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P26358

- DNMT1_HUMAN

UniProt

P26358 - DNMT1_HUMAN

Protein

DNA (cytosine-5)-methyltransferase 1

Gene

DNMT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 2 (11 Jan 2001)
      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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi353 – 3531Zinc
    Metal bindingi356 – 3561Zinc
    Metal bindingi414 – 4141Zinc
    Metal bindingi418 – 4181Zinc
    Sitei509 – 5091Important for activityBy similarity
    Active sitei1226 – 12261

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri646 – 69247CXXC-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular response to amino acid stimulus Source: Ensembl
    2. chromatin modification Source: UniProtKB-KW
    3. DNA methylation Source: ProtInc
    4. gene silencing Source: Ensembl
    5. maintenance of DNA methylation Source: UniProtKB
    6. negative regulation of histone H3-K9 methylation Source: UniProtKB
    7. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
    8. positive regulation of gene expression Source: UniProtKB
    9. positive regulation of histone H3-K4 methylation Source: UniProtKB
    10. regulation of cell proliferation Source: Ensembl
    11. 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. 2681.
    ReactomeiREACT_200808. PRC2 methylates histones and DNA.
    REACT_200856. NoRC negatively regulates rRNA expression.

    Protein family/group databases

    REBASEi1161. M.HsaDnmt1A.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA (cytosine-5)-methyltransferase 1 (EC:2.1.1.37)
    Short name:
    Dnmt1
    Alternative name(s):
    CXXC-type zinc finger protein 9
    DNA methyltransferase HsaI
    Short name:
    DNA MTase HsaI
    Short name:
    M.HsaI
    MCMT
    Gene namesi
    Name:DNMT1
    Synonyms:AIM, CXXC9, DNMT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:2976. DNMT1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: ProtInc
    2. pericentric heterochromatin Source: Ensembl
    3. replication fork Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Neuropathy, hereditary sensory, 1E (HSN1E) [MIM:614116]: A neurodegenerative disorder characterized by adult onset of progressive peripheral sensory loss associated with progressive hearing impairment and early-onset dementia.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti490 – 4912DP → EY in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase.
    VAR_065965
    Natural varianti495 – 4951Y → C in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase. 1 Publication
    VAR_065966
    Cerebellar ataxia, deafness, and narcolepsy, autosomal dominant (ADCADN) [MIM:604121]: An autosomal dominant neurologic disorder characterized by adult onset of progressive cerebellar ataxia, narcolepsy, cataplexy, sensorineural deafness, and dementia. More variable features include optic atrophy, sensory neuropathy, psychosis, and depression.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti554 – 5541A → V in ADCADN. 1 Publication
    VAR_070055
    Natural varianti589 – 5891G → A in ADCADN. 1 Publication
    VAR_070056
    Natural varianti590 – 5901V → F in ADCADN. 1 Publication
    VAR_070057

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi163 – 1631R → A: Abolishes interaction with PCNA. 1 Publication
    Mutagenesisi164 – 1641Q → A: Abolishes interaction with PCNA. 1 Publication
    Mutagenesisi166 – 1661T → A: Abolishes interaction with PCNA. 1 Publication
    Mutagenesisi167 – 1671I → A: Abolishes interaction with PCNA. 1 Publication
    Mutagenesisi169 – 1691S → A: No loss of interaction with PCNA. 1 Publication
    Mutagenesisi170 – 1701H → V: Abolishes interaction with PCNA. 1 Publication
    Mutagenesisi171 – 1711F → V: Abolishes interaction with PCNA. 1 Publication
    Mutagenesisi172 – 1721A → S: No loss of interaction with PCNA. 1 Publication
    Mutagenesisi173 – 1731K → A: No loss of interaction with PCNA. 1 Publication
    Mutagenesisi653 – 6531C → G: Reduces activity about 10-fold; when associated with G-656; G-659; G-664; G-667 and G-670. 2 Publications
    Mutagenesisi656 – 6561C → G: Reduces activity about 10-fold; when associated with G-653; G-659; G-664; G-667 and G-670. 2 Publications
    Mutagenesisi659 – 6591C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-664; G-667 and G-670. 2 Publications
    Mutagenesisi664 – 6641C → F: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-667 and G-670. 2 Publications
    Mutagenesisi667 – 6671C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-670. 2 Publications
    Mutagenesisi670 – 6701C → G: Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-667. 2 Publications
    Mutagenesisi1226 – 12261C → A: Loss of activity. 2 Publications

