[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3). DOI=10.1038/890; PubMed=9662389 [NCBI, ExPASy, EBI, Israel, Japan] Okano M., Xie S., Li E.; "Cloning and characterization of a family of novel mammalian DNA (cytosine-5) methyltransferases."; Nat. Genet. 19:219-220(1998).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4). STRAIN=KM; TISSUE=Embryo; PubMed=12567489 [NCBI, ExPASy, EBI, Israel, Japan] Yin B., Chen Y., Zhu N., Wu G., Shen Y.; "Cloning of full-length Dnmt3b cDNA and its alternative splicing isoforms in mouse embryo."; Zhongguo Yi Xue Ke Xue Yuan Xue Bao 21:431-438(1999).
[3]	FUNCTION, AND DEVELOPMENTAL STAGE. DOI=10.1016/S0092-8674(00)81656-6; PubMed=10555141 [NCBI, ExPASy, EBI, Israel, Japan] Okano M., Bell D.W., Haber D.A., Li E.; "DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo methylation and mammalian development."; Cell 99:247-257(1999).
[4]	INTERACTION WITH SUV39H1. DOI=10.1016/S0960-9822(03)00432-9; PubMed=12867029 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Suv39h-mediated histone H3 lysine 9 methylation directs DNA methylation to major satellite repeats at pericentric heterochromatin."; Curr. Biol. 13:1192-1200(2003).
[5]	INTERACTION WITH EED AND EZH2. DOI=10.1038/nature04431; PubMed=16357870 [NCBI, ExPASy, EBI, Israel, Japan] Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C., Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M., Esteller M., Di Croce L., de Launoit Y., Fuks F.; "The Polycomb group protein EZH2 directly controls DNA methylation."; Nature 439:871-874(2006).
[6]	ERRATUM. Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C., Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M., Esteller M., Di Croce L., de Launoit Y., Fuks F.; Nature 446:824-824(2006).
[7]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 219-362, FUNCTION, AND INTERACTION WITH DNA. DOI=10.1038/nsb759; PubMed=11836534 [NCBI, ExPASy, EBI, Israel, Japan] Qiu C., Sawada K., Zhang X., Cheng X.; "The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds."; Nat. Struct. Biol. 9:217-224(2002).

Comments

FUNCTION: Required for genome wide de novo methylation and is essential for development. DNA methylation is coordinated with methylation of histones.
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
SUBUNIT: Interacts with SETDB1, UBL1 and UBE2I9. Interacts with DNMT1 and DNMT3A (By similarity). Interacts with SUV39H1. Interacts with the PRC2/EED-EZH2 complex.
SUBCELLULAR LOCATION: Nucleus (Probable).

ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	5
Isoform ID	O88509-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	6
Isoform ID	O88509-2
Features which should be applied to build the isoform sequence: VSP_005642.

Name	3
Synonyms	8
Isoform ID	O88509-3
Features which should be applied to build the isoform sequence: VSP_005642, VSP_005643.

Name	4
Synonyms	7
Isoform ID	O88509-4
Features which should be applied to build the isoform sequence: VSP_005643.

DEVELOPMENTAL STAGE: 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.
SIMILARITY: Belongs to the C5-methyltransferase family.
SIMILARITY: Contains 1 ADD-type zinc finger.
SIMILARITY: Contains 1 PWWP domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF068626; AAC40178.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF068627; AAC40179.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF068628; AAC40180.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151969; AAF74515.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151970; AAF74516.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151971; AAF74517.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151972; AAF74518.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151973; AAF74519.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151974; AAF74520.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151975; AAF74521.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151976; AAF74522.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001003960.2; -.
NP_001003961.2; -.
NP_001003963.2; -.
NP_034198.3; -.

UniGene

Mm.89772

3D structure databases

PDB

1KHC; X-ray; 1.80 A; A=219-362.

[ExPASy / RCSB / EBI]

PDBsum

1KHC; -.

ModBase

O88509.

Protein family/group databases

REBASE

3748; M.MmuDnmt3B.

PTM databases

PhosphoSite

O88509; -.

Organism-specific databases

MGI

MGI:1261819; Dnmt3b.

Gene expression databases

ArrayExpress

O88509; -.

CleanEx

MM_DNMT3B; -.

GermOnline

ENSMUSG00000027478; Mus musculus.

Ontologies

GO:0005720;	Cellular component: nuclear heterochromatin (inferred from direct assay from MGI).
GO:0003886;	Molecular function: DNA (cytosine-5-)-methyltransferase activity (inferred from direct assay from MGI).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006306;	Biological process: DNA methylation (inferred from genetic interaction from MGI).
GO:0006349;	Biological process: genetic imprinting (inferred from mutant phenotype from MGI).
GO:0006346;	Biological process: methylation-dependent chromatin silencing (inferred from genetic interaction from MGI).
GO:0031503;	Biological process: protein complex localization (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR001525; C5_DNA_meth.
IPR000313; PWWP.
Graphical view of domain structure.

Pfam

PF00145; DNA_methylase; 1.
PF00855; PWWP; 1.
Pfam graphical view of domain structure.

