Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA (cytosine-5)-methyltransferase 1

Gene

Dnmt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Catalytic activityi

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

Enzyme 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
Active sitei12291

Regions

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

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
  • methyl-CpG binding Source: MGI
  • methyltransferase activity Source: UniProtKB
  • promoter-specific chromatin binding Source: UniProtKB
  • RNA binding Source: MGI
  • zinc ion binding Source: MGI

GO - Biological processi

  • cellular response to amino acid stimulus Source: MGI
  • chromatin modification Source: UniProtKB-KW
  • chromatin silencing at rDNA Source: Reactome
  • DNA methylation Source: MGI
  • DNA methylation involved in embryo development Source: MGI
  • DNA methylation on cytosine Source: MGI
  • gene silencing Source: UniProtKB
  • maintenance of DNA methylation Source: UniProtKB
  • negative regulation of histone H3-K9 methylation Source: MGI
  • negative regulation of transcription, DNA-templated Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of histone H3-K4 methylation Source: MGI
  • positive regulation of methylation-dependent chromatin silencing Source: UniProtKB
  • Ras protein signal transduction Source: UniProtKB
  • regulation of cell proliferation Source: MGI
  • regulation of gene expression Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-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-427413. NoRC negatively regulates rRNA expression.
R-MMU-5334118. DNA methylation.
R-MMU-573389. NoRC negatively regulates rRNA expression.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:94912. Dnmt1.

Subcellular locationi

  • Nucleus 1 Publication
  • 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.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • heterochromatin Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
  • pericentric heterochromatin Source: UniProtKB
  • replication fork Source: MGI
Complete GO annotation...

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-acetyllysineBy similarity1
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.
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

Protein-protein interaction databases

BioGridi199259. 22 interactors.
IntActiP13864. 9 interactors.
MINTiMINT-4093291.
STRINGi10090.ENSMUSP00000004202.

Chemistry databases

BindingDBiP13864.

Structurei

Secondary structure

11620
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni360 – 362Combined sources3
Helixi383 – 387Combined sources5
Beta strandi406 – 408Combined sources3
Beta strandi410 – 419Combined sources10
Beta strandi423 – 425Combined sources3
Turni432 – 436Combined sources5
Beta strandi440 – 445Combined sources6
Beta strandi454 – 458Combined sources5
Beta strandi459 – 465Combined sources7
Beta strandi469 – 473Combined sources5
Beta strandi475 – 479Combined sources5
Beta strandi482 – 486Combined sources5
Beta strandi491 – 494Combined sources4
Turni499 – 501Combined sources3
Helixi502 – 524Combined sources23
Helixi530 – 539Combined sources10
Helixi553 – 558Combined sources6
Helixi560 – 573Combined sources14
Helixi581 – 583Combined sources3
Helixi585 – 593Combined sources9
Helixi625 – 635Combined sources11
Beta strandi657 – 659Combined sources3
Turni660 – 663Combined sources4
Turni671 – 675Combined sources5
Turni677 – 680Combined sources4
Helixi690 – 692Combined sources3
Helixi695 – 704Combined sources10
Beta strandi734 – 739Combined sources6
Beta strandi741 – 743Combined sources3
Beta strandi745 – 755Combined sources11
Beta strandi758 – 761Combined sources4
Beta strandi765 – 768Combined sources4
Beta strandi774 – 776Combined sources3
Beta strandi778 – 788Combined sources11
Beta strandi793 – 802Combined sources10
Helixi803 – 805Combined sources3
Helixi809 – 811Combined sources3
Beta strandi816 – 827Combined sources12
Helixi828 – 830Combined sources3
Beta strandi833 – 835Combined sources3
Beta strandi837 – 839Combined sources3
Helixi846 – 848Combined sources3
Beta strandi867 – 874Combined sources8
Turni875 – 878Combined sources4
Beta strandi879 – 881Combined sources3
Turni890 – 895Combined sources6
Helixi898 – 910Combined sources13
Beta strandi913 – 920Combined sources8
Beta strandi922 – 924Combined sources3
Beta strandi925 – 932Combined sources8
Beta strandi935 – 938Combined sources4
Beta strandi942 – 945Combined sources4
Helixi947 – 949Combined sources3
Turni970 – 972Combined sources3
Helixi976 – 979Combined sources4
Beta strandi996 – 1008Combined sources13
Beta strandi1011 – 1023Combined sources13
Helixi1027 – 1029Combined sources3
Turni1031 – 1036Combined sources6
Turni1037 – 1039Combined sources3
Beta strandi1044 – 1047Combined sources4
Beta strandi1051 – 1055Combined sources5
Helixi1056 – 1058Combined sources3
Beta strandi1061 – 1067Combined sources7
Helixi1068 – 1070Combined sources3
Helixi1075 – 1081Combined sources7
Beta strandi1085 – 1091Combined sources7
Turni1094 – 1097Combined sources4
Beta strandi1098 – 1100Combined sources3
Helixi1104 – 1106Combined sources3
Beta strandi1142 – 1147Combined sources6
Helixi1153 – 1161Combined sources9
Beta strandi1163 – 1170Combined sources8
Helixi1174 – 1183Combined sources10
Beta strandi1187 – 1190Combined sources4
Helixi1194 – 1202Combined sources9
Turni1217 – 1219Combined sources3
Beta strandi1221 – 1225Combined sources5
Turni1230 – 1232Combined sources3
Beta strandi1234 – 1236Combined sources3
Helixi1240 – 1247Combined sources8
Helixi1250 – 1261Combined sources12
Beta strandi1264 – 1271Combined sources8
Helixi1272 – 1275Combined sources4
Turni1276 – 1280Combined sources5
Helixi1281 – 1292Combined sources12
Beta strandi1296 – 1303Combined sources8
Helixi1304 – 1307Combined sources4
Beta strandi1314 – 1321Combined sources8
Helixi1339 – 1341Combined sources3
Beta strandi1346 – 1348Combined sources3
Beta strandi1351 – 1353Combined sources3
Helixi1370 – 1374Combined sources5
Beta strandi1375 – 1377Combined sources3
Beta strandi1387 – 1390Combined sources4
Helixi1398 – 1404Combined sources7
Beta strandi1411 – 1413Combined sources3
Helixi1422 – 1429Combined sources8
Beta strandi1433 – 1436Combined sources4
Helixi1439 – 1441Combined sources3
Beta strandi1450 – 1452Combined sources3
Beta strandi1454 – 1456Combined sources3
Turni1465 – 1467Combined sources3
Beta strandi1477 – 1479Combined sources3
Helixi1480 – 1483Combined sources4
Beta strandi1489 – 1491Combined sources3
Beta strandi1495 – 1498Combined sources4
Helixi1501 – 1505Combined sources5
Helixi1506 – 1512Combined sources7
Turni1513 – 1516Combined sources4
Beta strandi1525 – 1527Combined sources3
Beta strandi1536 – 1538Combined sources3
Beta strandi1544 – 1549Combined sources6
Helixi1552 – 1558Combined sources7
Helixi1571 – 1580Combined sources10
Helixi1584 – 1596Combined sources13

