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P13864

- DNMT1_MOUSE

UniProt

P13864 - DNMT1_MOUSE

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Protein

DNA (cytosine-5)-methyltransferase 1

Gene

Dnmt1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 H3K9.3 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi359 – 3591ZincBy similarity
Metal bindingi362 – 3621ZincBy similarity
Metal bindingi420 – 4201ZincBy similarity
Metal bindingi424 – 4241ZincBy similarity
Active sitei1229 – 12291

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri649 – 69547CXXC-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. DNA (cytosine-5-)-methyltransferase activity Source: MGI
  3. DNA binding Source: MGI
  4. methyl-CpG binding Source: MGI
  5. methyltransferase activity Source: UniProtKB
  6. RNA binding Source: MGI
  7. zinc ion binding Source: MGI

GO - Biological processi

  1. cellular response to amino acid stimulus Source: MGI
  2. chromatin modification Source: UniProtKB-KW
  3. DNA methylation Source: MGI
  4. gene silencing Source: UniProtKB
  5. maintenance of DNA methylation Source: UniProtKB
  6. negative regulation of histone H3-K9 methylation Source: Ensembl
  7. negative regulation of transcription, DNA-templated Source: MGI
  8. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  9. positive regulation of gene expression Source: Ensembl
  10. positive regulation of histone H3-K4 methylation Source: Ensembl
  11. regulation of cell proliferation Source: MGI
  12. regulation of gene expression Source: MGI
  13. 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.
ReactomeiREACT_200667. NoRC negatively regulates rRNA expression.
REACT_214440. NoRC negatively regulates rRNA expression.
REACT_222475. PRC2 methylates histones and DNA.
REACT_268475. DNA methylation.

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
ProteomesiUP000000589: 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

  1. cytoplasm Source: UniProtKB-KW
  2. heterochromatin Source: MGI
  3. nucleus Source: MGI
  4. pericentric heterochromatin Source: UniProtKB
  5. replication fork Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi162 – 1621Q → E: Abolishes interaction with PCNA. No effect on activity. 1 Publication
Mutagenesisi169 – 1691F → S: Abolishes interaction with PCNA. No effect on activity. 1 Publication
Mutagenesisi515 – 5151S → A: Loss of activity. No effect on DNA-binding capacity. 1 Publication
Mutagenesisi515 – 5151S → E: Slightly reduces activity. 1 Publication
Mutagenesisi1229 – 12291C → W: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16201620DNA (cytosine-5)-methyltransferase 1PRO_0000088035Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6,N6-dimethyllysine; by EHMT2By similarity
Modified residuei139 – 1391N6-methyllysine; by SETD7By similarity
Modified residuei140 – 1401Phosphoserine; by PKB/AKT1By similarity
Modified residuei146 – 1461Phosphoserine; by CK11 Publication
Modified residuei150 – 1501PhosphoserineBy similarity
Modified residuei152 – 1521Phosphoserine1 Publication
Modified residuei171 – 1711N6-acetyllysineBy similarity
Modified residuei255 – 2551N6-acetyllysineBy similarity
Modified residuei372 – 3721N6-acetyllysineBy similarity
Modified residuei515 – 5151Phosphoserine2 Publications
Modified residuei717 – 7171Phosphoserine2 Publications
Modified residuei735 – 7351PhosphoserineBy similarity
Modified residuei752 – 7521N6-acetyllysineBy similarity
Modified residuei895 – 8951N6-acetyllysineBy similarity
Modified residuei961 – 9611N6-acetyllysineBy similarity
Modified residuei965 – 9651N6-acetyllysineBy similarity
Modified residuei979 – 9791N6-acetyllysineBy similarity
Modified residuei1114 – 11141N6-acetyllysineBy similarity
Modified residuei1116 – 11161N6-acetyllysineBy similarity
Modified residuei1118 – 11181N6-acetyllysineBy similarity
Modified residuei1120 – 11201N6-acetyllysineBy similarity
Modified residuei1122 – 11221N6-acetyllysine1 Publication
Modified residuei1124 – 11241N6-acetyllysine1 Publication
Modified residuei1352 – 13521N6-acetyllysineBy similarity
Modified residuei1418 – 14181N6-acetyllysineBy similarity

Post-translational modificationi

Sumoylated.By similarity
Phosphorylation at Ser-146 by CK1 reduces DNA-binding activity.5 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, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP13864.
PaxDbiP13864.
PRIDEiP13864.

