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O88508 (DNM3A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA (cytosine-5)-methyltransferase 3A

Short name=Dnmt3a
EC=2.1.1.37
Alternative name(s):
DNA methyltransferase MmuIIIA
Short name=DNA MTase MmuIIIA
Short name=M.MmuIIIA
Gene names
Name:Dnmt3a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length908 AA.
Sequence statusComplete.
Protein existenceEvidence 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. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZBTB18. Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. Can actively repress transcription through the recruitment of HDAC activity. Ref.5 Ref.6 Ref.8 Ref.9 Ref.12 Ref.15 Ref.19 Ref.20

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.14 Ref.19

Subunit structure

Heterotetramer composed of 1 DNMT3A homodimer and 2 DNMT3L subunits (DNMT3L-DNMT3A-DNMT3A-DNMT3L). Interacts with DNMT1 and DNMT3B. Interacts with MPHOSPH8. Interacts with histone H3 that is not methylated at 'Lys-4' (H3K4) By similarity. Binds the ZBTB18 transcriptional repressor. Interacts with SETDB1. Associates with HDAC1 through its ADD domain. Interacts with the PRC2/EED-EZH2 complex. Interacts with UBC9, PIAS1 and PIAS2. Ref.8 Ref.10 Ref.13 Ref.17 Ref.21

Subcellular location

Nucleus. Cytoplasm By similarity. Note: Accumulates in the major satellite repeats at pericentric heterochromatin. Ref.4 Ref.11 Ref.22

Tissue specificity

Isoform 1 is expressed ubiquitously at low levels. Expression of isoform 2 is restricted to tissues containing cells which are undergoing active de novo methylation, including spleen, testis and thymus. Ref.4

Developmental stage

At E7.5, the protein is moderately expressed in embryonic ectoderm and weakly in mesodermal cells. At E8.5 and E9.5, the expression become ubiquitous with an increase in the somites and in the ventral part of the embryo. Ref.5

Domain

The PWWP domain is essential for targeting to pericentric heterochromatin. It specifically recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3) (Ref.22).

Post-translational modification

Sumoylated; sumoylation disrupts the ability to interact with histone deacetylases (HDAC1 and HDAC2) and repress transcription. Ref.13

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

Contains 1 ADD domain.

Contains 1 GATA-type zinc finger.

Contains 1 PHD-type zinc finger.

Contains 1 PWWP domain.

Contains 1 SAM-dependent MTase C5-type domain.

Sequence caution

The sequence BAB28644.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative promoter usage
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionChromatin regulator
Methyltransferase
Repressor
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processC-5 methylation of cytosine

Inferred from direct assay Ref.6. Source: GOC

DNA methylation

Inferred from sequence or structural similarity. Source: UniProtKB

DNA methylation involved in embryo development

Inferred from mutant phenotype Ref.12. Source: UniProtKB

DNA methylation involved in gamete generation

Inferred from mutant phenotype Ref.12. Source: UniProtKB

DNA methylation on cytosine within a CG sequence

Inferred from electronic annotation. Source: Ensembl

S-adenosylhomocysteine metabolic process

Inferred from electronic annotation. Source: Ensembl

S-adenosylmethioninamine metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular response to amino acid stimulus

Inferred from direct assay PubMed 20548288. Source: MGI

hypermethylation of CpG island

Inferred from direct assay PubMed 21047779. Source: BHF-UCL

maintenance of DNA methylation

Traceable author statement PubMed 21047779. Source: BHF-UCL

methylation-dependent chromatin silencing

Inferred from direct assay PubMed 16322236. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16322236. Source: MGI

regulation of gene expression by genetic imprinting

Inferred from direct assay PubMed 21047779. Source: BHF-UCL

spermatogenesis

Inferred from mutant phenotype PubMed 11934864. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromosome, centromeric region

Inferred from direct assay Ref.11. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

euchromatin

Inferred from sequence or structural similarity. Source: UniProtKB

heterochromatin

Inferred from direct assay PubMed 16322236. Source: MGI

nuclear heterochromatin

Inferred from direct assay PubMed 11934864. Source: MGI

nuclear matrix

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.13. Source: UniProtKB

   Molecular_functionDNA (cytosine-5-)-methyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates

Inferred from electronic annotation. Source: Ensembl

DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin binding

Inferred from direct assay PubMed 16322236. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methyltransferase activity

Traceable author statement PubMed 11934864. Source: MGI

protein binding

Inferred from physical interaction Ref.13. Source: UniProtKB

unmethylated CpG binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Dnmt3lQ9CWR86EBI-995154,EBI-3043871
HellsQ608484EBI-995154,EBI-3043887

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform 1 (identifier: O88508-1)

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: O88508-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-219: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 908908DNA (cytosine-5)-methyltransferase 3A
PRO_0000088044

Regions

Domain288 – 34659PWWP
Domain478 – 610133ADD
Domain630 – 908279SAM-dependent MTase C5-type
Zinc finger489 – 51931GATA-type; atypical
Zinc finger530 – 58657PHD-type; atypical
Region195 – 399205Interaction with DNMT1 and DNMT3B By similarity
Region490 – 58293Interaction with the PRC2/EED-EZH2 complex
Region637 – 6415S-adenosyl-L-methionine binding By similarity
Region682 – 6843S-adenosyl-L-methionine binding By similarity
Region887 – 8893S-adenosyl-L-methionine binding By similarity

Sites

Active site7061 By similarity
Binding site6601S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity
Modified residue2391Phosphoserine By similarity
Modified residue2511Phosphoserine By similarity
Modified residue2571Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 219219Missing in isoform 2.
VSP_009423

Experimental info

Mutagenesis302 – 3032WP → ST: Prevents accumulation in pericentric heterochromatin. Ref.11
Mutagenesis6361F → A: Reduces activity about 20-fold. Loss of substrate binding. Ref.11 Ref.16
Mutagenesis6601E → A: Reduces activity about 15-fold. Loss of substrate binding. Ref.11 Ref.16
Mutagenesis6821D → A: Strongly reduces substrate binding. No effect on activity. Ref.11 Ref.16
Mutagenesis705 – 7062PC → VD: No effect on localization. Ref.11 Ref.16
Mutagenesis7061C → A: Reduces activity about 5-fold. Reduces DNA-binding capacity. Ref.11 Ref.16
Mutagenesis7071N → Q: Reduces activity about 3-fold. Ref.11 Ref.16
Mutagenesis7101S → A: No effect on activity. Ref.11 Ref.16
Mutagenesis7161R → A: Reduces activity about 30-fold. Reduces DNA-binding capacity. Ref.11 Ref.16
Mutagenesis7171K → A: Reduces activity about 3-fold. Ref.11 Ref.16
Mutagenesis7281F → A: Loss of activity du to the incapacity to bind the regulatory subunit DNMT3L. Ref.11 Ref.19
Mutagenesis7521E → A: Reduces activity about 10-fold. Ref.11 Ref.16
Mutagenesis7531N → A: Reduces activity about 10-fold. Ref.11 Ref.16
Mutagenesis7881R → A: Reduces activity about 15-fold. Ref.11 Ref.16
Mutagenesis8271R → A: Reduces activity about 2-fold. Reduces DNA-binding capacity. Ref.11 Ref.16
Mutagenesis8321R → A: Reduces DNA-binding capacity. No effect on activity. Ref.11 Ref.16
Mutagenesis8781R → A: Reduces activity about 6-fold. Reduces DNA-binding capacity. Ref.11 Ref.16
Mutagenesis8811R → A: Loss of activity. Strongly reduces substrate binding. Ref.11 Ref.16
Mutagenesis8831R → A: Reduces activity about 3-fold. Reduces DNA-binding capacity. Ref.11 Ref.16
Sequence conflict1511Q → P in AAH07466. Ref.4
Sequence conflict7751M → T in BAB28644. Ref.3
Sequence conflict7811V → G in BAB28644. Ref.3
Sequence conflict7911W → R in BAB28644. Ref.3
Sequence conflict8091L → P in BAB28644. Ref.3
Sequence conflict9041Y → I in BAB28644. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 2.
Checksum: 5F98D5A8092C84A5

FASTA908101,672
        10         20         30         40         50         60 
MPSSGPGDTS SSSLEREDDR KEGEEQEENR GKEERQEPSA TARKVGRPGR KRKHPPVESS 

        70         80         90        100        110        120 
DTPKDPAVTT KSQPMAQDSG PSDLLPNGDL EKRSEPQPEE GSPAAGQKGG APAEGEGTET 

       130        140        150        160        170        180 
PPEASRAVEN GCCVTKEGRG ASAGEGKEQK QTNIESMKME GSRGRLRGGL GWESSLRQRP 

       190        200        210        220        230        240 
MPRLTFQAGD PYYISKRKRD EWLARWKREA EKKAKVIAVM NAVEENQASG ESQKVEEASP 

       250        260        270        280        290        300 
PAVQQPTDPA SPTVATTPEP VGGDAGDKNA TKAADDEPEY EDGRGFGIGE LVWGKLRGFS 

       310        320        330        340        350        360 
WWPGRIVSWW MTGRSRAAEG TRWVMWFGDG KFSVVCVEKL MPLSSFCSAF HQATYNKQPM 

       370        380        390        400        410        420 
YRKAIYEVLQ VASSRAGKLF PACHDSDESD SGKAVEVQNK QMIEWALGGF QPSGPKGLEP 

       430        440        450        460        470        480 
PEEEKNPYKE VYTDMWVEPE AAAYAPPPPA KKPRKSTTEK PKVKEIIDER TRERLVYEVR 

       490        500        510        520        530        540 
QKCRNIEDIC ISCGSLNVTL EHPLFIGGMC QNCKNCFLEC AYQYDDDGYQ SYCTICCGGR 

       550        560        570        580        590        600 
EVLMCGNNNC CRCFCVECVD LLVGPGAAQA AIKEDPWNCY MCGHKGTYGL LRRREDWPSR 

       610        620        630        640        650        660 
LQMFFANNHD QEFDPPKVYP PVPAEKRKPI RVLSLFDGIA TGLLVLKDLG IQVDRYIASE 

       670        680        690        700        710        720 
VCEDSITVGM VRHQGKIMYV GDVRSVTQKH IQEWGPFDLV IGGSPCNDLS IVNPARKGLY 

       730        740        750        760        770        780 
EGTGRLFFEF YRLLHDARPK EGDDRPFFWL FENVVAMGVS DKRDISRFLE SNPVMIDAKE 

       790        800        810        820        830        840 
VSAAHRARYF WGNLPGMNRP LASTVNDKLE LQECLEHGRI AKFSKVRTIT TRSNSIKQGK 

       850        860        870        880        890        900 
DQHFPVFMNE KEDILWCTEM ERVFGFPVHY TDVSNMSRLA RQRLLGRSWS VPVIRHLFAP 


LKEYFACV 

« Hide

Isoform 2 [UniParc].

Checksum: 0C1093AF43717684
Show »

FASTA68977,824

References

« Hide 'large scale' 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] (ISOFORM 1).
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Mammary gland.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6 and C57BL/6J.
Tissue: Brain, Embryo and Skin.
[4]"A novel Dnmt3a isoform produced from an alternative promoter localizes to euchromatin and its expression correlates with active de novo methylation."
Chen T., Ueda Y., Xie S., Li E.
J. Biol. Chem. 277:38746-38754(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY.
Strain: 129/SvJ.
[5]"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.
[6]"Enzymatic properties of recombinant Dnmt3a DNA methyltransferase from mouse: the enzyme modifies DNA in a non-processive manner and also methylates non-CpG correction sites."
Gowher H., Jeltsch A.
J. Mol. Biol. 309:1201-1208(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]Erratum
Gowher H., Jeltsch A.
J. Mol. Biol. 310:951-951(2001)
[8]"Dnmt3a binds deacetylases and is recruited by a sequence-specific repressor to silence transcription."
Fuks F., Burgers W.A., Godin N., Kasai M., Kouzarides T.
EMBO J. 20:2536-2544(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ZBTB18 AND HDAC1.
[9]"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.
[10]"Biochemical fractionation reveals association of DNA methyltransferase (Dnmt) 3b with Dnmt1 and that of Dnmt 3a with a histone H3 methyltransferase and Hdac1."
Datta J., Ghoshal K., Sharma S.M., Tajima S., Jacob S.T.
J. Cell. Biochem. 88:855-864(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH HDAC1.
[11]"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 302-VAL-PRO-303 AND 705-PRO-CYS-706.
[12]"Essential role for de novo DNA methyltransferase Dnmt3a in paternal and maternal imprinting."
Kaneda M., Okano M., Hata K., Sado T., Tsujimoto N., Li E., Sasaki H.
Nature 429:900-903(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1 modulates its interaction with histone deacetylases (HDACs) and its capacity to repress transcription."
Ling Y., Sankpal U.T., Robertson A.K., McNally J.G., Karpova T., Robertson K.D.
Nucleic Acids Res. 32:598-610(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION, INTERACTION WITH UBC9; PIAS1 AND PIAS2.
[14]"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.
[15]"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.
[16]"Mutational analysis of the catalytic domain of the murine Dnmt3a DNA-(cytosine C5)-methyltransferase."
Gowher H., Loutchanwoot P., Vorobjeva O., Handa V., Jurkowska R.Z., Jurkowski T.P., Jeltsch A.
J. Mol. Biol. 357:928-941(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PHE-636; GLU-660; ASP-682; CYS-706; ASN-707; SER-710; ARG-716; LYS-717; GLU-752; ASN-753; ARG-788; ARG-827; ARG-832; ARG-878; ARG-881 AND ARG-883.
[17]"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 THE PRC2/EED-EZH2 COMPLEX.
[18]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)
[19]"Structure of Dnmt3a bound to Dnmt3L suggests a model for de novo DNA methylation."
Jia D., Jurkowska R.Z., Zhang X., Jeltsch A., Cheng X.
Nature 449:248-251(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF PHE-728.
[20]"Mouse Dnmt3a preferentially methylates linker DNA and is inhibited by histone H1."
Takeshima H., Suetake I., Tajima S.
J. Mol. Biol. 383:810-821(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"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.
[22]"The Dnmt3a PWWP domain reads histone 3 lysine 36 trimethylation and guides DNA methylation."
Dhayalan A., Rajavelu A., Rathert P., Tamas R., Jurkowska R.Z., Ragozin S., Jeltsch A.
J. Biol. Chem. 285:26114-26120(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF068625 mRNA. Translation: AAC40177.2.
AF480164 mRNA. Translation: AAN40038.1.
AK013096 mRNA. Translation: BAB28644.2. Different initiation.
AK090132 mRNA. Translation: BAC41110.1.
AK147263 mRNA. Translation: BAE27806.1.
AK147627 mRNA. Translation: BAE28033.1.
AK147642 mRNA. Translation: BAE28043.1.
AK147676 mRNA. Translation: BAE28067.1.
AK157792 mRNA. Translation: BAE34200.1.
BC007466 mRNA. Translation: AAH07466.1.
CCDSCCDS25784.1. [O88508-2]
CCDS36397.1. [O88508-1]
RefSeqNP_001258682.1. NM_001271753.1. [O88508-1]
NP_031898.1. NM_007872.4. [O88508-1]
NP_714965.1. NM_153743.4. [O88508-2]
XP_006515016.1. XM_006514953.1. [O88508-1]
XP_006515017.1. XM_006514954.1. [O88508-1]
XP_006515018.1. XM_006514955.1. [O88508-1]
XP_006515019.1. XM_006514956.1. [O88508-1]
XP_006515020.1. XM_006514957.1. [O88508-2]
UniGeneMm.470389.
Mm.5001.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3SW9X-ray3.05P/Q39-50[»]
3SWCX-ray2.33P/Q39-50[»]
ProteinModelPortalO88508.
SMRO88508. Positions 279-421, 469-908.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199261. 18 interactions.
DIPDIP-38005N.
IntActO88508. 10 interactions.
MINTMINT-2521021.

Protein family/group databases

REBASE3747. M.MmuDnmt3A.

PTM databases

PhosphoSiteO88508.

Proteomic databases

MaxQBO88508.
PaxDbO88508.
PRIDEO88508.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020991; ENSMUSP00000020991; ENSMUSG00000020661. [O88508-1]
ENSMUST00000111186; ENSMUSP00000106817; ENSMUSG00000020661. [O88508-2]
ENSMUST00000172689; ENSMUSP00000133543; ENSMUSG00000020661. [O88508-2]
ENSMUST00000174817; ENSMUSP00000134009; ENSMUSG00000020661. [O88508-1]
GeneID13435.
KEGGmmu:13435.
UCSCuc007mxb.1. mouse. [O88508-1]

Organism-specific databases

CTD1788.
MGIMGI:1261827. Dnmt3a.

Phylogenomic databases

eggNOGNOG70699.
GeneTreeENSGT00390000008341.
HOGENOMHOG000230875.
HOVERGENHBG051381.
InParanoidO88508.
KOK17398.
OMAFVGGMCQ.
OrthoDBEOG7MWGW6.
PhylomeDBO88508.
TreeFamTF329039.

Enzyme and pathway databases

BRENDA2.1.1.37. 3474.

Gene expression databases

ArrayExpressO88508.
BgeeO88508.
CleanExMM_DNMT3A.
GenevestigatorO88508.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR025766. ADD.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR025811. C5_MeTrfase_3.
IPR000313. PWWP_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamPF00145. DNA_methylase. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
SMARTSM00293. PWWP. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS51533. ADD. 1 hit.
PS00094. C5_MTASE_1. 1 hit.
PS50812. PWWP. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNMT3A. mouse.
NextBio283867.
PROO88508.
SOURCESearch...

Entry information

Entry nameDNM3A_MOUSE
AccessionPrimary (citable) accession number: O88508
Secondary accession number(s): Q3TZK8 expand/collapse secondary AC list , Q3UH24, Q8CJ60, Q922J0, Q9CSE1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot