Q9UBC3 (DNM3B_HUMAN) 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 HsaIIIB
Short name=DNA MTase HsaIIIB
Short name=M.HsaIIIB

Gene names

Name:

DNMT3B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	853 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 By similarity. 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. Isoforms 4 and 5 are probably not functional due to the deletion of two conserved methyltransferase motifs. Function as transcriptional corepressor by associating with ZHX1. Ref.11 Ref.13 Ref.15 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 By similarity.
Subunit structure	Interacts with BAZ2A/TIP5, SUV39H1 and CBX4. Interacts with UHRF1 By similarity. Interacts with DNMT1 and DNMT3A, SETDB1, UBL1, UBE2I9 and ZHX1. Interacts with the PRC2/EED-EZH2 complex. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13
Subcellular location	Nucleus Ref.8 Ref.9.
Tissue specificity	Ubiquitous; highly expressed in fetal liver, heart, kidney, placenta, and at lower levels in spleen, colon, brain, liver, small intestine, lung, peripheral blood mononuclear cells, and skeletal muscle. Isoform 1 is expressed in all tissues except brain, skeletal muscle and PBMC, 3 is ubiquitous, 4 is expressed in all tissues except brain, skeletal muscle, lung and prostate and 5 is detectable only in testis and at very low level in brain and prostate.
Domain	The PWWP domain is essential for targeting to pericentric heterochromatin.
Post-translational modification	Sumoylated. Ref.8
Involvement in disease	Immunodeficiency-centromeric instability-facial anomalies syndrome 1 (ICF1) [MIM:242860]: A rare disorder characterized by a variable immunodeficiency resulting in recurrent infections, facial anomalies, and branching of chromosomes 1, 9, and 16. Other variable symptoms include growth retardation, failure to thrive, and psychomotor retardation. Laboratory studies show limited hypomethylation of DNA in a small fraction of the genome in some, but not all, patients. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.21 Ref.22 Ref.23 Ref.24
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 Polymorphism
Disease	Disease mutation
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	cellular response to amino acid stimulus Inferred from electronic annotation. Source: Compara methylation-dependent chromatin silencing Inferred from electronic annotation. Source: Compara negative regulation of histone H3-K9 methylation Inferred from mutant phenotype Ref.15. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.13. Source: UniProtKB positive regulation of gene expression Inferred from mutant phenotype Ref.15. Source: UniProtKB positive regulation of histone H3-K4 methylation Inferred from mutant phenotype Ref.15. Source: UniProtKB protein complex localization Inferred from electronic annotation. Source: Compara regulation of gene expression by genetic imprinting Inferred from electronic annotation. Source: Compara
Cellular_component	nuclear heterochromatin Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay Ref.13. Source: UniProtKB
Molecular_function	DNA (cytosine-5-)-methyltransferase activity Non-traceable author statement Ref.2. Source: UniProtKB DNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transcription corepressor activity Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EED	O75530	4	EBI-80125,EBI-923794
EZH2	Q15910	6	EBI-80125,EBI-530054
SUMO1	P63165	4	EBI-80125,EBI-80140
UBE2I	P63279	3	EBI-80125,EBI-80168
ZHX1	Q9UKY1	4	EBI-6083193,EBI-347767

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UBC3-1)

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: Q9UBC3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     356-375: Missing.

Isoform 3 (identifier: Q9UBC3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     356-375: Missing.
     745-807: Missing.

Isoform 4 (identifier: Q9UBC3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     356-375: Missing.
     744-744: R → S
     745-853: Missing.

Isoform 5 (identifier: Q9UBC3-5)

The sequence of this isoform differs from the canonical sequence as follows:
     356-375: Missing.
     768-853: LKKVQTITTK...APLKDYFACE → DLWLSCALHR...LRPSEGLLCM

Isoform 6 (identifier: Q9UBC3-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEPSPEPPSLESM
     356-375: Missing.

Isoform 7 (identifier: Q9UBC3-7)

The sequence of this isoform differs from the canonical sequence as follows:
     69-144: Missing.
     356-375: Missing.
     744-806: Missing.

Note: No experimental confirmation available.