PTM databases

PhosphoSiteiP13864.

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

BgeeiP13864.
CleanExiMM_DNMT1.
ExpressionAtlasiP13864. baseline and differential.
GenevestigatoriP13864.

Interactioni

Subunit structurei

Homodimer. Interacts with HDAC1 and with PCNA. Binds MBD2 and MBD3. Component of complexes containing SUV39H1. Interacts with DNMT3A and DNMT3B (By similarity). Forms a complex with DMAP1 and HDAC2, with direct interaction. Interacts with the PRC2/EED-EZH2 complex. Interacts with UBC9 (By similarity). Interacts with BAZ2A/TIP5. Binds to CSNK1D. Interacts with UHRF1; promoting its recruitment to hemimethylated DNA. Interacts with USP7, promoting its deubiquitination.By similarity7 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi199259. 32 interactions.
IntActiP13864. 4 interactions.
MINTiMINT-4093291.

Structurei

Secondary structure

1
1620
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni360 – 3623Combined sources
Helixi383 – 3875Combined sources
Beta strandi406 – 4083Combined sources
Beta strandi410 – 41910Combined sources
Beta strandi423 – 4253Combined sources
Turni432 – 4365Combined sources
Beta strandi440 – 4456Combined sources
Beta strandi454 – 4585Combined sources
Beta strandi459 – 4657Combined sources
Beta strandi469 – 4735Combined sources
Beta strandi475 – 4795Combined sources
Beta strandi482 – 4865Combined sources
Beta strandi491 – 4944Combined sources
Turni499 – 5013Combined sources
Helixi502 – 52423Combined sources
Helixi530 – 53910Combined sources
Helixi553 – 5586Combined sources
Helixi560 – 57314Combined sources
Helixi581 – 5833Combined sources
Helixi585 – 5939Combined sources
Helixi625 – 63511Combined sources
Beta strandi657 – 6593Combined sources
Turni660 – 6634Combined sources
Turni671 – 6755Combined sources
Turni677 – 6804Combined sources
Helixi690 – 6923Combined sources
Helixi695 – 70410Combined sources
Beta strandi734 – 7396Combined sources
Beta strandi741 – 7433Combined sources
Beta strandi745 – 75511Combined sources
Beta strandi758 – 7614Combined sources
Beta strandi765 – 7684Combined sources
Beta strandi774 – 7763Combined sources
Beta strandi778 – 78811Combined sources
Beta strandi793 – 80210Combined sources
Helixi803 – 8053Combined sources
Helixi809 – 8113Combined sources
Beta strandi816 – 82712Combined sources
Helixi828 – 8303Combined sources
Beta strandi833 – 8353Combined sources
Beta strandi837 – 8393Combined sources
Helixi846 – 8483Combined sources
Beta strandi867 – 8748Combined sources
Turni875 – 8784Combined sources
Beta strandi879 – 8813Combined sources
Turni890 – 8956Combined sources
Helixi898 – 91013Combined sources
Beta strandi913 – 9208Combined sources
Beta strandi922 – 9243Combined sources
Beta strandi925 – 9328Combined sources
Beta strandi935 – 9384Combined sources
Beta strandi942 – 9454Combined sources
Helixi947 – 9493Combined sources
Turni970 – 9723Combined sources
Helixi976 – 9794Combined sources
Beta strandi996 – 100813Combined sources
Beta strandi1011 – 102313Combined sources
Helixi1027 – 10293Combined sources
Turni1031 – 10366Combined sources
Turni1037 – 10393Combined sources
Beta strandi1044 – 10474Combined sources
Beta strandi1051 – 10555Combined sources
Helixi1056 – 10583Combined sources
Beta strandi1061 – 10677Combined sources
Helixi1068 – 10703Combined sources
Helixi1075 – 10817Combined sources
Beta strandi1085 – 10917Combined sources
Turni1094 – 10974Combined sources
Beta strandi1098 – 11003Combined sources
Helixi1104 – 11063Combined sources
Beta strandi1142 – 11476Combined sources
Helixi1153 – 11619Combined sources
Beta strandi1163 – 11708Combined sources
Helixi1174 – 118310Combined sources
