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Q9Y6K1

- DNM3A_HUMAN

UniProt

Q9Y6K1 - DNM3A_HUMAN

Protein

DNA (cytosine-5)-methyltransferase 3A

Gene

DNMT3A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 4 (15 Jan 2008)
      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.1 Publication

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei664 – 6641S-adenosyl-L-methionineCurated
    Active sitei710 – 7101PROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri493 – 52331GATA-type; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri534 – 59057PHD-type; atypicalPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    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. protein binding Source: UniProtKB
    7. unmethylated CpG binding Source: Ensembl

    GO - Biological processi

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

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Repressor, Transferase

    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.

    Protein family/group databases

    REBASEi4119. M.HsaDnmt3A.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA (cytosine-5)-methyltransferase 3A (EC:2.1.1.37)
    Short name:
    Dnmt3a
    Alternative name(s):
    DNA methyltransferase HsaIIIA
    Short name:
    DNA MTase HsaIIIA
    Short name:
    M.HsaIIIA
    Gene namesi
    Name:DNMT3A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:2978. DNMT3A.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Accumulates in the major satellite repeats at pericentric heterochromatin.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi732 – 7321F → A: Loss of activity du to the incapacity to bind the regulatory subunit DNMT3L. 1 Publication

    Organism-specific databases

    PharmGKBiPA27445.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 912912DNA (cytosine-5)-methyltransferase 3APRO_0000088043Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei105 – 1051Phosphoserine3 Publications
    Modified residuei243 – 2431Phosphoserine2 Publications
    Modified residuei255 – 2551Phosphoserine1 Publication
    Modified residuei261 – 2611Phosphothreonine1 Publication
    Modified residuei267 – 2671Phosphoserine1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y6K1.
    PaxDbiQ9Y6K1.
    PRIDEiQ9Y6K1.

    PTM databases

    PhosphoSiteiQ9Y6K1.

    Expressioni

    Tissue specificityi

    Highly expressed in fetal tissues, skeletal muscle, heart, peripheral blood mononuclear cells, kidney, and at lower levels in placenta, brain, liver, colon, spleen, small intestine and lung.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y6K1.
    BgeeiQ9Y6K1.
    CleanExiHS_DNMT3A.
    GenevestigatoriQ9Y6K1.

    Organism-specific databases

    HPAiCAB009469.
    HPA026588.

    Interactioni

    Subunit structurei

    Heterotetramer composed of 1 DNMT3A homodimer and 2 DNMT3L subunits (DNMT3L-DNMT3A-DNMT3A-DNMT3L). Interacts with UBC9, PIAS1 and PIAS2 By similarity. Binds the ZBTB18 transcriptional repressor. Interacts with SETDB1. Associates with HDAC1 through its ADD domain. Interacts with UHRF1 By similarity. Interacts with DNMT1 and DNMT3B. Interacts with the PRC2/EED-EZH2 complex. Interacts with MPHOSPH8. Interacts with histone H3 that is not methylated at 'Lys-4' (H3K4).By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-923653,EBI-923653
    EEDO755302EBI-923653,EBI-923794
    EZH2Q159106EBI-923653,EBI-530054
    H3F3BP842437EBI-923653,EBI-120658
    SETDB1Q150477EBI-923653,EBI-79691
    UHRF1Q96T887EBI-923653,EBI-1548946

    Protein-protein interaction databases

    BioGridi108125. 53 interactions.
    DIPiDIP-38004N.
    IntActiQ9Y6K1. 20 interactions.
    STRINGi9606.ENSP00000264709.