SMART

SM00293; PWWP; 1.
SMART graphical view of domain structure.

PROSITE

PS00094; C5_MTASE_1; 1.
PS00095; C5_MTASE_2; FALSE_NEG.
PS50812; PWWP; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

O88509.

Genome annotation databases

Ensembl

ENSMUSG00000027478; Mus musculus. [Contig view]

GeneID

13436; -.

KEGG

mmu:13436; -.

Phylogenomic databases

HOVERGEN

O88509; -.

Other

NextBio

283873; -.

SOURCE

Dnmt3b; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; DNA-binding; Metal-binding; Methyltransferase; Nucleus; S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 859`	`859`	`DNA (cytosine-5)-methyltransferase 3B.`	`PRO_0000088046`
`DOMAIN`	`232 290`	`59`	`PWWP.`
`ZN_FING`	`440 532`	`93`	`ADD-type.`
`REGION`	`1 305`	`305`	`Interaction with DNMT1 and DNMT3A (By similarity).`
`REGION`	`440 532`	`93`	`Interaction with the PRC2/EED-EZH2 complex.`
`COMPBIAS`	`160 165`	`6`	`Poly-Arg.`
`ACT_SITE`	`657 657`		`By similarity.`
`VAR_SEQ`	`363 382`		`Missing (in isoform 2 and isoform 3).`	`VSP_005642`
`VAR_SEQ`	`750 812`		`Missing (in isoform 3 and isoform 4).`	`VSP_005643`
`CONFLICT`	`217 218`		`RD -> IY (in Ref. 2; AAF74515/AAF74516).`
`STRAND`	`226 229`	`4`
`STRAND`	`235 240`	`6`
`TURN`	`241 243`	`3`
`STRAND`	`244 251`	`8`
`HELIX`	`253 255`	`3`
`STRAND`	`265 270`	`6`
`TURN`	`271 273`	`3`
`STRAND`	`276 280`	`5`
`HELIX`	`281 283`	`3`
`HELIX`	`290 293`	`4`
`HELIX`	`296 301`	`6`
`HELIX`	`303 320`	`18`
`HELIX`	`332 344`	`13`
`TURN`	`348 350`	`3`
`HELIX`	`351 355`	`5`

Sequence information

Length: 859 AA [This is the length of the unprocessed precursor]

Molecular weight: 97228 Da [This is the MW of the unprocessed precursor]

CRC64: 93E334D9FBCC590E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKGDSRHLNE EEGASGYEEC IIVNGNFSDQ SSDTKDAPSP PVLEAICTEP VCTPETRGRR 

        70         80         90        100        110        120 
SSSRLSKREV SSLLNYTQDM TGDGDRDDEV DDGNGSDILM PKLTRETKDT RTRSESPAVR 

       130        140        150        160        170        180 
TRHSNGTSSL ERQRASPRIT RGRQGRHHVQ EYPVEFPATR SRRRRASSSA STPWSSPASV 

       190        200        210        220        230        240 
DFMEEVTPKS VSTPSVDLSQ DGDQEGMDTT QVDAESRDGD STEYQDDKEF GIGDLVWGKI 

       250        260        270        280        290        300 
KGFSWWPAMV VSWKATSKRQ AMPGMRWVQW FGDGKFSEIS ADKLVALGLF SQHFNLATFN 

       310        320        330        340        350        360 
KLVSYRKAMY HTLEKARVRA GKTFSSSPGE SLEDQLKPML EWAHGGFKPT GIEGLKPNKK 

       370        380        390        400        410        420 
QPVVNKSKVR RSDSRNLEPR RRENKSRRRT TNDSAASESP PPKRLKTNSY GGKDRGEDEE 

       430        440        450        460        470        480 
SRERMASEVT NNKGNLEDRC LSCGKKNPVS FHPLFEGGLC QSCRDRFLEL FYMYDEDGYQ 

       490        500        510        520        530        540 
SYCTVCCEGR ELLLCSNTSC CRCFCVECLE VLVGAGTAED AKLQEPWSCY MCLPQRCHGV 

       550        560        570        580        590        600 
LRRRKDWNMR LQDFFTTDPD LEEFEPPKLY PAIPAAKRRP IRVLSLFDGI ATGYLVLKEL 

       610        620        630        640        650        660 
GIKVEKYIAS EVCAESIAVG TVKHEGQIKY VNDVRKITKK NIEEWGPFDL VIGGSPCNDL 

       670        680        690        700        710        720 
SNVNPARKGL YEGTGRLFFE FYHLLNYTRP KEGDNRPFFW MFENVVAMKV NDKKDISRFL 

       730        740        750        760        770        780 
ACNPVMIDAI KVSAAHRARY FWGNLPGMNR PVMASKNDKL ELQDCLEFSR TAKLKKVQTI 

       790        800        810        820        830        840 
TTKSNSIRQG KNQLFPVVMN GKDDVLWCTE LERIFGFPAH YTDVSNMGRG ARQKLLGRSW 

       850 
SVPVIRHLFA PLKDYFACE

O88509 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools