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O88508

- DNM3A_MOUSE

UniProt

O88508 - DNM3A_MOUSE

Protein

DNA (cytosine-5)-methyltransferase 3A

Gene

Dnmt3a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (01 May 2000)
      Previous versions | rss
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    Functioni

    Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZBTB18. Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. Can actively repress transcription through the recruitment of HDAC activity.8 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Activated by binding to the regulatory factor DNMT3L.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei660 – 6601S-adenosyl-L-methionineBy similarity
    Active sitei706 – 7061PROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri489 – 51931GATA-type; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri530 – 58657PHD-type; atypicalPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. DNA (cytosine-5-)-methyltransferase activity Source: UniProtKB
    3. DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates Source: Ensembl
    4. DNA binding Source: UniProtKB
    5. metal ion binding Source: UniProtKB-KW
    6. methyltransferase activity Source: MGI
    7. protein binding Source: UniProtKB
    8. unmethylated CpG binding Source: Ensembl

    GO - Biological processi

    1. C-5 methylation of cytosine Source: GOC
    2. cellular response to amino acid stimulus Source: MGI
    3. DNA methylation Source: UniProtKB
    4. DNA methylation involved in embryo development Source: UniProtKB
    5. DNA methylation involved in gamete generation Source: UniProtKB
    6. DNA methylation on cytosine within a CG sequence Source: Ensembl
    7. hypermethylation of CpG island Source: BHF-UCL
    8. maintenance of DNA methylation Source: BHF-UCL
    9. methylation-dependent chromatin silencing Source: MGI
    10. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    11. regulation of gene expression by genetic imprinting Source: BHF-UCL
    12. S-adenosylhomocysteine metabolic process Source: Ensembl
    13. S-adenosylmethioninamine metabolic process Source: Ensembl
    14. spermatogenesis Source: MGI
    15. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    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_222475. PRC2 methylates histones and DNA.

    Protein family/group databases

    REBASEi3747. M.MmuDnmt3A.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA (cytosine-5)-methyltransferase 3A (EC:2.1.1.37)
    Short name:
    Dnmt3a
    Alternative name(s):
    DNA methyltransferase MmuIIIA
    Short name:
    DNA MTase MmuIIIA
    Short name:
    M.MmuIIIA
    Gene namesi
    Name:Dnmt3a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:1261827. Dnmt3a.

    Subcellular locationi

    Nucleus 3 Publications. Cytoplasm By similarity
    Note: Accumulates in the major satellite repeats at pericentric heterochromatin.

    GO - Cellular componenti

    1. chromosome, centromeric region Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. euchromatin Source: UniProtKB
    4. heterochromatin Source: MGI
    5. nuclear heterochromatin Source: MGI
    6. nuclear matrix Source: UniProtKB
    7. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi302 – 3032WP → ST: Prevents accumulation in pericentric heterochromatin. 1 Publication
    Mutagenesisi636 – 6361F → A: Reduces activity about 20-fold. Loss of substrate binding. 2 Publications
    Mutagenesisi660 – 6601E → A: Reduces activity about 15-fold. Loss of substrate binding. 2 Publications
    Mutagenesisi682 – 6821D → A: Strongly reduces substrate binding. No effect on activity. 2 Publications
    Mutagenesisi705 – 7062PC → VD: No effect on localization. 1 Publication
    Mutagenesisi706 – 7061C → A: Reduces activity about 5-fold. Reduces DNA-binding capacity. 2 Publications
    Mutagenesisi707 – 7071N → Q: Reduces activity about 3-fold. 2 Publications
    Mutagenesisi710 – 7101S → A: No effect on activity. 2 Publications
    Mutagenesisi716 – 7161R → A: Reduces activity about 30-fold. Reduces DNA-binding capacity. 2 Publications
    Mutagenesisi717 – 7171K → A: Reduces activity about 3-fold. 2 Publications
    Mutagenesisi728 – 7281F → A: Loss of activity du to the incapacity to bind the regulatory subunit DNMT3L. 2 Publications
    Mutagenesisi752 – 7521E → A: Reduces activity about 10-fold. 2 Publications
    Mutagenesisi753 – 7531N → A: Reduces activity about 10-fold. 2 Publications
    Mutagenesisi788 – 7881R → A: Reduces activity about 15-fold. 2 Publications
    Mutagenesisi827 – 8271R → A: Reduces activity about 2-fold. Reduces DNA-binding capacity. 2 Publications
    Mutagenesisi832 – 8321R → A: Reduces DNA-binding capacity. No effect on activity. 2 Publications
    Mutagenesisi878 – 8781R → A: Reduces activity about 6-fold. Reduces DNA-binding capacity. 2 Publications
    Mutagenesisi881 – 8811R → A: Loss of activity. Strongly reduces substrate binding. 2 Publications
    Mutagenesisi883 – 8831R → A: Reduces activity about 3-fold. Reduces DNA-binding capacity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 908908DNA (cytosine-5)-methyltransferase 3APRO_0000088044Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei102 – 1021PhosphoserineBy similarity
    Modified residuei239 – 2391PhosphoserineBy similarity
    Modified residuei251 – 2511PhosphoserineBy similarity
    Modified residuei257 – 2571PhosphothreonineBy similarity