    Keywords - Diseasei

    Deafness, Disease mutation, Neuropathy

    Organism-specific databases

    MIMi604121. phenotype.
    614116. phenotype.
    Orphaneti314404. Cerebellar ataxia-deafness-narcolepsy syndrome.
    PharmGKBiPA27443.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 16161616DNA (cytosine-5)-methyltransferase 1PRO_0000088034Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei70 – 701N6,N6-dimethyllysine1 Publication
    Modified residuei127 – 1271Phosphoserine4 Publications
    Modified residuei133 – 1331Phosphoserine1 Publication
    Modified residuei142 – 1421N6-methyllysine; by SETD71 Publication
    Modified residuei143 – 1431Phosphoserine; by PKB/AKT12 Publications
    Modified residuei152 – 1521Phosphoserine1 Publication
    Modified residuei154 – 1541Phosphoserine2 Publications
    Modified residuei160 – 1601N6-acetyllysine1 Publication
    Modified residuei173 – 1731N6-acetyllysine1 Publication
    Modified residuei188 – 1881N6-acetyllysine1 Publication
    Modified residuei259 – 2591N6-acetyllysine1 Publication
    Modified residuei366 – 3661N6-acetyllysine1 Publication
    Modified residuei394 – 3941Phosphoserine2 Publications
    Modified residuei509 – 5091PhosphoserineBy similarity
    Modified residuei714 – 7141Phosphoserine3 Publications
    Modified residuei732 – 7321Phosphoserine1 Publication
    Modified residuei749 – 7491N6-acetyllysine1 Publication
    Modified residuei891 – 8911N6-acetyllysine1 Publication
    Modified residuei957 – 9571N6-acetyllysine1 Publication
    Modified residuei961 – 9611N6-acetyllysine1 Publication
    Modified residuei975 – 9751N6-acetyllysine1 Publication
    Modified residuei1054 – 10541N6-acetyllysine1 Publication
    Modified residuei1111 – 11111N6-acetyllysine2 Publications
    Modified residuei1113 – 11131N6-acetyllysine2 Publications
    Modified residuei1115 – 11151N6-acetyllysine2 Publications
    Modified residuei1117 – 11171N6-acetyllysine; by EHMT21 Publication
    Modified residuei1119 – 11191N6-acetyllysineBy similarity
    Modified residuei1121 – 11211N6-acetyllysineBy similarity
    Modified residuei1349 – 13491N6-acetyllysine1 Publication
    Modified residuei1415 – 14151N6-acetyllysine1 Publication

    Post-translational modificationi

    Sumoylated; sumoylation increases activity.1 Publication
    Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates cell cycle G2/M transition. Deacetylation of Lys-1349 and Lys-1415 by SIRT1 increases methyltransferase activity.2 Publications
    Phosphorylation of Ser-154 by CDKs is important for enzymatic activity and protein stability. Phosphorylation of Ser-143 by AKT1 prevents methylation by SETD7 therebye increasing DNMT1 stability.8 Publications
    Methylation at Lys-142 by SETD7 promotes DNMT1 proteasomal degradation.2 Publications
    Ubiquitinated by UHRF1; interaction with USP7 counteracts ubiquitination by UHRF1 by promoting deubiquitination and preventing degradation by the proteasome.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP26358.
    PaxDbiP26358.
    PRIDEiP26358.

    PTM databases

    PhosphoSiteiP26358.

    Expressioni

    Tissue specificityi

    Ubiquitous; highly expressed in fetal tissues, heart, kidney, placenta, peripheral blood mononuclear cells, and expressed at lower levels in spleen, lung, brain, small intestine, colon, liver, and skeletal muscle. Isoform 2 is less expressed than isoform 1.1 Publication

    Inductioni

    Its abundance is reduced to non detectable levels at the G0 phase of the cell cycle and is dramatically induced upon entrance into the S-phase of the cell cycle.

    Gene expression databases

    ArrayExpressiP26358.
    BgeeiP26358.
    CleanExiHS_DNMT1.
    GenevestigatoriP26358.

    Organism-specific databases

    HPAiCAB005876.
    HPA002694.

    Interactioni

    Subunit structurei

    Binds to CSNK1D By similarity. Homodimer. Interacts with HDAC1 and with PCNA. Forms a complex with DMAP1 and HDAC2, with direct interaction. Forms also a stable complex with E2F1, BB1 and HDAC1. Binds MBD2 and MBD3. Component of complexes containing SUV39H1. Interacts with DNMT3A and DNMT3B. Interacts with the PRC2/EED-EZH2 complex. Interacts with UBC9 and BAZ2A/TIP5. Interacts with UHRF1; promoting its recruitment to hemimethylated DNA. Interacts with USP7, promoting its deubiquitination.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EEDO755303EBI-719459,EBI-923794
    EZH2Q159108EBI-719459,EBI-530054
    NRIP1P485523EBI-719459,EBI-746484
    SIRT1Q96EB611EBI-719459,EBI-1802965
    UHRF1Q96T8812EBI-719459,EBI-1548946

    Protein-protein interaction databases

    BioGridi108123. 75 interactions.
    DIPiDIP-39693N.
    IntActiP26358. 21 interactions.
    MINTiMINT-232346.
    STRINGi9606.ENSP00000352516.

    Structurei

    Secondary structure

    1
    1616
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni354 – 3563
    Helixi377 – 38913
    Beta strandi405 – 4139
    Beta strandi422 – 4254
    Turni426 – 4305
    Beta strandi434 – 4418
    Beta strandi453 – 4586
    Beta strandi462 – 4676
    Beta strandi476 – 4805
    Beta strandi485 – 4884
    Turni493 – 4953
    Helixi496 – 4994
    Helixi504 – 51815
    Helixi524 – 53310
    Helixi538 – 5403
    Helixi547 – 5515
    Helixi554 – 56714
    Helixi575 – 5773
    Helixi579 – 5879
    Helixi592 – 5987
    Helixi622 – 6298
    Turni657 – 6593
    Helixi670 – 6723
    Helixi687 – 6893
    Beta strandi731 – 7355
    Beta strandi744 – 7463
    Beta strandi748 – 7525
    Beta strandi755 – 7584
    Beta strandi762 – 7654
    Beta strandi767 – 7693
    Beta strandi775 – 78511
    Turni786 – 7883
    Beta strandi789 – 79911
    Helixi800 – 8023
    Helixi806 – 8083
    Beta strandi813 – 82412
    Helixi825 – 8273
    Beta strandi828 – 8325
    Beta strandi834 – 8363
    Helixi843 – 8453
    Helixi856 – 8605
    Beta strandi862 – 8709
    Turni871 – 8744
    Beta strandi875 – 8773
    Turni889 – 8913
    Helixi894 – 90512
    Beta strandi912 – 9165
    Beta strandi921 – 9288
    Beta strandi931 – 9344
    Beta strandi938 – 9414
    Turni966 – 9683
    Helixi973 – 9753
    Helixi976 – 9805
    Beta strandi992 – 100110
    Beta strandi1005 – 10084
    Beta strandi1015 – 10206
    Helixi1024 – 10263
    Helixi1031 – 10344
    Beta strandi1035 – 10373
    Beta strandi1041 – 10444
    Beta strandi1048 – 10525
    Helixi1053 – 10553
    Beta strandi1058 – 10647
    Helixi1065 – 10673
    Helixi1072 – 10776
    Beta strandi1079 – 109012
    Turni1091 – 10944
    Beta strandi1095 – 10973
    Beta strandi1139 – 11457
    Helixi1150 – 11589
    Beta strandi1160 – 11678
    Helixi1171 – 118010
    Beta strandi1184 – 11874
    Helixi1191 – 120010
    Turni1214 – 12163
    Beta strandi1218 – 12225
    Beta strandi1231 – 12333
    Helixi1237 – 12437
    Helixi1247 – 125812
    Beta strandi1261 – 12688
    Helixi1269 – 12724
    Helixi1275 – 12773
    Helixi1278 – 128912
    Beta strandi1293 – 13008
    Helixi1301 – 13044
    Beta strandi1311 – 13188
    Helixi1336 – 13383
    Beta strandi1343 – 13453
    Beta strandi1348 – 13503
    Helixi1367 – 13715
    Beta strandi1384 – 13863
    Helixi1395 – 14017
    Helixi1419 – 14268
    Helixi1436 – 14383
    Beta strandi1451 – 14533
    Turni1462 – 14643
    Helixi1477 – 14793
    Beta strandi1480 – 14823
    Helixi1487 – 14893
    Beta strandi1493 – 14964
    Helixi1499 – 15035
    Helixi1504 – 15063
    Helixi1508 – 15103
    Turni1511 – 15144
    Beta strandi1523 – 15253
    Beta strandi1542 – 15476
    Helixi1550 – 15567
    Helixi1569 – 157810
    Helixi1582 – 159817

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EPZX-ray2.31A/B351-600[»]
    3PTAX-ray3.60A646-1600[»]
    3SWRX-ray2.49A601-1600[»]
    ProteinModelPortaliP26358.
    SMRiP26358. Positions 351-599, 601-1600.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26358.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 10386DMAP-interactionAdd
    BLAST
    Domaini755 – 880126BAH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini972 – 1100129BAH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati1109 – 111021
    Repeati1111 – 111222
    Repeati1113 – 111423
    Repeati1115 – 111624
    Repeati1117 – 111825
    Repeati1119 – 112026; approximate
    Domaini1139 – 1599461SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 336336Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
    BLAST
    Regioni1 – 148148Interaction with DNMT3AAdd
    BLAST
    Regioni1 – 120120Interaction with DMAP1Add
    BLAST
    Regioni149 – 21769Interaction with DNMT3BAdd
    BLAST
    Regioni163 – 17412Interaction with PCNAAdd
    BLAST
    Regioni308 – 606299Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
    BLAST
    Regioni310 – 502193HomodimerizationAdd
    BLAST
    Regioni331 – 550220DNA replication foci-targeting sequenceBy similarityAdd
    BLAST
    Regioni651 – 69747Required for activityAdd
    BLAST
    Regioni693 – 75462Autoinhibitory linkerAdd
    BLAST
    Regioni1109 – 1120126 X 2 AA tandem repeats of K-GAdd
    BLAST
    Regioni1121 – 1616496Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
    BLAST
    Regioni1139 – 1616478CatalyticAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi177 – 20529Nuclear 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 fingeri646 – 69247CXXC-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0270.
    HOGENOMiHOG000082497.
    HOVERGENiHBG051384.
    KOiK00558.
    OMAiCPNLAVK.
    OrthoDBiEOG77WWBH.
    PhylomeDBiP26358.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P26358-1) [UniParc]FASTAAdd to Basket

    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 PTLAVPAISL PDDVRRRLKD LERDSLTEKE CVKEKLNLLH     50
    EFLQTEIKNQ LCDLETKLRK EELSEEGYLA KVKSLLNKDL SLENGAHAYN 100
    REVNGRLENG NQARSEARRV GMADANSPPK PLSKPRTPRR SKSDGEAKPE 150
    PSPSPRITRK STRQTTITSH FAKGPAKRKP QEESERAKSD ESIKEEDKDQ 200
    DEKRRRVTSR ERVARPLPAE EPERAKSGTR TEKEEERDEK EEKRLRSQTK 250
    EPTPKQKLKE EPDREARAGV QADEDEDGDE KDEKKHRSQP KDLAAKRRPE 300
    EKEPEKVNPQ ISDEKDEDEK EEKRRKTTPK EPTEKKMARA KTVMNSKTHP 350
    PKCIQCGQYL DDPDLKYGQH PPDAVDEPQM LTNEKLSIFD ANESGFESYE 400
    ALPQHKLTCF SVYCKHGHLC PIDTGLIEKN IELFFSGSAK PIYDDDPSLE 450
    GGVNGKNLGP INEWWITGFD GGEKALIGFS TSFAEYILMD PSPEYAPIFG 500
    LMQEKIYISK IVVEFLQSNS DSTYEDLINK IETTVPPSGL NLNRFTEDSL 550
    LRHAQFVVEQ VESYDEAGDS DEQPIFLTPC MRDLIKLAGV TLGQRRAQAR 600
    RQTIRHSTRE KDRGPTKATT TKLVYQIFDT FFAEQIEKDD REDKENAFKR 650
    RRCGVCEVCQ QPECGKCKAC KDMVKFGGSG RSKQACQERR CPNMAMKEAD 700
    DDEEVDDNIP EMPSPKKMHQ GKKKKQNKNR ISWVGEAVKT DGKKSYYKKV 750
    CIDAETLEVG DCVSVIPDDS SKPLYLARVT ALWEDSSNGQ MFHAHWFCAG 800
    TDTVLGATSD PLELFLVDEC EDMQLSYIHS KVKVIYKAPS ENWAMEGGMD 850
    PESLLEGDDG KTYFYQLWYD QDYARFESPP KTQPTEDNKF KFCVSCARLA 900
    EMRQKEIPRV LEQLEDLDSR VLYYSATKNG ILYRVGDGVY LPPEAFTFNI 950
    KLSSPVKRPR KEPVDEDLYP EHYRKYSDYI KGSNLDAPEP YRIGRIKEIF 1000
    CPKKSNGRPN ETDIKIRVNK FYRPENTHKS TPASYHADIN LLYWSDEEAV 1050
    VDFKAVQGRC TVEYGEDLPE CVQVYSMGGP NRFYFLEAYN AKSKSFEDPP 1100
    NHARSPGNKG KGKGKGKGKP KSQACEPSEP EIEIKLPKLR TLDVFSGCGG 1150
    LSEGFHQAGI SDTLWAIEMW DPAAQAFRLN NPGSTVFTED CNILLKLVMA 1200
    GETTNSRGQR LPQKGDVEML CGGPPCQGFS GMNRFNSRTY SKFKNSLVVS 1250
    FLSYCDYYRP RFFLLENVRN FVSFKRSMVL KLTLRCLVRM GYQCTFGVLQ 1300
    AGQYGVAQTR RRAIILAAAP GEKLPLFPEP LHVFAPRACQ LSVVVDDKKF 1350
    VSNITRLSSG PFRTITVRDT MSDLPEVRNG ASALEISYNG EPQSWFQRQL 1400
    RGAQYQPILR DHICKDMSAL VAARMRHIPL APGSDWRDLP NIEVRLSDGT 1450
    MARKLRYTHH DRKNGRSSSG ALRGVCSCVE AGKACDPAAR QFNTLIPWCL 1500
    PHTGNRHNHW AGLYGRLEWD GFFSTTVTNP EPMGKQGRVL HPEQHRVVSV 1550
    RECARSQGFP DTYRLFGNIL DKHRQVGNAV PPPLAKAIGL EIKLCMLAKA 1600
    RESASAKIKE EEAAKD 1616
    Length:1,616
    Mass (Da):183,165
    Last modified:January 11, 2001 - v2
    Checksum:i1E833192D22AFA5B
    GO
    Isoform 2 (identifier: P26358-2) [UniParc]FASTAAdd to Basket

    Also known as: Dnmt1b

    The sequence of this isoform differs from the canonical sequence as follows:
         149-149: P → RSRDPPASASQVTGIRA

    Show »
    Length:1,632
    Mass (Da):184,819
    Checksum:i650AA14F73A75649
    GO
    Isoform 3 (identifier: P26358-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-336: Missing.