    Structurei

    Secondary structure

    1
    912
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi295 – 2984
    Beta strandi306 – 3116
    Helixi313 – 3153
    Beta strandi325 – 3306
    Turni331 – 3333
    Beta strandi336 – 3405
    Helixi341 – 3433
    Beta strandi344 – 3463
    Helixi347 – 3493
    Helixi350 – 3534
    Helixi356 – 3616
    Helixi363 – 38018
    Helixi399 – 41113
    Turni415 – 4173
    Helixi419 – 4224
    Helixi476 – 4849
    Helixi490 – 4923
    Turni495 – 4973
    Beta strandi507 – 5137
    Helixi515 – 52410
    Beta strandi532 – 5365
    Turni538 – 5403
    Beta strandi544 – 5485
    Turni552 – 5543
    Beta strandi557 – 5593
    Helixi560 – 5667
    Helixi571 – 5766
    Beta strandi578 – 5803
    Turni584 – 5863
    Beta strandi595 – 5973
    Helixi601 – 6099
    Beta strandi634 – 6396
    Turni642 – 6443
    Helixi645 – 6528
    Beta strandi657 – 6637
    Helixi667 – 67610
    Turni677 – 6793
    Beta strandi681 – 6844
    Helixi687 – 6893
    Helixi692 – 6976
    Beta strandi702 – 7065
    Helixi711 – 7133
    Turni722 – 7243
    Turni726 – 7294
    Helixi730 – 74112
    Beta strandi752 – 76110
    Helixi763 – 77311
    Helixi782 – 7843
    Beta strandi786 – 7883
    Beta strandi791 – 7966
    Beta strandi801 – 8033
    Helixi815 – 8173
    Beta strandi824 – 8307
    Beta strandi850 – 8523
    Beta strandi855 – 8573
    Helixi861 – 8688
    Turni872 – 8754
    Helixi882 – 8909
    Helixi895 – 9028
    Helixi903 – 9086

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QRVX-ray2.89A/D/E/H627-912[»]
    3A1AX-ray2.30A476-614[»]
    3A1BX-ray2.29A476-614[»]
    3LLRX-ray2.30A/B/C/D/E275-427[»]
    3SVMX-ray2.31P40-53[»]
    ProteinModelPortaliQ9Y6K1.
    SMRiQ9Y6K1. Positions 283-425, 475-912.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y6K1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini292 – 35059PWWPPROSITE-ProRule annotationAdd
    BLAST
    Domaini482 – 614133ADDPROSITE-ProRule annotationAdd
    BLAST
    Domaini634 – 912279SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni199 – 403205Interaction with DNMT1 and DNMT3BAdd
    BLAST
    Regioni494 – 58693Interaction with the PRC2/EED-EZH2 complexBy similarityAdd
    BLAST
    Regioni641 – 6455S-adenosyl-L-methionine bindingCurated
    Regioni686 – 6883S-adenosyl-L-methionine bindingCurated
    Regioni891 – 8933S-adenosyl-L-methionine bindingCurated

    Domaini

    The PWWP domain is essential for targeting to pericentric heterochromatin. It specifically recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3) By similarity.By similarity

    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 fingeri493 – 52331GATA-type; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri534 – 59057PHD-type; atypicalPROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG70699.
    HOGENOMiHOG000230875.
    HOVERGENiHBG051381.
    InParanoidiQ9Y6K1.
    KOiK17398.
    OMAiFVGGMCQ.
    OrthoDBiEOG7MWGW6.
    PhylomeDBiQ9Y6K1.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 1 (identifier: Q9Y6K1-1) [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

