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P13864

- DNMT1_MOUSE

UniProt

P13864 - DNMT1_MOUSE

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
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 5 (21 Feb 2002)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    7. RNA binding Source: MGI
    8. 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

    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.

    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-SubCell
    2. heterochromatin Source: MGI
    3. nucleus Source: MGI
    4. pericentric heterochromatin Source: UniProtKB
    5. replication fork Source: MGI

    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

    ArrayExpressiP13864.
    BgeeiP13864.
    CleanExiMM_DNMT1.
    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 – 3623
    Helixi383 – 3875
    Beta strandi406 – 4083
    Beta strandi410 – 41910
    Beta strandi423 – 4253
    Turni432 – 4365
    Beta strandi440 – 4456
    Beta strandi454 – 4585
    Beta strandi459 – 4657
    Beta strandi469 – 4735
    Beta strandi475 – 4795
    Beta strandi482 – 4865
    Beta strandi491 – 4944
    Turni499 – 5013
    Helixi502 – 52423
    Helixi530 – 53910
    Helixi553 – 5586
    Helixi560 – 57314
    Helixi581 – 5833
    Helixi585 – 5939
    Helixi625 – 63511
    Beta strandi657 – 6593
    Turni660 – 6634
    Turni671 – 6755
    Turni677 – 6804
    Helixi690 – 6923
    Helixi695 – 70410
    Beta strandi734 – 7396
    Beta strandi741 – 7433
    Beta strandi745 – 75511
    Beta strandi758 – 7614
    Beta strandi765 – 7684
    Beta strandi774 – 7763
    Beta strandi778 – 78811
    Beta strandi793 – 80210
    Helixi803 – 8053
    Helixi809 – 8113
    Beta strandi816 – 82712
    Helixi828 – 8303
    Beta strandi833 – 8353
    Beta strandi837 – 8393
    Helixi846 – 8483
    Beta strandi867 – 8748
    Turni875 – 8784
    Beta strandi879 – 8813
    Turni890 – 8956
    Helixi898 – 91013
    Beta strandi913 – 9208
    Beta strandi922 – 9243
    Beta strandi925 – 9328
    Beta strandi935 – 9384
    Beta strandi942 – 9454
    Helixi947 – 9493
    Turni970 – 9723
    Helixi976 – 9794
    Beta strandi996 – 100813
    Beta strandi1011 – 102313
    Helixi1027 – 10293
    Turni1031 – 10366
    Turni1037 – 10393
    Beta strandi1044 – 10474
    Beta strandi1051 – 10555
    Helixi1056 – 10583
    Beta strandi1061 – 10677
    Helixi1068 – 10703
    Helixi1075 – 10817
    Beta strandi1085 – 10917
    Turni1094 – 10974
    Beta strandi1098 – 11003
    Helixi1104 – 11063
    Beta strandi1142 – 11476
    Helixi1153 – 11619
    Beta strandi1163 – 11708
    Helixi1174 – 118310
    Beta strandi1187 – 11904
    Helixi1194 – 12029
    Turni1217 – 12193
    Beta strandi1221 – 12255
    Turni1230 – 12323
    Beta strandi1234 – 12363
    Helixi1240 – 12478
    Helixi1250 – 126112
    Beta strandi1264 – 12718
    Helixi1272 – 12754
    Turni1276 – 12805
    Helixi1281 – 129212
    Beta strandi1296 – 13038
    Helixi1304 – 13074
    Beta strandi1314 – 13218
    Helixi1339 – 13413
    Beta strandi1346 – 13483
    Beta strandi1351 – 13533
    Helixi1370 – 13745
    Beta strandi1375 – 13773