    Show »
    Length:1,280
    Mass (Da):144,465
    Checksum:i70ECEE72AE313EE9
    GO

    Sequence cautioni

    The sequence AAD54507.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti97 – 971H → R.
    Corresponds to variant rs16999593 [ dbSNP | Ensembl ].
    VAR_024605
    Natural varianti311 – 3111I → V.
    Corresponds to variant rs2228612 [ dbSNP | Ensembl ].
    VAR_051960
    Natural varianti490 – 4912DP → EY in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase.
    VAR_065965
    Natural varianti495 – 4951Y → C in HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase. 1 Publication
    VAR_065966
    Natural varianti554 – 5541A → V in ADCADN. 1 Publication
    VAR_070055
    Natural varianti589 – 5891G → A in ADCADN. 1 Publication
    VAR_070056
    Natural varianti590 – 5901V → F in ADCADN. 1 Publication
    VAR_070057

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 336336Missing in isoform 3. 1 PublicationVSP_005617Add
    BLAST
    Alternative sequencei149 – 1491P → RSRDPPASASQVTGIRA in isoform 2. 1 PublicationVSP_005618

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63692 mRNA. Translation: CAA45219.1.
    AF180682 mRNA. Translation: AAF23609.1.
    AC010077 Genomic DNA. Translation: AAD54507.1. Sequence problems.
    AC011511 Genomic DNA. No translation available.
    AC020931 Genomic DNA. No translation available.
    BC126227 mRNA. Translation: AAI26228.1.
    BC144093 mRNA. Translation: AAI44094.1.
    AH008119 Genomic DNA. Translation: AAD51619.1.
    CCDSiCCDS12228.1. [P26358-1]
    CCDS45958.1. [P26358-2]
    PIRiS22610.
    RefSeqiNP_001124295.1. NM_001130823.1. [P26358-2]
    NP_001370.1. NM_001379.2. [P26358-1]
    UniGeneiHs.202672.

    Genome annotation databases

    EnsembliENST00000340748; ENSP00000345739; ENSG00000130816. [P26358-1]
    ENST00000359526; ENSP00000352516; ENSG00000130816. [P26358-2]
    GeneIDi1786.
    KEGGihsa:1786.
    UCSCiuc002mng.3. human. [P26358-1]
    uc010xlc.2. human. [P26358-2]

    Polymorphism databases

    DMDMi12231019.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63692 mRNA. Translation: CAA45219.1 .
    AF180682 mRNA. Translation: AAF23609.1 .
    AC010077 Genomic DNA. Translation: AAD54507.1 . Sequence problems.
    AC011511 Genomic DNA. No translation available.
    AC020931 Genomic DNA. No translation available.
    BC126227 mRNA. Translation: AAI26228.1 .
    BC144093 mRNA. Translation: AAI44094.1 .
    AH008119 Genomic DNA. Translation: AAD51619.1 .
    CCDSi CCDS12228.1. [P26358-1 ]
    CCDS45958.1. [P26358-2 ]
    PIRi S22610.
    RefSeqi NP_001124295.1. NM_001130823.1. [P26358-2 ]
    NP_001370.1. NM_001379.2. [P26358-1 ]
    UniGenei Hs.202672.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EPZ X-ray 2.31 A/B 351-600 [» ]
    3PTA X-ray 3.60 A 646-1600 [» ]
    3SWR X-ray 2.49 A 601-1600 [» ]
    ProteinModelPortali P26358.
    SMRi P26358. Positions 351-599, 601-1600.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108123. 75 interactions.
    DIPi DIP-39693N.
    IntActi P26358. 21 interactions.
    MINTi MINT-232346.
    STRINGi 9606.ENSP00000352516.

    Chemistry

    BindingDBi P26358.
    ChEMBLi CHEMBL1993.
    DrugBanki DB00928. Azacitidine.
    DB01262. Decitabine.
    DB01099. Flucytosine.
    DB01181. Ifosfamide.
    DB01035. Procainamide.

    Protein family/group databases

    REBASEi 1161. M.HsaDnmt1A.

    PTM databases

    PhosphoSitei P26358.

    Polymorphism databases

    DMDMi 12231019.

