI
- histone deacetylase binding Source: MGI
- methyl-CpG binding Source: MGI
- methyltransferase activity Source: UniProtKB
- promoter-specific chromatin binding Source: UniProtKB
- protein domain specific binding Source: MGI
- RNA binding Source: MGI
- zinc ion binding Source: MGI
GO - Biological processi
- cellular response to amino acid stimulus Source: MGI
- cellular response to bisphenol A Source: MGI
- cellular response to transforming growth factor beta stimulus Source: MGI
- DNA hypermethylation Source: MGI
- DNA methylation Source: MGI
- DNA methylation-dependent heterochromatin assembly Source: UniProtKB
- DNA methylation involved in embryo development Source: MGI
- DNA methylation on cytosine Source: MGI
- DNA methylation on cytosine within a CG sequence Source: MGI
- maintenance of DNA methylation Source: UniProtKB
- negative regulation of gene expression Source: MGI
- negative regulation of histone H3-K9 methylation Source: MGI
- negative regulation of transcription, DNA-templated Source: MGI
- negative regulation of transcription by RNA polymerase II Source: MGI
- negative regulation of vascular associated smooth muscle cell apoptotic process Source: MGI
- negative regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching Source: MGI
- positive regulation of DNA methylation-dependent heterochromatin assembly Source: UniProtKB
- positive regulation of gene expression Source: MGI
- positive regulation of histone H3-K4 methylation Source: MGI
- positive regulation of vascular associated smooth muscle cell proliferation Source: MGI
- Ras protein signal transduction Source: UniProtKB
- regulation of cell population proliferation Source: MGI
- regulation of gene expression Source: MGI
- response to xenobiotic stimulus Source: MGI
- S-adenosylmethionine metabolic process Source: MGI
Keywordsi
Molecular function | Activator, Allosteric enzyme, Chromatin regulator, DNA-binding, Methyltransferase, Repressor, Transferase |
Biological process | Transcription, Transcription regulation |
Ligand | Metal-binding, S-adenosyl-L-methionine, Zinc |
Enzyme and pathway databases
BRENDAi | 2.1.1.37, 3474 |
Reactomei | R-MMU-212300, PRC2 methylates histones and DNA R-MMU-4655427, SUMOylation of DNA methylation proteins |
Protein family/group databases
REBASEi | 2844, 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 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:94912, Dnmt1 |
VEuPathDBi | HostDB:ENSMUSG00000004099 |
Subcellular locationi
Nucleus
- Nucleus 1 Publication
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Note: It is nucleoplasmic through most of the cell cycle and associates with replication foci during S-phase. In germ cells, spermatogonia, preleptotene and leptotene spermatocytes all express high levels of nuclear protein, while the protein is not detected in pachytene spermatocytes, despite the fact they expressed high levels of mRNA. In females, the protein is not detected in non-growing oocytes, in contrast to the growing oocytes. During the growing, the protein is no longer detectable in nuclei but accumulates to very high levels first throughout the cytoplasm. At the time of ovulation, all the protein is cytoplasmic and is actively associated with the oocyte cortex. After fecondation, in the preimplantation embryo, the protein remains cytoplasmic and after implantation, it is exclusively nuclear in all tissue types. Isoform 2 is sequestered in the cytoplasm of maturing oocytes and of preimplantation embryos, except for the 8-cell stage, while isoform 1 is exclusively nuclear.
Nucleus
- nucleoplasm Source: Reactome
- nucleus Source: MGI
Other locations
- cytoplasm Source: MGI
- heterochromatin Source: MGI
- neuronal cell body Source: MGI
- pericentric heterochromatin Source: UniProtKB
- protein-containing complex Source: MGI
- replication fork Source: MGI
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 162 | Q → E: Abolishes interaction with PCNA. No effect on activity. 1 Publication | 1 | |
Mutagenesisi | 169 | F → S: Abolishes interaction with PCNA. No effect on activity. 1 Publication | 1 | |
Mutagenesisi | 515 | S → A: Loss of activity. No effect on DNA-binding capacity. 1 Publication | 1 | |
Mutagenesisi | 515 | S → E: Slightly reduces activity. 1 Publication | 1 | |
Mutagenesisi | 1229 | C → W: Loss of activity. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3351195 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000088035 | 1 – 1620 | DNA (cytosine-5)-methyltransferase 1Add BLAST | 1620 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 15 | PhosphoserineCombined sources | 1 | |
Modified residuei | 70 | N6,N6-dimethyllysine; by EHMT2By similarity | 1 | |
Modified residuei | 138 | PhosphoserineCombined sources | 1 | |
Modified residuei | 139 | N6-methyllysine; by SETD7By similarity | 1 | |
Modified residuei | 140 | PhosphoserineCombined sources | 1 | |
Modified residuei | 146 | Phosphoserine; by CK1Combined sources1 Publication | 1 | |
Modified residuei | 150 | PhosphoserineCombined sources | 1 | |
Modified residuei | 152 | PhosphoserineCombined sources | 1 | |
Modified residuei | 164 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 171 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 240 | PhosphoserineCombined sources | 1 | |
Modified residuei | 255 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 255 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 372 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 515 | Phosphoserine2 Publications | 1 | |
Modified residuei | 555 | PhosphoserineBy similarity | 1 | |
Modified residuei | 713 | PhosphoserineCombined sources | 1 | |
Modified residuei | 717 | PhosphoserineCombined sources | 1 | |
Modified residuei | 735 | PhosphoserineBy similarity | 1 | |
Modified residuei | 752 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 882 | PhosphoserineBy similarity | 1 | |
Modified residuei | 895 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 961 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 965 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 979 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1114 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1116 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1118 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1120 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1122 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 1124 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 1352 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1418 | N6-acetyllysineBy similarity | 1 | |
Cross-linki | 1611 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | P13864 |
jPOSTi | P13864 |
MaxQBi | P13864 |
PaxDbi | P13864 |
PeptideAtlasi | P13864 |
PRIDEi | P13864 |
ProteomicsDBi | 277482 [P13864-1] 277483 [P13864-2] |
PTM databases
iPTMneti | P13864 |
PhosphoSitePlusi | P13864 |
SwissPalmi | P13864 |
Expressioni
Tissue specificityi
Developmental stagei
Gene expression databases
Bgeei | ENSMUSG00000004099, Expressed in primary oocyte and 446 other tissues |
ExpressionAtlasi | P13864, baseline and differential |
Genevisiblei | P13864, 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).
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 PublicationsBinary interactionsi
P13864
With | #Exp. | IntAct |
---|---|---|
Hdac1 [O09106] | 3 | EBI-301927,EBI-301912 |
GO - Molecular functioni
- estrogen receptor binding Source: MGI
- histone deacetylase binding Source: MGI
- protein domain specific binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 199259, 37 interactors |
CORUMi | P13864 |
IntActi | P13864, 12 interactors |
MINTi | P13864 |
STRINGi | 10090.ENSMUSP00000004202 |
Chemistry databases
BindingDBi | P13864 |
Miscellaneous databases
RNActi | P13864, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P13864 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P13864 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 16 – 109 | DMAP1-bindingPROSITE-ProRule annotationAdd BLAST | 94 | |
Domaini | 758 – 884 | BAH 1PROSITE-ProRule annotationAdd BLAST | 127 | |