    Beta strandi1387 – 13904
    Helixi1398 – 14047
    Beta strandi1411 – 14133
    Helixi1422 – 14298
    Beta strandi1433 – 14364
    Helixi1439 – 14413
    Beta strandi1450 – 14523
    Beta strandi1454 – 14563
    Turni1465 – 14673
    Beta strandi1477 – 14793
    Helixi1480 – 14834
    Beta strandi1489 – 14913
    Beta strandi1495 – 14984
    Helixi1501 – 15055
    Helixi1506 – 15127
    Turni1513 – 15164
    Beta strandi1525 – 15273
    Beta strandi1536 – 15383
    Beta strandi1544 – 15496
    Helixi1552 – 15587
    Helixi1571 – 158010
    Helixi1584 – 159613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MPARTAPARV PALASPAGSL PDHVRRRLKD LERDGLTEKE CVREKLNLLH     50
    EFLQTEIKSQ LCDLETKLHK EELSEEGYLA KVKSLLNKDL SLENGTHTLT 100
    QKANGCPANG SRPTWRAEMA DSNRSPRSRP KPRGPRRSKS DSDTLSVETS 150
    PSSVATRRTT RQTTITAHFT KGPTKRKPKE ESEEGNSAES AAEERDQDKK 200
    RRVVDTESGA AAAVEKLEEV TAGTQLGPEE PCEQEDDNRS LRRHTRELSL 250
    RRKSKEDPDR EARPETHLDE DEDGKKDKRS SRPRSQPRDP AAKRRPKEAE 300
    PEQVAPETPE DRDEDEREEK RRKTTRKKLE SHTVPVQSRS ERKAAQSKSV 350
    IPKINSPKCP ECGQHLDDPN LKYQQHPEDA VDEPQMLTSE KLSIYDSTST 400
    WFDTYEDSPM HRFTSFSVYC SRGHLCPVDT GLIEKNVELY FSGCAKAIHD 450
    ENPSMEGGIN GKNLGPINQW WLSGFDGGEK VLIGFSTAFA EYILMEPSKE 500
    YEPIFGLMQE KIYISKIVVE FLQNNPDAVY EDLINKIETT VPPSTINVNR 550
    FTEDSLLRHA QFVVSQVESY DEAKDDDETP IFLSPCMRAL IHLAGVSLGQ 600
    RRATRRVMGA TKEKDKAPTK ATTTKLVYQI FDTFFSEQIE KYDKEDKENA 650
    MKRRRCGVCE VCQQPECGKC KACKDMVKFG GTGRSKQACL KRRCPNLAVK 700
    EADDDEEADD DVSEMPSPKK LHQGKKKKQN KDRISWLGQP MKIEENRTYY 750
    QKVSIDEEML EVGDCVSVIP DDSSKPLYLA RVTALWEDKN GQMMFHAHWF 800
    CAGTDTVLGA TSDPLELFLV GECENMQLSY IHSKVKVIYK APSENWAMEG 850
    GTDPETTLPG AEDGKTYFFQ LWYNQEYARF ESPPKTQPTE DNKHKFCLSC 900
    IRLAELRQKE MPKVLEQIEE VDGRVYCSSI TKNGVVYRLG DSVYLPPEAF 950
    TFNIKVASPV KRPKKDPVNE TLYPEHYRKY SDYIKGSNLD APEPYRIGRI 1000
    KEIHCGKKKG KVNEADIKLR LYKFYRPENT HRSYNGSYHT DINMLYWSDE 1050
    EAVVNFSDVQ GRCTVEYGED LLESIQDYSQ GGPDRFYFLE AYNSKTKNFE 1100
    DPPNHARSPG NKGKGKGKGK GKGKHQVSEP KEPEAAIKLP KLRTLDVFSG 1150
    CGGLSEGFHQ AGISETLWAI EMWDPAAQAF RLNNPGTTVF TEDCNVLLKL 1200
    VMAGEVTNSL GQRLPQKGDV EMLCGGPPCQ GFSGMNRFNS RTYSKFKNSL 1250
    VVSFLSYCDY YRPRFFLLEN VRNFVSYRRS MVLKLTLRCL VRMGYQCTFG 1300
    VLQAGQYGVA QTRRRAIILA AAPGEKLPLF PEPLHVFAPR ACQLSVVVDD 1350
    KKFVSNITRL SSGPFRTITV RDTMSDLPEI QNGASNSEIP YNGEPLSWFQ 1400
    RQLRGSHYQP ILRDHICKDM SPLVAARMRH IPLFPGSDWR DLPNIQVRLG 1450
    DGVIAHKLQY TFHDVKNGYS STGALRGVCS CAEGKACDPE SRQFSTLIPW 1500
    CLPHTGNRHN HWAGLYGRLE WDGFFSTTVT NPEPMGKQGR VLHPEQHRVV 1550
    SVRECARSQG FPDSYRFFGN ILDRHRQVGN AVPPPLAKAI GLEIKLCLLS 1600
    SARESASAAV KAKEEAATKD 1620
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.

    Miscellaneous databases

    ChiTaRSi DNMT1. mouse.
    EvolutionaryTracei P13864.
    NextBioi 283859.
    PROi P13864.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13864.
    Bgeei P13864.
    CleanExi MM_DNMT1.
    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

    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: October 1, 2014
    This is version 169 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