Isoform 8 (identifier: Q9UBC3-8)

The sequence of this isoform differs from the canonical sequence as follows:
     103-144: Missing.
     356-375: Missing.
     744-806: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 853

853

DNA (cytosine-5)-methyltransferase 3B

PRO_0000088045

Regions

Domain

225 – 283

59

PWWP

Domain

423 – 555

133

ADD

Zinc finger

434 – 464

31

GATA-type; atypical

Zinc finger

475 – 531

57

PHD-type; atypical

Region

1 – 298

298

Interaction with DNMT1 and DNMT3A

Region

435 – 527

93

Interaction with the PRC2/EED-EZH2 complex By similarity

Region

582 – 586

5

S-adenosyl-L-methionine binding By similarity

Region

627 – 629

3

S-adenosyl-L-methionine binding By similarity

Region

832 – 834

3

S-adenosyl-L-methionine binding By similarity

Sites

Active site

651

1

By similarity

Binding site

605

1

S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue

82

1

Phosphoserine Ref.18

Modified residue

96

1

Phosphothreonine Ref.18

Modified residue

100

1

Phosphoserine Ref.18

Modified residue

110

1

Phosphoserine Ref.18

Modified residue

136

1

Phosphoserine Ref.17 Ref.18

Modified residue

195

1

Phosphoserine Ref.18

Modified residue

202

1

Phosphoserine Ref.18

Modified residue

209

1

Phosphoserine Ref.18

Natural variations

Alternative sequence

1

1

M → MEPSPEPPSLESM in isoform 6.

VSP_005636

Alternative sequence

69 – 144

76

Missing in isoform 7.

VSP_045874

Alternative sequence

103 – 144

42

Missing in isoform 8.

VSP_045875

Alternative sequence

356 – 375

20

Missing in isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8.

VSP_005637

Alternative sequence

744 – 806

63

Missing in isoform 7 and isoform 8.

VSP_045876

Alternative sequence

744

1

R → S in isoform 4.

VSP_005639

Alternative sequence

745 – 853

109

Missing in isoform 4.

VSP_005640

Alternative sequence

745 – 807

63

Missing in isoform 3.

VSP_005638

Alternative sequence

768 – 853

86

LKKVQ…YFACE → DLWLSCALHRRVQHGPWCPP EAAGKVLERACHPTPLRPSE GLLCM in isoform 5.

VSP_005641

Natural variant

54

1

R → P.
Corresponds to variant rs17123590 [ dbSNP | Ensembl ].

VAR_033885

Natural variant

270

1

S → P in ICF1. Ref.24
Corresponds to variant rs121908947 [ dbSNP | Ensembl ].

VAR_022579

Natural variant

585

1

A → V in ICF1. Ref.23 Ref.24

VAR_011506

Natural variant

603

1

A → T in ICF1. Ref.21 Ref.22 Ref.23 Ref.24
Corresponds to variant rs121908943 [ dbSNP | Ensembl ].

VAR_011499

Natural variant

606

1

V → A in ICF1. Ref.23 Ref.24
Corresponds to variant rs146981624 [ dbSNP | Ensembl ].

VAR_011507

Natural variant

663

1

G → S in ICF1. Ref.2 Ref.24
Corresponds to variant rs121908942 [ dbSNP | Ensembl ].

VAR_011500

Natural variant

664

1

L → P in ICF1. Ref.24

VAR_022580

Natural variant

699

1

V → G in ICF1. Ref.23 Ref.24

VAR_011508

Natural variant

726

1

V → G in ICF1. Ref.2 Ref.22 Ref.23 Ref.24
Corresponds to variant rs121908941 [ dbSNP | Ensembl ].

VAR_011501

Natural variant

766

1

A → P in ICF1. Ref.23 Ref.24

VAR_011509

Natural variant

806

1

E → ESTP in ICF1.

VAR_011502

Natural variant

814

1

H → R in ICF1. Ref.23 Ref.24

VAR_011510

Natural variant

817

1

D → G in ICF1. Ref.2 Ref.24
Corresponds to variant rs121908939 [ dbSNP | Ensembl ].

VAR_011503

Natural variant

818

1

V → M in ICF1. Ref.2 Ref.23 Ref.24
Corresponds to variant rs121908940 [ dbSNP | Ensembl ].

VAR_011504

Natural variant

840

1

R → Q in ICF1. Ref.24
Corresponds to variant rs121908946 [ dbSNP | Ensembl ].

VAR_022581

Experimental info

Sequence conflict

575

1

I → T in BAG61690. Ref.4

Sequence conflict

583

1

G → D in BAG61753. Ref.4

Sequence conflict

655

1

S → P in BAG61690. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

853

Helix Strand Turn

Details...

Beta strand

228 – 231

4

Beta strand

239 – 244

6

Helix

246 – 249

4

Beta strand

258 – 263

6

Turn

264 – 266

3

Beta strand

269 – 273

5

Turn

274 – 276

3

Helix

283 – 286

4

Helix

289 – 294

6

Helix

296 – 313

18

Helix

325 – 337

13

Turn

341 – 343

3

Helix

345 – 348

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: F20A67CF78951532	FASTA	853	95,751
	10 20 30 40 50 60 MKGDTRHLNG EEDAGGREDS ILVNGACSDQ SSDSPPILEA IRTPEIRGRR SSSRLSKREV 70 80 90 100 110 120 SSLLSYTQDL TGDGDGEDGD GSDTPVMPKL FRETRTRSES PAVRTRNNNS VSSRERHRPS 130 140 150 160 170 180 PRSTRGRQGR NHVDESPVEF PATRSLRRRA TASAGTPWPS PPSSYLTIDL TDDTEDTHGT 190 200 210 220 230 240 PQSSSTPYAR LAQDSQQGGM ESPQVEADSG DGDSSEYQDG KEFGIGDLVW GKIKGFSWWP 250 260 270 280 290 300 AMVVSWKATS KRQAMSGMRW VQWFGDGKFS EVSADKLVAL GLFSQHFNLA TFNKLVSYRK 310 320 330 340 350 360 AMYHALEKAR VRAGKTFPSS PGDSLEDQLK PMLEWAHGGF KPTGIEGLKP NNTQPVVNKS 370 380 390 400 410 420 KVRRAGSRKL ESRKYENKTR RRTADDSATS DYCPAPKRLK TNCYNNGKDR GDEDQSREQM 430 440 450 460 470 480 ASDVANNKSS LEDGCLSCGR KNPVSFHPLF EGGLCQTCRD RFLELFYMYD DDGYQSYCTV 490 500 510 520 530 540 CCEGRELLLC SNTSCCRCFC VECLEVLVGT GTAAEAKLQE PWSCYMCLPQ RCHGVLRRRK 550 560 570 580 590 600 DWNVRLQAFF TSDTGLEYEA PKLYPAIPAA RRRPIRVLSL FDGIATGYLV LKELGIKVGK 610 620 630 640 650 660 YVASEVCEES IAVGTVKHEG NIKYVNDVRN ITKKNIEEWG PFDLVIGGSP CNDLSNVNPA 670 680 690 700 710 720 RKGLYEGTGR LFFEFYHLLN YSRPKEGDDR PFFWMFENVV AMKVGDKRDI SRFLECNPVM 730 740 750 760 770 780 IDAIKVSAAH RARYFWGNLP GMNRPVIASK NDKLELQDCL EYNRIAKLKK VQTITTKSNS 790 800 810 820 830 840 IKQGKNQLFP VVMNGKEDVL WCTELERIFG FPVHYTDVSN MGRGARQKLL GRSWSVPVIR 850 HLFAPLKDYF ACE
	Isoform 2 [UniParc]. Checksum: DAD71DB275947261	FASTA	833	93,407
	10 20 30 40 50 60 MKGDTRHLNG EEDAGGREDS ILVNGACSDQ SSDSPPILEA IRTPEIRGRR SSSRLSKREV 70 80 90 100 110 120 SSLLSYTQDL TGDGDGEDGD GSDTPVMPKL FRETRTRSES PAVRTRNNNS VSSRERHRPS 130 140 150 160 170 180 PRSTRGRQGR NHVDESPVEF PATRSLRRRA TASAGTPWPS PPSSYLTIDL TDDTEDTHGT 190 200 210 220 230 240 PQSSSTPYAR LAQDSQQGGM ESPQVEADSG DGDSSEYQDG KEFGIGDLVW GKIKGFSWWP 250 260 270 280 290 300 AMVVSWKATS KRQAMSGMRW VQWFGDGKFS EVSADKLVAL GLFSQHFNLA TFNKLVSYRK 310 320 330 340 350 360 AMYHALEKAR VRAGKTFPSS PGDSLEDQLK PMLEWAHGGF KPTGIEGLKP NNTQPENKTR 370 380 390 400 410 420 RRTADDSATS DYCPAPKRLK TNCYNNGKDR GDEDQSREQM ASDVANNKSS LEDGCLSCGR 430 440 450 460 470 480 KNPVSFHPLF EGGLCQTCRD RFLELFYMYD DDGYQSYCTV CCEGRELLLC SNTSCCRCFC 490 500 510 520 530 540 VECLEVLVGT GTAAEAKLQE PWSCYMCLPQ RCHGVLRRRK DWNVRLQAFF TSDTGLEYEA 550 560 570 580 590 600 PKLYPAIPAA RRRPIRVLSL FDGIATGYLV LKELGIKVGK YVASEVCEES IAVGTVKHEG 610 620 630 640 650 660 NIKYVNDVRN ITKKNIEEWG PFDLVIGGSP CNDLSNVNPA RKGLYEGTGR LFFEFYHLLN 670 680 690 700 710 720 YSRPKEGDDR PFFWMFENVV AMKVGDKRDI SRFLECNPVM IDAIKVSAAH RARYFWGNLP 730 740 750 760 770 780 GMNRPVIASK NDKLELQDCL EYNRIAKLKK VQTITTKSNS IKQGKNQLFP VVMNGKEDVL 790 800 810 820 830 WCTELERIFG FPVHYTDVSN MGRGARQKLL GRSWSVPVIR HLFAPLKDYF ACE
