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O88509

- DNM3B_MOUSE

UniProt

O88509 - DNM3B_MOUSE

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Protein

DNA (cytosine-5)-methyltransferase 3B

Gene

Dnmt3b

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. May preferentially methylates nucleosomal DNA within the nucleosome core region. May function as transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Seems to be involved in gene silencing. In association with DNMT1 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. Function as transcriptional corepressor by associating with ZHX1 (By similarity).By similarity

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei611 – 6111S-adenosyl-L-methionineBy similarity
Active sitei657 – 6571PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri439 – 46931GATA-type; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri480 – 53657PHD-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA (cytosine-5-)-methyltransferase activity Source: MGI
  2. DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates Source: Ensembl
  3. DNA binding Source: MGI
  4. metal ion binding Source: UniProtKB-KW
  5. methyltransferase activity Source: UniProtKB
  6. transcription corepressor activity Source: Ensembl
  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: MGI
  4. DNA methylation involved in embryo development Source: UniProtKB
  5. DNA methylation on cytosine within a CG sequence Source: Ensembl
  6. methylation-dependent chromatin silencing Source: MGI
  7. negative regulation of gene expression, epigenetic Source: UniProtKB
  8. negative regulation of histone H3-K9 methylation Source: Ensembl
  9. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  10. positive regulation of gene expression Source: Ensembl
  11. positive regulation of histone H3-K4 methylation Source: Ensembl
  12. positive regulation of neuron differentiation Source: Ensembl
  13. protein complex localization Source: MGI
  14. regulation of gene expression by genetic imprinting Source: MGI
  15. response to drug Source: Ensembl
  16. response to ionizing radiation Source: Ensembl
  17. S-adenosylhomocysteine metabolic process Source: Ensembl
  18. S-adenosylmethioninamine metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Methyltransferase, Repressor, Transferase

Keywords - Ligandi

DNA-binding, Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BRENDAi2.1.1.37. 3474.
ReactomeiREACT_200667. NoRC negatively regulates rRNA expression.
REACT_214440. NoRC negatively regulates rRNA expression.
REACT_222475. PRC2 methylates histones and DNA.

Protein family/group databases

REBASEi3748. M.MmuDnmt3B.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA (cytosine-5)-methyltransferase 3B (EC:2.1.1.37)
Short name:
Dnmt3b
Alternative name(s):
DNA methyltransferase MmuIIIB
Short name:
DNA MTase MmuIIIB
Short name:
M.MmuIIIB
Gene namesi
Name:Dnmt3b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1261819. Dnmt3b.

Subcellular locationi

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

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB
  2. cytoplasm Source: Ensembl
  3. heterochromatin Source: MGI
  4. nuclear heterochromatin Source: MGI
  5. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi236 – 2372VW → RR: Prevents accumulation in pericentric heterochromatin. 1 Publication
Mutagenesisi277 – 2771S → P: Prevents accumulation in pericentric heterochromatin. 1 Publication
Mutagenesisi609 – 6091A → T: Significantly reduces activity. 1 Publication
Mutagenesisi656 – 6572PC → GT: No effect on localization. 1 Publication
Mutagenesisi669 – 6691G → S: Significantly reduces activity. 1 Publication
Mutagenesisi670 – 6701L → T: Significantly reduces activity. 1 Publication
Mutagenesisi725 – 7251V → G: Loss of activity. 1 Publication
Mutagenesisi823 – 8231D → G: Significantly reduces activity. 1 Publication
Mutagenesisi824 – 8241V → M: Significantly reduces activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 859859DNA (cytosine-5)-methyltransferase 3BPRO_0000088046Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei96 – 961PhosphoserineBy similarity
Modified residuei112 – 1121PhosphothreonineBy similarity
Modified residuei116 – 1161PhosphoserineBy similarity
Modified residuei216 – 2161PhosphoserineBy similarity
Modified residuei415 – 4151Citrulline1 Publication

Post-translational modificationi

Sumoylated.By similarity
Citrullinated by PADI4.1 Publication

Keywords - PTMi

Citrullination, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO88509.
PaxDbiO88509.
PRIDEiO88509.

PTM databases

PhosphoSiteiO88509.

