Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA (cytosine-5)-methyltransferase 3B

Gene

Dnmt3b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 similarity6 Publications

Catalytic activityi

S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.PROSITE-ProRule annotation

Enzyme regulationi

Activated by binding to the regulatory factor DNMT3L.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei611S-adenosyl-L-methionineBy similarity1
Active sitei657PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri439 – 469GATA-type; atypicalPROSITE-ProRule annotationAdd BLAST31
Zinc fingeri480 – 536PHD-type; atypicalPROSITE-ProRule annotationAdd BLAST57

GO - Molecular functioni

  • DNA (cytosine-5-)-methyltransferase activity Source: MGI
  • DNA (cytosine-5-)-methyltransferase activity, acting on CpN substrates Source: Reactome
  • DNA binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • methyltransferase activity Source: UniProtKB
  • transcription corepressor activity Source: MGI

GO - Biological processi

  • cellular response to amino acid stimulus Source: MGI
  • chromatin silencing at rDNA Source: Reactome
  • DNA methylation Source: MGI
  • DNA methylation involved in embryo development Source: UniProtKB
  • DNA methylation on cytosine Source: Reactome
  • inactivation of X chromosome by DNA methylation Source: MGI
  • methylation-dependent chromatin silencing Source: MGI
  • negative regulation of gene expression, epigenetic Source: UniProtKB
  • negative regulation of histone H3-K9 methylation Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of histone H3-K4 methylation Source: MGI
  • protein complex localization Source: MGI
  • regulation of gene expression by genetic imprinting Source: MGI
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.
ReactomeiR-MMU-212300. PRC2 methylates histones and DNA.
R-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-5334118. DNA methylation.
R-MMU-573389. NoRC negatively regulates rRNA expression.

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
Proteomesi
  • UP000000589 Componenti: 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

  • chromosome, centromeric region Source: UniProtKB
  • heterochromatin Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • nuclear heterochromatin Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi236 – 237VW → RR: Prevents accumulation in pericentric heterochromatin. 1 Publication2
Mutagenesisi277S → P: Prevents accumulation in pericentric heterochromatin. 1 Publication1
Mutagenesisi609A → T: Significantly reduces activity. 1 Publication1
Mutagenesisi656 – 657PC → GT: No effect on localization. 1 Publication2
Mutagenesisi669G → S: Significantly reduces activity. 1 Publication1
Mutagenesisi670L → T: Significantly reduces activity. 1 Publication1
Mutagenesisi725V → G: Loss of activity. 1 Publication1
Mutagenesisi823D → G: Significantly reduces activity. 1 Publication1
Mutagenesisi824V → M: Significantly reduces activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2189115.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000880461 – 859DNA (cytosine-5)-methyltransferase 3BAdd BLAST859

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei96PhosphoserineBy similarity1
Modified residuei112PhosphothreonineBy similarity1
Modified residuei116PhosphoserineBy similarity1
Modified residuei216PhosphoserineBy similarity1
Modified residuei415Citrulline1 Publication1

Post-translational modificationi

Sumoylated.By similarity
Citrullinated by PADI4.1 Publication

Keywords - PTMi

Citrullination, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO88509.
PaxDbiO88509.
PeptideAtlasiO88509.
PRIDEiO88509.

PTM databases

iPTMnetiO88509.
PhosphoSitePlusiO88509.

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

BgeeiENSMUSG00000027478.
CleanExiMM_DNMT3B.
ExpressionAtlasiO88509. baseline and differential.
GenevisibleiO88509. MM.

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 interactors.
DIPiDIP-43736N.
IntActiO88509. 5 interactors.
MINTiMINT-2523761.
STRINGi10090.ENSMUSP00000051830.

Chemistry databases

BindingDBiO88509.

Structurei

Secondary structure

1859
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi226 – 229Combined sources4
Beta strandi235 – 240Combined sources6
Turni241 – 243Combined sources3
Beta strandi244 – 251Combined sources8
Helixi253 – 255Combined sources3
Beta strandi265 – 270Combined sources6
Turni271 – 273Combined sources3
Beta strandi276 – 280Combined sources5
Helixi281 – 283Combined sources3
Helixi290 – 293Combined sources4
Helixi296 – 301Combined sources6
Helixi303 – 320Combined sources18
Helixi332 – 344Combined sources13
Turni348 – 350Combined sources3
Helixi351 – 355Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KHCX-ray1.80A219-366[»]
ProteinModelPortaliO88509.
SMRiO88509.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88509.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini232 – 290PWWPPROSITE-ProRule annotationAdd BLAST59
Domaini428 – 560ADDPROSITE-ProRule annotationAdd BLAST133
Domaini581 – 859SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd BLAST279

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 305Interaction with DNMT1 and DNMT3ABy similarityAdd BLAST305
Regioni440 – 532Interaction with the PRC2/EED-EZH2 complexAdd BLAST93
Regioni588 – 592S-adenosyl-L-methionine bindingBy similarity5
Regioni633 – 635S-adenosyl-L-methionine bindingBy similarity3
Regioni838 – 840S-adenosyl-L-methionine bindingBy similarity3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi160 – 165Poly-Arg6

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)DescriptionActionsGraphical viewLength
Zinc fingeri439 – 469GATA-type; atypicalPROSITE-ProRule annotationAdd BLAST31
Zinc fingeri480 – 536PHD-type; atypicalPROSITE-ProRule annotationAdd BLAST57

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IGHW. Eukaryota.
ENOG410XQ4Y. LUCA.
GeneTreeiENSGT00390000008341.
HOGENOMiHOG000230875.
HOVERGENiHBG051381.
InParanoidiO88509.
KOiK17399.
TreeFamiTF329039.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR025766. ADD.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR030488. DNMT3B.
IPR000313. PWWP_dom.
IPR029063. SAM-dependent_MTases.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR23068:SF9. PTHR23068:SF9. 2 hits.
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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti217 – 218RD → IY in AAF74515 (PubMed:12567489).Curated2
Sequence conflicti217 – 218RD → IY in AAF74516 (PubMed:12567489).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005642363 – 382Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST20
Alternative sequenceiVSP_005643750 – 812Missing in isoform 3 and isoform 4. 2 PublicationsAdd BLAST63

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.3. mouse. [O88509-1]
uc008nic.3. mouse. [O88509-2]
uc008nie.3. mouse. [O88509-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KHCX-ray1.80A219-366[»]
ProteinModelPortaliO88509.
SMRiO88509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199262. 10 interactors.
DIPiDIP-43736N.
IntActiO88509. 5 interactors.
MINTiMINT-2523761.
STRINGi10090.ENSMUSP00000051830.

Chemistry databases

BindingDBiO88509.
ChEMBLiCHEMBL2189115.

Protein family/group databases

REBASEi3748. M.MmuDnmt3B.

PTM databases

iPTMnetiO88509.
PhosphoSitePlusiO88509.

Proteomic databases

MaxQBiO88509.
PaxDbiO88509.
PeptideAtlasiO88509.
PRIDEiO88509.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.3. mouse. [O88509-1]
uc008nic.3. mouse. [O88509-2]
uc008nie.3. mouse. [O88509-3]

Organism-specific databases

CTDi1789.
MGIiMGI:1261819. Dnmt3b.

Phylogenomic databases

eggNOGiENOG410IGHW. Eukaryota.
ENOG410XQ4Y. LUCA.
GeneTreeiENSGT00390000008341.
HOGENOMiHOG000230875.
HOVERGENiHBG051381.
InParanoidiO88509.
KOiK17399.
TreeFamiTF329039.

Enzyme and pathway databases

BRENDAi2.1.1.37. 3474.
ReactomeiR-MMU-212300. PRC2 methylates histones and DNA.
R-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-5334118. DNA methylation.
R-MMU-573389. NoRC negatively regulates rRNA expression.

Miscellaneous databases

ChiTaRSiDnmt3b. mouse.
EvolutionaryTraceiO88509.
PROiO88509.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027478.
CleanExiMM_DNMT3B.
ExpressionAtlasiO88509. baseline and differential.
GenevisibleiO88509. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR025766. ADD.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR030488. DNMT3B.
IPR000313. PWWP_dom.
IPR029063. SAM-dependent_MTases.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR23068:SF9. PTHR23068:SF9. 2 hits.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 152 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.