	Isoform 3 [UniParc]. Checksum: E7777E3879B1D93B	FASTA	770	86,177
	10 20 30 40 50 60 MKGDTRHLNG EEDAGGREDS ILVNGACSDQ SSDSPPILEA IRTPEIRGRR SSSRLSKREV 70 80 90 100 110 120 SSLLSYTQDL TGDGDGEDGD GSDTPVMPKL FRETRTRSES PAVRTRNNNS VSSRERHRPS 130 140 150 160 170 180 PRSTRGRQGR NHVDESPVEF PATRSLRRRA TASAGTPWPS PPSSYLTIDL TDDTEDTHGT 190 200 210 220 230 240 PQSSSTPYAR LAQDSQQGGM ESPQVEADSG DGDSSEYQDG KEFGIGDLVW GKIKGFSWWP 250 260 270 280 290 300 AMVVSWKATS KRQAMSGMRW VQWFGDGKFS EVSADKLVAL GLFSQHFNLA TFNKLVSYRK 310 320 330 340 350 360 AMYHALEKAR VRAGKTFPSS PGDSLEDQLK PMLEWAHGGF KPTGIEGLKP NNTQPENKTR 370 380 390 400 410 420 RRTADDSATS DYCPAPKRLK TNCYNNGKDR GDEDQSREQM ASDVANNKSS LEDGCLSCGR 430 440 450 460 470 480 KNPVSFHPLF EGGLCQTCRD RFLELFYMYD DDGYQSYCTV CCEGRELLLC SNTSCCRCFC 490 500 510 520 530 540 VECLEVLVGT GTAAEAKLQE PWSCYMCLPQ RCHGVLRRRK DWNVRLQAFF TSDTGLEYEA 550 560 570 580 590 600 PKLYPAIPAA RRRPIRVLSL FDGIATGYLV LKELGIKVGK YVASEVCEES IAVGTVKHEG 610 620 630 640 650 660 NIKYVNDVRN ITKKNIEEWG PFDLVIGGSP CNDLSNVNPA RKGLYEGTGR LFFEFYHLLN 670 680 690 700 710 720 YSRPKEGDDR PFFWMFENVV AMKVGDKRDI SRFLECNPVM IDAIKVSAAH RARYFWGNLP 730 740 750 760 770 GMNRIFGFPV HYTDVSNMGR GARQKLLGRS WSVPVIRHLF APLKDYFACE
	Isoform 4 [UniParc]. Checksum: 21173ED0988996FC	FASTA	724	80,845
	10 20 30 40 50 60 MKGDTRHLNG EEDAGGREDS ILVNGACSDQ SSDSPPILEA IRTPEIRGRR SSSRLSKREV 70 80 90 100 110 120 SSLLSYTQDL TGDGDGEDGD GSDTPVMPKL FRETRTRSES PAVRTRNNNS VSSRERHRPS 130 140 150 160 170 180 PRSTRGRQGR NHVDESPVEF PATRSLRRRA TASAGTPWPS PPSSYLTIDL TDDTEDTHGT 190 200 210 220 230 240 PQSSSTPYAR LAQDSQQGGM ESPQVEADSG DGDSSEYQDG KEFGIGDLVW GKIKGFSWWP 250 260 270 280 290 300 AMVVSWKATS KRQAMSGMRW VQWFGDGKFS EVSADKLVAL GLFSQHFNLA TFNKLVSYRK 310 320 330 340 350 360 AMYHALEKAR VRAGKTFPSS PGDSLEDQLK PMLEWAHGGF KPTGIEGLKP NNTQPENKTR 370 380 390 400 410 420 RRTADDSATS DYCPAPKRLK TNCYNNGKDR GDEDQSREQM ASDVANNKSS LEDGCLSCGR 430 440 450 460 470 480 KNPVSFHPLF EGGLCQTCRD RFLELFYMYD DDGYQSYCTV CCEGRELLLC SNTSCCRCFC 490 500 510 520 530 540 VECLEVLVGT GTAAEAKLQE PWSCYMCLPQ RCHGVLRRRK DWNVRLQAFF TSDTGLEYEA 550 560 570 580 590 600 PKLYPAIPAA RRRPIRVLSL FDGIATGYLV LKELGIKVGK YVASEVCEES IAVGTVKHEG 610 620 630 640 650 660 NIKYVNDVRN ITKKNIEEWG PFDLVIGGSP CNDLSNVNPA RKGLYEGTGR LFFEFYHLLN 670 680 690 700 710 720 YSRPKEGDDR PFFWMFENVV AMKVGDKRDI SRFLECNPVM IDAIKVSAAH RARYFWGNLP GMNS
	Isoform 5 [UniParc]. Checksum: C6721C7241B9283A	FASTA	792	88,572