Expressioni

Developmental stagei

Expressed in almost all blastocysts at embryonic day 3.0 (E3.0). Preferentially expressed in the trophectoderm (TE) in E3.5 and polar TE in E4.0 blastocysts. In E4.5 embryos, expressed in the polar TE and some inner cell mass (ICM) embryonic lineage cells. In post-implantation embryo at E5.5, expressed in the epiblast (embryonic lineage) derived from the ICM. Highly expressed, at E7.5, in the embryonic ectoderm, neural ectoderm, and chorionic ectoderm; a weak expression is also detected in mesodermal and endodermal cells. At later stages, the expression is detected predominantly in the forebrain and eyes but weakly throughout the embryo.2 Publications

Gene expression databases

BgeeiO88509.
CleanExiMM_DNMT3B.
ExpressionAtlasiO88509. baseline and differential.
GenevestigatoriO88509.

Interactioni

Subunit structurei

Interacts with CBX4, DNMT1, DNMT3A, SETDB1, UBE2I9, UBL1 and ZHX1 (By similarity). Interacts with SUV39H1 and BAZ2A/TIP5. Interacts with the PRC2/EED-EZH2 complex. Interacts with UHRF1.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dnmt3lQ9CWR85EBI-7987547,EBI-3043871
HellsQ608484EBI-7987547,EBI-3043887

Protein-protein interaction databases

BioGridi199262. 10 interactions.
DIPiDIP-43736N.
IntActiO88509. 5 interactions.
MINTiMINT-2523761.

Structurei

Secondary structure

1
859
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi226 – 2294
Beta strandi235 – 2406
Turni241 – 2433
Beta strandi244 – 2518
Helixi253 – 2553
Beta strandi265 – 2706
Turni271 – 2733
Beta strandi276 – 2805
Helixi281 – 2833
Helixi290 – 2934
Helixi296 – 3016
Helixi303 – 32018
Helixi332 – 34413
Turni348 – 3503
Helixi351 – 3555

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KHCX-ray1.80A219-366[»]
ProteinModelPortaliO88509.
SMRiO88509. Positions 223-357, 421-858.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88509.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini232 – 29059PWWPPROSITE-ProRule annotationAdd
BLAST
Domaini428 – 560133ADDPROSITE-ProRule annotationAdd
BLAST
Domaini581 – 859279SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 305305Interaction with DNMT1 and DNMT3ABy similarityAdd
BLAST
Regioni440 – 53293Interaction with the PRC2/EED-EZH2 complexAdd
BLAST
Regioni588 – 5925S-adenosyl-L-methionine bindingBy similarity
Regioni633 – 6353S-adenosyl-L-methionine bindingBy similarity
Regioni838 – 8403S-adenosyl-L-methionine bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi160 – 1656Poly-Arg

Domaini

The PWWP domain is essential for targeting to pericentric heterochromatin.

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 fingeri439 – 46931GATA-type; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri480 – 53657PHD-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG70699.
GeneTreeiENSGT00390000008341.
HOGENOMiHOG000230875.
HOVERGENiHBG051381.
InParanoidiO88509.
KOiK17399.
OrthoDBiEOG7MWGW6.
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.
IPR011011. Znf_FYVE_PHD.
[Graphical view]
PfamiPF00145. DNA_methylase. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
SMARTiSM00293. PWWP. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
SSF57903. SSF57903. 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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O88509-1) [UniParc]FASTAAdd to Basket

Also known as: 5

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
MKGDSRHLNE EEGASGYEEC IIVNGNFSDQ SSDTKDAPSP PVLEAICTEP
60 70 80 90 100
VCTPETRGRR SSSRLSKREV SSLLNYTQDM TGDGDRDDEV DDGNGSDILM
110 120 130 140 150
PKLTRETKDT RTRSESPAVR TRHSNGTSSL ERQRASPRIT RGRQGRHHVQ
160 170 180 190 200
EYPVEFPATR SRRRRASSSA STPWSSPASV DFMEEVTPKS VSTPSVDLSQ
210 220 230 240 250
DGDQEGMDTT QVDAESRDGD STEYQDDKEF GIGDLVWGKI KGFSWWPAMV
260 270 280 290 300
VSWKATSKRQ AMPGMRWVQW FGDGKFSEIS ADKLVALGLF SQHFNLATFN
310 320 330 340 350
KLVSYRKAMY HTLEKARVRA GKTFSSSPGE SLEDQLKPML EWAHGGFKPT
360 370 380 390 400
GIEGLKPNKK QPVVNKSKVR RSDSRNLEPR RRENKSRRRT TNDSAASESP
410 420 430 440 450
PPKRLKTNSY GGKDRGEDEE SRERMASEVT NNKGNLEDRC LSCGKKNPVS
460 470 480 490 500
FHPLFEGGLC QSCRDRFLEL FYMYDEDGYQ SYCTVCCEGR ELLLCSNTSC
510 520 530 540 550
CRCFCVECLE VLVGAGTAED AKLQEPWSCY MCLPQRCHGV LRRRKDWNMR
560 570 580 590 600
LQDFFTTDPD LEEFEPPKLY PAIPAAKRRP IRVLSLFDGI ATGYLVLKEL
610 620 630 640 650
GIKVEKYIAS EVCAESIAVG TVKHEGQIKY VNDVRKITKK NIEEWGPFDL
660 670 680 690 700
VIGGSPCNDL SNVNPARKGL YEGTGRLFFE FYHLLNYTRP KEGDNRPFFW
710 720 730 740 750
MFENVVAMKV NDKKDISRFL ACNPVMIDAI KVSAAHRARY FWGNLPGMNR
760 770 780 790 800
PVMASKNDKL ELQDCLEFSR TAKLKKVQTI TTKSNSIRQG KNQLFPVVMN
810 820 830 840 850
GKDDVLWCTE LERIFGFPAH YTDVSNMGRG ARQKLLGRSW SVPVIRHLFA

PLKDYFACE
Length:859
Mass (Da):97,228
Last modified:May 1, 2000 - v2
Checksum:i93E334D9FBCC590E
GO
Isoform 2 (identifier: O88509-2) [UniParc]FASTAAdd to Basket

Also known as: 6

The sequence of this isoform differs from the canonical sequence as follows:
     363-382: Missing.

Show »
Length:839
Mass (Da):94,793
Checksum:i59BF48AB459A1298
GO
Isoform 3 (identifier: O88509-3) [UniParc]FASTAAdd to Basket

Also known as: 8

The sequence of this isoform differs from the canonical sequence as follows:
     363-382: Missing.
     750-812: Missing.

Show »
Length:776
Mass (Da):87,586
Checksum:i211E2DE8BF06C48E
GO
Isoform 4 (identifier: O88509-4) [UniParc]FASTAAdd to Basket

Also known as: 7

The sequence of this isoform differs from the canonical sequence as follows:
     750-812: Missing.

Show »
Length:796
Mass (Da):90,021
Checksum:i0B7D93B4D802744E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti217 – 2182RD → IY in AAF74515. (PubMed:12567489)Curated
Sequence conflicti217 – 2182RD → IY in AAF74516. (PubMed:12567489)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei363 – 38220Missing in isoform 2 and isoform 3. 2 PublicationsVSP_005642Add
BLAST
Alternative sequencei750 – 81263Missing in isoform 3 and isoform 4. 2 PublicationsVSP_005643Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF068626 mRNA. Translation: AAC40178.2.
AF068627 mRNA. Translation: AAC40179.2.
AF068628 mRNA. Translation: AAC40180.2.
AF151969 mRNA. Translation: AAF74515.1.
AF151970 mRNA. Translation: AAF74516.1.
AF151971 mRNA. Translation: AAF74517.1.
AF151972 mRNA. Translation: AAF74518.1.
AF151973 mRNA. Translation: AAF74519.1.
AF151974 mRNA. Translation: AAF74520.1.
AF151975 mRNA. Translation: AAF74521.1.
AF151976 mRNA. Translation: AAF74522.1.
CCDSiCCDS16913.1. [O88509-2]
CCDS16914.1. [O88509-1]
CCDS16915.1. [O88509-4]
CCDS16916.1. [O88509-3]
RefSeqiNP_001003960.2. NM_001003960.4. [O88509-2]
NP_001003961.2. NM_001003961.4. [O88509-1]
NP_001258673.1. NM_001271744.1. [O88509-1]
NP_001258674.1. NM_001271745.1. [O88509-2]
NP_001258676.1. NM_001271747.1. [O88509-3]
NP_034198.3. NM_010068.5. [O88509-3]
UniGeneiMm.491804.
Mm.89772.