    Post-translational modificationi

    Sumoylated; sumoylation disrupts the ability to interact with histone deacetylases (HDAC1 and HDAC2) and repress transcription.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO88508.
    PaxDbiO88508.
    PRIDEiO88508.

    PTM databases

    PhosphoSiteiO88508.

    Expressioni

    Tissue specificityi

    Isoform 1 is expressed ubiquitously at low levels. Expression of isoform 2 is restricted to tissues containing cells which are undergoing active de novo methylation, including spleen, testis and thymus.1 Publication

    Developmental stagei

    At E7.5, the protein is moderately expressed in embryonic ectoderm and weakly in mesodermal cells. At E8.5 and E9.5, the expression become ubiquitous with an increase in the somites and in the ventral part of the embryo.1 Publication

    Gene expression databases

    ArrayExpressiO88508.
    BgeeiO88508.
    CleanExiMM_DNMT3A.
    GenevestigatoriO88508.

    Interactioni

    Subunit structurei

    Heterotetramer composed of 1 DNMT3A homodimer and 2 DNMT3L subunits (DNMT3L-DNMT3A-DNMT3A-DNMT3L). Interacts with DNMT1 and DNMT3B. Interacts with MPHOSPH8. Interacts with histone H3 that is not methylated at 'Lys-4' (H3K4) By similarity. Binds the ZBTB18 transcriptional repressor. Interacts with SETDB1. Associates with HDAC1 through its ADD domain. Interacts with the PRC2/EED-EZH2 complex. Interacts with UBC9, PIAS1 and PIAS2.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Dnmt3lQ9CWR86EBI-995154,EBI-3043871
    HellsQ608484EBI-995154,EBI-3043887

    Protein-protein interaction databases

    BioGridi199261. 18 interactions.
    DIPiDIP-38005N.
    IntActiO88508. 10 interactions.
    MINTiMINT-2521021.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3SW9X-ray3.05P/Q39-50[»]
    3SWCX-ray2.33P/Q39-50[»]
    ProteinModelPortaliO88508.
    SMRiO88508. Positions 279-421, 469-908.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini288 – 34659PWWPPROSITE-ProRule annotationAdd
    BLAST
    Domaini478 – 610133ADDPROSITE-ProRule annotationAdd
    BLAST
    Domaini630 – 908279SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni195 – 399205Interaction with DNMT1 and DNMT3BBy similarityAdd
    BLAST
    Regioni490 – 58293Interaction with the PRC2/EED-EZH2 complexAdd
    BLAST
    Regioni637 – 6415S-adenosyl-L-methionine bindingBy similarity
    Regioni682 – 6843S-adenosyl-L-methionine bindingBy similarity
    Regioni887 – 8893S-adenosyl-L-methionine bindingBy similarity

    Domaini

    The PWWP domain is essential for targeting to pericentric heterochromatin. It specifically recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3) (PubMed:20547484).1 Publication

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.PROSITE-ProRule annotation
    Contains 1 ADD domain.PROSITE-ProRule annotation
    Contains 1 GATA-type zinc finger.PROSITE-ProRule annotation
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
    Contains 1 PWWP domain.PROSITE-ProRule annotation
    Contains 1 SAM-dependent MTase C5-type domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri489 – 51931GATA-type; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri530 – 58657PHD-type; atypicalPROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG70699.
    GeneTreeiENSGT00390000008341.
    HOGENOMiHOG000230875.
    HOVERGENiHBG051381.
    InParanoidiO88508.
    KOiK17398.
    OMAiFVGGMCQ.
    OrthoDBiEOG7MWGW6.
    PhylomeDBiO88508.
    TreeFamiTF329039.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025766. ADD.
    IPR018117. C5_DNA_meth_AS.
    IPR001525. C5_MeTfrase.
    IPR025811. C5_MeTrfase_3.
    IPR000313. PWWP_dom.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF00145. DNA_methylase. 1 hit.
    PF00855. PWWP. 1 hit.
    [Graphical view]
    SMARTiSM00293. PWWP. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51533. ADD. 1 hit.
    PS00094. C5_MTASE_1. 1 hit.
    PS50812. PWWP. 1 hit.
    PS51679. SAM_MT_C5. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative promoter usage. Align

    Isoform 1 (identifier: O88508-1) [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

    MPSSGPGDTS SSSLEREDDR KEGEEQEENR GKEERQEPSA TARKVGRPGR    50
    KRKHPPVESS DTPKDPAVTT KSQPMAQDSG PSDLLPNGDL EKRSEPQPEE 100
    GSPAAGQKGG APAEGEGTET PPEASRAVEN GCCVTKEGRG ASAGEGKEQK 150
    QTNIESMKME GSRGRLRGGL GWESSLRQRP MPRLTFQAGD PYYISKRKRD 200
    EWLARWKREA EKKAKVIAVM NAVEENQASG ESQKVEEASP PAVQQPTDPA 250
    SPTVATTPEP VGGDAGDKNA TKAADDEPEY EDGRGFGIGE LVWGKLRGFS 300
    WWPGRIVSWW MTGRSRAAEG TRWVMWFGDG KFSVVCVEKL MPLSSFCSAF 350
    HQATYNKQPM YRKAIYEVLQ VASSRAGKLF PACHDSDESD SGKAVEVQNK 400
    QMIEWALGGF QPSGPKGLEP PEEEKNPYKE VYTDMWVEPE AAAYAPPPPA 450
    KKPRKSTTEK PKVKEIIDER TRERLVYEVR QKCRNIEDIC ISCGSLNVTL 500
    EHPLFIGGMC QNCKNCFLEC AYQYDDDGYQ SYCTICCGGR EVLMCGNNNC 550
    CRCFCVECVD LLVGPGAAQA AIKEDPWNCY MCGHKGTYGL LRRREDWPSR 600
    LQMFFANNHD QEFDPPKVYP PVPAEKRKPI RVLSLFDGIA TGLLVLKDLG 650
    IQVDRYIASE VCEDSITVGM VRHQGKIMYV GDVRSVTQKH IQEWGPFDLV 700
    IGGSPCNDLS IVNPARKGLY EGTGRLFFEF YRLLHDARPK EGDDRPFFWL 750
    FENVVAMGVS DKRDISRFLE SNPVMIDAKE VSAAHRARYF WGNLPGMNRP 800
    LASTVNDKLE LQECLEHGRI AKFSKVRTIT TRSNSIKQGK DQHFPVFMNE 850
    KEDILWCTEM ERVFGFPVHY TDVSNMSRLA RQRLLGRSWS VPVIRHLFAP 900
    LKEYFACV 908
    Length:908
    Mass (Da):101,672
    Last modified:May 1, 2000 - v2
    Checksum:i5F98D5A8092C84A5
    GO
    Isoform 2 (identifier: O88508-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-219: Missing.

    Show »
    Length:689
    Mass (Da):77,824
    Checksum:i0C1093AF43717684
    GO

    Sequence cautioni

    The sequence BAB28644.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti151 – 1511Q → P in AAH07466. (PubMed:12138111)Curated
    Sequence conflicti775 – 7751M → T in BAB28644. (PubMed:16141072)Curated
    Sequence conflicti781 – 7811V → G in BAB28644. (PubMed:16141072)Curated
    Sequence conflicti791 – 7911W → R in BAB28644. (PubMed:16141072)Curated
    Sequence conflicti809 – 8091L → P in BAB28644. (PubMed:16141072)Curated
    Sequence conflicti904 – 9041Y → I in BAB28644. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 219219Missing in isoform 2. 2 PublicationsVSP_009423Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF068625 mRNA. Translation: AAC40177.2.
    AF480164 mRNA. Translation: AAN40038.1.
    AK013096 mRNA. Translation: BAB28644.2. Different initiation.
    AK090132 mRNA. Translation: BAC41110.1.
    AK147263 mRNA. Translation: BAE27806.1.
    AK147627 mRNA. Translation: BAE28033.1.
    AK147642 mRNA. Translation: BAE28043.1.
    AK147676 mRNA. Translation: BAE28067.1.
    AK157792 mRNA. Translation: BAE34200.1.
    BC007466 mRNA. Translation: AAH07466.1.
    CCDSiCCDS25784.1. [O88508-2]
    CCDS36397.1. [O88508-1]
    RefSeqiNP_001258682.1. NM_001271753.1. [O88508-1]
    NP_031898.1. NM_007872.4. [O88508-1]
    NP_714965.1. NM_153743.4. [O88508-2]
    XP_006515016.1. XM_006514953.1. [O88508-1]
    XP_006515017.1. XM_006514954.1. [O88508-1]
    XP_006515018.1. XM_006514955.1. [O88508-1]
    XP_006515019.1. XM_006514956.1. [O88508-1]
    XP_006515020.1. XM_006514957.1. [O88508-2]
    UniGeneiMm.470389.
    Mm.5001.

    Genome annotation databases

    EnsembliENSMUST00000020991; ENSMUSP00000020991; ENSMUSG00000020661. [O88508-1]
    ENSMUST00000111186; ENSMUSP00000106817; ENSMUSG00000020661. [O88508-2]
    ENSMUST00000172689; ENSMUSP00000133543; ENSMUSG00000020661. [O88508-2]
    ENSMUST00000174817; ENSMUSP00000134009; ENSMUSG00000020661. [O88508-1]
    GeneIDi13435.
    KEGGimmu:13435.
    UCSCiuc007mxb.1. mouse. [O88508-1]

    Keywords - Coding sequence diversityi

    Alternative promoter usage

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF068625 mRNA. Translation: AAC40177.2 .
    AF480164 mRNA. Translation: AAN40038.1 .
    AK013096 mRNA. Translation: BAB28644.2 . Different initiation.
    AK090132 mRNA. Translation: BAC41110.1 .
    AK147263 mRNA. Translation: BAE27806.1 .
    AK147627 mRNA. Translation: BAE28033.1 .
    AK147642 mRNA. Translation: BAE28043.1 .
    AK147676 mRNA. Translation: BAE28067.1 .
    AK157792 mRNA. Translation: BAE34200.1 .
    BC007466 mRNA. Translation: AAH07466.1 .
    CCDSi CCDS25784.1. [O88508-2 ]
    CCDS36397.1. [O88508-1 ]
    RefSeqi NP_001258682.1. NM_001271753.1. [O88508-1 ]
    NP_031898.1. NM_007872.4. [O88508-1 ]
    NP_714965.1. NM_153743.4. [O88508-2 ]
    XP_006515016.1. XM_006514953.1. [O88508-1 ]
    XP_006515017.1. XM_006514954.1. [O88508-1 ]
    XP_006515018.1. XM_006514955.1. [O88508-1 ]
    XP_006515019.1. XM_006514956.1. [O88508-1 ]
    XP_006515020.1. XM_006514957.1. [O88508-2 ]
    UniGenei Mm.470389.
    Mm.5001.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3SW9 X-ray 3.05 P/Q 39-50 [» ]
    3SWC X-ray 2.33 P/Q 39-50 [» ]
    ProteinModelPortali O88508.
    SMRi O88508. Positions 279-421, 469-908.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199261. 18 interactions.
    DIPi DIP-38005N.
    IntActi O88508. 10 interactions.
    MINTi MINT-2521021.

    Protein family/group databases

    REBASEi 3747. M.MmuDnmt3A.

    PTM databases

    PhosphoSitei O88508.

    Proteomic databases

    MaxQBi O88508.
    PaxDbi O88508.
    PRIDEi O88508.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020991 ; ENSMUSP00000020991 ; ENSMUSG00000020661 . [O88508-1 ]
    ENSMUST00000111186 ; ENSMUSP00000106817 ; ENSMUSG00000020661 . [O88508-2 ]
    ENSMUST00000172689 ; ENSMUSP00000133543 ; ENSMUSG00000020661 . [O88508-2 ]
    ENSMUST00000174817 ; ENSMUSP00000134009 ; ENSMUSG00000020661 . [O88508-1 ]
    GeneIDi 13435.
    KEGGi mmu:13435.
    UCSCi uc007mxb.1. mouse. [O88508-1 ]

    Organism-specific databases

    CTDi 1788.
    MGIi MGI:1261827. Dnmt3a.

    Phylogenomic databases

    eggNOGi NOG70699.
    GeneTreei ENSGT00390000008341.
    HOGENOMi HOG000230875.
    HOVERGENi HBG051381.
    InParanoidi O88508.
    KOi K17398.
    OMAi FVGGMCQ.
    OrthoDBi EOG7MWGW6.
    PhylomeDBi O88508.
    TreeFami TF329039.

    Enzyme and pathway databases

    BRENDAi 2.1.1.37. 3474.
    Reactomei REACT_222475. PRC2 methylates histones and DNA.