Beta strandi1187 – 11904Combined sources
Helixi1194 – 12029Combined sources
Turni1217 – 12193Combined sources
Beta strandi1221 – 12255Combined sources
Turni1230 – 12323Combined sources
Beta strandi1234 – 12363Combined sources
Helixi1240 – 12478Combined sources
Helixi1250 – 126112Combined sources
Beta strandi1264 – 12718Combined sources
Helixi1272 – 12754Combined sources
Turni1276 – 12805Combined sources
Helixi1281 – 129212Combined sources
Beta strandi1296 – 13038Combined sources
Helixi1304 – 13074Combined sources
Beta strandi1314 – 13218Combined sources
Helixi1339 – 13413Combined sources
Beta strandi1346 – 13483Combined sources
Beta strandi1351 – 13533Combined sources
Helixi1370 – 13745Combined sources
Beta strandi1375 – 13773Combined sources
Beta strandi1387 – 13904Combined sources
Helixi1398 – 14047Combined sources
Beta strandi1411 – 14133Combined sources
Helixi1422 – 14298Combined sources
Beta strandi1433 – 14364Combined sources
Helixi1439 – 14413Combined sources
Beta strandi1450 – 14523Combined sources
Beta strandi1454 – 14563Combined sources
Turni1465 – 14673Combined sources
Beta strandi1477 – 14793Combined sources
Helixi1480 – 14834Combined sources
Beta strandi1489 – 14913Combined sources
Beta strandi1495 – 14984Combined sources
Helixi1501 – 15055Combined sources
Helixi1506 – 15127Combined sources
Turni1513 – 15164Combined sources
Beta strandi1525 – 15273Combined sources
Beta strandi1536 – 15383Combined sources
Beta strandi1544 – 15496Combined sources
Helixi1552 – 15587Combined sources
Helixi1571 – 158010Combined sources
Helixi1584 – 159613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 357-603, 651-1600.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13864.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 10689DMAP-interactionAdd
BLAST
Domaini758 – 884127BAH 1PROSITE-ProRule annotationAdd
BLAST
Domaini976 – 1103128BAH 2PROSITE-ProRule annotationAdd
BLAST
Repeati1112 – 111321
Repeati1114 – 111522
Repeati1116 – 111723
Repeati1118 – 111924
Repeati1120 – 112125
Repeati1122 – 112326
Repeati1124 – 112527; approximate
Domaini1142 – 1601460SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 343343Interaction with the PRC2/EED-EZH2 complexAdd
BLAST
Regioni1 – 145145Interaction with DNMT3ABy similarityAdd
BLAST
Regioni1 – 120120Interaction with DMAP1Add
BLAST
Regioni147 – 21771Interaction with DNMT3BBy similarityAdd
BLAST
Regioni161 – 17212Interaction with PCNAAdd
BLAST
Regioni305 – 609305Interaction with the PRC2/EED-EZH2 complexAdd
BLAST
Regioni328 – 556229DNA replication foci-targeting sequenceBy similarityAdd
BLAST
Regioni696 – 813118Interaction with HDAC1Add
BLAST
Regioni696 – 75762Autoinhibitory linkerAdd
BLAST
Regioni1112 – 1125147 X 2 AA tandem repeats of K-GAdd
BLAST
Regioni1124 – 1620497Interaction with the PRC2/EED-EZH2 complexAdd
BLAST
Regioni1142 – 1620479CatalyticAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi175 – 20228Nuclear localization signalSequence AnalysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri649 – 69547CXXC-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0270.
GeneTreeiENSGT00390000005100.
HOVERGENiHBG051384.
InParanoidiP13864.
KOiK00558.
OMAiCPNLAVK.
OrthoDBiEOG77WWBH.
PhylomeDBiP13864.
TreeFamiTF328926.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR001025. BAH_dom.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR022702. Cytosine_MeTrfase1_RFD.
IPR010506. DMAP1-bd.
IPR017198. DNA_C5-MeTrfase_1_euk.
IPR029063. SAM-dependent_MTases-like.
IPR002857. Znf_CXXC.
[Graphical view]
PANTHERiPTHR10629. PTHR10629. 1 hit.
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.
[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. Align

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 AAC52900.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1472SV → F in CAA32910. (PubMed:3210246)Curated
Sequence conflicti146 – 1472SV → F in AAC40061. (PubMed:9449671)Curated
Sequence conflicti299 – 30911AEPEQVAPETP → VRARAGSSRDS in CAA32910. (PubMed:3210246)CuratedAdd
BLAST
Sequence conflicti299 – 30911AEPEQVAPETP → VRARAGSSRDS in AAC40061. (PubMed:9449671)CuratedAdd
BLAST
Sequence conflicti936 – 9361V → C in CAA32910. (PubMed:3210246)Curated
Sequence conflicti936 – 9361V → C in AAC40061. (PubMed:9449671)Curated
Sequence conflicti947 – 9471P → R in CAA32910. (PubMed:3210246)Curated
Sequence conflicti947 – 9471P → R in AAC40061. (PubMed:9449671)Curated
Sequence conflicti969 – 9768NETLYPEH → KENPVPRDT in CAA32910. (PubMed:3210246)Curated
Sequence conflicti969 – 9768NETLYPEH → KENPVPRDT in AAC40061. (PubMed:9449671)Curated
Sequence conflicti987 – 9871S → R in CAA32910. (PubMed:3210246)Curated
Sequence conflicti987 – 9871S → R in AAC40061. (PubMed:9449671)Curated
Sequence conflicti1046 – 10461Y → C in CAA32910. (PubMed:3210246)Curated
Sequence conflicti1046 – 10461Y → C in AAC40061. (PubMed:9449671)Curated
Sequence conflicti1068 – 10681G → R in CAA32910. (PubMed:3210246)Curated
Sequence conflicti1068 – 10681G → R in AAC40061. (PubMed:9449671)Curated
Sequence conflicti1429 – 14291R → P in CAA32910. (PubMed:3210246)Curated
Sequence conflicti1429 – 14291R → P in AAC40061. (PubMed:9449671)Curated
Sequence conflicti1456 – 14561H → D in CAA32910. (PubMed:3210246)Curated
Sequence conflicti1456 – 14561H → D in AAC40061. (PubMed:9449671)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 118118Missing in isoform 2. 3 PublicationsVSP_005619Add
BLAST

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_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 .
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_034196.5. NM_010066.4.
UniGenei Mm.128580.
Mm.485562.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P13864.
SMRi P13864. Positions 357-603, 651-1600.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199259. 32 interactions.
IntActi P13864. 4 interactions.
MINTi MINT-4093291.

Chemistry

GuidetoPHARMACOLOGYi 2605.

Protein family/group databases

REBASEi 2844. M.MmuDnmt1.

PTM databases

PhosphoSitei P13864.

Proteomic databases

MaxQBi P13864.
PaxDbi P13864.
PRIDEi P13864.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000004202 ; ENSMUSP00000004202 ; ENSMUSG00000004099 . [P13864-1 ]
ENSMUST00000178110 ; ENSMUSP00000136669 ; ENSMUSG00000004099 . [P13864-2 ]
GeneIDi 13433.
KEGGi mmu:13433.
UCSCi uc009ojo.2. mouse. [P13864-1 ]

Organism-specific databases

CTDi 1786.
MGIi MGI:94912. Dnmt1.