	10 20 30 40 50 60 MKGDTRHLNG EEDAGGREDS ILVNGACSDQ SSDSPPILEA IRTPEIRGRR SSSRLSKREV 70 80 90 100 110 120 SSLLSYTQDL TGDGDGEDGD GSDTPVMPKL FRETRTRSES PAVRTRNNNS VSSRERHRPS 130 140 150 160 170 180 PRSTRGRQGR NHVDESPVEF PATRSLRRRA TASAGTPWPS PPSSYLTIDL TDDTEDTHGT 190 200 210 220 230 240 PQSSSTPYAR LAQDSQQGGM ESPQVEADSG DGDSSEYQDG KEFGIGDLVW GKIKGFSWWP 250 260 270 280 290 300 AMVVSWKATS KRQAMSGMRW VQWFGDGKFS EVSADKLVAL GLFSQHFNLA TFNKLVSYRK 310 320 330 340 350 360 AMYHALEKAR VRAGKTFPSS PGDSLEDQLK PMLEWAHGGF KPTGIEGLKP NNTQPENKTR 370 380 390 400 410 420 RRTADDSATS DYCPAPKRLK TNCYNNGKDR GDEDQSREQM ASDVANNKSS LEDGCLSCGR 430 440 450 460 470 480 KNPVSFHPLF EGGLCQTCRD RFLELFYMYD DDGYQSYCTV CCEGRELLLC SNTSCCRCFC 490 500 510 520 530 540 VECLEVLVGT GTAAEAKLQE PWSCYMCLPQ RCHGVLRRRK DWNVRLQAFF TSDTGLEYEA 550 560 570 580 590 600 PKLYPAIPAA RRRPIRVLSL FDGIATGYLV LKELGIKVGK YVASEVCEES IAVGTVKHEG 610 620 630 640 650 660 NIKYVNDVRN ITKKNIEEWG PFDLVIGGSP CNDLSNVNPA RKGLYEGTGR LFFEFYHLLN 670 680 690 700 710 720 YSRPKEGDDR PFFWMFENVV AMKVGDKRDI SRFLECNPVM IDAIKVSAAH RARYFWGNLP 730 740 750 760 770 780 GMNRPVIASK NDKLELQDCL EYNRIAKDLW LSCALHRRVQ HGPWCPPEAA GKVLERACHP 790 TPLRPSEGLL CM
	Isoform 6 [UniParc]. Checksum: CFA82BB96B59EFBF	FASTA	845	94,689
	10 20 30 40 50 60 MEPSPEPPSL ESMKGDTRHL NGEEDAGGRE DSILVNGACS DQSSDSPPIL EAIRTPEIRG 70 80 90 100 110 120 RRSSSRLSKR EVSSLLSYTQ DLTGDGDGED GDGSDTPVMP KLFRETRTRS ESPAVRTRNN 130 140 150 160 170 180 NSVSSRERHR PSPRSTRGRQ GRNHVDESPV EFPATRSLRR RATASAGTPW PSPPSSYLTI 190 200 210 220 230 240 DLTDDTEDTH GTPQSSSTPY ARLAQDSQQG GMESPQVEAD SGDGDSSEYQ DGKEFGIGDL 250 260 270 280 290 300 VWGKIKGFSW WPAMVVSWKA TSKRQAMSGM RWVQWFGDGK FSEVSADKLV ALGLFSQHFN 310 320 330 340 350 360 LATFNKLVSY RKAMYHALEK ARVRAGKTFP SSPGDSLEDQ LKPMLEWAHG GFKPTGIEGL 370 380 390 400 410 420 KPNNTQPENK TRRRTADDSA TSDYCPAPKR LKTNCYNNGK DRGDEDQSRE QMASDVANNK 430 440 450 460 470 480 SSLEDGCLSC GRKNPVSFHP LFEGGLCQTC RDRFLELFYM YDDDGYQSYC TVCCEGRELL 490 500 510 520 530 540 LCSNTSCCRC FCVECLEVLV GTGTAAEAKL QEPWSCYMCL PQRCHGVLRR RKDWNVRLQA 550 560 570 580 590 600 FFTSDTGLEY EAPKLYPAIP AARRRPIRVL SLFDGIATGY LVLKELGIKV GKYVASEVCE 610 620 630 640 650 660 ESIAVGTVKH EGNIKYVNDV RNITKKNIEE WGPFDLVIGG SPCNDLSNVN PARKGLYEGT 670 680 690 700 710 720 GRLFFEFYHL LNYSRPKEGD DRPFFWMFEN VVAMKVGDKR DISRFLECNP VMIDAIKVSA 730 740 750 760 770 780 AHRARYFWGN LPGMNRPVIA SKNDKLELQD CLEYNRIAKL KKVQTITTKS NSIKQGKNQL 790 800 810 820 830 840 FPVVMNGKED VLWCTELERI FGFPVHYTDV SNMGRGARQK LLGRSWSVPV IRHLFAPLKD YFACE
	Isoform 7 [UniParc]. Checksum: 6C59147487ABA6DC	FASTA	694	77,719
	10 20 30 40 50 60 MKGDTRHLNG EEDAGGREDS ILVNGACSDQ SSDSPPILEA IRTPEIRGRR SSSRLSKREV 70 80 90 100 110 120 SSLLSYTQSL RRRATASAGT PWPSPPSSYL TIDLTDDTED THGTPQSSST PYARLAQDSQ 130 140 150 160 170 180 QGGMESPQVE ADSGDGDSSE YQDGKEFGIG DLVWGKIKGF SWWPAMVVSW KATSKRQAMS 190 200 210 220 230 240 GMRWVQWFGD GKFSEVSADK LVALGLFSQH FNLATFNKLV SYRKAMYHAL EKARVRAGKT 250 260 270 280 290 300 FPSSPGDSLE DQLKPMLEWA HGGFKPTGIE GLKPNNTQPE NKTRRRTADD SATSDYCPAP 310 320 330 340 350 360 KRLKTNCYNN GKDRGDEDQS REQMASDVAN NKSSLEDGCL SCGRKNPVSF HPLFEGGLCQ 370 380 390 400 410 420 TCRDRFLELF YMYDDDGYQS YCTVCCEGRE LLLCSNTSCC RCFCVECLEV LVGTGTAAEA 430 440 450 460 470 480 KLQEPWSCYM CLPQRCHGVL RRRKDWNVRL QAFFTSDTGL EYEAPKLYPA IPAARRRPIR 490 500 510 520 530 540 VLSLFDGIAT GYLVLKELGI KVGKYVASEV CEESIAVGTV KHEGNIKYVN DVRNITKKNI 550 560 570 580 590 600 EEWGPFDLVI GGSPCNDLSN VNPARKGLYE GTGRLFFEFY HLLNYSRPKE GDDRPFFWMF 610 620 630 640 650 660 ENVVAMKVGD KRDISRFLEC NPVMIDAIKV SAAHRARYFW GNLPGMNRIF GFPVHYTDVS 670 680 690 NMGRGARQKL LGRSWSVPVI RHLFAPLKDY FACE
