O88509 (DNM3B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA (cytosine-5)-methyltransferase 3B
Short name=Dnmt3b
EC=2.1.1.37

Alternative name(s):
DNA methyltransferase MmuIIIB
Short name=DNA MTase MmuIIIB
Short name=M.MmuIIIB

Gene names

Name:

Dnmt3b

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	859 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.3 Ref.4 Ref.11 Ref.12 Ref.13 Ref.16
Catalytic activity	S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
Enzyme regulation	Activated by binding to the regulatory factor DNMT3L. Ref.10
Subunit structure	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. Ref.5 Ref.6 Ref.7 Ref.13 Ref.14 Ref.16
Subcellular location	Nucleus. Note: Accumulates in the major satellite repeats at pericentric heterochromatin. Ref.9
Developmental stage	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. Ref.3 Ref.15
Domain	The PWWP domain is essential for targeting to pericentric heterochromatin.
Post-translational modification	Sumoylated By similarity.
Sequence similarities	Belongs to the C5-methyltransferase family. Contains 1 ADD domain. Contains 1 GATA-type zinc finger. Contains 1 PHD-type zinc finger. Contains 1 PWWP domain.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Activator Methyltransferase Repressor Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA methylation involved in embryo development Inferred from expression pattern Ref.15. Source: UniProtKB cellular response to amino acid stimulus Inferred from direct assay PubMed 20548288. Source: MGI methylation-dependent chromatin silencing Inferred from genetic interaction PubMed 17938196. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 22133874. Source: MGI protein complex localization Inferred from direct assay PubMed 16543361. Source: MGI regulation of gene expression by genetic imprinting Inferred from mutant phenotype PubMed 11934864. Source: MGI
Cellular_component	chromosome, centromeric region Inferred from direct assay Ref.9. Source: UniProtKB nuclear heterochromatin Inferred from direct assay PubMed 11934864PubMed 16543361. Source: MGI
Molecular_function	DNA (cytosine-5-)-methyltransferase activity Inferred from direct assay PubMed 16543361. Source: MGI DNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O88509-1)

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.

Isoform 2 (identifier: O88509-2)

Also known as: 6;

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

Isoform 3 (identifier: O88509-3)

Also known as: 8;

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

Isoform 4 (identifier: O88509-4)

Also known as: 7;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 859

859

DNA (cytosine-5)-methyltransferase 3B

PRO_0000088046

Regions

Domain

232 – 290

59

PWWP

Domain

428 – 560

133

ADD

Zinc finger

439 – 469

31

GATA-type; atypical

Zinc finger

480 – 536

57

PHD-type; atypical

Region

1 – 305

305

Interaction with DNMT1 and DNMT3A By similarity

Region

440 – 532

93

Interaction with the PRC2/EED-EZH2 complex

Region

588 – 592

5

S-adenosyl-L-methionine binding By similarity

Region

633 – 635

3

S-adenosyl-L-methionine binding By similarity

Region

838 – 840

3

S-adenosyl-L-methionine binding By similarity

Compositional bias

160 – 165

6

Poly-Arg

Sites

Active site

657

1

By similarity

Binding site

611

1

S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue

96

1

Phosphoserine By similarity

Modified residue

112

1

Phosphothreonine By similarity

Modified residue

116

1

Phosphoserine By similarity

Modified residue

216

1

Phosphoserine By similarity

Natural variations

Alternative sequence

363 – 382

20

Missing in isoform 2 and isoform 3.

VSP_005642

Alternative sequence

750 – 812

63

Missing in isoform 3 and isoform 4.

VSP_005643

Experimental info

Mutagenesis

236 – 237

2

VW → RR: Prevents accumulation in pericentric heterochromatin.

Mutagenesis

277

1

S → P: Prevents accumulation in pericentric heterochromatin. Ref.9

Mutagenesis

609

1

A → T: Significantly reduces activity. Ref.4

Mutagenesis

656 – 657

2

PC → GT: No effect on localization.

Mutagenesis

669

1

G → S: Significantly reduces activity. Ref.4

Mutagenesis

670

1

L → T: Significantly reduces activity. Ref.4

Mutagenesis

725

1

V → G: Loss of activity. Ref.4

Mutagenesis

823

1

D → G: Significantly reduces activity. Ref.4

Mutagenesis

824

1

V → M: Significantly reduces activity. Ref.4

Sequence conflict

217 – 218

2

RD → IY in AAF74515. Ref.2

Sequence conflict

217 – 218

2

RD → IY in AAF74516. Ref.2

Secondary structure

1

.

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.

.

.

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.

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859

Helix Strand Turn

Details...

Beta strand

226 – 229

4

Beta strand

235 – 240

6

Turn

241 – 243

3

Beta strand

244 – 251

8

Helix

253 – 255

3

Beta strand

265 – 270

6

Turn

271 – 273

3

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (5) [UniParc]. Last modified May 1, 2000. Version 2. Checksum: 93E334D9FBCC590E	FASTA	859	97,228
	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
	Isoform 2 (6) [UniParc]. Checksum: 59BF48AB459A1298	FASTA	839	94,793
	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 QPENKSRRRT TNDSAASESP PPKRLKTNSY GGKDRGEDEE SRERMASEVT NNKGNLEDRC 430 440 450 460 470 480 LSCGKKNPVS FHPLFEGGLC QSCRDRFLEL FYMYDEDGYQ SYCTVCCEGR ELLLCSNTSC 490 500 510 520 530 540 CRCFCVECLE VLVGAGTAED AKLQEPWSCY MCLPQRCHGV LRRRKDWNMR LQDFFTTDPD 550 560 570 580 590 600 LEEFEPPKLY PAIPAAKRRP IRVLSLFDGI ATGYLVLKEL GIKVEKYIAS EVCAESIAVG 610 620 630 640 650 660 TVKHEGQIKY VNDVRKITKK NIEEWGPFDL VIGGSPCNDL SNVNPARKGL YEGTGRLFFE 670 680 690 700 710 720 FYHLLNYTRP KEGDNRPFFW MFENVVAMKV NDKKDISRFL ACNPVMIDAI KVSAAHRARY 730 740 750 760 770 780 FWGNLPGMNR PVMASKNDKL ELQDCLEFSR TAKLKKVQTI TTKSNSIRQG KNQLFPVVMN 790 800 810 820 830 GKDDVLWCTE LERIFGFPAH YTDVSNMGRG ARQKLLGRSW SVPVIRHLFA PLKDYFACE
	Isoform 3 (8) [UniParc]. Checksum: 211E2DE8BF06C48E	FASTA	776	87,586
	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 QPENKSRRRT TNDSAASESP PPKRLKTNSY GGKDRGEDEE SRERMASEVT NNKGNLEDRC 430 440 450 460 470 480 LSCGKKNPVS FHPLFEGGLC QSCRDRFLEL FYMYDEDGYQ SYCTVCCEGR ELLLCSNTSC 490 500 510 520 530 540 CRCFCVECLE VLVGAGTAED AKLQEPWSCY MCLPQRCHGV LRRRKDWNMR LQDFFTTDPD 550 560 570 580 590 600 LEEFEPPKLY PAIPAAKRRP IRVLSLFDGI ATGYLVLKEL GIKVEKYIAS EVCAESIAVG 610 620 630 640 650 660 TVKHEGQIKY VNDVRKITKK NIEEWGPFDL VIGGSPCNDL SNVNPARKGL YEGTGRLFFE 670 680 690 700 710 720 FYHLLNYTRP KEGDNRPFFW MFENVVAMKV NDKKDISRFL ACNPVMIDAI KVSAAHRARY 730 740 750 760 770 FWGNLPGMNR IFGFPAHYTD VSNMGRGARQ KLLGRSWSVP VIRHLFAPLK DYFACE
	Isoform 4 (7) [UniParc]. Checksum: 0B7D93B4D802744E	FASTA	796	90,021
	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 IFGFPAHYTD VSNMGRGARQ KLLGRSWSVP 790 VIRHLFAPLK DYFACE

References

[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]	"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.
[6]	"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.
[7]	"The Polycomb group protein EZH2 directly controls DNA methylation." 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 439:871-874(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EED AND EZH2.
[8]	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)
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00228733.
IPI00268106.
IPI00276159.
IPI00331143.

RefSeq

NP_001003960.2. NM_001003960.4.
NP_001003961.2. NM_001003961.4.
NP_001258673.1. NM_001271744.1.
NP_001258674.1. NM_001271745.1.
NP_001258676.1. NM_001271747.1.
NP_034198.3. NM_010068.5.

UniGene

Mm.89772.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KHC	X-ray	1.80	A	219-362	[»]

ProteinModelPortal

O88509.

SMR

O88509. Positions 223-357, 421-858.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-43736N.

MINT

MINT-2523761.

Protein family/group databases

REBASE

3748. M.MmuDnmt3B.

PTM databases

PhosphoSite

O88509.

Proteomic databases

PaxDb

O88509.

PRIDE

O88509.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000072997; ENSMUSP00000072761; ENSMUSG00000027478.
ENSMUST00000081628; ENSMUSP00000080334; ENSMUSG00000027478.
ENSMUST00000088976; ENSMUSP00000086370; ENSMUSG00000027478.
ENSMUST00000103150; ENSMUSP00000099439; ENSMUSG00000027478.
ENSMUST00000103151; ENSMUSP00000099440; ENSMUSG00000027478.
ENSMUST00000109772; ENSMUSP00000105394; ENSMUSG00000027478.
ENSMUST00000109773; ENSMUSP00000105395; ENSMUSG00000027478.
ENSMUST00000109774; ENSMUSP00000105396; ENSMUSG00000027478.

GeneID

13436.

KEGG

mmu:13436.

Organism-specific databases

CTD

1789.

MGI

MGI:1261819. Dnmt3b.

Phylogenomic databases

eggNOG

NOG70699.

GeneTree

ENSGT00390000008341.

HOGENOM

HOG000230875.

HOVERGEN

HBG051381.

KO

K00558.

OrthoDB

EOG4CVG68.

Enzyme and pathway databases

BRENDA

2.1.1.37. 3474.

Gene expression databases

ArrayExpress

O88509.

Bgee

O88509.

CleanEx

MM_DNMT3B.

Genevestigator

O88509.

GermOnline

ENSMUSG00000027478. Mus musculus.

Family and domain databases

InterPro

IPR025766. ADD.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR025811. C5_MeTrfase_3.
IPR000313. PWWP.
IPR011011. Znf_FYVE_PHD.
[Graphical view]

Pfam

PF00145. DNA_methylase. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]

SMART

SM00293. PWWP. 1 hit.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS51533. ADD. 1 hit.
PS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. False negative.
PS50812. PWWP. 1 hit.
[Graphical view]

ProtoNet

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Other

ChiTaRS

DNMT3B. mouse.

EvolutionaryTrace

O88509.

NextBio

283873.

SOURCE

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Entry information

Entry name

DNM3B_MOUSE

Accession

Primary (citable) accession number: O88509
Secondary accession number(s): O88510, O88511

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program