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[»]
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

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
Contains 2 BAH domains.PROSITE-ProRule annotation
Contains 1 CXXC-type zinc finger.PROSITE-ProRule annotation
Contains 1 DMAP-interaction domain.Curated
Contains 1 SAM-dependent MTase C5-type domain.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.
OMAiTQYQPIL.
OrthoDBiEOG091G02YU.
PhylomeDBiP13864.
TreeFamiTF328926.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR001025. BAH_dom.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR031303. C5_meth_CS.
IPR022702. Cytosine_MeTrfase1_RFD.
IPR010506. DMAP1-bd.
IPR017198. DNMT1_meta.
IPR029063. SAM-dependent_MTases.
IPR002857. Znf_CXXC.
[Graphical view]
PfamiPF01426. BAH. 2 hits.
PF06464. DMAP_binding. 1 hit.
PF00145. DNA_methylase. 1 hit.
PF12047. DNMT1-RFD. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
PIRSFiPIRSF037404. DNMT1. 1 hit.
PRINTSiPR00105. C5METTRFRASE.
SMARTiSM00439. BAH. 2 hits.
SM01137. DMAP_binding. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51038. 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.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

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]
ENSMUST00000178110; ENSMUSP00000136669; ENSMUSG00000004099. [P13864-2]
GeneIDi13433.
KEGGimmu:13433.
UCSCiuc009ojo.2. mouse. [P13864-1]

Keywords - Coding sequence diversityi

Alternative splicing

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[»]
ProteinModelPortaliP13864.
SMRiP13864.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199259. 22 interactors.
IntActiP13864. 9 interactors.
MINTiMINT-4093291.
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]
ENSMUST00000178110; ENSMUSP00000136669; 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.
OMAiTQYQPIL.
OrthoDBiEOG091G02YU.
PhylomeDBiP13864.
TreeFamiTF328926.

Enzyme and pathway databases

BRENDAi2.1.1.37. 3474.
ReactomeiR-MMU-212300. PRC2 methylates histones and DNA.
R-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-5334118. DNA methylation.
R-MMU-573389. NoRC negatively regulates rRNA expression.

Miscellaneous databases

ChiTaRSiDnmt1. mouse.
EvolutionaryTraceiP13864.
PROiP13864.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000004099.
CleanExiMM_DNMT1.
ExpressionAtlasiP13864. baseline and differential.
GenevisibleiP13864. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR001025. BAH_dom.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR031303. C5_meth_CS.
IPR022702. Cytosine_MeTrfase1_RFD.
IPR010506. DMAP1-bd.
IPR017198. DNMT1_meta.
IPR029063. SAM-dependent_MTases.
IPR002857. Znf_CXXC.
[Graphical view]
PfamiPF01426. BAH. 2 hits.
PF06464. DMAP_binding. 1 hit.
PF00145. DNA_methylase. 1 hit.
PF12047. DNMT1-RFD. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
PIRSFiPIRSF037404. DNMT1. 1 hit.
PRINTSiPR00105. C5METTRFRASE.
SMARTiSM00439. BAH. 2 hits.
SM01137. DMAP_binding. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51038. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDNMT1_MOUSE
AccessioniPrimary (citable) accession number: P13864
Secondary accession number(s): P97413
, Q80ZU3, Q9CSC6, Q9QXX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 21, 2002
Last modified: November 2, 2016
This is version 192 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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 differents 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.

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.