	Isoform 8 [UniParc]. Checksum: E4465A68EC2334A0	FASTA	728	81,311
	10 20 30 40 50 60 MKGDTRHLNG EEDAGGREDS ILVNGACSDQ SSDSPPILEA IRTPEIRGRR SSSRLSKREV 70 80 90 100 110 120 SSLLSYTQDL TGDGDGEDGD GSDTPVMPKL FRETRTRSES PASLRRRATA SAGTPWPSPP 130 140 150 160 170 180 SSYLTIDLTD DTEDTHGTPQ SSSTPYARLA QDSQQGGMES PQVEADSGDG DSSEYQDGKE 190 200 210 220 230 240 FGIGDLVWGK IKGFSWWPAM VVSWKATSKR QAMSGMRWVQ WFGDGKFSEV SADKLVALGL 250 260 270 280 290 300 FSQHFNLATF NKLVSYRKAM YHALEKARVR AGKTFPSSPG DSLEDQLKPM LEWAHGGFKP 310 320 330 340 350 360 TGIEGLKPNN TQPENKTRRR TADDSATSDY CPAPKRLKTN CYNNGKDRGD EDQSREQMAS 370 380 390 400 410 420 DVANNKSSLE DGCLSCGRKN PVSFHPLFEG GLCQTCRDRF LELFYMYDDD GYQSYCTVCC 430 440 450 460 470 480 EGRELLLCSN TSCCRCFCVE CLEVLVGTGT AAEAKLQEPW SCYMCLPQRC HGVLRRRKDW 490 500 510 520 530 540 NVRLQAFFTS DTGLEYEAPK LYPAIPAARR RPIRVLSLFD GIATGYLVLK ELGIKVGKYV 550 560 570 580 590 600 ASEVCEESIA VGTVKHEGNI KYVNDVRNIT KKNIEEWGPF DLVIGGSPCN DLSNVNPARK 610 620 630 640 650 660 GLYEGTGRLF FEFYHLLNYS RPKEGDDRPF FWMFENVVAM KVGDKRDISR FLECNPVMID 670 680 690 700 710 720 AIKVSAAHRA RYFWGNLPGM NRIFGFPVHY TDVSNMGRGA RQKLLGRSWS VPVIRHLFAP LKDYFACE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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] (ISOFORMS 1; 2 AND 3). Tissue: Fetal testis and Small intestine.
[2]	"Chromosome instability and immunodeficiency syndrome caused by mutations in a DNA methyltransferase gene." Xu G.-L., Bestor T.H., Bourc'his D., Hsieh C.-L., Tommerup N., Bugge M., Hulten M., Qu X., Russo J.J., Viegas-Pequignot E. Nature 402:187-191(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), VARIANTS ICF1 SER-663; GLY-726; GLY-817 AND MET-818. Tissue: Testis.
[3]	"Cloning, expression and characterization of human DNMT3 genes." Ni J., Pradhan S., Roberts R.J. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 8). Tissue: Brain.
[5]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: NUCLEOTIDE SEQUENCE [MRNA] OF 636-853 (ISOFORMS 1; 4 AND 5). Tissue: Testis.
[8]	"Dnmt3b, de novo DNA methyltransferase, interacts with SUMO-1 and Ubc9 through its N-terminal region and is subject to modification by SUMO-1." Kang E.S., Park C.W., Chung J.H. Biochem. Biophys. Res. Commun. 289:862-868(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UBL1 AND UBE2I9, SUMOYLATION, SUBCELLULAR LOCATION.
[9]	"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: INTERACTION WITH DNMT1 AND DNMT3A, SUBCELLULAR LOCATION.
[10]	"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.
[11]	"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: FUNCTION, INTERACTION WITH THE PRC2/EED-EZH2 COMPLEX.
[12]	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)
[13]	"Zinc-fingers and homeoboxes 1 (ZHX1) binds DNA methyltransferase (DNMT) 3B to enhance DNMT3B-mediated transcriptional repression." Kim S.H., Park J., Choi M.C., Kim H.P., Park J.H., Jung Y., Lee J.H., Oh D.Y., Im S.A., Bang Y.J., Kim T.Y. Biochem. Biophys. Res. Commun. 355:318-323(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ZHX1.
[14]	"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.
[15]	"DNA methyltransferase 1 and 3B activate BAG-1 expression via recruitment of CTCFL/BORIS and modulation of promoter histone methylation." Sun L., Huang L., Nguyen P., Bisht K.S., Bar-Sela G., Ho A.S., Bradbury C.M., Yu W., Cui H., Lee S., Trepel J.B., Feinberg A.P., Gius D. Cancer Res. 68:2726-2735(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"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.
[17]	"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-136, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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-82; THR-96; SER-100; SER-110; SER-136; SER-195; SER-202 AND SER-209, MASS SPECTROMETRY.
[19]	"Crystal structure of the PWWP domain of human DNA (cytosine-5-)-methyltransferase 3 beta." Structural genomics consortium (SGC) Submitted (MAR-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 206-355.
[20]	"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 (2.04 ANGSTROMS) OF 380-509.
[21]	"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: VARIANTS ICF1 THR-603 AND SER-THR-PRO-806 INS.
[22]	"The DNMT3B DNA methyltransferase gene is mutated in the ICF immunodeficiency syndrome." Hansen R.S., Wijmenga C., Luo P., Stanek A.M., Canfield T.K., Weemaes C.M.R., Gartler S.M. Proc. Natl. Acad. Sci. U.S.A. 96:14412-14417(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ICF1 THR-603; GLY-726 AND SER-THR-PRO-806 INS.
[23]	"Genetic variation in ICF syndrome: evidence for genetic heterogeneity." Wijmenga C., Hansen R.S., Gimelli G., Bjoerck E.J., Davies E.G., Valentine D., Belohradsky B.H., van Dongen J.J., Smeets D.F.C.M., van den Heuvel L.P.W.J., Luyten J.A.F.M., Strengman E., Weemaes C.M.R., Pearson P.L. Hum. Mutat. 16:509-517(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ICF1 VAL-585; THR-603; ALA-606; GLY-699; GLY-726; PRO-766; ARG-814 AND MET-818.
[24]	"DNMT3B mutations and DNA methylation defect define two types of ICF syndrome." Jiang Y.L., Rigolet M., Bourc'his D., Nigon F., Bokesoy I., Fryns J.-P., Hulten M., Jonveaux P., Maraschio P., Megarbane A., Moncla A., Viegas-Pequignot E. Hum. Mutat. 25:56-63(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ICF1 PRO-270; VAL-585; THR-603; ALA-606; SER-663; PRO-664; GLY-699; GLY-726; PRO-766; ARG-814; GLY-817; MET-818 AND GLN-840.
+	Additional computationally mapped references.

Web resources

DNMT3Bbase

DNMT3B mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF156487 mRNA. Translation: AAD53062.1.
AF156488 mRNA. Translation: AAD53063.1.
AF176228 mRNA. Translation: AAF04015.1.
AF331857 mRNA. Translation: AAL57040.1.
AK299821 mRNA. Translation: BAG61690.1.
AK299915 mRNA. Translation: BAG61753.1.
AL035071 Genomic DNA. Translation: CAB53069.1.
AL035071 Genomic DNA. Translation: CAB53070.1.
AL035071 Genomic DNA. Translation: CAB53071.1.
AL035071 Genomic DNA. Translation: CAM27373.1.
CH471077 Genomic DNA. Translation: EAW76351.1.
CH471077 Genomic DNA. Translation: EAW76352.1.
CH471077 Genomic DNA. Translation: EAW76353.1.
CH471077 Genomic DNA. Translation: EAW76354.1.
CH471077 Genomic DNA. Translation: EAW76356.1.
AF129267 mRNA. Translation: AAD31432.1.
AF129268 mRNA. Translation: AAD31433.1.
AF129269 mRNA. Translation: AAD31434.1.

IPI

IPI00012593.
IPI00180702.
IPI00218357.
IPI00218358.
IPI00218359.
IPI00218360.
IPI00908348.
IPI00942456.

RefSeq

NP_001193984.1. NM_001207055.1.
NP_001193985.1. NM_001207056.1.
NP_008823.1. NM_006892.3.
NP_787044.1. NM_175848.1.
NP_787045.1. NM_175849.1.
NP_787046.1. NM_175850.2.

UniGene

Hs.713611.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FLG	X-ray	1.80	A	206-355	[»]
3QKJ	X-ray	2.04	A/B/C/D	380-509	[»]

ProteinModelPortal

Q9UBC3.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-30000N.

IntAct

Q9UBC3. 10 interactions.

MINT

MINT-2820816.

STRING

9606.ENSP00000328547.

Protein family/group databases

REBASE

4120. M.HsaDnmt3B.

PTM databases

PhosphoSite

Q9UBC3.

Polymorphism databases

DMDM

17375667.

Proteomic databases

PaxDb

Q9UBC3.

PRIDE

Q9UBC3.

Protocols and materials databases

DNASU

1789.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000201963; ENSP00000201963; ENSG00000088305.
ENST00000328111; ENSP00000328547; ENSG00000088305.
ENST00000344505; ENSP00000345105; ENSG00000088305.
ENST00000348286; ENSP00000337764; ENSG00000088305.
ENST00000353855; ENSP00000313397; ENSG00000088305.
ENST00000443239; ENSP00000403169; ENSG00000088305.
ENST00000456297; ENSP00000412305; ENSG00000088305.

GeneID

1789.

KEGG

hsa:1789.

UCSC

uc002wyc.3. human.
uc002wyd.3. human.
uc002wye.3. human.
uc002wyf.3. human.

Organism-specific databases

CTD

1789.

GeneCards

GC20P031350.

HGNC

HGNC:2979. DNMT3B.

HPA

HPA001595.

MIM

242860. phenotype.
602900. gene.

neXtProt

NX_Q9UBC3.

Orphanet

2268. ICF syndrome.

PharmGKB

PA27446.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG70699.

HOVERGEN

HBG051381.

InParanoid

Q9UBC3.

KO

K00558.

OMA

RRKDWNV.

OrthoDB

EOG4CVG68.

PhylomeDB

Q9UBC3.

Gene expression databases

ArrayExpress

Q9UBC3.

Bgee

Q9UBC3.

CleanEx

HS_DNMT3B.

Genevestigator

Q9UBC3.

GermOnline

ENSG00000088305. Homo sapiens.

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

Search...

Other

BindingDB

Q9UBC3.

ChEMBL

CHEMBL6095.

EvolutionaryTrace

Q9UBC3.

GenomeRNAi

1789.

NextBio

7289.

SOURCE

Search...

Entry information

Entry name

DNM3B_HUMAN

Accession

Primary (citable) accession number: Q9UBC3
Secondary accession number(s): A2A2E2 , B4DSM8, B4DSU1, E1P5M6, E1P5M7, E7EN63, E9PBF2, Q9UBD4, Q9UJQ5, Q9UKA6, Q9UNE5, Q9Y5R9, Q9Y5S0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 130 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.