Genome annotation databases

EnsembliENSMUST00000072997; ENSMUSP00000072761; ENSMUSG00000027478. [O88509-1]
ENSMUST00000081628; ENSMUSP00000080334; ENSMUSG00000027478. [O88509-2]
ENSMUST00000088976; ENSMUSP00000086370; ENSMUSG00000027478. [O88509-4]
ENSMUST00000103150; ENSMUSP00000099439; ENSMUSG00000027478. [O88509-3]
ENSMUST00000103151; ENSMUSP00000099440; ENSMUSG00000027478. [O88509-3]
ENSMUST00000109772; ENSMUSP00000105394; ENSMUSG00000027478. [O88509-4]
ENSMUST00000109773; ENSMUSP00000105395; ENSMUSG00000027478. [O88509-2]
ENSMUST00000109774; ENSMUSP00000105396; ENSMUSG00000027478. [O88509-1]
GeneIDi13436.
KEGGimmu:13436.
UCSCiuc008nib.2. mouse. [O88509-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF068626 mRNA. Translation: AAC40178.2 .
AF068627 mRNA. Translation: AAC40179.2 .
AF068628 mRNA. Translation: AAC40180.2 .
AF151969 mRNA. Translation: AAF74515.1 .
AF151970 mRNA. Translation: AAF74516.1 .
AF151971 mRNA. Translation: AAF74517.1 .
AF151972 mRNA. Translation: AAF74518.1 .
AF151973 mRNA. Translation: AAF74519.1 .
AF151974 mRNA. Translation: AAF74520.1 .
AF151975 mRNA. Translation: AAF74521.1 .
AF151976 mRNA. Translation: AAF74522.1 .
CCDSi CCDS16913.1. [O88509-2 ]
CCDS16914.1. [O88509-1 ]
CCDS16915.1. [O88509-4 ]
CCDS16916.1. [O88509-3 ]
RefSeqi NP_001003960.2. NM_001003960.4. [O88509-2 ]
NP_001003961.2. NM_001003961.4. [O88509-1 ]
NP_001258673.1. NM_001271744.1. [O88509-1 ]
NP_001258674.1. NM_001271745.1. [O88509-2 ]
NP_001258676.1. NM_001271747.1. [O88509-3 ]
NP_034198.3. NM_010068.5. [O88509-3 ]
UniGenei Mm.491804.
Mm.89772.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KHC X-ray 1.80 A 219-366 [» ]
ProteinModelPortali O88509.
SMRi O88509. Positions 223-357, 421-858.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199262. 10 interactions.
DIPi DIP-43736N.
IntActi O88509. 5 interactions.
MINTi MINT-2523761.

Chemistry

ChEMBLi CHEMBL2189115.

Protein family/group databases

REBASEi 3748. M.MmuDnmt3B.

PTM databases

PhosphoSitei O88509.

Proteomic databases

MaxQBi O88509.
PaxDbi O88509.
PRIDEi O88509.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000072997 ; ENSMUSP00000072761 ; ENSMUSG00000027478 . [O88509-1 ]
ENSMUST00000081628 ; ENSMUSP00000080334 ; ENSMUSG00000027478 . [O88509-2 ]
ENSMUST00000088976 ; ENSMUSP00000086370 ; ENSMUSG00000027478 . [O88509-4 ]
ENSMUST00000103150 ; ENSMUSP00000099439 ; ENSMUSG00000027478 . [O88509-3 ]
ENSMUST00000103151 ; ENSMUSP00000099440 ; ENSMUSG00000027478 . [O88509-3 ]
ENSMUST00000109772 ; ENSMUSP00000105394 ; ENSMUSG00000027478 . [O88509-4 ]
ENSMUST00000109773 ; ENSMUSP00000105395 ; ENSMUSG00000027478 . [O88509-2 ]
ENSMUST00000109774 ; ENSMUSP00000105396 ; ENSMUSG00000027478 . [O88509-1 ]
GeneIDi 13436.
KEGGi mmu:13436.
UCSCi uc008nib.2. mouse. [O88509-1 ]

Organism-specific databases

CTDi 1789.
MGIi MGI:1261819. Dnmt3b.

Phylogenomic databases

eggNOGi NOG70699.
GeneTreei ENSGT00390000008341.
HOGENOMi HOG000230875.
HOVERGENi HBG051381.
InParanoidi O88509.
KOi K17399.
OrthoDBi EOG7MWGW6.
TreeFami TF329039.

Enzyme and pathway databases

BRENDAi 2.1.1.37. 3474.
Reactomei REACT_200667. NoRC negatively regulates rRNA expression.
REACT_214440. NoRC negatively regulates rRNA expression.
REACT_222475. PRC2 methylates histones and DNA.

Miscellaneous databases

ChiTaRSi DNMT3B. mouse.
EvolutionaryTracei O88509.
NextBioi 283873.
PROi O88509.
SOURCEi Search...

Gene expression databases

Bgeei O88509.
CleanExi MM_DNMT3B.
ExpressionAtlasi O88509. baseline and differential.
Genevestigatori O88509.

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.
IPR011011. Znf_FYVE_PHD.
[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.
SSF57903. SSF57903. 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] (ISOFORMS 1; 2 AND 3).
  2. "Cloning of full-length Dnmt3b cDNA and its alternative splicing isoforms in mouse embryo."
    Yin B., Chen Y., Zhu N., Wu G., Shen Y.
    Zhongguo Yi Xue Ke Xue Yuan Xue Bao 21:431-438(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
    Strain: KM.
    Tissue: Embryo.
  3. "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.
  4. "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, MUTAGENESIS OF ALA-609; GLY-669; LEU-670; VAL-725; ASP-823 AND VAL-824.
  5. Cited for: CITRULLINATION AT ARG-415.
  6. "Suv39h-mediated histone H3 lysine 9 methylation directs DNA methylation to major satellite repeats at pericentric heterochromatin."
    Lehnertz B., Ueda Y., Derijck A.A.H.A., Braunschweig U., Perez-Burgos L., Kubicek S., Chen T., Li E., Jenuwein T., Peters A.H.F.M.
    Curr. Biol. 13:1192-1200(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUV39H1.
  7. "The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 and is sufficient for rDNA silencing."
    Zhou Y., Grummt I.
    Curr. Biol. 15:1434-1438(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAZ2A.
  8. Cited for: INTERACTION WITH EED AND EZH2.
  9. "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 236-VAL-TRP-237; SER-277 AND 656-PRO-CYS-657.
  10. "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.
  11. "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.
  12. "Dnmt3b promotes tumorigenesis in vivo by gene-specific de novo methylation and transcriptional silencing."
    Linhart H.G., Lin H., Yamada Y., Moran E., Steine E.J., Gokhale S., Lo G., Cantu E., Ehrich M., He T., Meissner A., Jaenisch R.
    Genes Dev. 21:3110-3122(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "DNA methyltransferase 3B acts as a co-repressor of the human polycomb protein hPc2 to repress fibroblast growth factor receptor 3 transcription."
    Kim S.-H., Park J., Choi M.-C., Park J.-H., Kim H.-P., Lee J.-H., Oh D.-Y., Im S.-A., Bang Y.-J., Kim T.-Y.
    Int. J. Biochem. Cell Biol. 40:2462-2471(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CBX4.
  14. "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.
  15. "Dynamic transition of Dnmt3b expression in mouse pre- and early post-implantation embryos."
    Hirasawa R., Sasaki H.
    Gene Expr. Patterns 9:27-30(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  16. "The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds."
    Qiu C., Sawada K., Zhang X., Cheng X.
    Nat. Struct. Biol. 9:217-224(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 219-362, FUNCTION, INTERACTION WITH DNA.

Entry informationi

Entry nameiDNM3B_MOUSE
AccessioniPrimary (citable) accession number: O88509
Secondary accession number(s): O88510, O88511
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 132 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