    Miscellaneous databases

    ChiTaRSi DNMT3A. mouse.
    NextBioi 283867.
    PROi O88508.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O88508.
    Bgeei O88508.
    CleanExi MM_DNMT3A.
    Genevestigatori O88508.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025766. ADD.
    IPR018117. C5_DNA_meth_AS.
    IPR001525. C5_MeTfrase.
    IPR025811. C5_MeTrfase_3.
    IPR000313. PWWP_dom.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF00145. DNA_methylase. 1 hit.
    PF00855. PWWP. 1 hit.
    [Graphical view ]
    SMARTi SM00293. PWWP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51533. ADD. 1 hit.
    PS00094. C5_MTASE_1. 1 hit.
    PS50812. PWWP. 1 hit.
    PS51679. SAM_MT_C5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a family of novel mammalian DNA (cytosine-5) methyltransferases."
      Okano M., Xie S., Li E.
      Nat. Genet. 19:219-220(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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).
      Tissue: Mammary gland.
    3. "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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6 and C57BL/6J.
      Tissue: Brain, Embryo and Skin.
    4. "A novel Dnmt3a isoform produced from an alternative promoter localizes to euchromatin and its expression correlates with active de novo methylation."
      Chen T., Ueda Y., Xie S., Li E.
      J. Biol. Chem. 277:38746-38754(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY.
      Strain: 129/SvJ.
    5. "DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo methylation and mammalian development."
      Okano M., Bell D.W., Haber D.A., Li E.
      Cell 99:247-257(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.
    6. "Enzymatic properties of recombinant Dnmt3a DNA methyltransferase from mouse: the enzyme modifies DNA in a non-processive manner and also methylates non-CpG correction sites."
      Gowher H., Jeltsch A.
      J. Mol. Biol. 309:1201-1208(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. Erratum
      Gowher H., Jeltsch A.
      J. Mol. Biol. 310:951-951(2001)
    8. "Dnmt3a binds deacetylases and is recruited by a sequence-specific repressor to silence transcription."
      Fuks F., Burgers W.A., Godin N., Kasai M., Kouzarides T.
      EMBO J. 20:2536-2544(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ZBTB18 AND HDAC1.
    9. "Molecular enzymology of the catalytic domains of the Dnmt3a and Dnmt3b DNA methyltransferases."
      Gowher H., Jeltsch A.
      J. Biol. Chem. 277:20409-20414(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Biochemical fractionation reveals association of DNA methyltransferase (Dnmt) 3b with Dnmt1 and that of Dnmt 3a with a histone H3 methyltransferase and Hdac1."
      Datta J., Ghoshal K., Sharma S.M., Tajima S., Jacob S.T.
      J. Cell. Biochem. 88:855-864(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH HDAC1.
    11. "The PWWP domain of Dnmt3a and Dnmt3b is required for directing DNA methylation to the major satellite repeats at pericentric heterochromatin."
      Chen T., Tsujimoto N., Li E.
      Mol. Cell. Biol. 24:9048-9058(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 302-VAL-PRO-303 AND 705-PRO-CYS-706.
    12. "Essential role for de novo DNA methyltransferase Dnmt3a in paternal and maternal imprinting."
      Kaneda M., Okano M., Hata K., Sado T., Tsujimoto N., Li E., Sasaki H.
      Nature 429:900-903(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1 modulates its interaction with histone deacetylases (HDACs) and its capacity to repress transcription."
      Ling Y., Sankpal U.T., Robertson A.K., McNally J.G., Karpova T., Robertson K.D.
      Nucleic Acids Res. 32:598-610(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION, INTERACTION WITH UBC9; PIAS1 AND PIAS2.
    14. "Mechanism of stimulation of catalytic activity of Dnmt3A and Dnmt3B DNA-(cytosine-C5)-methyltransferases by Dnmt3L."
      Gowher H., Liebert K., Hermann A., Xu G., Jeltsch A.
      J. Biol. Chem. 280:13341-13348(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    15. "Distinct DNA methylation activity of Dnmt3a and Dnmt3b towards naked and nucleosomal DNA."
      Takeshima H., Suetake I., Shimahara H., Ura K., Tate S., Tajima S.
      J. Biochem. 139:503-515(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Mutational analysis of the catalytic domain of the murine Dnmt3a DNA-(cytosine C5)-methyltransferase."
      Gowher H., Loutchanwoot P., Vorobjeva O., Handa V., Jurkowska R.Z., Jurkowski T.P., Jeltsch A.
      J. Mol. Biol. 357:928-941(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PHE-636; GLU-660; ASP-682; CYS-706; ASN-707; SER-710; ARG-716; LYS-717; GLU-752; ASN-753; ARG-788; ARG-827; ARG-832; ARG-878; ARG-881 AND ARG-883.
    17. Cited for: INTERACTION WITH THE PRC2/EED-EZH2 COMPLEX.
    18. "Structure of Dnmt3a bound to Dnmt3L suggests a model for de novo DNA methylation."
      Jia D., Jurkowska R.Z., Zhang X., Jeltsch A., Cheng X.
      Nature 449:248-251(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF PHE-728.
    19. "Mouse Dnmt3a preferentially methylates linker DNA and is inhibited by histone H1."
      Takeshima H., Suetake I., Tajima S.
      J. Mol. Biol. 383:810-821(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Np95 interacts with de novo DNA methyltransferases, Dnmt3a and Dnmt3b, and mediates epigenetic silencing of the viral CMV promoter in embryonic stem cells."
      Meilinger D., Fellinger K., Bultmann S., Rothbauer U., Bonapace I.M., Klinkert W.E., Spada F., Leonhardt H.
      EMBO Rep. 10:1259-1264(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UHRF1.
    21. "The Dnmt3a PWWP domain reads histone 3 lysine 36 trimethylation and guides DNA methylation."
      Dhayalan A., Rajavelu A., Rathert P., Tamas R., Jurkowska R.Z., Ragozin S., Jeltsch A.
      J. Biol. Chem. 285:26114-26120(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiDNM3A_MOUSE
    AccessioniPrimary (citable) accession number: O88508
    Secondary accession number(s): Q3TZK8
    , Q3UH24, Q8CJ60, Q922J0, Q9CSE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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