    MPAMPSSGPG DTSSSAAERE EDRKDGEEQE EPRGKEERQE PSTTARKVGR    50
    PGRKRKHPPV ESGDTPKDPA VISKSPSMAQ DSGASELLPN GDLEKRSEPQ 100
    PEEGSPAGGQ KGGAPAEGEG AAETLPEASR AVENGCCTPK EGRGAPAEAG 150
    KEQKETNIES MKMEGSRGRL RGGLGWESSL RQRPMPRLTF QAGDPYYISK 200
    RKRDEWLARW KREAEKKAKV IAGMNAVEEN QGPGESQKVE EASPPAVQQP 250
    TDPASPTVAT TPEPVGSDAG DKNATKAGDD EPEYEDGRGF GIGELVWGKL 300
    RGFSWWPGRI VSWWMTGRSR AAEGTRWVMW FGDGKFSVVC VEKLMPLSSF 350
    CSAFHQATYN KQPMYRKAIY EVLQVASSRA GKLFPVCHDS DESDTAKAVE 400
    VQNKPMIEWA LGGFQPSGPK GLEPPEEEKN PYKEVYTDMW VEPEAAAYAP 450
    PPPAKKPRKS TAEKPKVKEI IDERTRERLV YEVRQKCRNI EDICISCGSL 500
    NVTLEHPLFV GGMCQNCKNC FLECAYQYDD DGYQSYCTIC CGGREVLMCG 550
    NNNCCRCFCV ECVDLLVGPG AAQAAIKEDP WNCYMCGHKG TYGLLRRRED 600
    WPSRLQMFFA NNHDQEFDPP KVYPPVPAEK RKPIRVLSLF DGIATGLLVL 650
    KDLGIQVDRY IASEVCEDSI TVGMVRHQGK IMYVGDVRSV TQKHIQEWGP 700
    FDLVIGGSPC NDLSIVNPAR KGLYEGTGRL FFEFYRLLHD ARPKEGDDRP 750
    FFWLFENVVA MGVSDKRDIS RFLESNPVMI DAKEVSAAHR ARYFWGNLPG 800
    MNRPLASTVN DKLELQECLE HGRIAKFSKV RTITTRSNSI KQGKDQHFPV 850
    FMNEKEDILW CTEMERVFGF PVHYTDVSNM SRLARQRLLG RSWSVPVIRH 900
    LFAPLKEYFA CV 912
    Length:912
    Mass (Da):101,858
    Last modified:January 15, 2008 - v4
    Checksum:iBD1FF7C5B4F54A33
    GO
    Isoform 2 (identifier: Q9Y6K1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-213: MPAMPSSGPG...DEWLARWKRE → MGILERVVRRNGRVDRSLKDECDT

    Note: It is uncertain whether Met-1 or Met-35 is the initiator.

    Show »
    Length:723
    Mass (Da):81,613
    Checksum:i19341BDAE1B71C8B
    GO
    Isoform 3 (identifier: Q9Y6K1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         151-166: KEQKETNIESMKMEGS → ESSAPGAASSGPTSIP
         167-912: Missing.

    Note: Produced by alternative splicing.

    Show »
    Length:166
    Mass (Da):16,866
    Checksum:i78756A71196D61B5
    GO

    Sequence cautioni

    The sequence AAL57039.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAN40037.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti699 – 6991G → D in a patient with chronic myelomonocytic leukemia. 1 Publication
    VAR_067234
    Natural varianti731 – 7311Missing in a patient with chronic myelomonocytic leukemia. 1 Publication
    VAR_067235
    Natural varianti882 – 8821R → C in a patient with chronic myelomonocytic leukemia; somatic mutation. 1 Publication
    VAR_067236
    Natural varianti882 – 8821R → H in a patient with chronic myelomonocytic leukemia; somatic mutation. 1 Publication
    VAR_067237
    Natural varianti882 – 8821R → P in a patient with chronic myelomonocytic leukemia; somatic mutation. 1 Publication
    VAR_067238

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 213213MPAMP…RWKRE → MGILERVVRRNGRVDRSLKD ECDT in isoform 2. 1 PublicationVSP_046254Add
    BLAST
    Alternative sequencei151 – 16616KEQKE…KMEGS → ESSAPGAASSGPTSIP in isoform 3. 1 PublicationVSP_040998Add
    BLAST
    Alternative sequencei167 – 912746Missing in isoform 3. 1 PublicationVSP_040999Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF067972 mRNA. Translation: AAD33084.2.
    AF480163 mRNA. Translation: AAN40037.1. Different initiation.
    AF331856 mRNA. Translation: AAL57039.1. Different initiation.
    AC012074 Genomic DNA. Translation: AAY14761.1.
    CH471053 Genomic DNA. Translation: EAX00727.1.
    BC032392 mRNA. Translation: AAH32392.1.
    BC043617 mRNA. Translation: AAH43617.1.
    BC051864 mRNA. Translation: AAH51864.1.
    CCDSiCCDS1718.2. [Q9Y6K1-2]
    CCDS33157.1. [Q9Y6K1-1]
    CCDS46232.1. [Q9Y6K1-3]
    RefSeqiNP_072046.2. NM_022552.4. [Q9Y6K1-1]
    NP_715640.2. NM_153759.3. [Q9Y6K1-2]
    NP_783328.1. NM_175629.2. [Q9Y6K1-1]
    NP_783329.1. NM_175630.1. [Q9Y6K1-3]
    XP_005264232.1. XM_005264175.2. [Q9Y6K1-1]
    XP_005264233.1. XM_005264176.1. [Q9Y6K1-1]
    XP_005264234.1. XM_005264177.2.
    UniGeneiHs.515840.