    Proteomic databases

    MaxQBi P26358.
    PaxDbi P26358.
    PRIDEi P26358.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340748 ; ENSP00000345739 ; ENSG00000130816 . [P26358-1 ]
    ENST00000359526 ; ENSP00000352516 ; ENSG00000130816 . [P26358-2 ]
    GeneIDi 1786.
    KEGGi hsa:1786.
    UCSCi uc002mng.3. human. [P26358-1 ]
    uc010xlc.2. human. [P26358-2 ]

    Organism-specific databases

    CTDi 1786.
    GeneCardsi GC19M010244.
    GeneReviewsi DNMT1.
    HGNCi HGNC:2976. DNMT1.
    HPAi CAB005876.
    HPA002694.
    MIMi 126375. gene.
    604121. phenotype.
    614116. phenotype.
    neXtProti NX_P26358.
    Orphaneti 314404. Cerebellar ataxia-deafness-narcolepsy syndrome.
    PharmGKBi PA27443.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0270.
    HOGENOMi HOG000082497.
    HOVERGENi HBG051384.
    KOi K00558.
    OMAi CPNLAVK.
    OrthoDBi EOG77WWBH.
    PhylomeDBi P26358.
    TreeFami TF328926.

    Enzyme and pathway databases

    BRENDAi 2.1.1.37. 2681.
    Reactomei REACT_200808. PRC2 methylates histones and DNA.
    REACT_200856. NoRC negatively regulates rRNA expression.

    Miscellaneous databases

    ChiTaRSi DNMT1. human.
    EvolutionaryTracei P26358.
    GeneWikii DNMT1.
    GenomeRNAii 1786.
    NextBioi 7267.
    PROi P26358.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26358.
    Bgeei P26358.
    CleanExi HS_DNMT1.
    Genevestigatori P26358.