Phylogenomic databases

eggNOGi COG0270.
GeneTreei ENSGT00390000005100.
HOVERGENi HBG051384.
InParanoidi P13864.
KOi K00558.
OMAi CPNLAVK.
OrthoDBi EOG77WWBH.
PhylomeDBi P13864.
TreeFami TF328926.

Enzyme and pathway databases

BRENDAi 2.1.1.37. 3474.
Reactomei REACT_200667. NoRC negatively regulates rRNA expression.
REACT_214440. NoRC negatively regulates rRNA expression.
REACT_222475. PRC2 methylates histones and DNA.
REACT_268475. DNA methylation.

Miscellaneous databases

ChiTaRSi Dnmt1. mouse.
EvolutionaryTracei P13864.
NextBioi 283859.
PROi P13864.
SOURCEi Search...

Gene expression databases

Bgeei P13864.
CleanExi MM_DNMT1.
ExpressionAtlasi P13864. baseline and differential.
Genevestigatori P13864.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR001025. BAH_dom.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR022702. Cytosine_MeTrfase1_RFD.
IPR010506. DMAP1-bd.
IPR017198. DNA_C5-MeTrfase_1_euk.
IPR029063. SAM-dependent_MTases-like.
IPR002857. Znf_CXXC.
[Graphical view ]
PANTHERi PTHR10629. PTHR10629. 1 hit.
Pfami PF01426. 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 ]
PIRSFi PIRSF037404. DNMT1. 1 hit.
PRINTSi PR00105. C5METTRFRASE.
SMARTi SM00439. BAH. 2 hits.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 2 hits.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of a cDNA encoding DNA methyltransferase of mouse cells. The carboxyl-terminal domain of the mammalian enzymes is related to bacterial restriction methyltransferases."
    Bestor T.H., Laudano A., Mattaliano R., Ingram V.
    J. Mol. Biol. 203:971-983(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "New 5' regions of the murine and human genes for DNA (cytosine-5)-methyltransferase."
    Yoder J.A., Yen R.-W.C., Vertino P.M., Bestor T.H., Baylin S.B.
    J. Biol. Chem. 271:31092-31097(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO N-TERMINUS.
    Tissue: Embryo.
  3. "Expression of an alternative Dnmt1 isoform during muscle differentiation."
    Aguirre-Arteta A.M., Grunewald I., Cardoso M.C., Leonhardt H.
    Cell Growth Differ. 11:551-559(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: C57BL/6.
    Tissue: Skeletal muscle.
  4. "Structure and function of the mouse DNA methyltransferase gene: Dnmt1 shows a tripartite structure."
    Margot J.B., Aguirre-Arteta A.M., Di Giacco B.V., Pradhan S., Roberts R.J., Cardoso M.C., Leonhardt H.
    J. Mol. Biol. 297:293-300(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Brain.
  6. "Sex-specific exons control DNA methyltransferase in mammalian germ cells."
    Mertineit C., Yoder J.A., Taketo T., Laird D.W., Trasler J.M., Bestor T.H.
    Development 125:889-897(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-27 AND 119-1619 (ISOFORMS 1 AND 2).
  7. "A short DNA methyltransferase isoform restores methylation in vivo."
    Gaudet F., Talbot D., Leonhardt H., Jaenisch R.
    J. Biol. Chem. 273:32725-32729(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-144 (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 3-6.
    Strain: 129/Sv and BALB/c.
    Tissue: Embryonic stem cell.
  8. "Complementation of methylation deficiency in embryonic stem cells by a DNA methyltransferase minigene."
    Tucker K.L., Talbot D., Lee M.A., Leonhardt H., Jaenisch R.
    Proc. Natl. Acad. Sci. U.S.A. 93:12920-12925(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-119 (ISOFORM 1).
    Strain: 129/Sv.
    Tissue: Embryonic stem cell and Kidney.
  9. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-272 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Embryo.
  10. "Activation of mammalian DNA methyltransferase by cleavage of a Zn binding regulatory domain."
    Bestor T.H.
    EMBO J. 11:2611-2617(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1108-1154, ENZYME REGULATION.