    Genome annotation databases

    EnsembliENST00000264709; ENSP00000264709; ENSG00000119772. [Q9Y6K1-1]
    ENST00000321117; ENSP00000324375; ENSG00000119772. [Q9Y6K1-1]
    ENST00000380746; ENSP00000370122; ENSG00000119772. [Q9Y6K1-2]
    ENST00000402667; ENSP00000384237; ENSG00000119772.
    ENST00000406659; ENSP00000384852; ENSG00000119772. [Q9Y6K1-3]
    GeneIDi1788.
    KEGGihsa:1788.
    UCSCiuc002rgc.4. human. [Q9Y6K1-1]
    uc002rgf.3. human. [Q9Y6K1-3]

    Polymorphism databases

    DMDMi166215081.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF067972 mRNA. Translation: AAD33084.2 .
    AF480163 mRNA. Translation: AAN40037.1 . Different initiation.
    AF331856 mRNA. Translation: AAL57039.1 . Different initiation.
    AC012074 Genomic DNA. Translation: AAY14761.1 .
    CH471053 Genomic DNA. Translation: EAX00727.1 .
    BC032392 mRNA. Translation: AAH32392.1 .
    BC043617 mRNA. Translation: AAH43617.1 .
    BC051864 mRNA. Translation: AAH51864.1 .
    CCDSi CCDS1718.2. [Q9Y6K1-2 ]
    CCDS33157.1. [Q9Y6K1-1 ]
    CCDS46232.1. [Q9Y6K1-3 ]
    RefSeqi NP_072046.2. NM_022552.4. [Q9Y6K1-1 ]
    NP_715640.2. NM_153759.3. [Q9Y6K1-2 ]
    NP_783328.1. NM_175629.2. [Q9Y6K1-1 ]
    NP_783329.1. NM_175630.1. [Q9Y6K1-3 ]
    XP_005264232.1. XM_005264175.2. [Q9Y6K1-1 ]
    XP_005264233.1. XM_005264176.1. [Q9Y6K1-1 ]
    XP_005264234.1. XM_005264177.2.
    UniGenei Hs.515840.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QRV X-ray 2.89 A/D/E/H 627-912 [» ]
    3A1A X-ray 2.30 A 476-614 [» ]
    3A1B X-ray 2.29 A 476-614 [» ]
    3LLR X-ray 2.30 A/B/C/D/E 275-427 [» ]
    3SVM X-ray 2.31 P 40-53 [» ]
    ProteinModelPortali Q9Y6K1.
    SMRi Q9Y6K1. Positions 283-425, 475-912.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108125. 53 interactions.
    DIPi DIP-38004N.
    IntActi Q9Y6K1. 20 interactions.
    STRINGi 9606.ENSP00000264709.

    Chemistry

    ChEMBLi CHEMBL1992.

    Protein family/group databases

    REBASEi 4119. M.HsaDnmt3A.

    PTM databases

    PhosphoSitei Q9Y6K1.

    Polymorphism databases

    DMDMi 166215081.

    Proteomic databases

    MaxQBi Q9Y6K1.
    PaxDbi Q9Y6K1.
    PRIDEi Q9Y6K1.

    Protocols and materials databases

    DNASUi 1788.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264709 ; ENSP00000264709 ; ENSG00000119772 . [Q9Y6K1-1 ]
    ENST00000321117 ; ENSP00000324375 ; ENSG00000119772 . [Q9Y6K1-1 ]
    ENST00000380746 ; ENSP00000370122 ; ENSG00000119772 . [Q9Y6K1-2 ]
    ENST00000402667 ; ENSP00000384237 ; ENSG00000119772 .
    ENST00000406659 ; ENSP00000384852 ; ENSG00000119772 . [Q9Y6K1-3 ]
    GeneIDi 1788.
    KEGGi hsa:1788.
    UCSCi uc002rgc.4. human. [Q9Y6K1-1 ]
    uc002rgf.3. human. [Q9Y6K1-3 ]

    Organism-specific databases

    CTDi 1788.
    GeneCardsi GC02M025455.
    HGNCi HGNC:2978. DNMT3A.
    HPAi CAB009469.
    HPA026588.
    MIMi 602769. gene.
    neXtProti NX_Q9Y6K1.
    PharmGKBi PA27445.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG70699.
    HOGENOMi HOG000230875.
    HOVERGENi HBG051381.
    InParanoidi Q9Y6K1.
    KOi K17398.
    OMAi FVGGMCQ.
    OrthoDBi EOG7MWGW6.
    PhylomeDBi Q9Y6K1.
    TreeFami TF329039.

    Enzyme and pathway databases

    BRENDAi 2.1.1.37. 2681.
    Reactomei REACT_200808. PRC2 methylates histones and DNA.

    Miscellaneous databases

    EvolutionaryTracei Q9Y6K1.
    GenomeRNAii 1788.
    NextBioi 7279.
    PROi Q9Y6K1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y6K1.
    Bgeei Q9Y6K1.
    CleanExi HS_DNMT3A.
    Genevestigatori Q9Y6K1.

    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, expression and chromosome locations of the human DNMT3 gene family."
      Xie S., Wang Z., Okano M., Nogami M., Li Y., He W.-W., Okumura K., Li E.
      Gene 236:87-95(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal testis.
    2. "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).
    3. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DNMT1 AND DNMT3B, SUBCELLULAR LOCATION.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 3).
      Tissue: Lung, PNS and Skin.
    7. "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.
    8. "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-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "The histone methyltransferase SETDB1 and the DNA methyltransferase DNMT3A interact directly and localize to promoters silenced in cancer cells."
      Li H., Rauch T., Chen Z.-X., Szabo P.E., Riggs A.D., Pfeifer G.P.
      J. Biol. Chem. 281:19489-19500(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SETDB1.
    10. Cited for: FUNCTION, INTERACTION WITH THE PRC2/EED-EZH2 COMPLEX.
    11. "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.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing and promotes tumour cell motility and invasion."
      Kokura K., Sun L., Bedford M.T., Fang J.
      EMBO J. 29:3673-3687(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MPHOSPH8.
    14. "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-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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-105; SER-243; SER-255; THR-261 AND SER-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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: X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 627-909 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, SUBUNIT, MUTAGENESIS OF PHE-732.
    17. "Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX-DNMT3-DNMT3L domain."
      Otani J., Nankumo T., Arita K., Inamoto S., Ariyoshi M., Shirakawa M.
      EMBO Rep. 10:1235-1241(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 476-614 IN COMPLEXES WITH ZINC AND WITH HISTONE H3 PEPTIDE, SUBUNIT.
    18. "MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a."
      Chang Y., Sun L., Kokura K., Horton J.R., Fukuda M., Espejo A., Izumi V., Koomen J.M., Bedford M.T., Zhang X., Shinkai Y., Fang J., Cheng X.
      Nat. Commun. 2:533-533(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 40-53 IN COMPLEX WITH MPHOSPH8, INTERACTION WITH MPHOSPH8.
    19. "Structural and histone binding ability characterizations of human PWWP domains."
      Wu H., Zeng H., Lam R., Tempel W., Amaya M.F., Xu C., Dombrovski L., Qiu W., Wang Y., Min J.
      PLoS ONE 6:E18919-E18919(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 275-427.
    20. "Mutational spectrum analysis of chronic myelomonocytic leukemia includes genes associated with epigenetic regulation: UTX, EZH2, and DNMT3A."
      Jankowska A.M., Makishima H., Tiu R.V., Szpurka H., Huang Y., Traina F., Visconte V., Sugimoto Y., Prince C., O'Keefe C., Hsi E.D., List A., Sekeres M.A., Rao A., McDevitt M.A., Maciejewski J.P.
      Blood 118:3932-3941(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ASP-699; PHE-731 DEL; CYS-882; HIS-882 AND PRO-882.

    Entry informationi

    Entry nameiDNM3A_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6K1
    Secondary accession number(s): E9PEB8
    , Q86TE8, Q86XF5, Q8IZV0, Q8WXU9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 131 of the entry and version 4 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 2
      Human chromosome 2: 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

    Dasty 3