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O88508

- DNM3A_MOUSE

UniProt

O88508 - DNM3A_MOUSE

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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

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. 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
Complete GO annotation...

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
  8. XY body Source: MGI
Complete GO annotation...

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

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

BgeeiO88508.
CleanExiMM_DNMT3A.
ExpressionAtlasiO88508. baseline and differential.
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

        10         20         30         40         50
MPSSGPGDTS SSSLEREDDR KEGEEQEENR GKEERQEPSA TARKVGRPGR
60 70 80 90 100
KRKHPPVESS DTPKDPAVTT KSQPMAQDSG PSDLLPNGDL EKRSEPQPEE
110 120 130 140 150
GSPAAGQKGG APAEGEGTET PPEASRAVEN GCCVTKEGRG ASAGEGKEQK
160 170 180 190 200
QTNIESMKME GSRGRLRGGL GWESSLRQRP MPRLTFQAGD PYYISKRKRD
210 220 230 240 250
EWLARWKREA EKKAKVIAVM NAVEENQASG ESQKVEEASP PAVQQPTDPA
260 270 280 290 300
SPTVATTPEP VGGDAGDKNA TKAADDEPEY EDGRGFGIGE LVWGKLRGFS
310 320 330 340 350
WWPGRIVSWW MTGRSRAAEG TRWVMWFGDG KFSVVCVEKL MPLSSFCSAF
360 370 380 390 400
HQATYNKQPM YRKAIYEVLQ VASSRAGKLF PACHDSDESD SGKAVEVQNK
410 420 430 440 450
QMIEWALGGF QPSGPKGLEP PEEEKNPYKE VYTDMWVEPE AAAYAPPPPA
460 470 480 490 500
KKPRKSTTEK PKVKEIIDER TRERLVYEVR QKCRNIEDIC ISCGSLNVTL
510 520 530 540 550
EHPLFIGGMC QNCKNCFLEC AYQYDDDGYQ SYCTICCGGR EVLMCGNNNC
560 570 580 590 600
CRCFCVECVD LLVGPGAAQA AIKEDPWNCY MCGHKGTYGL LRRREDWPSR
610 620 630 640 650
LQMFFANNHD QEFDPPKVYP PVPAEKRKPI RVLSLFDGIA TGLLVLKDLG
660 670 680 690 700
IQVDRYIASE VCEDSITVGM VRHQGKIMYV GDVRSVTQKH IQEWGPFDLV
710 720 730 740 750
IGGSPCNDLS IVNPARKGLY EGTGRLFFEF YRLLHDARPK EGDDRPFFWL
760 770 780 790 800
FENVVAMGVS DKRDISRFLE SNPVMIDAKE VSAAHRARYF WGNLPGMNRP
810 820 830 840 850
LASTVNDKLE LQECLEHGRI AKFSKVRTIT TRSNSIKQGK DQHFPVFMNE
860 870 880 890 900
KEDILWCTEM ERVFGFPVHY TDVSNMSRLA RQRLLGRSWS VPVIRHLFAP

LKEYFACV
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.

Chemistry

ChEMBLi CHEMBL3108652.

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

Bgeei O88508.
CleanExi MM_DNMT3A.
ExpressionAtlasi O88508. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 149 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