  11. "Peptide mapping of the murine DNA methyltransferase reveals a major phosphorylation site and the start of translation."
    Glickman J.F., Pavlovich J.G., Reich N.O.
    J. Biol. Chem. 272:17851-17857(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-515, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Erythroleukemia.
  12. "DNA methyltransferase Dnmt1 associates with histone deacetylase activity."
    Fuks F., Burgers W.A., Brehm A., Hughes-Davies L., Kouzarides T.
    Nat. Genet. 24:88-91(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC1.
  13. "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci."
    Rountree M.R., Bachman K.E., Baylin S.B.
    Nat. Genet. 25:269-277(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC2 AND DMAP1.
  14. "Genomic imprinting disrupted by a maternal effect mutation in the Dnmt1 gene."
    Howell C.Y., Bestor T.H., Ding F., Latham K.E., Mertineit C., Trasler J.M., Chaillet J.R.
    Cell 104:829-838(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "The activity of the murine DNA methyltransferase Dnmt1 is controlled by interaction of the catalytic domain with the N-terminal part of the enzyme leading to an allosteric activation of the enzyme after binding to methylated DNA."
    Fatemi M., Hermann A., Pradhan S., Jeltsch A.
    J. Mol. Biol. 309:1189-1199(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALLOSTERIC REGULATION.
  16. "Replication-independent chromatin loading of Dnmt1 during G2 and M phases."
    Easwaran H.P., Schermelleh L., Leonhardt H., Cardoso M.C.
    EMBO Rep. 5:1181-1186(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 and is sufficient for rDNA silencing."
    Zhou Y., Grummt I.
    Curr. Biol. 15:1434-1438(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAZ2A.
  18. Cited for: INTERACTION WITH THE PRC2 COMPLEX.
  19. "Phosphorylation of serine-515 activates the mammalian maintenance methyltransferase Dnmt1."
    Goyal R., Rathert P., Laser H., Gowher H., Jeltsch A.
    Epigenetics 2:155-160(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-515, MUTAGENESIS OF SER-515.
  20. "Dynamics of Dnmt1 interaction with the replication machinery and its role in postreplicative maintenance of DNA methylation."
    Schermelleh L., Haemmer A., Spada F., Roesing N., Meilinger D., Rothbauer U., Cardoso M.C., Leonhardt H.
    Nucleic Acids Res. 35:4301-4312(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLN-162; PHE-169 AND CYS-1229.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-717, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-717, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Usp7 and Uhrf1 control ubiquitination and stability of the maintenance DNA methyltransferase Dnmt1."
    Qin W., Leonhardt H., Spada F.
    J. Cell. Biochem. 112:439-444(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP7, INTERACTION WITH USP7 AND UHRF1.
  24. "The DNA-binding activity of mouse DNA methyltransferase 1 is regulated by phosphorylation with casein kinase 1delta/epsilon."
    Sugiyama Y., Hatano N., Sueyoshi N., Suetake I., Tajima S., Kinoshita E., Kinoshita-Kikuta E., Koike T., Kameshita I.
    Biochem. J. 427:489-497(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-146 BY CSNK1D/CK1, INTERACTION WITH CSNK1D.
  25. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1122 AND LYS-1124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  26. "Structure of DNMT1-DNA complex reveals a role for autoinhibition in maintenance DNA methylation."
    Song J., Rechkoblit O., Bestor T.H., Patel D.J.
    Science 331:1036-1040(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 731-1602 IN COMPLEX WITH SAH AND DNA, AUTOINHIBITORY LINKER.

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 26, 2014
This is version 171 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

External Data

Dasty 3