Domaini | 976 – 1103 | BAH 2PROSITE-ProRule annotationAdd BLAST | 128 | |
Repeati | 1112 – 1113 | 1 | 2 | |
Repeati | 1114 – 1115 | 2 | 2 | |
Repeati | 1116 – 1117 | 3 | 2 | |
Repeati | 1118 – 1119 | 4 | 2 | |
Repeati | 1120 – 1121 | 5 | 2 | |
Repeati | 1122 – 1123 | 6 | 2 | |
Repeati | 1124 – 1125 | 7; approximate | 2 | |
Domaini | 1142 – 1601 | SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd BLAST | 460 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 343 | Interaction with the PRC2/EED-EZH2 complexAdd BLAST | 343 | |
Regioni | 1 – 145 | Interaction with DNMT3ABy similarityAdd BLAST | 145 | |
Regioni | 1 – 120 | Interaction with DMAP11 PublicationAdd BLAST | 120 | |
Regioni | 1 – 21 | DisorderedSequence analysisAdd BLAST | 21 | |
Regioni | 96 – 369 | DisorderedSequence analysisAdd BLAST | 274 | |
Regioni | 147 – 217 | Interaction with DNMT3BBy similarityAdd BLAST | 71 | |
Regioni | 161 – 172 | Interaction with PCNAAdd BLAST | 12 | |
Regioni | 305 – 609 | Interaction with the PRC2/EED-EZH2 complexAdd BLAST | 305 | |
Regioni | 328 – 556 | DNA replication foci-targeting sequenceBy similarityAdd BLAST | 229 | |
Regioni | 696 – 813 | Interaction with HDAC11 PublicationAdd BLAST | 118 | |
Regioni | 696 – 757 | Autoinhibitory linkerAdd BLAST | 62 | |
Regioni | 702 – 732 | DisorderedSequence analysisAdd BLAST | 31 | |
Regioni | 1097 – 1136 | DisorderedSequence analysisAdd BLAST | 40 | |
Regioni | 1112 – 1125 | 7 X 2 AA tandem repeats of K-GAdd BLAST | 14 | |
Regioni | 1124 – 1620 | Interaction with the PRC2/EED-EZH2 complexAdd BLAST | 497 | |
Regioni | 1142 – 1620 | CatalyticAdd BLAST | 479 | |
Regioni | 1153 – 1154 | S-adenosyl-L-methionine bindingCombined sources1 Publication | 2 | |
Regioni | 1171 – 1172 | S-adenosyl-L-methionine bindingCombined sources1 Publication | 2 | |
Regioni | 1193 – 1194 | S-adenosyl-L-methionine bindingCombined sources1 Publication | 2 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 175 – 202 | Nuclear localization signalSequence analysisAdd BLAST | 28 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 144 – 170 | Polar residuesSequence analysisAdd BLAST | 27 | |
Compositional biasi | 173 – 206 | Basic and acidic residuesSequence analysisAdd BLAST | 34 | |
Compositional biasi | 232 – 306 | Basic and acidic residuesSequence analysisAdd BLAST | 75 | |
Compositional biasi | 314 – 337 | Basic and acidic residuesSequence analysisAdd BLAST | 24 | |
Compositional biasi | 338 – 353 | Polar residuesSequence analysisAdd BLAST | 16 | |
Compositional biasi | 1122 – 1136 | Basic and acidic residuesSequence analysisAdd BLAST | 15 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 649 – 695 | CXXC-typePROSITE-ProRule annotationAdd BLAST | 47 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | ENOG502QPKK, Eukaryota |
GeneTreei | ENSGT00390000005100 |
InParanoidi | P13864 |
OMAi | RDHVCKD |
OrthoDBi | 898916at2759 |
PhylomeDBi | P13864 |
TreeFami | TF328926 |
Family and domain databases
Gene3Di | 2.30.30.490, 2 hits |
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 |
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 |
PIRSFi | PIRSF037404, DNMT1, 1 hit |
PRINTSi | PR00105, C5METTRFRASE |
SMARTi | View protein in SMART SM00439, BAH, 2 hits SM01137, DMAP_binding, 1 hit |
SUPFAMi | SSF53335, SSF53335, 1 hit |
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 |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketJ3QNW0 | J3QNW0_MOUSE | DNA (cytosine-5)-methyltransferase | Dnmt1 | 1,501 | Annotation score: |
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 146 – 147 | SV → F in CAA32910 (PubMed:3210246).Curated | 2 | |
Sequence conflicti | 146 – 147 | SV → F in AAC40061 (PubMed:9449671).Curated | 2 | |
Sequence conflicti | 299 – 309 | AEPEQVAPETP → VRARAGSSRDS in CAA32910 (PubMed:3210246).CuratedAdd BLAST | 11 | |
Sequence conflicti | 299 – 309 | AEPEQVAPETP → VRARAGSSRDS in AAC40061 (PubMed:9449671).CuratedAdd BLAST | 11 | |
Sequence conflicti | 936 | V → C in CAA32910 (PubMed:3210246).Curated | 1 | |
Sequence conflicti | 936 | V → C in AAC40061 (PubMed:9449671).Curated | 1 | |
Sequence conflicti | 947 | P → R in CAA32910 (PubMed:3210246).Curated | 1 | |
Sequence conflicti | 947 | P → R in AAC40061 (PubMed:9449671).Curated | 1 | |
Sequence conflicti | 969 – 976 | NETLYPEH → KENPVPRDT in CAA32910 (PubMed:3210246).Curated | 8 | |
Sequence conflicti | 969 – 976 | NETLYPEH → KENPVPRDT in AAC40061 (PubMed:9449671).Curated | 8 | |
Sequence conflicti | 987 | S → R in CAA32910 (PubMed:3210246).Curated | 1 | |