    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. 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.
    3. "Human DNA methyltransferase (DNMT1) is alternatively spliced."
      Li L.C., Au H., Chui R., Dahiya R.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Prostatic carcinoma.
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 2).
    6. "Two major forms of DNA (cytosine-5) methyltransferase in human somatic tissues."
      Hsu D.-W., Lin M.-J., Lee T.-L., Wen S.-C., Chen X., Shen C.-K.J.
      Proc. Natl. Acad. Sci. U.S.A. 96:9751-9756(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
    7. "Characterization of the human DNA methyltransferase splice variant Dnmt1b."
      Bonfils C., Beaulieu N., Chan E., Cotton-Montpetit J., MacLeod A.R.
      J. Biol. Chem. 275:10754-10760(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
    8. "Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1."
      Chuang L.S.-H., Ian H.-I., Koh T.-W., Ng H.-H., Xu G., Li B.F.L.
      Science 277:1996-2000(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PCNA, MUTAGENESIS.
    9. "MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase."
      Tatematsu K., Yamazaki T., Ishikawa F.
      Genes Cells 5:677-688(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MBD2 AND MBD3.
    10. "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.
    11. "DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters."
      Robertson K.D., Ait-Si-Ali S., Yokochi T., Wade P.A., Jones P.L., Wolffe A.P.
      Nat. Genet. 25:338-342(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RB1; E2F1 AND HDAC1.
    12. "The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate mRNA expression in normal tissues and overexpression in tumors."
      Robertson K.D., Uzvolgyi E., Liang G., Talmadge C., Sumegi J., Gonzales F.A., Jones P.A.
      Nucleic Acids Res. 27:2291-2298(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    13. "Co-operation and communication between the human maintenance and de novo DNA (cytosine-5) methyltransferases."
      Kim G.-D., Ni J., Kelesoglu N., Roberts R.J., Pradhan S.
      EMBO J. 21:4183-4195(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNMT3A AND DNMT3B, SUBCELLULAR LOCATION.
    14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: FUNCTION, INTERACTION WITH EED AND EZH2.
    16. "Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer."
      Schlesinger Y., Straussman R., Keshet I., Farkash S., Hecht M., Zimmerman J., Eden E., Yakhini Z., Ben-Shushan E., Reubinoff B.E., Bergman Y., Simon I., Cedar H.
      Nat. Genet. 39:232-236(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DE NOVO DNA METHYLATION OF TARGET GENES.
    17. "CXXC domain of human DNMT1 is essential for enzymatic activity."
      Pradhan M., Esteve P.-O., Chin H.G., Samaranayke M., Kim G.-D., Pradhan S.
      Biochemistry 47:10000-10009(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-653; CYS-656; CYS-659; CYS-664; CYS-667 AND CYS-670.
    18. "DNA methyltransferase 1 and 3B activate BAG-1 expression via recruitment of CTCFL/BORIS and modulation of promoter histone methylation."
      Sun L., Huang L., Nguyen P., Bisht K.S., Bar-Sela G., Ho A.S., Bradbury C.M., Yu W., Cui H., Lee S., Trepel J.B., Feinberg A.P., Gius D.
      Cancer Res. 68:2726-2735(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: METHYLATION AT LYS-70, IDENTIFICATION BY MASS SPECTROMETRY.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-143; SER-152; SER-154 AND SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "SUMOylation enhances DNA methyltransferase 1 activity."
      Lee B., Muller M.T.
      Biochem. J. 421:449-461(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION, INTERACTION WITH UBC9, MUTAGENESIS OF CYS-1226.
    24. "Dimerization of DNA methyltransferase 1 is mediated by its regulatory domain."
      Fellinger K., Rothbauer U., Felle M., Laengst G., Leonhardt H.
      J. Cell. Biochem. 106:521-528(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION.
    25. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    26. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173; LYS-1111; LYS-1113 AND LYS-1115, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Phosphorylation of human DNMT1: implication of cyclin-dependent kinases."
      Lavoie G., St-Pierre Y.
      Biochem. Biophys. Res. Commun. 409:187-192(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-154.
    30. "SIRT1 deacetylates the DNA methyltransferase 1 (DNMT1) protein and alters its activities."
      Peng L., Yuan Z., Ling H., Fukasawa K., Robertson K., Olashaw N., Koomen J., Chen J., Lane W.S., Seto E.
      Mol. Cell. Biol. 31:4720-4734(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-160; LYS-188; LYS-259; LYS-366; LYS-749; LYS-891; LYS-957; LYS-961; LYS-975; LYS-1054; LYS-1111; LYS-1113; LYS-1115; LYS-1117; LYS-1349 AND LYS-1415, DEACETYLATION BY SIRT1.
    31. "A methylation and phosphorylation switch between an adjacent lysine and serine determines human DNMT1 stability."
      Esteve P.O., Chang Y., Samaranayake M., Upadhyay A.K., Horton J.R., Feehery G.R., Cheng X., Pradhan S.
      Nat. Struct. Mol. Biol. 18:42-48(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-142, PHOSPHORYLATION AT SER-143.
    32. "The USP7/Dnmt1 complex stimulates the DNA methylation activity of Dnmt1 and regulates the stability of UHRF1."
      Felle M., Joppien S., Nemeth A., Diermeier S., Thalhammer V., Dobner T., Kremmer E., Kappler R., Langst G.
      Nucleic Acids Res. 39:8355-8365(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH USP7 AND UHRF1.
    33. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-133 AND SER-714, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "The replication focus targeting sequence (RFTS) domain is a DNA-competitive inhibitor of Dnmt1."
      Syeda F., Fagan R.L., Wean M., Avvakumov G.V., Walker J.R., Xue S., Dhe-Paganon S., Brenner C.
      J. Biol. Chem. 286:15344-15351(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 351-600 IN COMPLEX WITH ZINC IONS.
    35. "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 (3.6 ANGSTROMS) OF 646-1600 IN COMPLEX WITH SAH AND DNA, AUTOINHIBITORY LINKER.
    36. Cited for: VARIANTS HSN1E 490-GLU-TYR-491 AND CYS-495, CHARACTERIZATION OF VARIANTS HSN1E 490-GLU-TYR-491 AND CYS-495.
    37. Cited for: VARIANTS ADCADN VAL-554; ALA-589 AND PHE-590.

    Entry informationi

    Entry nameiDNMT1_HUMAN
    AccessioniPrimary (citable) accession number: P26358
    Secondary accession number(s): A0AV63
    , B7ZLW6, Q9UHG5, Q9ULA2, Q9UMZ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: January 11, 2001
    Last modified: October 1, 2014
    This is version 168 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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