Sequence conflicti | 987 | S → R in AAC40061 (PubMed:9449671).Curated | 1 | |
Sequence conflicti | 1046 | Y → C in CAA32910 (PubMed:3210246).Curated | 1 | |
Sequence conflicti | 1046 | Y → C in AAC40061 (PubMed:9449671).Curated | 1 | |
Sequence conflicti | 1068 | G → R in CAA32910 (PubMed:3210246).Curated | 1 | |
Sequence conflicti | 1068 | G → R in AAC40061 (PubMed:9449671).Curated | 1 | |
Sequence conflicti | 1429 | R → P in CAA32910 (PubMed:3210246).Curated | 1 | |
Sequence conflicti | 1429 | R → P in AAC40061 (PubMed:9449671).Curated | 1 | |
Sequence conflicti | 1456 | H → D in CAA32910 (PubMed:3210246).Curated | 1 | |
Sequence conflicti | 1456 | H → D in AAC40061 (PubMed:9449671).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_005619 | 1 – 118 | Missing in isoform 2. 3 PublicationsAdd BLAST | 118 |
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 |
CCDSi | CCDS57654.1 [P13864-2] CCDS57655.1 [P13864-1] |
PIRi | S01845 |
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
Ensembli | ENSMUST00000004202; ENSMUSP00000004202; ENSMUSG00000004099 [P13864-1] ENSMUST00000216540; ENSMUSP00000150433; ENSMUSG00000004099 [P13864-2] |
GeneIDi | 13433 |
KEGGi | mmu:13433 |
UCSCi | uc009ojo.2, mouse [P13864-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar 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 |
CCDSi | CCDS57654.1 [P13864-2] CCDS57655.1 [P13864-1] |
PIRi | S01845 |
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 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3AV4 | X-ray | 2.75 | A | 291-1620 | [»] | |
3AV5 | X-ray | 3.25 | A | 291-1620 | [»] | |
3AV6 | X-ray | 3.09 | A | 291-1620 | [»] | |
3PT6 | X-ray | 3.00 | A/B | 650-1602 | [»] | |
3PT9 | X-ray | 2.50 | A | 731-1602 | [»] | |
4DA4 | X-ray | 2.60 | A/B | 731-1602 | [»] | |
5GUT | X-ray | 2.10 | A | 731-1602 | [»] | |
5GUV | X-ray | 3.08 | A | 731-1602 | [»] | |
5WY1 | X-ray | 3.27 | A | 291-1620 | [»] | |
6W8V | X-ray | 3.12 | A/B | 731-1602 | [»] | |
6W8W | X-ray | 3.00 | A/B | 731-1602 | [»] | |
SMRi | P13864 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 199259, 37 interactors |
CORUMi | P13864 |
IntActi | P13864, 12 interactors |
MINTi | P13864 |
STRINGi | 10090.ENSMUSP00000004202 |
Chemistry databases
BindingDBi | P13864 |
ChEMBLi | CHEMBL3351195 |
Protein family/group databases
REBASEi | 2844, M.MmuDnmt1 |
PTM databases
iPTMneti | P13864 |
PhosphoSitePlusi | P13864 |
SwissPalmi | P13864 |
Proteomic databases
EPDi | P13864 |
jPOSTi | P13864 |
MaxQBi | P13864 |
PaxDbi | P13864 |
PeptideAtlasi | P13864 |
PRIDEi | P13864 |
ProteomicsDBi | 277482 [P13864-1] 277483 [P13864-2] |
Protocols and materials databases
Antibodypediai | 1052, 1592 antibodies from 50 providers |
DNASUi | 13433 |
Genome annotation databases
Ensembli | ENSMUST00000004202; ENSMUSP00000004202; ENSMUSG00000004099 [P13864-1] ENSMUST00000216540; ENSMUSP00000150433; ENSMUSG00000004099 [P13864-2] |
GeneIDi | 13433 |
KEGGi | mmu:13433 |
UCSCi | uc009ojo.2, mouse [P13864-1] |
Organism-specific databases
CTDi | 1786 |
MGIi | MGI:94912, Dnmt1 |
VEuPathDBi | HostDB:ENSMUSG00000004099 |
Phylogenomic databases
eggNOGi | ENOG502QPKK, Eukaryota |
GeneTreei | ENSGT00390000005100 |
InParanoidi | P13864 |
OMAi | RDHVCKD |
OrthoDBi | 898916at2759 |
PhylomeDBi | P13864 |
TreeFami | TF328926 |
Enzyme and pathway databases
BRENDAi | 2.1.1.37, 3474 |
Reactomei | R-MMU-212300, PRC2 methylates histones and DNA R-MMU-4655427, SUMOylation of DNA methylation proteins |
Miscellaneous databases
BioGRID-ORCSi | 13433, 10 hits in 66 CRISPR screens |
ChiTaRSi | Dnmt1, mouse |
EvolutionaryTracei | P13864 |
PROi | PR:P13864 |
RNActi | P13864, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000004099, Expressed in primary oocyte and 446 other tissues |
ExpressionAtlasi | P13864, baseline and differential |
Genevisiblei | P13864, MM |
Family and domain databases
Gene3Di | 2.30.30.490, 2 hits |
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 |
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 |
PIRSFi | PIRSF037404, DNMT1, 1 hit |
PRINTSi | PR00105, C5METTRFRASE |
SMARTi | View protein in SMART SM00439, BAH, 2 hits SM01137, DMAP_binding, 1 hit |
SUPFAMi | SSF53335, SSF53335, 1 hit |
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 |
MobiDBi | Search... |
Entry informationi
Entry namei | DNMT1_MOUSE | |
Accessioni | P13864Primary (citable) accession number: P13864 Secondary accession number(s): P97413 Q9QXX6 | |
Entry historyi | Integrated 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. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families